|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-460 |
0e+00 |
|
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439825 [Multi-domain] Cd Length: 468 Bit Score: 1001.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 1 MATGKIVQVIGAVVDVEFPQDAVPRVYDALEVQN-GNESLVLEVQQQLGGGIVRTIAMGSSDGLRRGLEVKDLEHPIEVP 79
Cdd:COG0055 3 MNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENeGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 80 VGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVN 159
Cdd:COG0055 83 VGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 160 MMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD-EGRDV 238
Cdd:COG0055 163 IMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 239 LLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDA 318
Cdd:COG0055 243 LLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 319 TVVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQEHYDTARGVQSLLQRYQELKDIIAILGMDELSEEDKLVVARARKIQ 398
Cdd:COG0055 323 TTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKIQ 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578257540 399 RFLSQPFFVAEVFTGAPGKYVSLKDTIRGFKGIMEGEYDHLPEQAFYMVGSIEEAVEKAKKL 460
Cdd:COG0055 403 RFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKL 464
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
2-460 |
0e+00 |
|
ATP synthase, F1 beta 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. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 211621 [Multi-domain] Cd Length: 461 Bit Score: 926.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 2 ATGKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNES-LVLEVQQQLGGGIVRTIAMGSSDGLRRGLEVKDLEHPIEVPV 80
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNRAESeLTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 81 GKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVNM 160
Cdd:TIGR01039 81 GKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 161 MELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE-GRDVL 239
Cdd:TIGR01039 161 QELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 240 LFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDAT 319
Cdd:TIGR01039 241 LFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 320 VVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQEHYDTARGVQSLLQRYQELKDIIAILGMDELSEEDKLVVARARKIQR 399
Cdd:TIGR01039 321 TVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQR 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578257540 400 FLSQPFFVAEVFTGAPGKYVSLKDTIRGFKGIMEGEYDHLPEQAFYMVGSIEEAVEKAKKL 460
Cdd:TIGR01039 401 FLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
3-460 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 804.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 3 TGKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNE-----SLVLEVQQQLGGGIVRTIAMGSSDGLRRGLEVKDLEHPIE 77
Cdd:CHL00060 16 LGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTagqeiNVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 78 VPVGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKT 157
Cdd:CHL00060 96 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 158 VNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVLD-------KVSLVYGQMNEPPGNRLRVALTGLTMAEK 230
Cdd:CHL00060 176 VLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 231 FRDEGR-DVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSP 309
Cdd:CHL00060 256 FRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 310 ATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQEHYDTARGVQSLLQRYQELKDIIAILGMDELSEEDKL 389
Cdd:CHL00060 336 ATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRL 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578257540 390 VVARARKIQRFLSQPFFVAEVFTGAPGKYVSLKDTIRGFKGIMEGEYDHLPEQAFYMVGSIEEAVEKAKKL 460
Cdd:CHL00060 416 TVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANL 486
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
77-347 |
0e+00 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 564.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 77 EVPVGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 156
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 157 TVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNV-----LDKVSLVYGQMNEPPGNRLRVALTGLTMAEKF 231
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVinldgLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 232 RD-EGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPA 310
Cdd:cd01133 161 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPA 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 578257540 311 TTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDP 347
Cdd:cd01133 241 TTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
4-453 |
0e+00 |
|
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 beta subunit of this apparent second ATP synthase.
Pssm-ID: 132348 [Multi-domain] Cd Length: 449 Bit Score: 564.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 4 GKIVQVIGAVVDVEFPQDaVPRVYDALEVQNGNEsLVLEVQQQLGGGIVRTIAMGSSDGLRRGLEVKDLEHPIEVPVGKA 83
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGE-LPAIHSVLRAGREGE-VVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 84 TLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMEL 163
Cdd:TIGR03305 79 TLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 164 IRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD-EGRDVLLFV 242
Cdd:TIGR03305 159 IHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDdEKQDVLLLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 243 DNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVL 322
Cdd:TIGR03305 239 DNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSASLVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 323 SRQIASLGIYPAVDPLDSTSRQLDPLVVGQEHYDTARGVQSLLQRYQELKDIIAILGMDELSEEDKLVVARARKIQRFLS 402
Cdd:TIGR03305 319 SRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLERFLT 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 578257540 403 QPFFVAEVFTGAPGKYVSLKDTIRGFKGIMEGEYDHLPEQAFYMVGSIEEA 453
Cdd:TIGR03305 399 QPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
78-343 |
4.32e-126 |
|
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: 366.78 E-value: 4.32e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 78 VPVGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKT 157
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 158 VNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRD 237
Cdd:cd19476 82 VLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 238 VLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT--GSITSVQAVYVPADDLTDPSPATTFAH 315
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDggGSITAIPAVSTPGDDLTDPIPDNTFAI 241
|
250 260
....*....|....*....|....*...
gi 578257540 316 LDATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:cd19476 242 LDGQIVLSRELARKGIYPAINVLDSTSR 269
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
130-342 |
2.02e-94 |
|
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: 283.86 E-value: 2.02e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 130 GIKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAiehSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQ 209
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQAS---ADVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 210 MNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITST--K 287
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVkgK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578257540 288 TGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTS 342
Cdd:pfam00006 158 GGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
349-456 |
1.71e-78 |
|
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-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 extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic.
