|
Name |
Accession |
Description |
Interval |
E-value |
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
4-421 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 856.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 4 IKLQDLKSKSPTELLALAEENDIENASTMRKQDMMFAILKELAEQGIFIIGEGVVEVLPDGFGFLRSPDANYLPGPDDIY 83
Cdd:PRK09376 1 MNLSELKNKSLSELLELAEELGIENASRLRKQELIFAILKAQAEKGGDIFGEGVLEILPDGFGFLRSPDANYLPGPDDIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 84 VSPSQIRRFSLRTGDTVEGDIRSPKDGERYFALLKVNSINFEDPDKIRHKVNFDNLTPLYPEERILMEFDNPaeKDRSSR 163
Cdd:PRK09376 81 VSPSQIRRFNLRTGDTVEGKIRPPKEGERYFALLKVETVNGEDPEKARNRPLFENLTPLYPNERLRLETGNP--EDLSTR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 164 IIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANHPECYLIVLLIDERPEEVTDMQRSVSGEVVSSTFDEPAARHV 243
Cdd:PRK09376 159 IIDLIAPIGKGQRGLIVAPPKAGKTVLLQNIANSITTNHPEVHLIVLLIDERPEEVTDMQRSVKGEVVASTFDEPAERHV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 244 QVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSGKVLTGGVDANALQRPKRFFGAARNIEQGGSLTIISTAL 323
Cdd:PRK09376 239 QVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKVLSGGVDANALHRPKRFFGAARNIEEGGSLTIIATAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 324 IDTGSRMDEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTRKEELLIDKETLSKIYVLRRILNPMGTVDAIEFLL 403
Cdd:PRK09376 319 IDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINRSGTRKEELLLSPEELQKVWILRKILSPMDEVEAMEFLL 398
|
410
....*....|....*...
gi 402510804 404 DKLKQTKTNDDFFDSMNT 421
Cdd:PRK09376 399 DKLKKTKTNEEFFDSMNR 416
|
|
| Rho |
COG1158 |
Transcription termination factor Rho [Transcription]; |
46-421 |
0e+00 |
|
Transcription termination factor Rho [Transcription];
Pssm-ID: 440772 [Multi-domain] Cd Length: 373 Bit Score: 784.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 46 AEQGIFIIGEGVVEVLPDGFGFLRSpdANYLPGPDDIYVSPSQIRRFSLRTGDTVEGDIRSPKDGERYFALLKVNSINFE 125
Cdd:COG1158 1 AEDDGLIPVEGVLEILPDGYGFLRS--SNYLPGPDDIYVSPSQIRRFGLRTGDAVTGQVRPPKEGEKYFALLRVESVNGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 126 DPDKIRHKVNFDNLTPLYPEERILMEFDNpaeKDRSSRIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANHPEC 205
Cdd:COG1158 79 DPEEARKRPDFDNLTPLYPDERLRLETTP---DDLSTRVIDLVAPIGKGQRGLIVAPPKAGKTTLLQDIANAITANHPEV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 206 YLIVLLIDERPEEVTDMQRSVSGEVVSSTFDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSG 285
Cdd:COG1158 156 HLIVLLIDERPEEVTDMQRSVKGEVIASTFDEPAERHVQVAELVIERAKRLVELGKDVVILLDSITRLARAYNLVVPASG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 286 KVLTGGVDANALQRPKRFFGAARNIEQGGSLTIISTALIDTGSRMDEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMK 365
Cdd:COG1158 236 RTLSGGVDANALYKPKRFFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINK 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 402510804 366 SGTRKEELLIDKETLSKIYVLRRILNPMGTVDAIEFLLDKLKQTKTNDDFFDSMNT 421
Cdd:COG1158 316 SGTRREELLLSPEELEKVWILRRALSGMDPVEAMEFLLDRLKKTKSNAEFLESMNK 371
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
4-421 |
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: 756.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 4 IKLQDLKSKSPTELLALAEENDIENASTMRKQDMMFAILKELAEQGIFIIGEGVVEVLPDGFGFLRSPDANYLPGPDDIY 83
Cdd:TIGR00767 1 YNIEELKNMPLEELRKLAEQLGVENTSSLKKQELIFAILKAHAEQGGLIFGEGVLEILPDGFGFLRSPDSSYLPGPDDIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 84 VSPSQIRRFSLRTGDTVEGDIRSPKDGERYFALLKVNSINFEDPDKIRHKVNFDNLTPLYPEERILMEFDNpaeKDRSSR 163
Cdd:TIGR00767 81 VSPSQIRRFNLRTGDTIEGQIRSPKEGERYFALLKVESVNGDDPEKAKNRVLFENLTPLYPNERLRLETST---EDLSTR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 164 IIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANHPECYLIVLLIDERPEEVTDMQRSVSGEVVSSTFDEPAARHV 243
Cdd:TIGR00767 158 VLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVELIVLLIDERPEEVTDMQRSVKGEVVASTFDEPASRHV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 244 QVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSGKVLTGGVDANALQRPKRFFGAARNIEQGGSLTIISTAL 323
Cdd:TIGR00767 238 QVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLSGGVDANALHRPKRFFGAARNIEEGGSLTIIATAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 324 IDTGSRMDEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTRKEELLIDKETLSKIYVLRRILNPMGTVDAIEFLL 403
Cdd:TIGR00767 318 IDTGSRMDEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKKSGTRKEELLLTPEELQKIWVLRKIISPMDSIEAMEFLI 397
|
410
....*....|....*...
