|
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 16131600 1 MATGKIVQVIGAVVDVEFPQDAVPRVYDALEVQN-GNERLVLEVQQQLGGGIVRTIAMGSSDGLRRGLDVKDLEHPIEVP 79
Cdd:COG0055 3 MNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENeGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 80 VGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVN 159
Cdd:COG0055 83 VGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 160 MMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD-EGRDV 238
Cdd:COG0055 163 IMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 239 LLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDA 318
Cdd:COG0055 243 LLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 319 TVVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQEHYDTARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQ 398
Cdd:COG0055 323 TTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKIQ 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131600 399 RFLSQPFFVAEVFTGSPGKYVSLKDTIRGFKGIMEGEYDHLPEQAFYMVGSIEEAVEKAKKL 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: 930.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 2 ATGKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNE-RLVLEVQQQLGGGIVRTIAMGSSDGLRRGLDVKDLEHPIEVPV 80
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNRAEsELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 81 GKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVNM 160
Cdd:TIGR01039 81 GKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 161 MELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE-GRDVL 239
Cdd:TIGR01039 161 QELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 240 LFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDAT 319
Cdd:TIGR01039 241 LFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 320 VVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQEHYDTARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQR 399
Cdd:TIGR01039 321 TVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQR 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131600 400 FLSQPFFVAEVFTGSPGKYVSLKDTIRGFKGIMEGEYDHLPEQAFYMVGSIEEAVEKAKKL 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: 808.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 3 TGKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNE-----RLVLEVQQQLGGGIVRTIAMGSSDGLRRGLDVKDLEHPIE 77
Cdd:CHL00060 16 LGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTagqeiNVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 78 VPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKT 157
Cdd:CHL00060 96 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 158 VNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVID-------KVSLVYGQMNEPPGNRLRVALTGLTMAEK 230
Cdd:CHL00060 176 VLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 231 FRDEGR-DVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSP 309
Cdd:CHL00060 256 FRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 310 ATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLVVGQEHYDTARGVQSILQRYQELKDIIAILGMDELSEEDKL 389
Cdd:CHL00060 336 ATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRL 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131600 390 VVARARKIQRFLSQPFFVAEVFTGSPGKYVSLKDTIRGFKGIMEGEYDHLPEQAFYMVGSIEEAVEKAKKL 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: 566.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 77 EVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 156
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 157 TVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVI-----DKVSLVYGQMNEPPGNRLRVALTGLTMAEKF 231
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVInldglSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 232 RD-EGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPA 310
Cdd:cd01133 161 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPA 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 16131600 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: 559.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 4 GKIVQVIGAVVDVEFPQDaVPRVYDALEVQNGNErLVLEVQQQLGGGIVRTIAMGSSDGLRRGLDVKDLEHPIEVPVGKA 83
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGE-LPAIHSVLRAGREGE-VVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 84 TLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMEL 163
Cdd:TIGR03305 79 TLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 164 IRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD-EGRDVLLFV 242
Cdd:TIGR03305 159 IHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDdEKQDVLLLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 243 DNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVL 322
Cdd:TIGR03305 239 DNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSASLVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 323 SRQIASLGIYPAVDPLDSTSRQLDPLVVGQEHYDTARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQRFLS 402
Cdd:TIGR03305 319 SRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLERFLT 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 16131600 403 QPFFVAEVFTGSPGKYVSLKDTIRGFKGIMEGEYDHLPEQAFYMVGSIEEA 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 |
5.09e-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: 5.09e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 78 VPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKT 157
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 158 VNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRD 237
Cdd:cd19476 82 VLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 238 VLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT--GSITSVQAVYVPADDLTDPSPATTFAH 315
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDggGSITAIPAVSTPGDDLTDPIPDNTFAI 241
|
250 260
....*....|....*....|....*...
gi 16131600 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 |
5.23e-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: 282.71 E-value: 5.23e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 130 GIKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAiehSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQ 209
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQAS---ADVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 210 MNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITST--K 287
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVkgK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131600 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 |
7.43e-80 |
|
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: 242.77 E-value: 7.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 349 VVGQEHYDTARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQRFLSQPFFVAEVFTGSPGKYVSLKDTIRGF 428
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 16131600 429 KGIMEGEYDHLPEQAFYMVGSIEEAVEK 456
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
3-432 |
9.85e-68 |
|
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: 222.60 E-value: 9.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 3 TGKIVQVIGAVVDVEFPQdavPRVYDALEVQNGNERLVL-EVqqqLG--GGIVRTIAMGSSDGLRRGLDVKDLEHPIEVP 79
Cdd:COG1157 20 SGRVTRVVGLLIEAVGPD---ASIGELCEIETADGRPVLaEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRPLSVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 80 VGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVN 159
Cdd:COG1157 94 VGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 160 MMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVL 239
Cdd:COG1157 174 LGMIARNTEAD---VNVIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 240 LFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDAT 319
Cdd:COG1157 251 LLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILDGH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 320 VVLSRQIASLGIYPAVDPLDSTSRqLDPLVVGQEHYDTARGVQSILQRYQELKDIIAI----LGMDELSEEdklVVARAR 395
Cdd:COG1157 331 IVLSRKLAERGHYPAIDVLASISR-VMPDIVSPEHRALARRLRRLLARYEENEDLIRIgayqPGSDPELDE---AIALIP 406
|
410 420 430
....*....|....*....|....*....|....*..