Pssm-ID: 349745 [Multi-domain] Cd Length: 108 Bit Score: 239.30 E-value: 1.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 349 VVGQEHYDTARGVQSLLQRYQELKDIIAILGMDELSEEDKLVVARARKIQRFLSQPFFVAEVFTGAPGKYVSLKDTIRGF 428
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 578257540 429 KGIMEGEYDHLPEQAFYMVGSIEEAVEK 456
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
3-432 |
5.66e-70 |
|
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: 228.38 E-value: 5.66e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 3 TGKIVQVIGAVVDVEFPQdavPRVYDALEVQNGNESLVL-EVqqqLG--GGIVRTIAMGSSDGLRRGLEVKDLEHPIEVP 79
Cdd:COG1157 20 SGRVTRVVGLLIEAVGPD---ASIGELCEIETADGRPVLaEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRPLSVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 80 VGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVN 159
Cdd:COG1157 94 VGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 160 MMELIRNIA--IehsgySVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRD 237
Cdd:COG1157 174 LGMIARNTEadV-----NVIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 238 VLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLD 317
Cdd:COG1157 249 VLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 318 ATVVLSRQIASLGIYPAVDPLDSTSRqLDPLVVGQEHYDTARGVQSLLQRYQELKDIIAI----LGMDELSEEdklVVAR 393
Cdd:COG1157 329 GHIVLSRKLAERGHYPAIDVLASISR-VMPDIVSPEHRALARRLRRLLARYEENEDLIRIgayqPGSDPELDE---AIAL 404
|
410 420 430
....*....|....*....|....*....|....*....
gi 578257540 394 ARKIQRFLSQPffvaevftgaPGKYVSLKDTIRGFKGIM 432
Cdd:COG1157 405 IPAIEAFLRQG----------MDERVSFEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
77-343 |
1.30e-61 |
|
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: 201.25 E-value: 1.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 77 EVPVGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 156
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 157 TVNMMELIRNIAiehSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGR 236
Cdd:cd01136 81 STLLGMIARNTD---ADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 237 DVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHL 316
Cdd:cd01136 158 KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSIL 237
|
250 260
....*....|....*....|....*..
gi 578257540 317 DATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:cd01136 238 DGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
59-403 |
1.08e-52 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 183.09 E-value: 1.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 59 SSDGLRRGLEVKDLEHPIEVPVGKATLGRIMNVLGQPIDMKGDIGEEERwAIHRAAPSYEELSSSQELLETGIKVIDLMC 138
Cdd:PRK06820 80 SSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWR-ELDCPPPSPLTRQPIEQMLTTGIRAIDGIL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 139 PFAKGGKVGLFGGAGVGKTVnmmeLIRNIAiEHSGYSV--FAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGN 216
Cdd:PRK06820 159 SCGEGQRIGIFAAAGVGKST----LLGMLC-ADSAADVmvLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 217 RLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQA 296
Cdd:PRK06820 234 RLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 297 VYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDTARGVQSLLQRYQELKDIIA 376
Cdd:PRK06820 314 VLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIELLVR 392
|
330 340 350
....*....|....*....|....*....|.
gi 578257540 377 I----LGMDELSEEdklVVARARKIQRFLSQ 403
Cdd:PRK06820 393 VgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
57-405 |
9.07e-52 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 180.58 E-value: 9.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 57 MGSSDGLRRGLEVKDLEHPIEVPVGKATLGRIMNVLGQPIDMKG----DIGEEERWAIHRAAPSYEELSSSQELLETGIK 132
Cdd:PRK08149 61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDapptVGPISEERVIDVAPPSYAERRPIREPLITGVR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 133 VID--LMCpfAKGGKVGLFGGAGVGKTVNMmelirNIAIEHSGYSVF--AGVGERTREGNDFYHEMTDSNVLDKVSLVYG 208
Cdd:PRK08149 141 AIDglLTC--GVGQRMGIFASAGCGKTSLM-----NMLIEHSEADVFviGLIGERGREVTEFVESLRASSRREKCVLVYA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 209 QMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT 288
Cdd:PRK08149 214 TSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 289 GSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPlVVGQEHYDTARGVQSLLQRY 368
Cdd:PRK08149 294 GSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQ-VTDPKHRQLAAAFRKLLTRL 372
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 578257540 369 QELKDIIAiLG---MDELSEEDKLVVARArKIQRFLSQPF 405
Cdd:PRK08149 373 EELQLFID-LGeyrRGENADNDRAMDKRP-ALEAFLKQDV 410
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
61-433 |
9.14e-52 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 180.65 E-value: 9.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 61 DGLRRGLEVKDLEHPIEVPVGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPF 140
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTC 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 141 AKGGKVGLFGGAGVGKTVNMMELIRNiaiEHSGYSVFAGVGERTREGNDFYHEMTDSNvLDKVSLVYGQMNEPPGNRLRV 220
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKSTLMGMIVKG---CLAPIKVVALIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSPLMRKYG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 221 ALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT-GSITSVQAVYV 299
Cdd:PRK08472 231 AFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGkGSITAFFTVLV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 300 PADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPlVVGQEHYDTARGVQSLLQRYQELKDIIAI-- 377
Cdd:PRK08472 311 EGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMND-IISPEHKLAARKFKRLYSLLKENEVLIRIga 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 578257540 378 --LGMD-ELSEedklVVARARKIQRFLSQpffvaevftgAPGKYVSLKDTIRGFKGIME 433
Cdd:PRK08472 390 yqKGNDkELDE----AISKKEFMEQFLKQ----------NPNELFPFEQTFEQLEEILR 434
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
62-377 |
1.59e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 177.58 E-value: 1.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 62 GLRRGLEVKDLEHPIEVPVGKATLGRIMNVLGQPIDMKGDIGEEERwaIHRAAPSYEELSSSQ--ELLETGIKVIDLMCP 139
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQR--ASRHSPPINPLSRRPitEPLDVGVRAINAMLT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 140 FAKGGKVGLFGGAGVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLR 219
Cdd:PRK08972 159 VGKGQRMGLFAGSGVGKSVLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 220 VALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAV 297
Cdd:PRK08972 236 GCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAgnGGPGQGSITAFYTV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 298 YVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDTARGVQSLLQRYQELKDIIAI 377
Cdd:PRK08972 316 LTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
2-404 |
3.25e-49 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 173.80 E-value: 3.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 2 ATGKIVQVIGAVVDVefpqdavprvyDALEVQNGNeslVLEVQQQLGG--------GIVRTIAM----GSSDGLRRGLEV 69
Cdd:PRK09099 24 RTGKVVEVIGTLLRV-----------SGLDVTLGE---LCELRQRDGTllqraevvGFSRDVALlspfGELGGLSRGTRV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 70 KDLEHPIEVPVGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLF 149
Cdd:PRK09099 90 IGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 150 GGAGVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAE 229
Cdd:PRK09099 170 APAGVGKSTLMGMFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 230 KFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSP 309
Cdd:PRK09099 247 YFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 310 ATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDTARGVQSLLQRYQELKDIIAI----LGMDELSE 385
Cdd:PRK09099 327 EEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVAD 405
|
410
....*....|....*....