gi 402510804 404 DKLKQTKTNDDFFDSMNT 421
Cdd:TIGR00767 398 SKLKKTKTNEEFLESMKR 415
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
55-420 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 587.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 55 EGVVEVLPDGFGFLRSPDANYLPGPDDIYVSPSQIRRFSLRTGDTVEGDIRSPkdgERYFALLKVNSINFEDPDKIRHKV 134
Cdd:PRK12608 20 LGVLEILGDGFGFLRSARRNYLPSPDDVFVPPALIRRFNLRTGDVVEGVARPR---ERYRVLVRVDSVNGTDPEKLARRP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 135 NFDNLTPLYPEERILMEFDNpaeKDRSSRIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANHPECYLIVLLIDE 214
Cdd:PRK12608 97 HFDDLTPLHPRERLRLETGS---DDLSMRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLLIDE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 215 RPEEVTDMQRSVSGEVVSSTFDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSGKVLTGGVDA 294
Cdd:PRK12608 174 RPEEVTDMRRSVKGEVYASTFDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGRTLSGGVDA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 295 NALQRPKRFFGAARNIEQGGSLTIISTALIDTGSRMDEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTRKEELL 374
Cdd:PRK12608 254 RALQRPKRLFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMEIVLDRELADKRVFPAIDIAKSGTRREELL 333
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 402510804 375 IDKETLSKIYVLRRILNPMGTVDAIEFLLDKLKQTKTNDDFFDSMN 420
Cdd:PRK12608 334 LDSKELEKVRRLRRALASRKPVEAMEALLEKLRETPDNAEFLNSVQ 379
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
56-415 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 584.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 56 GVVEVLpDGFGFLRspDANYLPGPDDIYVSPSQIRRFSLRTGDTVEGDIRSPKDGER------YFALLKVNSINFEDPDK 129
Cdd:PRK12678 298 GILDVL-DNYAFVR--TSGYLPGPNDVYVSMNQVRKNGLRKGDAVTGAVRAPREGEQgnqrqkFNPLVRLDSVNGMSPEE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 130 IRHKVNFDNLTPLYPEERILMEFDnPaeKDRSSRIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANHPECYLIV 209
Cdd:PRK12678 375 AKKRPEFGKLTPLYPNERLRLETE-P--KKLTTRVIDLIMPIGKGQRGLIVSPPKAGKTTILQNIANAITTNNPECHLMV 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 210 LLIDERPEEVTDMQRSVSGEVVSSTFDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSGKVLT 289
Cdd:PRK12678 452 VLVDERPEEVTDMQRSVKGEVIASTFDRPPSDHTTVAELAIERAKRLVELGKDVVVLLDSITRLGRAYNLAAPASGRILS 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 290 GGVDANALQRPKRFFGAARNIEQGGSLTIISTALIDTGSRMDEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTR 369
Cdd:PRK12678 532 GGVDSTALYPPKRFFGAARNIENGGSLTIIATALVETGSKMDEVIFEEFKGTGNMELKLDRKLADKRIFPAVDVNASGTR 611
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 402510804 370 KEELLIDKETLSKIYVLRRILNPMGTVDAIEFLLDKLKQTKTNDDF 415
Cdd:PRK12678 612 KEELLLSPDELAIVHKLRRVLSGLDSQQAIDLLISRLKKTKSNYEF 657
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
161-407 |
1.03e-180 |
|
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: 502.89 E-value: 1.03e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 161 SSRIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANHPECYLIVLLIDERPEEVTDMQRSVSGEVVSSTFDEPAA 240
Cdd:cd01128 3 STRVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLLIDERPEEVTDMRRSVKGEVVASTFDEPPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 241 RHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSGKVLTGGVDANALQRPKRFFGAARNIEQGGSLTIIS 320
Cdd:cd01128 83 RHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSGGVDANALHKPKRFFGAARNIEEGGSLTIIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 321 TALIDTGSRMDEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTRKEELLIDKETLSKIYVLRRILNPMGTVDAIE 400
Cdd:cd01128 163 TALVDTGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWLLRRILSPMDPIEAME 242
|
....*..
