|
Name |
Accession |
Description |
Interval |
E-value |
| Rho |
COG1158 |
Transcription termination factor Rho [Transcription]; |
76-448 |
0e+00 |
|
Transcription termination factor Rho [Transcription];
Pssm-ID: 440772 [Multi-domain] Cd Length: 373 Bit Score: 627.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 76 EGLLDLHEDGFGFLRTELYESSNDDIYVSPKQVKMFRLKTGDFIKGIARVKKDKDKFSPLIFVSDVNGLKAADAFNRSNF 155
Cdd:COG1158 10 EGVLEILPDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDAVTGQVRPPKEGEKYFALLRVESVNGEDPEEARKRPDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 156 ESLTPIYPNQKLKLETSKDKISQRIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKNFDDLKILVLLIDERPEEV 235
Cdd:COG1158 90 DNLTPLYPDERLRLETTPDDLSTRVIDLVAPIGKGQRGLIVAPPKAGKTTLLQDIANAITANHPEVHLIVLLIDERPEEV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 236 TDFKRFVnqyrdkdneltRTEVAASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAYNIMTPQSGRTL 315
Cdd:COG1158 170 TDMQRSV-----------KGEVIASTFDEPAERHVQVAELVIERAKRLVELGKDVVILLDSITRLARAYNLVVPASGRTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 316 SGGLDPLALIGPKKFFGAARNIENGGSLTIIATALVDTGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSST 395
Cdd:COG1158 239 SGGVDANALYKPKRFFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINKSGT 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1080175760 396 RKDNLLLNNKELEAVYKLRN--SDMkDKIDFTNELINLMAKCKSNDEFVELINKT 448
Cdd:COG1158 319 RREELLLSPEELEKVWILRRalSGM-DPVEAMEFLLDRLKKTKSNAEFLESMNKT 372
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
3-447 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 595.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 3 ININDLDKLKLDELREIGKNLSIKSLSSYRKNELVEIIKEAYSNSknfennesssndlddsnenfdlGEKFNCEGLLDLH 82
Cdd:PRK09376 1 MNLSELKNKSLSELLELAEELGIENASRLRKQELIFAILKAQAEK----------------------GGDIFGEGVLEIL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 83 EDGFGFLRTEL--YESSNDDIYVSPKQVKMFRLKTGDFIKGIARVKKDKDKFSPLIFVSDVNGLKAADAFNRSNFESLTP 160
Cdd:PRK09376 59 PDGFGFLRSPDanYLPGPDDIYVSPSQIRRFNLRTGDTVEGKIRPPKEGERYFALLKVETVNGEDPEKARNRPLFENLTP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 161 IYPNQKLKLETSK-DKISQRIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKNFDDLKILVLLIDERPEEVTDFK 239
Cdd:PRK09376 139 LYPNERLRLETGNpEDLSTRIIDLIAPIGKGQRGLIVAPPKAGKTVLLQNIANSITTNHPEVHLIVLLIDERPEEVTDMQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 240 RFVnqyrdkdneltRTEVAASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAYNIMTPQSGRTLSGGL 319
Cdd:PRK09376 219 RSV-----------KGEVVASTFDEPAERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKVLSGGV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 320 DPLALIGPKKFFGAARNIENGGSLTIIATALVDTGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSSTRKDN 399
Cdd:PRK09376 288 DANALHRPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINRSGTRKEE 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1080175760 400 LLLNNKELEAVYKLRN--SDMkDKIDFTNELINLMAKCKSNDEFVELINK 447
Cdd:PRK09376 368 LLLSPEELQKVWILRKilSPM-DEVEAMEFLLDKLKKTKTNEEFFDSMNR 416
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
3-447 |
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: 528.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 3 ININDLDKLKLDELREIGKNLSIKSLSSYRKNELVEIIKEAYSNSknfennesssndlddsnenfdlGEKFNCEGLLDLH 82
Cdd:TIGR00767 1 YNIEELKNMPLEELRKLAEQLGVENTSSLKKQELIFAILKAHAEQ----------------------GGLIFGEGVLEIL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 83 EDGFGFLRTEL--YESSNDDIYVSPKQVKMFRLKTGDFIKGIARVKKDKDKFSPLIFVSDVNGLKAADAFNRSNFESLTP 160
Cdd:TIGR00767 59 PDGFGFLRSPDssYLPGPDDIYVSPSQIRRFNLRTGDTIEGQIRSPKEGERYFALLKVESVNGDDPEKAKNRVLFENLTP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 161 IYPNQKLKLETSKDKISQRIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKNFDDLKILVLLIDERPEEVTDFKR 240
Cdd:TIGR00767 139 LYPNERLRLETSTEDLSTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVELIVLLIDERPEEVTDMQR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 241 FVnqyrdkdneltRTEVAASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAYNIMTPQSGRTLSGGLD 320
Cdd:TIGR00767 219 SV-----------KGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLSGGVD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 321 PLALIGPKKFFGAARNIENGGSLTIIATALVDTGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSSTRKDNL 400
Cdd:TIGR00767 288 ANALHRPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKKSGTRKEEL 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1080175760 401 LLNNKELEAVYKLRN--SDMkDKIDFTNELINLMAKCKSNDEFVELINK 447
Cdd:TIGR00767 368 LLTPEELQKIWVLRKiiSPM-DSIEAMEFLISKLKKTKTNEEFLESMKR 415
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
176-433 |
1.40e-144 |
|
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: 412.75 E-value: 1.40e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 176 ISQRIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKNFDDLKILVLLIDERPEEVTDFKRFVnqyrdkdneltRT 255
Cdd:cd01128 2 LSTRVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLLIDERPEEVTDMRRSV-----------KG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 256 EVAASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAYNIMTPQSGRTLSGGLDPLALIGPKKFFGAAR 335
Cdd:cd01128 71 EVVASTFDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSGGVDANALHKPKRFFGAAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 336 NIENGGSLTIIATALVDTGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSSTRKDNLLLNNKELEAVYKLRN 415
Cdd:cd01128 151 NIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWLLRR 230
|
250
....*....|....*....