gi 578257540 386 EdklVVARARKIQRFLSQP 404
Cdd:PRK09099 406 E---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
4-377 |
4.46e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 173.63 E-value: 4.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 4 GKIVQVIGAVVDVEFPQDAVpRVYDALEVQN-GNESLVLEVqqqLGGGIVRTIAM--GSSDGLRRGLEVKDLEHPIEVPV 80
Cdd:PRK08927 19 GRVVAVRGLLVEVAGPIHAL-SVGARIVVETrGGRPVPCEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVRP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 81 GKATLGRIMNVLGQPIDMKGDIGE-EERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVN 159
Cdd:PRK08927 95 SRAWLGRVVNALGEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 160 MMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVL 239
Cdd:PRK08927 175 LSMLARNADAD---VSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 240 LFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAVYVPADDLTDPSPATTFAHLD 317
Cdd:PRK08927 252 CLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILD 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 318 ATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDTARGVQSLLQRYQELKDIIAI 377
Cdd:PRK08927 332 GHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
4-403 |
7.74e-49 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 173.01 E-value: 7.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 4 GKIVQVIGAVVdvefpQDAVP--RVYDALEVQNGNESLVL--EVQqqlggGIVRTIA----MGSSDGLRRGLEVKDLEHP 75
Cdd:PRK06936 25 GRVTQVTGTIL-----KAVVPgvRIGELCYLRNPDNSLSLqaEVI-----GFAQHQAlltpLGEMYGISSNTEVSPTGTM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 76 IEVPVGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVG 155
Cdd:PRK06936 95 HQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 156 KTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEG 235
Cdd:PRK06936 175 KSTLLASLIRSAEVD---VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 236 RDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAH 315
Cdd:PRK06936 252 KRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 316 LDATVVLSRQIASLGIYPAVDPLDSTSRQLDPlVVGQEHYDTARGVQSLLQRYQELKDIIAI----LGMDELSEEdklVV 391
Cdd:PRK06936 332 LDGHIILSRKLAAANHYPAIDVLRSASRVMNQ-IVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKEADQ---AI 407
|
410
....*....|..
gi 578257540 392 ARARKIQRFLSQ 403
Cdd:PRK06936 408 ERIGAIRGFLRQ 419
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
86-379 |
9.34e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 170.18 E-value: 9.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 86 GRIMNVLGQPIDMKGDIGE-EERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELI 164
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 165 RNIAIEHSgysVFAGVGERTREGNDFYHEMTDSNvLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDN 244
Cdd:PRK06002 187 RADAFDTV---VIALVGERGREVREFLEDTLADN-LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDS 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 245 IYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVL 322
Cdd:PRK06002 263 VTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVL 342
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 578257540 323 SRQIASLGIYPAVDPLDSTSRqLDPLVVGQEHYDTARGVQSLLQRYQELKDIIAILG 379
Cdd:PRK06002 343 DRAIAEQGRYPAVDPLASISR-LARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
4-377 |
4.32e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 165.67 E-value: 4.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 4 GKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNESLVLEVQQQLGGGI-------VRTIAMGSSdglrrgleVKDLEHPI 76
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESSIGDVCYIHTKGGGDKAIKAEVVGFKDEHVllmpyteVAEIAPGCL--------VEATGKPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 77 EVPVGKATLGRIMNVLGQPIDM----KGDigeeERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGA 152
Cdd:PRK07721 92 EVKVGSGLIGQVLDALGEPLDGsalpKGL----APVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 153 GVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFR 232
Cdd:PRK07721 168 GVGKSTLMGMIARNTSAD---LNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 233 DEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATT 312
Cdd:PRK07721 245 DQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTV 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578257540 313 FAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDTARGVQSLLQRYQELKDIIAI 377
Cdd:PRK07721 325 RGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
2-403 |
1.14e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 164.52 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 2 ATGKIVQVIGAVVDVEFPQDAVPRvydALEVQNGNESLVLEVQQQL---GGGIVRTIAMGSSDGLRRGLEVKDLEHPIEV 78
Cdd:PRK05688 27 VEGRLLRMVGLTLEAEGLRAAVGS---RCLVINDDSYHPVQVEAEVmgfSGDKVFLMPVGSVAGIAPGARVVPLADTGRL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 79 PVGKATLGRIMNVLGQPIDMKGDIGEEERwaIHRAAPSYEELSSS--QELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 156
Cdd:PRK05688 104 PMGMSMLGRVLDGAGRALDGKGPMKAEDW--VPMDGPTINPLNRHpiSEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 157 TV--NMMELIRNIAIehsgySVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE 234
Cdd:PRK05688 182 SVllGMMTRFTEADI-----IVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 235 GRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT--GSITSVQAVYVPADDLTDPSPATT 312
Cdd:PRK05688 257 GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPggGSITAFYTVLSEGDDQQDPIADSA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 313 FAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDTARGVQSLLQRYQELKDIIAI----LGMDelsEEDK 388
Cdd:PRK05688 337 RGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLISVgayvAGGD---PETD 412
|
410
....*....|....*
gi 578257540 389 LVVARARKIQRFLSQ 403
Cdd:PRK05688 413 LAIARFPHLVQFLRQ 427
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
62-403 |
5.42e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 162.37 E-value: 5.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 62 GLRRGLEVKDLEHPIEVPVGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFA 141
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 142 KGGKVGLFGGAGVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVA 221
Cdd:PRK07196 154 KGQRVGLMAGSGVGKSVLLGMITRYTQAD---VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKAT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 222 LTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT-------LAEEMGvlqeriTSTKTGSITSV 294
Cdd:PRK07196 231 ELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSafsiiprLAESAG------NSSGNGTMTAI 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 295 QAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPlVVGQEHYDTARGVQSLLQRYQELKDI 374
Cdd:PRK07196 305 YTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQ-VIGSQQAKAASLLKQCYADYMAIKPL 383
|
330 340 350
....*....|....*....|....*....|...