gi 402510804 401 FLLDKLK 407
Cdd:cd01128 243 FLLKKLK 249
|
|
| Rho_RNA_bind |
pfam07497 |
Rho termination factor, RNA-binding domain; The Rho termination factor disengages newly ... |
55-128 |
2.50e-43 |
|
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: 145.98 E-value: 2.50e-43
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 402510804 55 EGVVEVLPDGFGFLRSPdaNYLPGPDDIYVSPSQIRRFSLRTGDTVEGDIRSPKDGERYFALLKVNSINFEDPD 128
Cdd:pfam07497 1 EGILEILPDGYGFLRSS--NYLPGPDDIYVSPSQIRRFGLRTGDIVEGQVRPPKEGEKYFALLRVESVNGEDPE 72
|
|
| Rho_CSD |
cd04459 |
Rho_CSD: Rho protein cold-shock domain (CSD). Rho protein is a transcription termination ... |
54-121 |
8.20e-40 |
|
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: 136.60 E-value: 8.20e-40
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 402510804 54 GEGVVEVLPDGFGFLRSPDANYLPGPDDIYVSPSQIRRFSLRTGDTVEGDIRSPKDGERYFALLKVNS 121
Cdd:cd04459 1 GSGVLEILPDGFGFLRSSGYNYLPGPDDIYVSPSQIRRFNLRTGDTVVGQIRPPKEGERYFALLKVEA 68
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
163-366 |
6.80e-29 |
|
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: 112.06 E-value: 6.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 163 RIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANhpecYLIVLLIDERPEEVTD----------MQRSVsgeVVS 232
Cdd:pfam00006 3 RAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASAD----VVVYALIGERGREVREfieellgsgaLKRTV---VVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 233 STFDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSGKVL-----TGGVD---ANALQRpkrff 304
Cdd:pfam00006 76 ATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPgregyPPSVFsllARLLER----- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402510804 305 gAARNIEQGGSLTIISTALIDtGSRMDEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKS 366
Cdd:pfam00006 151 -AGRVKGKGGSITALPTVLVP-GDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLAS 210
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
163-369 |
4.16e-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: 100.71 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 163 RIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANhpecyLIVL-LIDERPEEVTD----------MQRSVsgeVV 231
Cdd:cd01136 56 RAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDAD-----VNVIaLIGERGREVREfiekdlgeegLKRSV---LV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 232 SSTFDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSGKVLT-GGVDANALQRPKRFFGAARNI 310
Cdd:cd01136 128 VATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTrRGYPPSVFALLPRLLERAGNG 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 402510804 311 EQgGSLTIISTALIDtGSRMDEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTR 369
Cdd:cd01136 208 EK-GSITAFYTVLVE-GDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
163-369 |
1.60e-21 |
|
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: 93.29 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 163 RIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANHPEcYLIVLLIDERPEEVTD----------MQRSVsgeVVS 232
Cdd:cd19476 56 KVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKAHAG-VVVFAGIGERGREVNDlyeeftksgaMERTV---VVA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 233 STFDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTV------VPSS----GKVLTggvDANALQrpKR 302
Cdd:cd19476 132 NTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEALREMsallgePPGRegypPYLFT---KLATLY--ER 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 402510804 303 ffgAARNIEQGGSLTIISTALIDTGSRMDEVIFEEFKGTgNSEIVLDRKISDKRVFPSIDIMKSGTR 369
Cdd:cd19476 207 ---AGKVKDGGGSITAIPAVSTPGDDLTDPIPDNTFAIL-DGQIVLSRELARKGIYPAINVLDSTSR 269
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
163-390 |
2.11e-21 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 95.79 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 163 RIIDIVAPLGKGQRALIVAPPRTGKTVLLqniakSIAANHPECYLIVL-LIDERPEEVTD-MQRSVSGE------VVSST 234
Cdd:PRK07594 144 RAIDSVATCGEGQRVGIFSAPGVGKSTLL-----AMLCNAPDADSNVLvLIGERGREVREfIDFTLSEEtrkrcvIVVAT 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 235 FDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSGKVLTGGvdanalQRPKRFFGA-ARNIEQG 313
Cdd:PRK07594 219 SDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSG------EYPPGVFSAlPRLLERT 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 314 G-----SLTIISTALIDtGSRMDEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTRKEELLIDKETLSKIYVLRR 388
Cdd:PRK07594 293 GmgekgSITAFYTVLVE-GDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRR 371
|
..