gi 16131600 396 KIQRFLSQpffvaevftgSPGKYVSLKDTIRGFKGIM 432
Cdd:COG1157 407 AIEAFLRQ----------GMDERVSFEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
77-343 |
3.81e-60 |
|
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: 197.40 E-value: 3.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 77 EVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 156
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 157 TVNMMELIRNIAiehSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGR 236
Cdd:cd01136 81 STLLGMIARNTD---ADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 237 DVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHL 316
Cdd:cd01136 158 KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSIL 237
|
250 260
....*....|....*....|....*..
gi 16131600 317 DATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:cd01136 238 DGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
57-405 |
5.01e-52 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 180.96 E-value: 5.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 57 MGSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPV---DMKGEIGEEERW-AIHRAAPSYEELSNSQELLETGIK 132
Cdd:PRK08149 61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVerfDAPPTVGPISEErVIDVAPPSYAERRPIREPLITGVR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 133 VID--LMCpfAKGGKVGLFGGAGVGKTVNMmelirNIAIEHSGYSVF--AGVGERTREGNDFYHEMTDSNVIDKVSLVYG 208
Cdd:PRK08149 141 AIDglLTC--GVGQRMGIFASAGCGKTSLM-----NMLIEHSEADVFviGLIGERGREVTEFVESLRASSRREKCVLVYA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 209 QMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT 288
Cdd:PRK08149 214 TSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 289 GSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPlVVGQEHYDTARGVQSILQRY 368
Cdd:PRK08149 294 GSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQ-VTDPKHRQLAAAFRKLLTRL 372
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 16131600 369 QELKDIIAiLG---MDELSEEDKLVVARArKIQRFLSQPF 405
Cdd:PRK08149 373 EELQLFID-LGeyrRGENADNDRAMDKRP-ALEAFLKQDV 410
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
59-403 |
5.55e-52 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 181.17 E-value: 5.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 59 SSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERwAIHRAAPSYEELSNSQELLETGIKVIDLMC 138
Cdd:PRK06820 80 SSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWR-ELDCPPPSPLTRQPIEQMLTTGIRAIDGIL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 139 PFAKGGKVGLFGGAGVGKTVnmmeLIRNIAiEHSGYSV--FAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGN 216
Cdd:PRK06820 159 SCGEGQRIGIFAAAGVGKST----LLGMLC-ADSAADVmvLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 217 RLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQA 296
Cdd:PRK06820 234 RLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 297 VYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDTARGVQSILQRYQELKDIIA 376
Cdd:PRK06820 314 VLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIELLVR 392
|
330 340 350
....*....|....*....|....*....|.
gi 16131600 377 I----LGMDELSEEdklVVARARKIQRFLSQ 403
Cdd:PRK06820 393 VgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
61-433 |
1.66e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 177.18 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 61 DGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPF 140
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTC 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 141 AKGGKVGLFGGAGVGKTVNMMELIRNiaiEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVsLVYGQMNEPPGNRLRV 220
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKSTLMGMIVKG---CLAPIKVVALIGERGREIPEFIEKNLGGDLENTV-IVVATSDDSPLMRKYG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 221 ALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT-GSITSVQAVYV 299
Cdd:PRK08472 231 AFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGkGSITAFFTVLV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 300 PADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPlVVGQEHYDTARGVQSILQRYQELKDIIAI-- 377
Cdd:PRK08472 311 EGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMND-IISPEHKLAARKFKRLYSLLKENEVLIRIga 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131600 378 --LGMD-ELSEedklVVARARKIQRFLSQpffvaevftgSPGKYVSLKDTIRGFKGIME 433
Cdd:PRK08472 390 yqKGNDkELDE----AISKKEFMEQFLKQ----------NPNELFPFEQTFEQLEEILR 434
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
62-377 |
8.41e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 175.66 E-value: 8.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 62 GLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERwaIHRAAPSYEELSNSQ--ELLETGIKVIDLMCP 139
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQR--ASRHSPPINPLSRRPitEPLDVGVRAINAMLT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 140 FAKGGKVGLFGGAGVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLR 219
Cdd:PRK08972 159 VGKGQRMGLFAGSGVGKSVLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 220 VALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAV 297
Cdd:PRK08972 236 GCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAgnGGPGQGSITAFYTV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 298 YVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDTARGVQSILQRYQELKDIIAI 377
Cdd:PRK08972 316 LTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
4-377 |
1.78e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 172.09 E-value: 1.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 4 GKIVQVIGAVVDVEFPQDAVpRVYDALEVQNGNERLVL-EVqqqLGGGIVRTIAM--GSSDGLRRGLDVKDLEHPIEVPV 80
Cdd:PRK08927 19 GRVVAVRGLLVEVAGPIHAL-SVGARIVVETRGGRPVPcEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVRP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 81 GKATLGRIMNVLGEPVDMKGEIGE-EERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVN 159
Cdd:PRK08927 95 SRAWLGRVVNALGEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 160 MMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVL 239
Cdd:PRK08927 175 LSMLARNADAD---VSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 240 LFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAVYVPADDLTDPSPATTFAHLD 317
Cdd:PRK08927 252 CLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILD 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 318 ATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDTARGVQSILQRYQELKDIIAI 377
Cdd:PRK08927 332 GHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
2-404 |
2.09e-48 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 171.87 E-value: 2.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 2 ATGKIVQVIGAVVDVEFPQDAVPRVydaLEVQNGNERLVlevQQQLGGGIVRTIAM----GSSDGLRRGLDVKDLEHPIE 77
Cdd:PRK09099 24 RTGKVVEVIGTLLRVSGLDVTLGEL---CELRQRDGTLL---QRAEVVGFSRDVALlspfGELGGLSRGTRVIGLGRPLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 78 VPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKT 157
Cdd:PRK09099 98 VPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 158 VNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRD 237
Cdd:PRK09099 178 TLMGMFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 238 VLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLD 317
Cdd:PRK09099 255 VLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGILD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 318 ATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDTARGVQSILQRYQELKDIIAI----LGMDELSEEdklVVAR 393
Cdd:PRK09099 335 GHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE---AIAK 410
|
410
....*....|.