gi 578257540 375 IA----ILGMDELSEEdklVVARARKIQRFLSQ 403
Cdd:PRK07196 384 IPlggyVAGADPMADQ---AVHYYPAITQFLRQ 413
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
58-377 |
9.71e-45 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 161.66 E-value: 9.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 58 GSSDGLRRGLEVKDLEHPIEVPVGKATLGRIMNVLGQPIDMKGDigEEERWAIHRA--APSYEELSSSQELLeTGIKVID 135
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGREL--PDVCWKDYDAmpPPAMVRQPITQPLM-TGIRAID 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 136 LMCPFAKGGKVGLFGGAGVGKTVNMMELIrniAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPG 215
Cdd:PRK07594 148 SVATCGEGQRVGIFSAPGVGKSTLLAMLC---NAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPAL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 216 NRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQ 295
Cdd:PRK07594 225 ERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFY 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 296 AVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDTARGVQSLLQRYQELKDII 375
Cdd:PRK07594 305 TVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVELLI 383
|
..
gi 578257540 376 AI 377
Cdd:PRK07594 384 RI 385
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
76-403 |
2.83e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 155.14 E-value: 2.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 76 IEVPVGKATLGRIMNVLGQPIDMKGDIGEEERwaIHRAAPSYEELSSSQ--ELLETGIKVIDLMCPFAKGGKVGLFGGAG 153
Cdd:PRK06793 89 VVIPRGNHLLGKVLSANGEVLNEEAENIPLQK--IKLDAPPIHAFEREEitDVFETGIKSIDSMLTIGIGQKIGIFAGSG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 154 VGKTVNMMELIRNiaiEHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD 233
Cdd:PRK06793 167 VGKSTLLGMIAKN---AKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRD 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 234 EGRDVLLFVDNIYRYTLAGTEVSALLGRMPsaVGYQPTLAEE-MGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATT 312
Cdd:PRK06793 244 QGNNVLLMMDSVTRFADARRSVDIAVKELP--IGGKTLLMESyMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 313 FAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPlVVGQEHYDTARGVQSLLQRYQElKDIIAILGMDELSEEDKLVVA 392
Cdd:PRK06793 322 RGILDGHIVLKRELATLSHYPAISVLDSVSRIMEE-IVSPNHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAYIFE 399
|
330
....*....|....
gi 578257540 393 RARK---IQRFLSQ 403
Cdd:PRK06793 400 CKNKvegINTFLKQ 413
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
77-377 |
1.48e-36 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 139.92 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 77 EVPVGKATLGRIMNVLGQPIDmkGDIGEEERWAIHRAAPSYEELSSS--QELLETGIKVIDLMCPFAKGGKVGLFGGAGV 154
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLD--GLPAPDTGETGALITPPFNPLQRTpiEHVLDTGVRAINALLTVGRGQRMGLFAGSGV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 155 GKTVNMMELIRniaIEHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE 234
Cdd:PRK07960 187 GKSVLLGMMAR---YTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDR 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 235 GRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITS--TKTGSITSVQAVYVPADDLTDPSPATT 312
Cdd:PRK07960 264 GQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSA 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578257540 313 FAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLvVGQEHYDTARGVQSLLQRYQELKDIIAI 377
Cdd:PRK07960 344 RAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAL-IDEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
7-439 |
9.20e-36 |
|
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: 138.29 E-value: 9.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 7 VQVIGAVVDVefpQDAVPRVY--------DALEVQNGNESLVLEVQQQLGGGIVrtiaMGSSDGLRRGLEVKDLEHPIEV 78
Cdd:TIGR00962 24 AEEVGTVVSV---GDGIARVYglenvmsgELIEFEGGVQGIALNLEEDSVGAVI----MGDYSDIREGSTVKRTGRILEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 79 PVGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTV 158
Cdd:TIGR00962 97 PVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 159 NMMELIRNIAIEHSgYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDV 238
Cdd:TIGR00962 177 VAIDTIINQKDSDV-YCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDNGKHA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 239 LLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTK----TGSITSVQAVYVPADDLTDPSPATTFA 314
Cdd:TIGR00962 256 LIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNdekgGGSLTALPIIETQAGDVSAYIPTNVIS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 315 HLDATVVLSRQIASLGIYPAVDPLDSTSRqldplvVG-----QEHYDTARGVQSLLQRYQELkDIIAILGMDeLSEEDKL 389
Cdd:TIGR00962 336 ITDGQIFLESDLFNSGIRPAINVGLSVSR------VGgaaqiKAMKQVAGSLRLELAQYREL-EAFSQFASD-LDEATKK 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 390 VVARARKIQRFLSQPFF--------VAEVFTGAPG--KYVSLKDtIRGFKgimEGEYDHL 439
Cdd:TIGR00962 408 QLERGQRVVELLKQPQYkplsveeqVVILFAGTKGylDDIPVDK-IRKFE---QALLAYL 463
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
5-405 |
1.94e-35 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 136.88 E-value: 1.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 5 KIVQVIGAVVDVEfpqdAVPRV-YDAL---EVQNGNESL--VLEVQqqlgGGIVRTIAMGSSDGL-RRGLEVKDLEHPIE 77
Cdd:PRK04196 6 TVSEIKGPLLFVE----GVEGVaYGEIveiELPNGEKRRgqVLEVS----EDKAVVQVFEGTTGLdLKDTKVRFTGEPLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 78 VPVGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAA--PSYEElsSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVG 155
Cdd:PRK04196 78 LPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVARE--YPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 156 KTVNMMELIRNIAIEHSGYS---VFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRL---RVAltgLTMAE 229
Cdd:PRK04196 156 HNELAAQIARQAKVLGEEENfavVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERIltpRMA---LTAAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 230 --KFrDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQER--ITSTKTGSITSVQAVYVPADDLT 305
Cdd:PRK04196 233 ylAF-EKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 306 DPSPattfahlDAT-------VVLSRQIASLGIYPAVDPLDSTSRQLDpLVVG-----QEHYDTARGVQSLLQRYQELKD 373
Cdd:PRK04196 312 HPIP-------DLTgyitegqIVLSRELHRKGIYPPIDVLPSLSRLMK-DGIGegktrEDHKDVANQLYAAYARGKDLRE 383
|
410 420 430
....*....|....*....|....*....|...