gi 1080175760 416 -SDMKDKIDFTNELINLMA 433
Cdd:cd01128 231 iLSPMDPIEAMEFLLKKLK 249
|
|
| Rho_RNA_bind |
pfam07497 |
Rho termination factor, RNA-binding domain; The Rho termination factor disengages newly ... |
76-144 |
1.00e-26 |
|
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: 102.07 E-value: 1.00e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080175760 76 EGLLDLHEDGFGFLRTELYESSNDDIYVSPKQVKMFRLKTGDFIKGIARVKKDKDKFSPLIFVSDVNGL 144
Cdd:pfam07497 1 EGILEILPDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDIVEGQVRPPKEGEKYFALLRVESVNGE 69
|
|
| CSP |
smart00357 |
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria ... |
76-136 |
1.49e-06 |
|
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria and is involved in regulating translation in eukaryotes. Contains sub-family of RNA-binding domains in the Rho transcription termination factor.
Pssm-ID: 214633 [Multi-domain] Cd Length: 64 Bit Score: 45.28 E-value: 1.49e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080175760 76 EGLLDLHEDGFGFLRTELYessNDDIYVSPKQVK--MFRLKTGDFIKGIARVKKDKDKFSPLI 136
Cdd:smart00357 1 TGVVKWFNKGFGFIRPDDG---GKDVFVHPSQIQggLKSLREGDEVEFKVVSPEGGEKPEAEN 60
|
|
| Rho_N |
smart00959 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
7-47 |
1.55e-06 |
|
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: 44.67 E-value: 1.55e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1080175760 7 DLDKLKLDELREIGKNLSIKSLSSYRKNELVEIIKEAYSNS 47
Cdd:smart00959 1 ELKKKTLSELLEIAKELGIENASRLRKQELIFAILKAQAKK 41
|
|
| Rho_N |
pfam07498 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
7-47 |
3.84e-05 |
|
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: 40.83 E-value: 3.84e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1080175760 7 DLDKLKLDELREIGKNLSIKSLSSYRKNELVEIIKEAYSNS 47
Cdd:pfam07498 1 ELKEKTLSELREIAKELGIENYSRLRKQELIFAILKAQAEK 41
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
6-43 |
3.04e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 3.04e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1080175760 6 NDLDKLKLDELREIGKNLSIKSLSSYRKNELVEIIKEA 43
Cdd:PRK12678 21 GGLAGMKLPELRALAKQLGIKGTSGMRKGELIAAIKEA 58
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rho |
COG1158 |
Transcription termination factor Rho [Transcription]; |
76-448 |
0e+00 |
|
Transcription termination factor Rho [Transcription];
Pssm-ID: 440772 [Multi-domain] Cd Length: 373 Bit Score: 627.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 76 EGLLDLHEDGFGFLRTELYESSNDDIYVSPKQVKMFRLKTGDFIKGIARVKKDKDKFSPLIFVSDVNGLKAADAFNRSNF 155
Cdd:COG1158 10 EGVLEILPDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDAVTGQVRPPKEGEKYFALLRVESVNGEDPEEARKRPDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 156 ESLTPIYPNQKLKLETSKDKISQRIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKNFDDLKILVLLIDERPEEV 235
Cdd:COG1158 90 DNLTPLYPDERLRLETTPDDLSTRVIDLVAPIGKGQRGLIVAPPKAGKTTLLQDIANAITANHPEVHLIVLLIDERPEEV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 236 TDFKRFVnqyrdkdneltRTEVAASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAYNIMTPQSGRTL 315
Cdd:COG1158 170 TDMQRSV-----------KGEVIASTFDEPAERHVQVAELVIERAKRLVELGKDVVILLDSITRLARAYNLVVPASGRTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 316 SGGLDPLALIGPKKFFGAARNIENGGSLTIIATALVDTGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSST 395
Cdd:COG1158 239 SGGVDANALYKPKRFFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINKSGT 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1080175760 396 RKDNLLLNNKELEAVYKLRN--SDMkDKIDFTNELINLMAKCKSNDEFVELINKT 448
Cdd:COG1158 319 RREELLLSPEELEKVWILRRalSGM-DPVEAMEFLLDRLKKTKSNAEFLESMNKT 372
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
3-447 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 595.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 3 ININDLDKLKLDELREIGKNLSIKSLSSYRKNELVEIIKEAYSNSknfennesssndlddsnenfdlGEKFNCEGLLDLH 82
Cdd:PRK09376 1 MNLSELKNKSLSELLELAEELGIENASRLRKQELIFAILKAQAEK----------------------GGDIFGEGVLEIL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 83 EDGFGFLRTEL--YESSNDDIYVSPKQVKMFRLKTGDFIKGIARVKKDKDKFSPLIFVSDVNGLKAADAFNRSNFESLTP 160
Cdd:PRK09376 59 PDGFGFLRSPDanYLPGPDDIYVSPSQIRRFNLRTGDTVEGKIRPPKEGERYFALLKVETVNGEDPEKARNRPLFENLTP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 161 IYPNQKLKLETSK-DKISQRIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKNFDDLKILVLLIDERPEEVTDFK 239
Cdd:PRK09376 139 LYPNERLRLETGNpEDLSTRIIDLIAPIGKGQRGLIVAPPKAGKTVLLQNIANSITTNHPEVHLIVLLIDERPEEVTDMQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 240 RFVnqyrdkdneltRTEVAASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAYNIMTPQSGRTLSGGL 319
Cdd:PRK09376 219 RSV-----------KGEVVASTFDEPAERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKVLSGGV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 320 DPLALIGPKKFFGAARNIENGGSLTIIATALVDTGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSSTRKDN 399
Cdd:PRK09376 288 DANALHRPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINRSGTRKEE 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1080175760 400 LLLNNKELEAVYKLRN--SDMkDKIDFTNELINLMAKCKSNDEFVELINK 447
Cdd:PRK09376 368 LLLSPEELQKVWILRKilSPM-DEVEAMEFLLDKLKKTKTNEEFFDSMNR 416