gi 16131600 394 ARKIQRFLSQP 404
Cdd:PRK09099 411 IDAIRDFLSQR 421
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
4-403 |
2.08e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 166.47 E-value: 2.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 4 GKIVQVIGAVVdvefpQDAVP--RVYDALEVQNGNERLVL--EVQqqlggGIVRTIA----MGSSDGLRRGLDVKDLEHP 75
Cdd:PRK06936 25 GRVTQVTGTIL-----KAVVPgvRIGELCYLRNPDNSLSLqaEVI-----GFAQHQAlltpLGEMYGISSNTEVSPTGTM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 76 IEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVG 155
Cdd:PRK06936 95 HQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 156 KTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEG 235
Cdd:PRK06936 175 KSTLLASLIRSAEVD---VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 236 RDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAH 315
Cdd:PRK06936 252 KRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 316 LDATVVLSRQIASLGIYPAVDPLDSTSRQLDPlVVGQEHYDTARGVQSILQRYQELKDIIAI----LGMDELSEEdklVV 391
Cdd:PRK06936 332 LDGHIILSRKLAAANHYPAIDVLRSASRVMNQ-IVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKEADQ---AI 407
|
410
....*....|..
gi 16131600 392 ARARKIQRFLSQ 403
Cdd:PRK06936 408 ERIGAIRGFLRQ 419
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
86-379 |
3.76e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 165.94 E-value: 3.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 86 GRIMNVLGEPVDMKGEIGE-EERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELI 164
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 165 RNIAIEHSgysVFAGVGERTREGNDFYHEMTDSNvIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDN 244
Cdd:PRK06002 187 RADAFDTV---VIALVGERGREVREFLEDTLADN-LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDS 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 245 IYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVL 322
Cdd:PRK06002 263 VTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVL 342
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131600 323 SRQIASLGIYPAVDPLDSTSRqLDPLVVGQEHYDTARGVQSILQRYQELKDIIAILG 379
Cdd:PRK06002 343 DRAIAEQGRYPAVDPLASISR-LARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
2-403 |
7.51e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 162.59 E-value: 7.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 2 ATGKIVQVIGAVVDVEFPQDAVPRvydALEVQNGNERLVLEVQQQL---GGGIVRTIAMGSSDGLRRGLDVKDLEHPIEV 78
Cdd:PRK05688 27 VEGRLLRMVGLTLEAEGLRAAVGS---RCLVINDDSYHPVQVEAEVmgfSGDKVFLMPVGSVAGIAPGARVVPLADTGRL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 79 PVGKATLGRIMNVLGEPVDMKGEIGEEERwaIHRAAPSYEELSNS--QELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 156
Cdd:PRK05688 104 PMGMSMLGRVLDGAGRALDGKGPMKAEDW--VPMDGPTINPLNRHpiSEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 157 TV--NMMELIRNIAIehsgySVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE 234
Cdd:PRK05688 182 SVllGMMTRFTEADI-----IVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 235 GRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT--GSITSVQAVYVPADDLTDPSPATT 312
Cdd:PRK05688 257 GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPggGSITAFYTVLSEGDDQQDPIADSA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 313 FAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDTARGVQSILQRYQELKDIIAI----LGMDelsEEDK 388
Cdd:PRK05688 337 RGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLISVgayvAGGD---PETD 412
|
410
....*....|....*
gi 16131600 389 LVVARARKIQRFLSQ 403
Cdd:PRK05688 413 LAIARFPHLVQFLRQ 427
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
62-403 |
1.24e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 161.60 E-value: 1.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 62 GLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFA 141
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 142 KGGKVGLFGGAGVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVA 221
Cdd:PRK07196 154 KGQRVGLMAGSGVGKSVLLGMITRYTQAD---VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKAT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 222 LTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT-------LAEEMGvlqeriTSTKTGSITSV 294
Cdd:PRK07196 231 ELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSafsiiprLAESAG------NSSGNGTMTAI 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 295 QAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPlVVGQEHYDTARGVQSILQRYQELKDI 374
Cdd:PRK07196 305 YTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQ-VIGSQQAKAASLLKQCYADYMAIKPL 383
|
330 340 350
....*....|....*....|....*....|...