gi 402510804 389 IL 390
Cdd:PRK07594 372 CL 373
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
163-390 |
2.36e-19 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 89.40 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 163 RIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANhpecYLIVLLIDERPEEVTD----------MQRSVsgeVVS 232
Cdd:PRK07721 147 RAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTSAD----LNVIALIGERGREVREfierdlgpegLKRSI---VVV 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 233 STFDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTV-----VPSSGKVLTGGVDAnalQRPKRFFGAA 307
Cdd:PRK07721 220 ATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIglavgEPPTTKGYTPSVFA---ILPKLLERTG 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 308 RNieQGGSLTIISTALIDtGSRMDEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTRKEELLIDKETLSKIYVLR 387
Cdd:PRK07721 297 TN--ASGSITAFYTVLVD-GDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFR 373
|
...
gi 402510804 388 RIL 390
Cdd:PRK07721 374 ELL 376
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
149-403 |
1.01e-18 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 87.56 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 149 LMEFDNPAEKDRSSRIIDIVAPLG-----------KGQRALIVAPPRTGKTVLLQNIAKSIAANhpecyLIVL-LIDERP 216
Cdd:PRK06820 127 WRELDCPPPSPLTRQPIEQMLTTGiraidgilscgEGQRIGIFAAAGVGKSTLLGMLCADSAAD-----VMVLaLIGERG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 217 EEVTDM----------QRSVsgeVVSSTFDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSGK 286
Cdd:PRK06820 202 REVREFleqvltpearARTV---VVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 287 V-LTGGVDANALQRPKRFFGAARNIEQGgSLTIISTALIDtGSRMDEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMK 365
Cdd:PRK06820 279 PpAAGSFPPSVFANLPRLLERTGNSDRG-SITAFYTVLVE-GDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAA 356
|
250 260 270
....*....|....*....|....*....|....*...
gi 402510804 366 SGTRKEELLIDKETLSKIYVLRRILnpmGTVDAIEFLL 403
Cdd:PRK06820 357 SVSRIMPQIVSAGQLAMAQKLRRML---ACYQEIELLV 391
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
163-369 |
1.91e-17 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 83.88 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 163 RIIDIVAPLGKGQRALIVAPPRTGKTVLLqniakSIAANHPECYLIVL-LIDERPEEVTD----------MQRSVsgeVV 231
Cdd:PRK08927 147 RALNTFLTCCRGQRMGIFAGSGVGKSVLL-----SMLARNADADVSVIgLIGERGREVQEflqddlgpegLARSV---VV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 232 SSTFDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSG-----KVLTGGVDAnalQRPKRFFGA 306
Cdd:PRK08927 219 VATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGeppttKGYTPTVFA---ELPRLLERA 295
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 402510804 307 ARNIEQGGSLTIISTALIDtGSRMDEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTR 369
Cdd:PRK08927 296 GPGPIGEGTITGLFTVLVD-GDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSR 357
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
163-390 |
2.41e-17 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 83.65 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 163 RIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANhpecYLIVLLIDERPEEVTD----------MQRSVsgeVVS 232
Cdd:PRK06936 151 RVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVD----VTVLALIGERGREVREfiesdlgeegLRKAV---LVV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 233 STFDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSGKVLTggvdanalQR---PKRFFGAARN 309
Cdd:PRK06936 224 ATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPT--------RRgypPSVFAALPRL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 310 IEQGG-----SLTIISTALIDtGSRMDEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTRKEELLIDKETLSKIY 384
Cdd:PRK06936 296 MERAGqsdkgSITALYTVLVE-GDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAG 374
|
....*.