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
3-447 |
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: 528.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 3 ININDLDKLKLDELREIGKNLSIKSLSSYRKNELVEIIKEAYSNSknfennesssndlddsnenfdlGEKFNCEGLLDLH 82
Cdd:TIGR00767 1 YNIEELKNMPLEELRKLAEQLGVENTSSLKKQELIFAILKAHAEQ----------------------GGLIFGEGVLEIL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 83 EDGFGFLRTEL--YESSNDDIYVSPKQVKMFRLKTGDFIKGIARVKKDKDKFSPLIFVSDVNGLKAADAFNRSNFESLTP 160
Cdd:TIGR00767 59 PDGFGFLRSPDssYLPGPDDIYVSPSQIRRFNLRTGDTIEGQIRSPKEGERYFALLKVESVNGDDPEKAKNRVLFENLTP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 161 IYPNQKLKLETSKDKISQRIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKNFDDLKILVLLIDERPEEVTDFKR 240
Cdd:TIGR00767 139 LYPNERLRLETSTEDLSTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVELIVLLIDERPEEVTDMQR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 241 FVnqyrdkdneltRTEVAASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAYNIMTPQSGRTLSGGLD 320
Cdd:TIGR00767 219 SV-----------KGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLSGGVD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 321 PLALIGPKKFFGAARNIENGGSLTIIATALVDTGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSSTRKDNL 400
Cdd:TIGR00767 288 ANALHRPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKKSGTRKEEL 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1080175760 401 LLNNKELEAVYKLRN--SDMkDKIDFTNELINLMAKCKSNDEFVELINK 447
Cdd:TIGR00767 368 LLTPEELQKIWVLRKiiSPM-DSIEAMEFLISKLKKTKTNEEFLESMKR 415
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
77-448 |
1.24e-176 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 509.83 E-value: 1.24e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 77 GLLDLhEDGFGFLRTELYESSNDDIYVSPKQVKMFRLKTGDFIKGIARVKKD------KDKFSPLIFVSDVNGLKAADAF 150
Cdd:PRK12678 298 GILDV-LDNYAFVRTSGYLPGPNDVYVSMNQVRKNGLRKGDAVTGAVRAPREgeqgnqRQKFNPLVRLDSVNGMSPEEAK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 151 NRSNFESLTPIYPNQKLKLETSKDKISQRIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKNFDDLKILVLLIDE 230
Cdd:PRK12678 377 KRPEFGKLTPLYPNERLRLETEPKKLTTRVIDLIMPIGKGQRGLIVSPPKAGKTTILQNIANAITTNNPECHLMVVLVDE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 231 RPEEVTDFKRFVNqyrdkdneltrTEVAASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAYNIMTPQ 310
Cdd:PRK12678 457 RPEEVTDMQRSVK-----------GEVIASTFDRPPSDHTTVAELAIERAKRLVELGKDVVVLLDSITRLGRAYNLAAPA 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 311 SGRTLSGGLDPLALIGPKKFFGAARNIENGGSLTIIATALVDTGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDI 390
Cdd:PRK12678 526 SGRILSGGVDSTALYPPKRFFGAARNIENGGSLTIIATALVETGSKMDEVIFEEFKGTGNMELKLDRKLADKRIFPAVDV 605
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080175760 391 EKSSTRKDNLLLNNKELEAVYKLR----NSDMKDKIDFtneLINLMAKCKSNDEFVELINKT 448
Cdd:PRK12678 606 NASGTRKEELLLSPDELAIVHKLRrvlsGLDSQQAIDL---LISRLKKTKSNYEFLMQVSKT 664
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
76-441 |
1.35e-165 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 471.11 E-value: 1.35e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 76 EGLLDLHEDGFGFLRTEL--YESSNDDIYVSPKQVKMFRLKTGDFIKGIARVKKDKdkfSPLIFVSDVNGLKAADAFNRS 153
Cdd:PRK12608 20 LGVLEILGDGFGFLRSARrnYLPSPDDVFVPPALIRRFNLRTGDVVEGVARPRERY---RVLVRVDSVNGTDPEKLARRP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 154 NFESLTPIYPNQKLKLETSKDKISQRIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKNFDDLKILVLLIDERPE 233
Cdd:PRK12608 97 HFDDLTPLHPRERLRLETGSDDLSMRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLLIDERPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 234 EVTDFKRFVnqyrdkdneltRTEVAASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAYNIMTPQSGR 313
Cdd:PRK12608 177 EVTDMRRSV-----------KGEVYASTFDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 314 TLSGGLDPLALIGPKKFFGAARNIENGGSLTIIATALVDTGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKS 393
Cdd:PRK12608 246 TLSGGVDARALQRPKRLFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMEIVLDRELADKRVFPAIDIAKS 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1080175760 394 STRKDNLLLNNKELEAVYKLRNS-DMKDKIDFTNELINLMAKCKSNDEF 441
Cdd:PRK12608 326 GTRREELLLDSKELEKVRRLRRAlASRKPVEAMEALLEKLRETPDNAEF 374
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
176-433 |
1.40e-144 |
|
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: 412.75 E-value: 1.40e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 176 ISQRIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKNFDDLKILVLLIDERPEEVTDFKRFVnqyrdkdneltRT 255
Cdd:cd01128 2 LSTRVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLLIDERPEEVTDMRRSV-----------KG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 256 EVAASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAYNIMTPQSGRTLSGGLDPLALIGPKKFFGAAR 335
Cdd:cd01128 71 EVVASTFDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSGGVDANALHKPKRFFGAAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 336 NIENGGSLTIIATALVDTGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSSTRKDNLLLNNKELEAVYKLRN 415
Cdd:cd01128 151 NIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWLLRR 230
|
250
....*....|....*....