gi 16131600 375 IA----ILGMDELSEEdklVVARARKIQRFLSQ 403
Cdd:PRK07196 384 IPlggyVAGADPMADQ---AVHYYPAITQFLRQ 413
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
4-377 |
1.31e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 161.43 E-value: 1.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 4 GKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNERLVLEVQQQLGGGI-------VRTIAMGSSdglrrgldVKDLEHPI 76
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESSIGDVCYIHTKGGGDKAIKAEVVGFKDEHVllmpyteVAEIAPGCL--------VEATGKPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 77 EVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGK 156
Cdd:PRK07721 92 EVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 157 TVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGR 236
Cdd:PRK07721 172 STLMGMIARNTSAD---LNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 237 DVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHL 316
Cdd:PRK07721 249 NVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGIL 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131600 317 DATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDTARGVQSILQRYQELKDIIAI 377
Cdd:PRK07721 329 DGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
58-377 |
1.73e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 158.58 E-value: 1.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 58 GSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDmkGEIGEEERWAIHRAAPSYEELSN--SQELLeTGIKVID 135
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLD--GRELPDVCWKDYDAMPPPAMVRQpiTQPLM-TGIRAID 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 136 LMCPFAKGGKVGLFGGAGVGKTVNMMELIrniAIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPG 215
Cdd:PRK07594 148 SVATCGEGQRVGIFSAPGVGKSTLLAMLC---NAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPAL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 216 NRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQ 295
Cdd:PRK07594 225 ERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFY 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 296 AVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLdPLVVGQEHYDTARGVQSILQRYQELKDII 375
Cdd:PRK07594 305 TVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVELLI 383
|
..
gi 16131600 376 AI 377
Cdd:PRK07594 384 RI 385
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
76-403 |
2.99e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 157.83 E-value: 2.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 76 IEVPVGKATLGRIMNVLGEPVDMKGEIGEEERwaIHRAAPSYEELSNSQ--ELLETGIKVIDLMCPFAKGGKVGLFGGAG 153
Cdd:PRK06793 89 VVIPRGNHLLGKVLSANGEVLNEEAENIPLQK--IKLDAPPIHAFEREEitDVFETGIKSIDSMLTIGIGQKIGIFAGSG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 154 VGKTVNMMELIRNiaiEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD 233
Cdd:PRK06793 167 VGKSTLLGMIAKN---AKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRD 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 234 EGRDVLLFVDNIYRYTLAGTEVSALLGRMPsaVGYQPTLAEE-MGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATT 312
Cdd:PRK06793 244 QGNNVLLMMDSVTRFADARRSVDIAVKELP--IGGKTLLMESyMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 313 FAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPlVVGQEHYDTARGVQSILQRYQElKDIIAILGMDELSEEDKLVVA 392
Cdd:PRK06793 322 RGILDGHIVLKRELATLSHYPAISVLDSVSRIMEE-IVSPNHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAYIFE 399
|
330
....*....|....
gi 16131600 393 RARK---IQRFLSQ 403
Cdd:PRK06793 400 CKNKvegINTFLKQ 413
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
77-377 |
1.14e-35 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 137.22 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 77 EVPVGKATLGRIMNVLGEPVDmkGEIGEEERWAIHRAAPSYEELSNS--QELLETGIKVIDLMCPFAKGGKVGLFGGAGV 154
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLD--GLPAPDTGETGALITPPFNPLQRTpiEHVLDTGVRAINALLTVGRGQRMGLFAGSGV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 155 GKTVNMMELIRniaIEHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE 234
Cdd:PRK07960 187 GKSVLLGMMAR---YTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDR 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 235 GRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITS--TKTGSITSVQAVYVPADDLTDPSPATT 312
Cdd:PRK07960 264 GQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSA 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131600 313 FAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLvVGQEHYDTARGVQSILQRYQELKDIIAI 377
Cdd:PRK07960 344 RAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAL-IDEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
5-405 |
3.09e-35 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 136.11 E-value: 3.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 5 KIVQVIGAVVDVEfpqdAVPRV-YDAL---EVQNGNERL--VLEVQqqlgGGIVRTIAMGSSDGL-RRGLDVKDLEHPIE 77
Cdd:PRK04196 6 TVSEIKGPLLFVE----GVEGVaYGEIveiELPNGEKRRgqVLEVS----EDKAVVQVFEGTTGLdLKDTKVRFTGEPLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 78 VPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAA--PSYEELsnSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVG 155
Cdd:PRK04196 78 LPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVAREY--PEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 156 KTVNMMELIRNIAIEHSGYS---VFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRL---RVAltgLTMAE 229
Cdd:PRK04196 156 HNELAAQIARQAKVLGEEENfavVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERIltpRMA---LTAAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 230 --KFrDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQER--ITSTKTGSITSVQAVYVPADDLT 305
Cdd:PRK04196 233 ylAF-EKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 306 DPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDpLVVG-----QEHYDTARGVQSILQRYQELKDIIAILGM 380
Cdd:PRK04196 312 HPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMK-DGIGegktrEDHKDVANQLYAAYARGKDLRELAAIVGE 390
|
410 420
....*....|....*....|....*.