gi 578257540 374 IIAILGMDELSEEDKLVVARARKI-QRFLSQPF 405
Cdd:PRK04196 384 LAAIVGEEALSERDRKYLKFADAFeREFVNQGF 416
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
66-435 |
9.52e-35 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 134.26 E-value: 9.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 66 GLEVKDLEHPIEVPVGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGK 145
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 146 VGLFGGAGVGKTvnmmELIRNIAI-EHSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTG 224
Cdd:PRK05922 160 IGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 225 LTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAV-YVP--A 301
Cdd:PRK05922 236 MTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnhP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 302 DDLTDPSPATtfahLDATVVLSRQIASLGiYPAVDPLDSTSRQLDPLVVgQEHYDTARGVQSLLQRYQELKDIIAiLGMD 381
Cdd:PRK05922 316 DIFTDYLKSL----LDGHFFLTPQGKALA-SPPIDILTSLSRSARQLAL-PHHYAAAEELRSLLKAYHEALDIIQ-LGAY 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 578257540 382 ELSEEDKL--VVARARKIQRFLSQPFfvaevftgapGKYVSLKDTIRGFKGIMEGE 435
Cdd:PRK05922 389 VPGQDAHLdrAVKLLPSIKQFLSQPL----------SSYCALHNTLKQLEALLKHE 434
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
2-76 |
1.34e-34 |
|
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-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 extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic.
Pssm-ID: 349739 [Multi-domain] Cd Length: 76 Bit Score: 123.78 E-value: 1.34e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578257540 2 ATGKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNE-SLVLEVQQQLGGGIVRTIAMGSSDGLRRGLEVKDLEHPI 76
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDDGkKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
75-343 |
1.09e-32 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. 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. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 125.41 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 75 PIEVPVGKATLGRIMNVLGQPIDMKGDIGEEERWAIH--------RAAPsyeelsssQELLETGIKVIDLMCPFAKGGKV 146
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINgppinpvaRIYP--------EEMIQTGISAIDVMNTLVRGQKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 147 GLFGGAGVGKTVNMMELIRNIAIEHSGYS---VFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALT 223
Cdd:cd01135 73 PIFSGSGLPHNELAAQIARQAGVVGSEENfaiVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 224 GLTMAEKFR-DEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQER--ITSTKTGSITSVQAVYVP 300
Cdd:cd01135 153 ALTTAEYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMP 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 578257540 301 ADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
7-343 |
2.03e-30 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 123.10 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 7 VQVIGAVVDVefpQDAVPRVY--------DALEVQNGNESLVLEVQQQLGGGIVrtiaMGSSDGLRRGLEVKDLEHPIEV 78
Cdd:PRK13343 25 AREIGRVESV---GDGIAFVSglpdaaldELLRFEGGSRGFAFNLEEELVGAVL----LDDTADILAGTEVRRTGRVLEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 79 PVGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTV 158
Cdd:PRK13343 98 PVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 159 NMMELIrnIAIEHSG-YSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRD 237
Cdd:PRK13343 178 IAIDAI--INQKDSDvICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 238 VLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERIT----STKTGSITSVQAVYVPADDLTDPSPATTF 313
Cdd:PRK13343 256 ALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAklspELGGGSLTALPIIETLAGELSAYIPTNLI 335
|
330 340 350
....*....|....*....|....*....|
gi 578257540 314 AHLDATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:PRK13343 336 SITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
1-433 |
3.12e-28 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 117.58 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 1 MATGKIVQVIGAVVDVEFPQDAvpRVYDALEVqnGNESLVLEVQQ--------------------------------QLG 48
Cdd:PRK04192 2 MTKGKIVRVSGPLVVAEGMGGA--RMYEVVRV--GEEGLIGEIIRiegdkatiqvyeetsgikpgepveftgeplsvELG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 49 GGIVRTIAMG-----------SSDGLRRGLEVKDL---------------------------------EHPIEVPVGKAt 84
Cdd:PRK04192 78 PGLLGSIFDGiqrpldelaekSGDFLERGVYVPALdrekkweftptvkvgdkveagdilgtvqetpsiEHKIMVPPGVS- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 85 lGRIMNVLGQ----------PIDMKGDIGEE----ERWAIHRAAPSYEELSSSqELLETGIKVIDLMCPFAKGGKVGLFG 150
Cdd:PRK04192 157 -GTVKEIVSEgdytvddtiaVLEDEDGEGVEltmmQKWPVRRPRPYKEKLPPV-EPLITGQRVIDTFFPVAKGGTAAIPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 151 GAGVGKTVnmmeLIRNIAiehsGYS-----VFAGVGERtreGNdfyhEMTDsnVLdkvslvygqmNEPP-------GNRL 218
Cdd:PRK04192 235 PFGSGKTV----TQHQLA----KWAdadivIYVGCGER---GN----EMTE--VL----------EEFPelidpktGRPL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 219 --R-----------VA------LTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLA------ 273
Cdd:PRK04192 288 meRtvliantsnmpVAareasiYTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLAsrlaef 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 274 -EEMGVLqeRITSTKTGSITSVQAVYVPADDLTDP-SPAT-----TFAHLDATVVLSRQiaslgiYPAVDPLDSTSRQLD 346
Cdd:PRK04192 368 yERAGRV--KTLGGEEGSVTIIGAVSPPGGDFSEPvTQNTlrivkVFWALDAELADRRH------FPAINWLTSYSLYLD 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 347 PL------VVGQEHYDTARGVQSLLQRYQELKDIIAILGMDELSEEDKLVVARARKI-QRFLSQPFFvAEVFTgapgkYV 419
Cdd:PRK04192 440 QVapwweeNVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQNAF-DPVDT-----YC 513
|
570
....*....|....