gi 1080175760 416 -SDMKDKIDFTNELINLMA 433
Cdd:cd01128 231 iLSPMDPIEAMEFLLKKLK 249
|
|
| Rho_RNA_bind |
pfam07497 |
Rho termination factor, RNA-binding domain; The Rho termination factor disengages newly ... |
76-144 |
1.00e-26 |
|
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: 102.07 E-value: 1.00e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080175760 76 EGLLDLHEDGFGFLRTELYESSNDDIYVSPKQVKMFRLKTGDFIKGIARVKKDKDKFSPLIFVSDVNGL 144
Cdd:pfam07497 1 EGILEILPDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDIVEGQVRPPKEGEKYFALLRVESVNGE 69
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
179-396 |
7.50e-22 |
|
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: 94.55 E-value: 7.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 179 RIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIeyALEKNFDdlKILVLLIDERPEEVTDFKRFVNQyrdkDNELTRTEVA 258
Cdd:cd01136 56 RAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMI--ARNTDAD--VNVIALIGERGREVREFIEKDLG----EEGLKRSVLV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 259 ASTFDKAPqnhiymqemvLER----------AKRLVEDNKDVVILLDSITRLARAYNIMTPQSGRTL-SGGLDPLALIGP 327
Cdd:cd01136 128 VATSDESP----------LLRvraaytataiAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPtRRGYPPSVFALL 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1080175760 328 KKFFGAARNIENGgSLTIIATALVDtGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSSTR 396
Cdd:cd01136 198 PRLLERAGNGEKG-SITAFYTVLVE-GDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
178-393 |
4.55e-21 |
|
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: 90.88 E-value: 4.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 178 QRIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIeyalEKNFDDLKILVLLIDERPEEVTDFKRfvnqyRDKDNE-LTRTE 256
Cdd:pfam00006 2 IRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMI----ARQASADVVVYALIGERGREVREFIE-----ELLGSGaLKRTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 257 VAASTFDKAPQnhiyMQEMVLERAKRLVE---DN-KDVVILLDSITRLARAYnimtpqsgRTLSGGLD--PlaliGPKKF 330
Cdd:pfam00006 73 VVVATSDEPPL----ARYRAPYTALTIAEyfrDQgKDVLLIMDSLTRFAEAL--------REISLALGepP----GREGY 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1080175760 331 FG------------AARNIENGGSLTIIATALVDtGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKS 393
Cdd:pfam00006 137 PPsvfsllarllerAGRVKGKGGSITALPTVLVP-GDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLAS 210
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
178-396 |
3.95e-18 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 84.04 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 178 QRIIDIIAPIGRGQRGLIVSQPKAGKTTLIKD-IEYALEKnfDDLKILVLLIDERPEEVTDF-KRFVnqyrdKDNELTRT 255
Cdd:cd19476 55 IKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQlARNQAKA--HAGVVVFAGIGERGREVNDLyEEFT-----KSGAMERT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 256 EVAASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAYNIMTPQSGRTLSG-GLDP-LALIGPKKFFGA 333
Cdd:cd19476 128 VVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGReGYPPyLFTKLATLYERA 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080175760 334 ARNIENGGSLTIIATALVDTGSRMD---DMVYEEFKGTgnmeLHLDRKLAQRRIFPAIDIEKSSTR 396
Cdd:cd19476 208 GKVKDGGGSITAIPAVSTPGDDLTDpipDNTFAILDGQ----IVLSRELARKGIYPAINVLDSTSR 269
|
|
| Rho_CSD |
cd04459 |
Rho_CSD: Rho protein cold-shock domain (CSD). Rho protein is a transcription termination ... |
75-138 |
1.97e-17 |
|
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: 76.12 E-value: 1.97e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080175760 75 CEGLLDLHEDGFGFLRTELYE--SSNDDIYVSPKQVKMFRLKTGDFIKGIARVKKDKDKFSPLIFV 138
Cdd:cd04459 1 GSGVLEILPDGFGFLRSSGYNylPGPDDIYVSPSQIRRFNLRTGDTVVGQIRPPKEGERYFALLKV 66
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
179-396 |
2.37e-16 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 80.77 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 179 RIIDIIAPIGRGQRGLIVSQPKAGKTTLIkdieyALEKNFDDLKILVL-LIDERPEEVtdfKRFVNQYRDKDNElTRTEV 257
Cdd:PRK07594 144 RAIDSVATCGEGQRVGIFSAPGVGKSTLL-----AMLCNAPDADSNVLvLIGERGREV---REFIDFTLSEETR-KRCVI 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 258 AASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAYNIMTPQSGRTLSGGLDPlaligPKKFFGAARNI 337
Cdd:PRK07594 215 VVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYP-----PGVFSALPRLL 289
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080175760 338 ENGG-----SLTIIATALVDtGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSSTR 396
Cdd:PRK07594 290 ERTGmgekgSITAFYTVLVE-GDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSR 352
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
158-414 |
2.79e-15 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 77.62 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 158 LTPIYPNQKLKLETSKDkISQRIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKNFddlkILVLLIDERPEEVtd 237
Cdd:PRK07196 124 LPQIHPLQRRAVDTPLD-VGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADV----VVVGLIGERGREV-- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 238 fKRFVNQYRDKDNeLTRTEVAASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAynimtpQSGRTLSG 317
Cdd:PRK07196 197 -KEFIEHSLQAAG-MAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMA------QREIALSL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 318 GLDPLALIGPKKFFG-------AARNIENGGSLTIIATALVDtGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDI 390
Cdd:PRK07196 269 GEPPATKGYPPSAFSiiprlaeSAGNSSGNGTMTAIYTVLAE-GDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDI 347
|
250 260
....*....|....*....|....