gi 16131600 381 DELSEEDKLVVARARKI-QRFLSQPF 405
Cdd:PRK04196 391 EALSERDRKYLKFADAFeREFVNQGF 416
|
|
| 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 |
2.69e-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: 123.01 E-value: 2.69e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131600 2 ATGKIVQVIGAVVDVEFPQDAVPRVYDALEVQNGNE-RLVLEVQQQLGGGIVRTIAMGSSDGLRRGLDVKDLEHPI 76
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDDGkKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
66-435 |
9.15e-33 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 128.87 E-value: 9.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 66 GLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGK 145
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 146 VGLFGGAGVGKTvnmmELIRNIAI-EHSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTG 224
Cdd:PRK05922 160 IGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 225 LTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAV-YVP--A 301
Cdd:PRK05922 236 MTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnhP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 302 DDLTDPSPATtfahLDATVVLSRQIASLGiYPAVDPLDSTSRQLDPLVVgQEHYDTARGVQSILQRYQELKDIIAiLGMD 381
Cdd:PRK05922 316 DIFTDYLKSL----LDGHFFLTPQGKALA-SPPIDILTSLSRSARQLAL-PHHYAAAEELRSLLKAYHEALDIIQ-LGAY 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131600 382 ELSEEDKL--VVARARKIQRFLSQPFfvaevftgspGKYVSLKDTIRGFKGIMEGE 435
Cdd:PRK05922 389 VPGQDAHLdrAVKLLPSIKQFLSQPL----------SSYCALHNTLKQLEALLKHE 434
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
75-343 |
2.25e-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: 124.26 E-value: 2.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 75 PIEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIH--------RAAPsyeelsnsQELLETGIKVIDLMCPFAKGGKV 146
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINgppinpvaRIYP--------EEMIQTGISAIDVMNTLVRGQKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 147 GLFGGAGVGKTVNMMELIRNIAIEHSGYS---VFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALT 223
Cdd:cd01135 73 PIFSGSGLPHNELAAQIARQAGVVGSEENfaiVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 224 GLTMAEKFR-DEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQER--ITSTKTGSITSVQAVYVP 300
Cdd:cd01135 153 ALTTAEYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMP 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 16131600 301 ADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
1-433 |
3.19e-29 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 120.27 E-value: 3.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 1 MATGKIVQVIGAVVDVEFPQDAvpRVYDALEVqnGNERLVLEVQQ--------------------------------QLG 48
Cdd:PRK04192 2 MTKGKIVRVSGPLVVAEGMGGA--RMYEVVRV--GEEGLIGEIIRiegdkatiqvyeetsgikpgepveftgeplsvELG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 49 GGIVRTIAMG-----------SSDGLRRGLDVKDL---------------------------------EHPIEVPVGKAt 84
Cdd:PRK04192 78 PGLLGSIFDGiqrpldelaekSGDFLERGVYVPALdrekkweftptvkvgdkveagdilgtvqetpsiEHKIMVPPGVS- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 85 lGRIMNVLGE---PVD-----MKGEIGEEE------RWAIHRAAPSYEELsNSQELLETGIKVIDLMCPFAKGGKVGLFG 150
Cdd:PRK04192 157 -GTVKEIVSEgdyTVDdtiavLEDEDGEGVeltmmqKWPVRRPRPYKEKL-PPVEPLITGQRVIDTFFPVAKGGTAAIPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 151 GAGVGKTVnmmeLIRNIAiehsGYS-----VFAGVGERtreGNdfyhEMTDsnVIdkvslvygqmNEPP-------GNRL 218
Cdd:PRK04192 235 PFGSGKTV----TQHQLA----KWAdadivIYVGCGER---GN----EMTE--VL----------EEFPelidpktGRPL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 219 --R-----------VA------LTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLA------ 273
Cdd:PRK04192 288 meRtvliantsnmpVAareasiYTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLAsrlaef 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 274 -EEMGVLqeRITSTKTGSITSVQAVYVPADDLTDP-SPAT-----TFAHLDATVVLSRQiaslgiYPAVDPLDSTSRQLD 346
Cdd:PRK04192 368 yERAGRV--KTLGGEEGSVTIIGAVSPPGGDFSEPvTQNTlrivkVFWALDAELADRRH------FPAINWLTSYSLYLD 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 347 PL------VVGQEHYDTARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKI-QRFLSQPFFvAEVFTgspgkYV 419
Cdd:PRK04192 440 QVapwweeNVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQNAF-DPVDT-----YC 513
|
570
....*....|....