gi 402510804 385 VLRRIL 390
Cdd:PRK06936 375 RLRELL 380
|
|
| CSP |
smart00357 |
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria ... |
55-119 |
1.06e-16 |
|
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria and is involved in regulating translation in eukaryotes. Contains sub-family of RNA-binding domains in the Rho transcription termination factor.
Pssm-ID: 214633 [Multi-domain] Cd Length: 64 Bit Score: 73.79 E-value: 1.06e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 402510804 55 EGVVEVLPDGFGFLRSPDanylpGPDDIYVSPSQI--RRFSLRTGDTVEGDIRSPKDGERYFALLKV 119
Cdd:smart00357 1 TGVVKWFNKGFGFIRPDD-----GGKDVFVHPSQIqgGLKSLREGDEVEFKVVSPEGGEKPEAENVV 62
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
165-420 |
1.81e-16 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 80.79 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 165 IDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANhpecYLIVLLIDERPEEVTDMQRSVSGE-------VVSSTFDE 237
Cdd:PRK06793 147 IDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKAD----INVISLVGERGREVKDFIRKELGEegmrksvVVVATSDE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 238 PAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTV------VPSSGK-VLTGGVDANALQRPKRffgaarni 310
Cdd:PRK06793 223 SHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVdiavkeLPIGGKtLLMESYMKKLLERSGK-------- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 311 EQGGSLTIISTALIDtGSRMDEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTRKEELLIDKETLSKIYVLRRIL 390
Cdd:PRK06793 295 TQKGSITGIYTVLVD-GDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKIL 373
|
250 260 270
....*....|....*....|....*....|
gi 402510804 391 NpMGTVDAIEFLLDKLKQTKTNDDFFDSMN 420
Cdd:PRK06793 374 S-IYKENELYFKLGTIQENAENAYIFECKN 402
|
|
| Rho_N |
pfam07498 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
8-49 |
1.94e-16 |
|
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: 72.41 E-value: 1.94e-16
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 402510804 8 DLKSKSPTELLALAEENDIENASTMRKQDMMFAILKELAEQG 49
Cdd:pfam07498 1 ELKEKTLSELREIAKELGIENYSRLRKQELIFAILKAQAEKG 42
|
|
| Rho_N |
smart00959 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
8-49 |
8.37e-16 |
|
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: 70.87 E-value: 8.37e-16
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 402510804 8 DLKSKSPTELLALAEENDIENASTMRKQDMMFAILKELAEQG 49
Cdd:smart00959 1 ELKKKTLSELLEIAKELGIENASRLRKQELIFAILKAQAKKG 42
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
159-378 |
1.93e-15 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 77.62 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 159 DRSSRIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANhpecYLIVLLIDERPEEVTDMQRSVSGE-------VV 231
Cdd:PRK07196 140 DVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQAD----VVVVGLIGERGREVKEFIEHSLQAagmaksvVV 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 232 SSTFDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSGK-VLTGGVDANALQRPKRFFGAARNI 310
Cdd:PRK07196 216 AAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEpPATKGYPPSAFSIIPRLAESAGNS 295
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 402510804 311 EQGGSLTIISTALIDTGSRMDEVIfEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTRKEELLIDKE 378
Cdd:PRK07196 296 SGNGTMTAIYTVLAEGDDQQDPIV-DCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQ 362
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
137-390 |
2.77e-15 |
|
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: 77.38 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 137 DNLTPLYPEERILMEFD--NPAEKDRSS-------RIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANhpecyL 207
Cdd:COG1157 111 DGKGPLPGEERRPLDAPppNPLERARITepldtgvRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARNTEAD-----V 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 208 IVL-LIDERPEEVTD----------MQRSVsgeVVSSTFDEPAARHVQVAEMviekAKRLVEH----GRDVVILLDSITR 272
Cdd:COG1157 186 NVIaLIGERGREVREfieddlgeegLARSV---VVVATSDEPPLMRLRAAYT----ATAIAEYfrdqGKNVLLLMDSLTR 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 273 LGRAyntvvpssgkvltggvdanalQR---------------PKRFFGA-ARNIE-----QGGSLTIISTALIDtGSRMD 331
Cdd:COG1157 259 FAMA---------------------QReiglaageppatrgyPPSVFALlPRLLEragngGKGSITAFYTVLVE-GDDMN 316
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 402510804 332 EVIFEEFKGT--GNseIVLDRKISDKRVFPSIDIMKSGTRKEELLIDKETLSKIYVLRRIL 390
Cdd:COG1157 317 DPIADAVRGIldGH--IVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLL 375
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
163-369 |