gi 1080175760 391 EKSSTRKDNLLLNNKELEAVYKLR 414
Cdd:PRK07196 348 SQSISRCMSQVIGSQQAKAASLLK 371
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
179-414 |
3.70e-14 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 74.08 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 179 RIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKNFddlkILVLLIDERPEEVTDFKRFVnqyrdkdneLT----- 253
Cdd:PRK06820 152 RAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCADSAADV----MVLALIGERGREVREFLEQV---------LTpeara 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 254 RTEVAASTFDKAPqnhiymqemvLERAKRLV----------EDNKDVVILLDSITRLARAYNIMTPQSGRT-LSGGLDPL 322
Cdd:PRK06820 219 RTVVVVATSDRPA----------LERLKGLStattiaeyfrDRGKKVLLMADSLTRYARAAREIGLAAGEPpAAGSFPPS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 323 ALIGPKKFFGAARNIENGgSLTIIATALVDtGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSSTRKDNLLL 402
Cdd:PRK06820 289 VFANLPRLLERTGNSDRG-SITAFYTVLVE-GDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIV 366
|
250
....*....|..
gi 1080175760 403 NNKELEAVYKLR 414
Cdd:PRK06820 367 SAGQLAMAQKLR 378
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
179-445 |
4.77e-14 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 73.60 E-value: 4.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 179 RIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIeyalEKNFD-DLKILVlLIDERPEEVTDFKRfvnqyRDKDNE-LTRTE 256
Cdd:PRK07721 147 RAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMI----ARNTSaDLNVIA-LIGERGREVREFIE-----RDLGPEgLKRSI 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 257 VAASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAYNIMTPQSGR--TLSGGLDPLALIGPKKFFGAA 334
Cdd:PRK07721 217 VVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEppTTKGYTPSVFAILPKLLERTG 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 335 RNieNGGSLTIIATALVDtGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSSTRKDNLLLNNKELEAVYKLR 414
Cdd:PRK07721 297 TN--ASGSITAFYTVLVD-GDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFR 373
|
250 260 270
....*....|....*....|....*....|....
gi 1080175760 415 N--SDMKDKIDftneLINLMA-KCKSNDEFVELI 445
Cdd:PRK07721 374 EllSTYQNSED----LINIGAyKRGSSREIDEAI 403
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
179-431 |
1.67e-12 |
|
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: 68.90 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 179 RIIDIIAPIGRGQR-GLI----VsqpkaGKTTLIKDI-EYAlekNFDdlkILVL-LIDERPEEVTDFKRfvnqyRDKDNE 251
Cdd:COG1157 146 RAIDGLLTVGRGQRiGIFagsgV-----GKSTLLGMIaRNT---EAD---VNVIaLIGERGREVREFIE-----DDLGEE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 252 -LTRTEVAASTFDKAPqnhiymqemvLERAK------RLVED----NKDVVILLDSITRLARAynimtpQsgR--TLSGG 318
Cdd:COG1157 210 gLARSVVVVATSDEPP----------LMRLRaaytatAIAEYfrdqGKNVLLLMDSLTRFAMA------Q--ReiGLAAG 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 319 lDPLALIG-PKKFFGA-ARNIE-----NGGSLTIIATALVDtGSRMDDMVYEEFKGT--GnmelH--LDRKLAQRRIFPA 387
Cdd:COG1157 272 -EPPATRGyPPSVFALlPRLLEragngGKGSITAFYTVLVE-GDDMNDPIADAVRGIldG----HivLSRKLAERGHYPA 345
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1080175760 388 IDIEKSSTRKDNLLLNNKELEAVYKLRN-----SDMKDkidftneLINL 431
Cdd:COG1157 346 IDVLASISRVMPDIVSPEHRALARRLRRllaryEENED-------LIRI 387
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
141-418 |
3.00e-12 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 68.27 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 141 VNGLKAADAFNRSNFESlTPIYPNQKLKLETSKDkISQRIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKNFdd 220
Cdd:PRK07960 128 LDGLPAPDTGETGALIT-PPFNPLQRTPIEHVLD-TGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADV-- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 221 lkILVLLIDERPEEVTDFKRFVNqyrdKDNELTRTEVAASTFDKAPQnhIYMQEMVLerAKRLVEDNKD----VVILLDS 296
Cdd:PRK07960 204 --IVVGLIGERGREVKDFIENIL----GAEGRARSVVIAAPADVSPL--LRMQGAAY--ATRIAEDFRDrgqhVLLIMDS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 297 ITRLARAynimtpQSGRTLSGGlDPLALIG-PKKFFG--------AARNIENGGSLTIIATALVDtGSRMDDMVYEEFKG 367
Cdd:PRK07960 274 LTRYAMA------QREIALAIG-EPPATKGyPPSVFAklpalverAGNGISGGGSITAFYTVLTE-GDDQQDPIADSARA 345
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 368 TGNMELHLDRKLAQRRIFPAIDIEKSSTRKDNLLLNN---------KELEAVYKlRNSDM 418
Cdd:PRK07960 346 ILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEqhyarvrqfKQLLSSFQ-RNRDL 404
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
179-414 |
4.13e-12 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 67.86 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 179 RIIDIIAPIGRGQRGLIVSQPKAGKTTLIKdieyALEKNFDDLKILVLLIDERPEEVTDFKRfvnqyRDKDNE-LTRTEV 257
Cdd:PRK06936 151 RVIDGLLTCGEGQRMGIFAAAGGGKSTLLA----SLIRSAEVDVTVLALIGERGREVREFIE-----SDLGEEgLRKAVL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 258 AASTFDKAPqnhiymqemvLERAKR----------LVEDNKDVVILLDSITRLARAynimtpQSGRTLSGGLDPLALIGP 327
Cdd:PRK06936 222 VVATSDRPS----------MERAKAgfvatsiaeyFRDQGKRVLLLMDSVTRFARA------QREIGLAAGEPPTRRGYP 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 328 KKFFGA-ARNIENGG-----SLTIIATALVDtGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSSTRKDNLL 401
Cdd:PRK06936 286 PSVFAAlPRLMERAGqsdkgSITALYTVLVE-GDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQI 364
|
250
....*....|...