gi 578257540 420 SLKDTIRGFKGIME 433
Cdd:PRK04192 514 PPEKQYEMLKLILT 527
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
46-343 |
1.51e-27 |
|
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: 111.13 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 46 QLGGGIVRTIAmgssDGLRRGLEVKDLEHPIEVPVGKATlgrimnvlgqpidmkgdigeeERWAIHRAAPSYEELSSSQE 125
Cdd:cd01134 5 ELGPGLLGSIF----DGIQRPLEVIAETGSIFIPRGVNV---------------------QRWPVRQPRPVKEKLPPNVP 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 126 LLeTGIKVIDLMCPFAKGGKVGLFGGAGVGKTVnmmelirniaIEH--SGYS-----VFAGVGER----TREGNDFYH-- 192
Cdd:cd01134 60 LL-TGQRVLDTLFPVAKGGTAAIPGPFGCGKTV----------ISQslSKWSnsdvvIYVGCGERgnemAEVLEEFPElk 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 193 -EMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 271
Cdd:cd01134 129 dPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAY 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578257540 272 LAEEMGVLQERITSTKT-------GSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:cd01134 209 LGARLAEFYERAGRVRClgspgreGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
76-343 |
1.07e-25 |
|
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: 105.72 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 76 IEVPVGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVG 155
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 156 KTVNMMELIrniaIEHSG---YSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFR 232
Cdd:cd01132 82 KTAIAIDTI----INQKGkkvYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 233 DEGRDVLLFVDNIYRYTLAGTEVSALLGR------MPSAVGY-QPTLAEEMGVLQERItstKTGSITSVQAVYVPADDLT 305
Cdd:cd01132 158 DNGKHALIIYDDLSKQAVAYRQMSLLLRRppgreaYPGDVFYlHSRLLERAAKLSDEL---GGGSLTALPIIETQAGDVS 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 578257540 306 DPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:cd01132 235 AYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
76-403 |
9.81e-21 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 94.40 E-value: 9.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 76 IEVPVGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVG 155
Cdd:TIGR01040 74 LRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 156 KTVNMMELIRNIAI-------EHSGYS-----VFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALT 223
Cdd:TIGR01040 154 HNEIAAQICRQAGLvklptkdVHDGHEdnfaiVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 224 GLTMAEKFRDE-GRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAVYVP 300
Cdd:TIGR01040 234 ALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 301 ADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLV-VGQEHYDTARGVQSLLQRYQELKDII---A 376
Cdd:TIGR01040 314 NDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIgEGMTRKDHSDVSNQLYACYAIGKDVQamkA 393
|
330 340
....*....|....*....|....*...
gi 578257540 377 ILGMDELSEEDKLVVARARKIQR-FLSQ 403
Cdd:TIGR01040 394 VVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
159-415 |
1.38e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 95.09 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 159 NMMELIRNIAIEH-------SGYSVFAGVGERTREGNDFYHEM-------TDSNVLDKVSLVYGQMNEPPGNRLRVALTG 224
Cdd:PRK14698 662 NMPTLLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEFpklkdpkTGKPLMERTVLIANTSNMPVAAREASIYTG 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 225 LTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI-------TSTKTGSITSVQAV 297
Cdd:PRK14698 742 ITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAV 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 298 YVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLV------VGQEHYDTARGVQSLLQRYQEL 371
Cdd:PRK14698 822 SPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKdwwhknVDPEWKAMRDKAMELLQKEAEL 901
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 578257540 372 KDIIAILGMDELSEEDKLVVARARKIQR-FLSQPFFvAEVFTGAP 415
Cdd:PRK14698 902 QEIVRIVGPDALPERERAILLVARMLREdYLQQDAF-DEVDTYCP 945
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
10-263 |
1.45e-20 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 93.98 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 10 IGAVVDVefpQDAVPRVY---DA-----LEVQNGNESLVLEVQQQLGGGIVrtiaMGSSDGLRRGLEVKDLEHPIEVPVG 81
Cdd:PRK09281 28 VGTVISV---GDGIARVYgldNVmagelLEFPGGVYGIALNLEEDNVGAVI----LGDYEDIKEGDTVKRTGRILEVPVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 82 KATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVnmm 161
Cdd:PRK09281 101 EALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTA--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 162 elirnIAIE------HSG-YSVFAGVGERtregndfyhEMTDSNVLDKVSlVYGQM----------NEPPGNRLRVALTG 224
Cdd:PRK09281 178 -----IAIDtiinqkGKDvICIYVAIGQK---------ASTVAQVVRKLE-EHGAMeytivvaataSDPAPLQYLAPYAG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 578257540 225 LTMAEKFRDEGRDVLLFVDNI------YRytlagtEVSALLGRMP 263
Cdd:PRK09281 243 CAMGEYFMDNGKDALIVYDDLskqavaYR------QLSLLLRRPP 281
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
10-263 |
2.73e-20 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 93.18 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 10 IGAVVDVefpQDAVPRVY---DA-----LEVQNGNESLVLEVQQQLGGGIVrtiaMGSSDGLRRGLEVKDLEHPIEVPVG 81
Cdd:COG0056 28 VGTVLSV---GDGIARVYglpNAmagelLEFPGGVYGMALNLEEDNVGVVL----LGDYEGIKEGDTVKRTGRILSVPVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 82 KATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVnmm 161
Cdd:COG0056 101 EALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTA--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 162 elirnIAIE------HSG-YSVFAGVGERtregndfyhemtDSNVldkVSLV-----YGQM----------NEPPGNRLR 219
Cdd:COG0056 178 -----IAIDtiinqkGKDvICIYVAIGQK------------ASTV---AQVVetleeHGAMeytivvaataSDPAPLQYI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 578257540 220 VALTGLTMAEKFRDEGRDVLLFVDNI------YRytlagtEVSALLGRMP 263
Cdd:COG0056 238 APYAGCAMGEYFMDQGKDVLIVYDDLskhavaYR------ELSLLLRRPP 281
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
5-388 |
6.45e-20 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 91.63 E-value: 6.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 5 KIVQVIGAVVDVEfpqdAVPRVYDAL-EVQNGNESLVLEVQQqLGGGIVRTIAMGSSDGLRRGLEVKDLEHPIEVPVGKA 83