6.45e-15 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 76.19 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 163 RIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANHpecyLIVLLIDERPEEVTD---------MQRSVsgeVVSS 233
Cdd:PRK06002 154 RVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDT----VVIALVGERGREVREfledtladnLKKAV---AVVA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 234 TFDE-PAARhvqvaEMVIEKAKRLVEHGRD----VVILLDSITRLGRAYNTVVPSSGK--VLTGGVDANALQRPKRFFGA 306
Cdd:PRK06002 227 TSDEsPMMR-----RLAPLTATAIAEYFRDrgenVLLIVDSVTRFAHAAREVALAAGEppVARGYPPSVFSELPRLLERA 301
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 402510804 307 ARNIEQGGSLTIISTALIDtGSRMDEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTR 369
Cdd:PRK06002 302 GPGAEGGGSITGIFSVLVD-GDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISR 363
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
163-369 |
1.36e-14 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 75.03 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 163 RIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAksiaaNHPECYLIVL-LIDERPEEVTD----MQRSVSGE---VVSST 234
Cdd:PRK08149 140 RAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLI-----EHSEADVFVIgLIGERGREVTEfvesLRASSRREkcvLVYAT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 235 FDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSGKV-LTGGVDANA-------LQRPKRFfga 306
Cdd:PRK08149 215 SDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELpARRGYPASVfdslprlLERPGAT--- 291
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 402510804 307 arnieQGGSLTIISTALIDTGSRMDeVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTR 369
Cdd:PRK08149 292 -----LAGSITAFYTVLLESEEEPD-PIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSR 348
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
163-390 |
3.94e-14 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 73.65 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 163 RIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIaanhpECYL-IVLLIDERPEEVTD----------MQRSVsgeVV 231
Cdd:PRK09099 152 RIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGT-----QCDVnVIALIGERGREVREfielilgedgMARSV---VV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 232 SSTFDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSGKVLTggvdanalQR---PKRFFGAAR 308
Cdd:PRK09099 224 CATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPA--------RRgfpPSVFAELPR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 309 NIEQGG-----SLTIISTALI--DTGSrmdEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTRKEELLIDKETLS 381
Cdd:PRK09099 296 LLERAGmgetgSITALYTVLAedESGS---DPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQ 372
|
....*....
gi 402510804 382 KIYVLRRIL 390
Cdd:PRK09099 373 AAGRLRQLL 381
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
159-390 |
2.11e-11 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 65.19 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 159 DRSSRIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANhpecYLIVLLIDERPEEVTDMQRSVSGE-------VV 231
Cdd:PRK07960 160 DTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQAD----VIVVGLIGERGREVKDFIENILGAegrarsvVI 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 232 SSTFDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSGKV-LTGGVDANALQR-PKRFFGAARN 309
Cdd:PRK07960 236 AAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPpATKGYPPSVFAKlPALVERAGNG 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 310 IEQGGSLTIISTALIDTGSRMDEvIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTRKEELLIDKETLSKIYVLRRI 389
Cdd:PRK07960 316 ISGGGSITAFYTVLTEGDDQQDP-IADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQL 394
|
.
gi 402510804 390 L 390
Cdd:PRK07960 395 L 395
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
137-382 |
2.26e-10 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 62.06 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 137 DNLTPLYPEERILMEFD--NPAEKDRSS-------RIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANhpecYL 207
Cdd:PRK05688 122 DGKGPMKAEDWVPMDGPtiNPLNRHPISepldvgiRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEAD----II 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 208 IVLLIDERPEEVTD----------MQRSVsgeVVSSTFDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAY 277
Cdd:PRK05688 198 VVGLIGERGREVKEfiehilgeegLKRSV---VVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQ 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 278 NTVVPSSGKV-LTGGVDANALQRPKRFFGAARNIEQG-GSLTIISTALIDtGSRMDEVIFEEFKGTGNSEIVLDRKISDK 355
Cdd:PRK05688 275 REIALAIGEPpATKGYPPSVFAKLPKLVERAGNAEPGgGSITAFYTVLSE-GDDQQDPIADSARGVLDGHIVLSRRLAEE 353
|
250 260
....*....|....*....|....*..