gi 1080175760 402 LNNKELEAVYKLR 414
Cdd:PRK06936 365 VSKEHKTWAGRLR 377
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
172-396 |
6.78e-12 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 67.06 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 172 SKDKISQ------RIIDIIAPIGRGQRGLIVSQPKAGKTTLIkdieyALEKNFDDLKILVL-LIDERPEEVtdfKRFVNQ 244
Cdd:PRK05688 144 NRHPISEpldvgiRSINGLLTVGRGQRLGLFAGTGVGKSVLL-----GMMTRFTEADIIVVgLIGERGREV---KEFIEH 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 245 YRDkDNELTRTEVAASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAynimtpQSGRTLSGGlDPLAL 324
Cdd:PRK05688 216 ILG-EEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQA------QREIALAIG-EPPAT 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 325 IG-PKKFFG--------AARNIENGGSLTIIATALVDtGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSST 395
Cdd:PRK05688 288 KGyPPSVFAklpklverAGNAEPGGGSITAFYTVLSE-GDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASIS 366
|
.
gi 1080175760 396 R 396
Cdd:PRK05688 367 R 367
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
179-396 |
7.08e-12 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 66.94 E-value: 7.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 179 RIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIeyALEKNFDdlKILVLLIDERPEEVTDFKRFVNQyrdkDNeLTRTEVA 258
Cdd:PRK06002 154 RVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML--ARADAFD--TVVIALVGERGREVREFLEDTLA----DN-LKKAVAV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 259 ASTFDKAPQnhiyMQEMVLERAKRLVEDNKD----VVILLDSITRLARAynimtpqsGR--TLSGGLDPLALIGPKKFFG 332
Cdd:PRK06002 225 VATSDESPM----MRRLAPLTATAIAEYFRDrgenVLLIVDSVTRFAHA--------ARevALAAGEPPVARGYPPSVFS 292
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080175760 333 --------AARNIENGGSLTIIATALVDtGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSSTR 396
Cdd:PRK06002 293 elprllerAGPGAEGGGSITGIFSVLVD-GDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISR 363
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
179-414 |
5.42e-11 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 64.40 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 179 RIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKnfdDLKILVLlIDERPEEVtdfKRFVNQYRDKDNeLTRTEVA 258
Cdd:PRK09099 152 RIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQC---DVNVIAL-IGERGREV---REFIELILGEDG-MARSVVV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 259 ASTFDKAPqnhiymqemvLERAKR------LVEDNKD----VVILLDSITRLARAynimtpQSGRTLSGGlDPLALIG-- 326
Cdd:PRK09099 224 CATSDRSS----------IERAKAayvataIAEYFRDrglrVLLMMDSLTRFARA------QREIGLAAG-EPPARRGfp 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 327 PKKFFGAARNIENGG-----SLTIIATALV--DTGSrmdDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSSTRKDN 399
Cdd:PRK09099 287 PSVFAELPRLLERAGmgetgSITALYTVLAedESGS---DPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMP 363
|
250
....*....|....*
gi 1080175760 400 LLLNNKELEAVYKLR 414
Cdd:PRK09099 364 QVVPREHVQAAGRLR 378
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
163-445 |
5.49e-10 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 61.15 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 163 PNQKLKLET------SKDKISQ------RIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKNFDdlkiLVLLIDE 230
Cdd:PRK06793 117 PLQKIKLDAppihafEREEITDvfetgiKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADIN----VISLVGE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 231 RPEEVTDFKRfvnqyRDKDNE-LTRTEVAASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLA---RAYNI 306
Cdd:PRK06793 193 RGREVKDFIR-----KELGEEgMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFAdarRSVDI 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 307 MT---PQSGRTLsggldpLALIGPKKFFGAARNIENgGSLTIIATALVDtGSRMDDMVYEEFKGTGNMELHLDRKLAQRR 383
Cdd:PRK06793 268 AVkelPIGGKTL------LMESYMKKLLERSGKTQK-GSITGIYTVLVD-GDDLNGPVPDLARGILDGHIVLKRELATLS 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 384 IFPAIDIEKSSTR-------KDNLLLNN---------KELEAVYKL----RNSD------MKDKIDFTNELI-NLMAKCK 436
Cdd:PRK06793 340 HYPAISVLDSVSRimeeivsPNHWQLANemrkilsiyKENELYFKLgtiqENAEnayifeCKNKVEGINTFLkQGRSDSF 419
|
....*....