Cdd:PRK02118 7 KITDITGNVITVE----AEGVGYGELaTVERKDGSSLAQVIR-LDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 84 TLGRIMNVLGQPIDmKGDIGEEERWAIhrAAPSYEELSSSQ--ELLETGIKVIDLMCPFAKGGKVGLFGGAgvGKTVNmm 161
Cdd:PRK02118 82 LLGRRFNGSGKPID-GGPELEGEPIEI--GGPSVNPVKRIVprEMIRTGIPMIDVFNTLVESQKIPIFSVS--GEPYN-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 162 ELIRNIAIE-HSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFR-DEGRDVL 239
Cdd:PRK02118 155 ALLARIALQaEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 240 LFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTK-TGSITSVQAVYVPADDLTDPSPATTFAHLDA 318
Cdd:PRK02118 235 VLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEdGGSITIIAVTTMPGDDVTHPVPDNTGYITEG 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578257540 319 TVVLSRQiaslgiypAVDPLDSTSRqLDPLVVGQEHYDTARGV-QSLLQRYQELKDIIAILGMD-ELSEEDK 388
Cdd:PRK02118 315 QFYLRRG--------RIDPFGSLSR-LKQLVIGKKTREDHGDLmNAMIRLYADSREAKEKMAMGfKLSNWDE 377
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
354-413 |
5.03e-19 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 80.95 E-value: 5.03e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 354 HYDTARGVQSLLQRYQELKDIIAILGMDELSEEDKLVVARARKIQRFLSQPFFVAEVFTG 413
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIED 60
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-72 |
2.46e-17 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 76.04 E-value: 2.46e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578257540 6 IVQVIGAVVDVEFPQDAVPRVYDALEVQNGN-ESLVLEVQQQLGGGIVRTIAMGSSDGLRRGLEVKDL 72
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVEfGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRT 68
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
7-343 |
1.05e-15 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 79.24 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 7 VQV--IGAVVDVefpQDAVPRVYDALEVQNGNeslVLEVQQQLGG----------GIVrtiAMGSSDGLRRGLEVKDLEH 74
Cdd:CHL00059 2 VKIvnTGTVLQV---GDGIARIYGLDEVMAGE---LVEFEDGTIGialnlesnnvGVV---LMGDGLMIQEGSSVKATGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 75 PIEVPVGKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLETGIKVIDLMCPFAKGGKVGLFGGAGV 154
Cdd:CHL00059 73 IAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 155 GKTVNMMELIRNIAIEhSGYSVFAGVGERTREGNDFYHEMTDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE 234
Cdd:CHL00059 153 GKTAVATDTILNQKGQ-NVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 235 GRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGY-------QPTLAEEMGVLQERITStktGSITSVQAVYVPADDLTDP 307
Cdd:CHL00059 232 GRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYpgdvfylHSRLLERAAKLSSQLGE---GSMTALPIVETQAGDVSAY 308
|
330 340 350
....*....|....*....|....*....|....*.
gi 578257540 308 SPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:CHL00059 309 IPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR 344
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
50-343 |
6.70e-13 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 70.45 E-value: 6.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 50 GIVRTIAMGSSDGLRRGLEVKDLEHPIEVPVGKATLGRIMNVLGQPIDMkGDIGEEERW--------AIHRAAPSYEELS 121
Cdd:PTZ00185 89 GRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPV-GLLTRSRALleseqtlgKVDAGAPNIVSRS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 122 SSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKT-------VNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEM 194
Cdd:PTZ00185 168 PVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsiavstiINQVRINQQILSKNAVISIYVSIGQRCSNVARIHRLL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 195 TDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAE 274
Cdd:PTZ00185 248 RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFY 327
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578257540 275 EMGVLQERITSTKT----GSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:PTZ00185 328 LHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR 400
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
62-354 |
9.76e-08 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 53.94 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 62 GLRRGLEVKDLEHPIEvpvGKATLGRIMNVLGQPidmkgdigeEERWAihrAAPSYEELSS---SQEL-LETG-----IK 132
Cdd:PRK12608 58 NLRTGDVVEGVARPRE---RYRVLVRVDSVNGTD---------PEKLA---RRPHFDDLTPlhpRERLrLETGsddlsMR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 133 VIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAG-VGERTREGNDFYHEMTdsnvldkvSLVYGQMN 211
Cdd:PRK12608 123 VVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSVK--------GEVYASTF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 212 -EPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLA--------------GTEVSALLGrmPSAVGYQPTLAEEM 276
Cdd:PRK12608 195 dRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAynnevessgrtlsgGVDARALQR--PKRLFGAARNIEEG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 277 GVLQerITST---KTGSitsvqavyvPADDLtdpspatTFAHLDAT----VVLSRQIASLGIYPAVDPLDSTSRQLDPLV 349
Cdd:PRK12608 273 GSLT--IIATalvDTGS---------RMDEV-------IFEEFKGTgnmeIVLDRELADKRVFPAIDIAKSGTRREELLL 334
|
....*
gi 578257540 350 VGQEH 354
Cdd:PRK12608 335 DSKEL 339
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
132-382 |
1.59e-05 |
|
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: 46.99 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 132 KVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSG-YSVFAGVGERTREgndfyheMTDSNVLDKVSLVYGQM 210
Cdd:TIGR00767 157 RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEvELIVLLIDERPEE-------VTDMQRSVKGEVVASTF 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 211 NEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAvGYQPTL-------------AEEMG 277
Cdd:TIGR00767 230 DEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLSG-GVDANAlhrpkrffgaarnIEEGG 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 278 VLQerITST---KTGSitsvqavyvPADDLtdpspatTFAHLDAT----VVLSRQIASLGIYPAVDPLDSTSRQlDPLVV 350
Cdd:TIGR00767 309 SLT--IIATaliDTGS---------RMDEV-------IFEEFKGTgnmeLHLDRKLADRRIFPAIDIKKSGTRK-EELLL 369
|
250 260 270
....*....|....*....|....*....|..