gi 16131600 420 SLKDTIRGFKGIME 433
Cdd:PRK04192 514 PPEKQYEMLKLILT 527
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
7-343 |
1.90e-28 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 117.32 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 7 VQVIGAVVDVefpQDAVPRVY--------DALEVQNGNERLVLEVQQQLGGGIVrtiaMGSSDGLRRGLDVKDLEHPIEV 78
Cdd:PRK13343 25 AREIGRVESV---GDGIAFVSglpdaaldELLRFEGGSRGFAFNLEEELVGAVL----LDDTADILAGTEVRRTGRVLEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 79 PVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTV 158
Cdd:PRK13343 98 PVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 159 NMMELIrnIAIEHSG-YSVFAGVGERTRegndfyhemTDSNVIDKV---------SLVYGQMNEPPGNRLRVALTGLTMA 228
Cdd:PRK13343 178 IAIDAI--INQKDSDvICVYVAIGQKAS---------AVARVIETLrehgaleytTVVVAEASDPPGLQYLAPFAGCAIA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 229 EKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERIT----STKTGSITSVQAVYVPADDL 304
Cdd:PRK13343 247 EYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAklspELGGGSLTALPIIETLAGEL 326
|
330 340 350
....*....|....*....|....*....|....*....
gi 16131600 305 TDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:PRK13343 327 SAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
46-343 |
3.19e-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: 110.36 E-value: 3.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 46 QLGGGIVRTIAmgssDGLRRGLDVKDLEHPIEVPVGKATlgrimnvlgepvdmkgeigeeERWAIHRAAPSYEELSnSQE 125
Cdd:cd01134 5 ELGPGLLGSIF----DGIQRPLEVIAETGSIFIPRGVNV---------------------QRWPVRQPRPVKEKLP-PNV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 126 LLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVnmmelirniaIEH--SGYS-----VFAGVGER----TREGNDFYH-- 192
Cdd:cd01134 59 PLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTV----------ISQslSKWSnsdvvIYVGCGERgnemAEVLEEFPElk 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 193 -EMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT 271
Cdd:cd01134 129 dPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAY 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131600 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 |
1.58e-23 |
|
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: 99.56 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 76 IEVPVGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVG 155
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 156 KTVNMMELIrniaIEHSG---YSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFR 232
Cdd:cd01132 82 KTAIAIDTI----INQKGkkvYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 233 DEGRDVLLFVDNIYRYTLAGTEVSALLGR------MPSAVGY-QPTLAEEMGVLQERItstKTGSITSVQAVYVPADDLT 305
Cdd:cd01132 158 DNGKHALIIYDDLSKQAVAYRQMSLLLRRppgreaYPGDVFYlHSRLLERAAKLSDEL---GGGSLTALPIIETQAGDVS 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 16131600 306 DPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:cd01132 235 AYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
159-415 |
5.60e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 93.16 E-value: 5.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 159 NMMELIRNIAIEH-------SGYSVFAGVGERTREGNDFYHEM-------TDSNVIDKVSLVYGQMNEPPGNRLRVALTG 224
Cdd:PRK14698 662 NMPTLLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEFpklkdpkTGKPLMERTVLIANTSNMPVAAREASIYTG 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 225 LTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI-------TSTKTGSITSVQAV 297
Cdd:PRK14698 742 ITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAV 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 298 YVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSRQLDPLV------VGQEHYDTARGVQSILQRYQEL 371
Cdd:PRK14698 822 SPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKdwwhknVDPEWKAMRDKAMELLQKEAEL 901
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 16131600 372 KDIIAILGMDELSEEDKLVVARARKIQR-FLSQPFFvAEVFTGSP 415
Cdd:PRK14698 902 QEIVRIVGPDALPERERAILLVARMLREdYLQQDAF-DEVDTYCP 945
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
354-422 |
7.33e-20 |
|
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: 83.26 E-value: 7.33e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131600 354 HYDTARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQRFLSQPFFVAEVFTGSPGKYVSLK 422
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIK 69
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
30-403 |
2.59e-19 |
|
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: 90.17 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 30 LEVQNGNERL--VLEVQqqlGGGIVRTIAMGSSdglrrGLDVKDLE-----HPIEVPVGKATLGRIMNVLGEPVDMKGEI 102
Cdd:TIGR01040 29 LTLPDGTVRSgqVLEVS---GNKAVVQVFEGTS-----GIDAKKTTceftgDILRTPVSEDMLGRVFNGSGKPIDKGPPV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 103 GEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAI-------EHSGYS 175
Cdd:TIGR01040 101 LAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvklptkdVHDGHE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 176 -----VFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE-GRDVLLFVDNIYRYT 249
Cdd:TIGR01040 181 dnfaiVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 250 LAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQIA 327
Cdd:TIGR01040 261 DALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLH 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 328 SLGIYPAVDPLDSTSRqLDPLVVGQ-----EHYDTARGVQSILQRYQELKDIIAILGMDELSEEDKLVVARARKIQR-FL 401
Cdd:TIGR01040 341 NRQIYPPINVLPSLSR-LMKSAIGEgmtrkDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFI 419
|
..