gi 1080175760 437 SNDEFVELI 445
Cdd:PRK06793 420 QFDDIVEAM 428
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
179-396 |
4.26e-09 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 58.45 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 179 RIIDIIAPIGRGQRGLIVSQPKAGKTTLIKdieyALEKNFDDLKILVLLIDERPEEVTDFKRfvnqyRDKDNE-LTRTEV 257
Cdd:PRK08927 147 RALNTFLTCCRGQRMGIFAGSGVGKSVLLS----MLARNADADVSVIGLIGERGREVQEFLQ-----DDLGPEgLARSVV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 258 AASTFDKAP---QNHIYMqemVLERAKRLVEDNKDVVILLDSITRLARAynimtpQSGRTLSGGlDPLALIG-------- 326
Cdd:PRK08927 218 VVATSDEPAlmrRQAAYL---TLAIAEYFRDQGKDVLCLMDSVTRFAMA------QREIGLSAG-EPPTTKGytptvfae 287
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080175760 327 -PKKFFGAARNIENGGSLTIIATALVDtGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSSTR 396
Cdd:PRK08927 288 lPRLLERAGPGPIGEGTITGLFTVLVD-GDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSR 357
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
181-447 |
5.31e-09 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 58.16 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 181 IDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKnfdDLKIlVLLIDERPEEVTDFKRfvnqyRDKDNELTRTEVAAS 260
Cdd:PRK08472 148 IDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLA---PIKV-VALIGERGREIPEFIE-----KNLGGDLENTVIVVA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 261 TFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAYNIMTPQSGR-TLSGGLDPLALIGPKKFFGAARNIEN 339
Cdd:PRK08472 219 TSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEpPTSKGYPPSVLSLLPQLMERAGKEEG 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 340 GGSLTIIATALVDtGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSSTRKDNLLLNNKELEAVYKLR--NSD 417
Cdd:PRK08472 299 KGSITAFFTVLVE-GDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKrlYSL 377
|
250 260 270
....*....|....*....|....*....|..
gi 1080175760 418 MKDkidftNE-LINLMAKCKSND-EFVELINK 447
Cdd:PRK08472 378 LKE-----NEvLIRIGAYQKGNDkELDEAISK 404
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
179-396 |
1.30e-07 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 53.46 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 179 RIIDIIAPIGRGQRGLIVSQPKAGKTTLIKD-IEYAleknfdDLKILVL-LIDERPEEVTDFKRFVNQYRDKDneltRTE 256
Cdd:PRK08149 140 RAIDGLLTCGVGQRMGIFASAGCGKTSLMNMlIEHS------EADVFVIgLIGERGREVTEFVESLRASSRRE----KCV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 257 VAASTFDKAPQ---NHIYMQEMVlerAKRLVEDNKDVVILLDSITRLARAYNIMtpqsgrTLSGGLDPLALIGPKKFF-- 331
Cdd:PRK08149 210 LVYATSDFSSVdrcNAALVATTV---AEYFRDQGKRVVLFIDSMTRYARALRDV------ALAAGELPARRGYPASVFds 280
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080175760 332 --------GAARNiengGSLTIIATALVDtGSRMDDMVYEEFKGTGNMELHLDRKLAQRRIFPAIDIEKSSTR 396
Cdd:PRK08149 281 lprllerpGATLA----GSITAFYTVLLE-SEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSR 348
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
156-414 |
1.70e-07 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 53.17 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 156 ESLTPIYPNQKLKLET------SKDKISQ------RIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKNFddlkI 223
Cdd:PRK08972 116 DGLGPIYTDQRASRHSppinplSRRPITEpldvgvRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTADV----I 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 224 LVLLIDERPEEVtdfKRFVNQYRDKDnELTRTEVAASTFDKAPqnhiYMQEMVLERAKRLVEDNKD----VVILLDSITR 299
Cdd:PRK08972 192 VVGLVGERGREV---KEFIEEILGEE-GRARSVVVAAPADTSP----LMRLKGCETATTIAEYFRDqglnVLLLMDSLTR 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 300 LARAynimtpQSGRTLSGGlDPLALIG--PKKFFGAARNIE---NG----GSLTIIATALVDtGSRMDDMVYEEFKGTGN 370
Cdd:PRK08972 264 YAQA------QREIALAVG-EPPATKGypPSVFAKLPALVEragNGgpgqGSITAFYTVLTE-GDDLQDPIADASRAILD 335
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1080175760 371 MELHLDRKLAQRRIFPAIDIEKSSTRKDNLLLNNKELEAVYKLR 414
Cdd:PRK08972 336 GHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVK 379
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
179-316 |
8.86e-07 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 51.06 E-value: 8.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 179 RIIDIIAPIGRGQRGLIVSQPKAGKTTLIKDIEYALEKNFDdlkiLVLLIDERPEEVTDfkrFVNQYRDKDNElTRTEVA 258
Cdd:PRK05922 146 KAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKSTIN----VIALIGERGREVRE---YIEQHKEGLAA-QRTIII 217
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080175760 259 ASTFDKAPQNHIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAYNIMTPQSGRTLS 316
Cdd:PRK05922 218 ASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLS 275
|
|
| CSP |
smart00357 |
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria ... |
76-136 |
1.49e-06 |
|
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria and is involved in regulating translation in eukaryotes. Contains sub-family of RNA-binding domains in the Rho transcription termination factor.