gi 578257540 351 GQEHydtargvqslLQRYQELKDIIAilGMDE 382
Cdd:TIGR00767 370 TPEE----------LQKIWVLRKIIS--PMDS 389
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
132-366 |
2.12e-04 |
|
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: 42.96 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 132 KVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAG-VGERTREGNDFyHEMTDSNVldkvslVYGQM 210
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTDM-RRSVKGEV------VASTF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 211 NEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAvGYQPTLA-------------EEMG 277
Cdd:cd01128 78 DEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-GVDANALhkpkrffgaarniEEGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 278 VLQerITST---KTGSitsvqavyvPADDLtdpspatTFAHLDAT----VVLSRQIASLGIYPAVDPLDSTSRQlDPLVV 350
Cdd:cd01128 157 SLT--IIATalvDTGS---------RMDEV-------IFEEFKGTgnmeLVLDRKLAEKRIFPAIDILKSGTRK-EELLL 217
|
250
....*....|....*.
gi 578257540 351 GQEHYDTARGVQSLLQ 366
Cdd:cd01128 218 TPEELQKIWLLRRILS 233
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
81-194 |
5.61e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 42.70 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 81 GKATLGRIMNVLGQPIDMKGDIGEEERWAIHRAAPSYEELSSSQELLeTGIKVIDLMCPFAKGGKVGLFGGAGVGKTVNM 160
Cdd:PRK14698 166 GEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLI-TGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDG 244
|
90 100 110
....*....|....*....|....*....|....*....
gi 578257540 161 MELIRN-----IAIEHSgYSVFAGVGERTREGNDFYHEM 194
Cdd:PRK14698 245 DTLILTkefglIKIKDL-YEILDGKGKKTVEGNEEWTEL 282
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
3-71 |
6.58e-04 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 38.06 E-value: 6.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578257540 3 TGKIVQVIGAVVDVEFPQDavPRVYDALEVQNGNESLVLEVQQQ---LGGGIVRTIAMGSSDGLRRGLEVKD 71
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGE--VAIGEVCEIERGDGNNETVLKAEvigFRGDRAILQLFESTRGLSRGALVEP 70
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
142-262 |
1.04e-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: 39.66 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578257540 142 KGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGvgertregndfyhEMTDSNVLDKVSLVYGQMNEPPGNRLRVA 221
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------EDILEEVLDQLLLIIVGGKKASGSGELRL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 578257540 222 LTGLTMAEKFRDEgrdvLLFVDNIYRYTLAGTEVSALLGRM 262
Cdd:smart00382 68 RLALALARKLKPD----VLILDEITSLLDAEQEALLLLLEE 104
|
|
| ATP-synt_V_A-type_alpha_C |
cd18111 |
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of ... |
363-393 |
2.84e-03 |
|
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of the V1/A1 complex of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349746 [Multi-domain] Cd Length: 105 Bit Score: 37.37 E-value: 2.84e-03
10 20 30
....*....|....*....|....*....|...
gi 578257540 363 SLLQRYQELKDIIAILGMDELSEEDKLV--VAR 393
Cdd:cd18111 10 EILQEEAELQEIVQLVGPDALPEEDRLTleVAR 42
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
350-404 |
3.18e-03 |
|
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family of ATPases that form part of the Type III secretion system (T3SS) present in Escherichia coli. T3SS is a macromolecular complex that creates a syringe-like apparatus extending from the bacterial cytosol across three membranes to the eukaryotic cytosol. This process is essential for pathogenicity. EscN is a functionally unique ATPase that provides an inner-membrane recognition gate for the T3SS chaperone-virulence effector complexes as well as a potential source of energy for their subsequent secretion.The C-terminal domain of T3SS ATPases mediates binding with multiple contact points along the chaperone.
Pssm-ID: 465691 [Multi-domain] Cd Length: 70 Bit Score: 36.26 E-value: 3.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 578257540 350 VGQEHYDTARGVQSLLQRYQELKDIIAI----LGMDelSEEDKlVVARARKIQRFLSQP 404
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIgayqAGSD--PEIDE-AIAKRPAINAFLRQG 56
|
|
| ATP-synt_V_A-type_beta_C |
cd18112 |
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 ... |
369-403 |
4.98e-03 |
|
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349747 [Multi-domain] Cd Length: 95 Bit Score: 36.26 E-value: 4.98e-03
10 20 30
....*....|....*....|....*....|....*.
gi 578257540 369 QELKDIIAILGMDELSEEDKLVVARARKI-QRFLSQ 403
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFeREFINQ 57
|
|
| |