gi 16131600 402 SQ 403
Cdd:TIGR01040 420 AQ 421
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
5-352 |
3.52e-18 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 86.24 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 5 KIVQVIGAVVDVEfpqdAVPRVYDAL-EVQNGNERLVLEVQQqLGGGIVRTIAMGSSDGLRRGLDVKDLEHPIEVPVGKA 83
Cdd:PRK02118 7 KITDITGNVITVE----AEGVGYGELaTVERKDGSSLAQVIR-LDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 84 TLGRIMNVLGEPVDMKGEIGEEErwaIHRAAPSYEELSNSQ--ELLETGIKVIDLMCPFAKGGKVGLFGGAgvGKTVNmm 161
Cdd:PRK02118 82 LLGRRFNGSGKPIDGGPELEGEP---IEIGGPSVNPVKRIVprEMIRTGIPMIDVFNTLVESQKIPIFSVS--GEPYN-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 162 ELIRNIAIE-HSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFR-DEGRDVL 239
Cdd:PRK02118 155 ALLARIALQaEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 240 LFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTK-TGSITSVQAVYVPADDLTDPSPATTFAHLDA 318
Cdd:PRK02118 235 VLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEdGGSITIIAVTTMPGDDVTHPVPDNTGYITEG 314
|
330 340 350
....*....|....*....|....*....|....
gi 16131600 319 TVVLSRQiaslgiypAVDPLDSTSRqLDPLVVGQ 352
Cdd:PRK02118 315 QFYLRRG--------RIDPFGSLSR-LKQLVIGK 339
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
10-263 |
5.09e-18 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 86.27 E-value: 5.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 10 IGAVVDVefpQDAVPRVY---DA-----LEVQNGNERLVLEVQQQLGGGIVrtiaMGSSDGLRRGLDVKDLEHPIEVPVG 81
Cdd:PRK09281 28 VGTVISV---GDGIARVYgldNVmagelLEFPGGVYGIALNLEEDNVGAVI----LGDYEDIKEGDTVKRTGRILEVPVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 82 KATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVnmm 161
Cdd:PRK09281 101 EALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTA--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 162 elirnIAIE------HSG-YSVFAGVGERtregndfyhEMTDSNVIDKVSlVYGQM----------NEPPGNRLRVALTG 224
Cdd:PRK09281 178 -----IAIDtiinqkGKDvICIYVAIGQK---------ASTVAQVVRKLE-EHGAMeytivvaataSDPAPLQYLAPYAG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 16131600 225 LTMAEKFRDEGRDVLLFVDNI------YRytlagtEVSALLGRMP 263
Cdd:PRK09281 243 CAMGEYFMDNGKDALIVYDDLskqavaYR------QLSLLLRRPP 281
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-72 |
3.15e-16 |
|
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: 72.96 E-value: 3.15e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131600 6 IVQVIGAVVDVEFPQDAVPRVYDALEVQNGN-ERLVLEVQQQLGGGIVRTIAMGSSDGLRRGLDVKDL 72
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVEfGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRT 68
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
7-343 |
4.43e-13 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 70.76 E-value: 4.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 7 VQV--IGAVVDVefpQDAVPRVYDALEVQNGnERLVLE-----VQQQLGGGIVRTIAMGSSDGLRRGLDVKDLEHPIEVP 79
Cdd:CHL00059 2 VKIvnTGTVLQV---GDGIARIYGLDEVMAG-ELVEFEdgtigIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 80 VGKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKTVN 159
Cdd:CHL00059 78 VSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 160 MMELIRNIAIEhSGYSVFAGVGERTREGNDFYHEMTDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVL 239
Cdd:CHL00059 158 ATDTILNQKGQ-NVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 240 LFVDNIYRYTLAGTEVSALLGRMPSAVGY-------QPTLAEEMGVLQERITStktGSITSVQAVYVPADDLTDPSPATT 312
Cdd:CHL00059 237 IIYDDLSKQAQAYRQMSLLLRRPPGREAYpgdvfylHSRLLERAAKLSSQLGE---GSMTALPIVETQAGDVSAYIPTNV 313
|
330 340 350
....*....|....*....|....*....|.