gi 402510804 356 RVFPSIDIMKSGTRKEELLIDKETLSK 382
Cdd:PRK05688 354 GHYPAIDIEASISRVMPQVVDPEHLRR 380
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
165-390 |
2.70e-09 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 58.54 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 165 IDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANhpecYLIVLLIDERPEEVTD-MQRSVSGE------VVSSTFDE 237
Cdd:PRK08472 148 IDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLAP----IKVVALIGERGREIPEfIEKNLGGDlentviVVATSDDS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 238 PAARH------VQVAEMVIEKakrlvehGRDVVILLDSITRLGRAYNTVVPSSGKVLTG-GVDANALQRPKRFFGAARNI 310
Cdd:PRK08472 224 PLMRKygafcaMSVAEYFKNQ-------GLDVLFIMDSVTRFAMAQREIGLALGEPPTSkGYPPSVLSLLPQLMERAGKE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 311 EQGGSLTIISTALIDtGSRMDEVIFEEFKGTGNSEIVLDRKISDKRVFPSIDIMKSGTRKEELLIDKETLSKIYVLRRIL 390
Cdd:PRK08472 297 EGKGSITAFFTVLVE-GDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLY 375
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
137-390 |
4.33e-09 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 58.17 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 137 DNLTPLYPEERIlmEFD----NPAEK-------DRSSRIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANhpec 205
Cdd:PRK08972 116 DGLGPIYTDQRA--SRHsppiNPLSRrpiteplDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTAD---- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 206 YLIVLLIDERPEEVTDMQRSVSGEvvsstfdEPAARHVQVAE-------MVI---EKAKRLVEHGRD----VVILLDSIT 271
Cdd:PRK08972 190 VIVVGLVGERGREVKEFIEEILGE-------EGRARSVVVAApadtsplMRLkgcETATTIAEYFRDqglnVLLLMDSLT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 272 RLGRAYNTVVPSSGKV-LTGGVDANALQRPKRFFGAARNIEQG-GSLTIISTALIDtGSRMDEVIFEEFKGTGNSEIVLD 349
Cdd:PRK08972 263 RYAQAQREIALAVGEPpATKGYPPSVFAKLPALVERAGNGGPGqGSITAFYTVLTE-GDDLQDPIADASRAILDGHIVLS 341
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 402510804 350 RKISDKRVFPSIDIMKSGTRKEELLIDKETLSKIYVLRRIL 390
Cdd:PRK08972 342 RELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVY 382
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
163-289 |
8.93e-09 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 57.22 E-value: 8.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 163 RIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSiaanHPECYLIVLLIDERPEEVTD----------MQRSVsgeVVS 232
Cdd:PRK05922 146 KAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKG----SKSTINVIALIGERGREVREyieqhkeglaAQRTI---IIA 218
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 402510804 233 STFDEPAARHVQVAEMVIEKAKRLVEHGRDVVILLDSITRLGRAYNTVVPSSGKVLT 289
Cdd:PRK05922 219 SPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLS 275
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
173-322 |
4.23e-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: 46.21 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 173 KGQRALIVAPPRTGKTVLLQNIAKSIAANHPECYLIVLlidERPEEVTDMQRSVSGEVVSSTFDEPAARhvqvaemvIEK 252
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG---EDILEEVLDQLLLIIVGGKKASGSGELR--------LRL 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 253 AKRLVEHGRDVVILLDSITRLGRAyNTVVPSSGKVLTGGVDANALQRPKRFFGAARNIEQGGSLTIISTA 322
Cdd:smart00382 70 ALALARKLKPDVLILDEITSLLDA-EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| VacB |
COG0557 |
Exoribonuclease R [Transcription]; |
2-113 |
6.04e-06 |
|