Pssm-ID: 214633 [Multi-domain] Cd Length: 64 Bit Score: 45.28 E-value: 1.49e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080175760 76 EGLLDLHEDGFGFLRTELYessNDDIYVSPKQVK--MFRLKTGDFIKGIARVKKDKDKFSPLI 136
Cdd:smart00357 1 TGVVKWFNKGFGFIRPDDG---GKDVFVHPSQIQggLKSLREGDEVEFKVVSPEGGEKPEAEN 60
|
|
| Rho_N |
smart00959 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
7-47 |
1.55e-06 |
|
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: 44.67 E-value: 1.55e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1080175760 7 DLDKLKLDELREIGKNLSIKSLSSYRKNELVEIIKEAYSNS 47
Cdd:smart00959 1 ELKKKTLSELLEIAKELGIENASRLRKQELIFAILKAQAKK 41
|
|
| Rho_N |
pfam07498 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
7-47 |
3.84e-05 |
|
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: 40.83 E-value: 3.84e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1080175760 7 DLDKLKLDELREIGKNLSIKSLSSYRKNELVEIIKEAYSNS 47
Cdd:pfam07498 1 ELKEKTLSELREIAKELGIENYSRLRKQELIFAILKAQAEK 41
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
181-316 |
4.49e-05 |
|
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: 45.84 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 181 IDIIAPIGRGQRGLIVSQPKAGKTTLIkdIEYALEKNFDDLKILVLLIDERPEEVTdfkRFVNQYRDKDNELTRTEVAAS 260
Cdd:TIGR00962 152 IDAMIPIGRGQRELIIGDRQTGKTAVA--IDTIINQKDSDVYCIYVAIGQKASTVA---QVVRKLEEHGAMAYTIVVAAT 226
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080175760 261 TFDKA------PQNHIYMQEMVLERAkrlvednKDVVILLDSITRLARAYnimtpqsgRTLS 316
Cdd:TIGR00962 227 ASDSAslqylaPYTGCTMGEYFRDNG-------KHALIIYDDLSKQAVAY--------RQIS 273
|
|
| OB_RNB |
pfam08206 |
Ribonuclease B OB domain; This family includes the N-terminal OB domain found in ribonuclease ... |
77-134 |
1.96e-04 |
|
Ribonuclease B OB domain; This family includes the N-terminal OB domain found in ribonuclease B proteins in one or two copies.
Pssm-ID: 429863 [Multi-domain] Cd Length: 58 Bit Score: 39.06 E-value: 1.96e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1080175760 77 GLLDLHEDGFGFLRTelyESSNDDIYVSPKQVKMfrLKTGDFIkgIARVKKDKDKFSP 134
Cdd:pfam08206 1 GTVRGHKKGFGFLIP---DDEEDDIFIPPNQMKK--AMHGDRV--LVRITKGDRRGRR 51
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
181-307 |
2.90e-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: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 181 IDIIAPIGRGQRGLIVSQPKAGKTTLIKDIeyALEKNFDDLKILVLLIDERPEEVtdfKRFVNQYRDKDNELTRTEVAAS 260
Cdd:cd01132 60 IDSLIPIGRGQRELIIGDRQTGKTAIAIDT--IINQKGKKVYCIYVAIGQKRSTV---AQIVKTLEEHGAMEYTIVVAAT 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1080175760 261 TFDKAPQNHI--Y----MQEMVLERAkrlvednKDVVILLDSITRLARAYNIM 307
Cdd:cd01132 135 ASDPAPLQYLapYagcaMGEYFRDNG-------KHALIIYDDLSKQAVAYRQM 180
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
6-43 |
3.04e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 3.04e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1080175760 6 NDLDKLKLDELREIGKNLSIKSLSSYRKNELVEIIKEA 43
Cdd:PRK12678 21 GGLAGMKLPELRALAKQLGIKGTSGMRKGELIAAIKEA 58
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
179-206 |
1.79e-03 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 40.67 E-value: 1.79e-03
10 20
....*....|....*....|....*...
gi 1080175760 179 RIIDIIAPIGRGQRGLIVSQPKAGKTTL 206
Cdd:PRK13343 151 KVVDALIPIGRGQRELIIGDRQTGKTAI 178
|
|
| PRK11642 |
PRK11642 |
ribonuclease R; |
82-110 |
3.58e-03 |
|
ribonuclease R;
Pssm-ID: 236944 [Multi-domain] Cd Length: 813 Bit Score: 39.73 E-value: 3.58e-03
10 20
....*....|....*....|....*....
gi 1080175760 82 HEDGFGFLRTelyESSNDDIYVSPKQVKM 110
Cdd:PRK11642 92 HRDGYGFLRV---EGRKDDLYLSSEQMKT 117
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
189-349 |
5.83e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.35 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 189 RGQRGLIVSQPKAGKTTLIKDIEYALEKNFDDLKILvlliderpeevtdfkrfvnqyrDKDNELTRTEVAASTFDKAPQN 268
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI----------------------DGEDILEEVLDQLLLIIVGGKK 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080175760 269 HIYMQEMVLERAKRLVEDNKDVVILLDSITRLARAYNIMTPQSGRTLSgGLDPLALIGPKKFFGAARNIENGGSLTIIAT 348
Cdd:smart00382 59 ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELR-LLLLLKSEKNLTVILTTNDEKDLGPALLRRR 137
|
.
gi 1080175760 349 A 349
Cdd:smart00382 138 F 138
|
|
| |