gi 16131600 313 FAHLDATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:CHL00059 314 ISITDGQIFLSADLFNAGIRPAINVGISVSR 344
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
50-343 |
1.83e-12 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 69.30 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 50 GIVRTIAMGSSDGLRRGLDVKDLEHPIEVPVGKATLGRIMNVLGEPVDMkGEIGEEERW--------AIHRAAPSYEELS 121
Cdd:PTZ00185 89 GRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPV-GLLTRSRALleseqtlgKVDAGAPNIVSRS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 122 NSQELLETGIKVIDLMCPFAKGGKVGLFGGAGVGKT-------VNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEM 194
Cdd:PTZ00185 168 PVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsiavstiINQVRINQQILSKNAVISIYVSIGQRCSNVARIHRLL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 195 TDSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAE 274
Cdd:PTZ00185 248 RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFY 327
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131600 275 EMGVLQERITSTKT----GSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRQIASLGIYPAVDPLDSTSR 343
Cdd:PTZ00185 328 LHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR 400
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
62-354 |
1.13e-07 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 53.55 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 62 GLRRGLDVKDLEHPIEvpvGKATLGRIMNVLGEPvdmkgeigeEERWAihrAAPSYEELS--NSQE--LLETG-----IK 132
Cdd:PRK12608 58 NLRTGDVVEGVARPRE---RYRVLVRVDSVNGTD---------PEKLA---RRPHFDDLTplHPRErlRLETGsddlsMR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 133 VIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAG-VGERTREGNDFYHEMTdsnvidkvSLVYGQMN 211
Cdd:PRK12608 123 VVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSVK--------GEVYASTF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 212 -EPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLA--------------GTEVSALLGrmPSAVGYQPTLAEEM 276
Cdd:PRK12608 195 dRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAynnevessgrtlsgGVDARALQR--PKRLFGAARNIEEG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 277 GVLQerITST---KTGSitsvqavyvPADDLtdpspatTFAHLDAT----VVLSRQIASLGIYPAVDPLDSTSRQLDPLV 349
Cdd:PRK12608 273 GSLT--IIATalvDTGS---------RMDEV-------IFEEFKGTgnmeIVLDRELADKRVFPAIDIAKSGTRREELLL 334
|
....*
gi 16131600 350 VGQEH 354
Cdd:PRK12608 335 DSKEL 339
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
122-382 |
8.25e-06 |
|
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: 47.76 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 122 NSQELLETG-----IKVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSG-YSVFAGVGERTREgndfyheMT 195
Cdd:TIGR00767 142 NERLRLETStedlsTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEvELIVLLIDERPEE-------VT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 196 DSNVIDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAvGYQPTL--- 272
Cdd:TIGR00767 215 DMQRSVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLSG-GVDANAlhr 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 273 ----------AEEMGVLQerITST---KTGSitsvqavyvPADDLtdpspatTFAHLDAT----VVLSRQIASLGIYPAV 335
Cdd:TIGR00767 294 pkrffgaarnIEEGGSLT--IIATaliDTGS---------RMDEV-------IFEEFKGTgnmeLHLDRKLADRRIFPAI 355
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 16131600 336 DPLDSTSRQlDPLVVGQEHydtargvqsiLQRYQELKDIIAilGMDE 382
Cdd:TIGR00767 356 DIKKSGTRK-EELLLTPEE----------LQKIWVLRKIIS--PMDS 389
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
132-366 |
1.20e-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: 43.35 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 132 KVIDLMCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAG-VGERTREgndfyheMTDSNVIDKVSLVYGQM 210
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEE-------VTDMRRSVKGEVVASTF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 211 NEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAvGYQPTLA-------------EEMG 277
Cdd:cd01128 78 DEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-GVDANALhkpkrffgaarniEEGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 278 VLQerITST---KTGSitsvqavyvPADDLtdpspatTFAHLDAT----VVLSRQIASLGIYPAVDPLDSTSRQlDPLVV 350
Cdd:cd01128 157 SLT--IIATalvDTGS---------RMDEV-------IFEEFKGTgnmeLVLDRKLAEKRIFPAIDILKSGTRK-EELLL 217
|
250
....*....|....*.
gi 16131600 351 GQEHYDTARGVQSILQ 366
Cdd:cd01128 218 TPEELQKIWLLRRILS 233
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
81-194 |
2.63e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 43.47 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 81 GKATLGRIMNVLGEPVDMKGEIGEEERWAIHRAAPSYEELSNSQELLeTGIKVIDLMCPFAKGGKVGLFGGAGVGKTVNM 160
Cdd:PRK14698 166 GEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLI-TGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDG 244
|
90 100 110
....*....|....*....|....*....|....*....
gi 16131600 161 MELIRN-----IAIEHSgYSVFAGVGERTREGNDFYHEM 194
Cdd:PRK14698 245 DTLILTkefglIKIKDL-YEILDGKGKKTVEGNEEWTEL 282
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
142-262 |
1.24e-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: 39.28 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131600 142 KGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGvgertregndfyhEMTDSNVIDKVSLVYGQMNEPPGNRLRVA 221
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------EDILEEVLDQLLLIIVGGKKASGSGELRL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 16131600 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 |
1.48e-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: 38.14 E-value: 1.48e-03
10 20 30
....*....|....*....|....*....|...
gi 16131600 363 SILQRYQELKDIIAILGMDELSEEDKLV--VAR 393
Cdd:cd18111 10 EILQEEAELQEIVQLVGPDALPEEDRLTleVAR 42
|
|
| 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 16131600 369 QELKDIIAILGMDELSEEDKLVVARARKI-QRFLSQ 403
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFeREFINQ 57
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
350-404 |
6.78e-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: 35.10 E-value: 6.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131600 350 VGQEHYDTARGVQSILQRYQELKDIIAI----LGMDelSEEDKlVVARARKIQRFLSQP 404
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIgayqAGSD--PEIDE-AIAKRPAINAFLRQG 56
|
|
| 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 |
7.52e-03 |
|
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: 35.37 E-value: 7.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131600 3 TGKIVQVIGAVVDVEFPQDavPRVYDALEVQNGNERLVLEVQQQ---LGGGIVRTIAMGSSDGLRRGLDVKD 71
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGE--VAIGEVCEIERGDGNNETVLKAEvigFRGDRAILQLFESTRGLSRGALVEP 70
|
|
| |