Exoribonuclease R [Transcription];
Pssm-ID: 440323 [Multi-domain] Cd Length: 711 Bit Score: 48.56 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 2 EQIkLQDLKSKSPTELLA--LAEENDIENASTMRKqdmMFAILKELAEQGIFIIG--------------EGVVEVLPDGF 65
Cdd:COG0557 6 ETI-LAFLKEDAYKPLSKkeLAKALGLKDEESREA---LKRRLRALEREGQLVKTrrgryrlpekldlvEGRVRGHRDGF 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 402510804 66 GFLRSPDanylpGPDDIYVSPSQIRRfsLRTGDTVEGDIRSPKDGERY 113
Cdd:COG0557 82 GFVIPDD-----GEEDIFIPPRELNG--ALHGDRVLVRVTKEDRRGRP 122
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
163-366 |
4.27e-05 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 44.87 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 163 RIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANhpecylIVLLI--DERPEEVTD-----------------MQ 223
Cdd:cd01134 65 RVLDTLFPVAKGGTAAIPGPFGCGKTVISQSLSKWSNSD------VVIYVgcGERGNEMAEvleefpelkdpitgeslME 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 224 RSVsgeVVSSTFDEP-AARhvqvaEMVIEKAKRLVEHGRD----VVILLDSITRLGRAYNTVvpsSGKV----LTGGVDA 294
Cdd:cd01134 139 RTV---LIANTSNMPvAAR-----EASIYTGITIAEYFRDmgynVSLMADSTSRWAEALREI---SGRLeempAEEGYPA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 295 NALQRPKRFFG-AAR-----NIEQGGSLTIISTALIDTGSRMDEVifeefkgTGNS-EIV-----LDRKISDKRVFPSID 362
Cdd:cd01134 208 YLGARLAEFYErAGRvrclgSPGREGSVTIVGAVSPPGGDFSEPV-------TQATlRIVqvfwgLDKKLAQRRHFPSIN 280
|
....
gi 402510804 363 IMKS 366
Cdd:cd01134 281 WLIS 284
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
178-333 |
5.74e-05 |
|
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410865 [Multi-domain] Cd Length: 119 Bit Score: 42.49 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 178 LIVAPPRTGKTVLLQNIAKSIAanHPECYLIVLLIderpeevtdmqrsvsgevvsstfdepaarhvqvAEMVIEKAKRLV 257
Cdd:cd01120 2 LITGPPGSGKTTLLLQFAEQAL--LSDEPVIFISF---------------------------------LDTILEAIEDLI 46
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 402510804 258 EHGRDVVILLDSITRLGRAYntvvpssgkvlTGGVDANALQRPKRFFGAARNieqgGSLTIISTALIDTGSRMDEV 333
Cdd:cd01120 47 EEKKLDIIIIDSLSSLARAS-----------QGDRSSELLEDLAKLLRAARN----TGITVIATIHSDKFDIDRGG 107
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
163-222 |
4.69e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 42.46 E-value: 4.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 402510804 163 RIIDIVAPLGKGQRALIVAPPRTGKTVLLQNIAKSIAANhpecylIVLLI--DERPEEVTDM 222
Cdd:PRK04192 216 RVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQLAKWADAD------IVIYVgcGERGNEMTEV 271
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
165-188 |
4.86e-03 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 39.19 E-value: 4.86e-03
10 20
....*....|....*....|....
gi 402510804 165 IDIVAPLGKGQRALIVAPPRTGKT 188
Cdd:PRK07165 134 IDLLIPIGKGQRELIIGDRQTGKT 157
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
141-277 |
8.87e-03 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 38.36 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402510804 141 PLYPEERILMEFDNPAEKDRSS---------RIIDIVAPLGKGQRALIVAPPRTGKTVL-LQNIaksIAANHPECYLIVL 210
Cdd:PRK13343 120 PLQATARRPLERPAPAIIERDFvteplqtgiKVVDALIPIGRGQRELIIGDRQTGKTAIaIDAI---INQKDSDVICVYV 196
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 402510804 211 LIDERP---EEVTD-------MQRSVSgeVVSSTFDEPAARHVQ-VAEMVIekAKRLVEHGRDVVILLDSITRLGRAY 277
Cdd:PRK13343 197 AIGQKAsavARVIEtlrehgaLEYTTV--VVAEASDPPGLQYLApFAGCAI--AEYFRDQGQDALIVYDDLSKHAAAY 270
|
|
| |
