|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-457 |
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: 990.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 1 MATGKIVQIIGAVIDVEFPQDAVPKVYDALKVESG----LTLEVQQQLGGGVVRCIALGSSDGLKRGLKVENTNKAIEVP 76
Cdd:COG0055 3 MNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEgggeLVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 77 VGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKTVN 156
Cdd:COG0055 83 VGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 157 MMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD-EGRDV 235
Cdd:COG0055 163 IMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 236 LFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDS 315
Cdd:COG0055 243 LLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 316 TVVLSRNIASLGIYPAVDPLDSTSRQLDPLVVGEEHYNVARGVQGTLQRYKELKDIIAILGMDELSEDDKRLVARARKIE 395
Cdd:COG0055 323 TTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKIQ 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493291288 396 RFLSQPFHVAEVFNGVPGKFVPLKETIRGFKGILEGEYDHIPEQAFYMAGSIDEVVERAKQM 457
Cdd:COG0055 403 RFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKL 464
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
2-457 |
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: 903.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 2 ATGKIVQIIGAVIDVEFPQDAVPKVYDALKVESG----LTLEVQQQLGGGVVRCIALGSSDGLKRGLKVENTNKAIEVPV 77
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNRaeseLTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 78 GTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKTVNM 157
Cdd:TIGR01039 81 GKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 158 MELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDE-GRDVL 236
Cdd:TIGR01039 161 QELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 237 FFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDST 316
Cdd:TIGR01039 241 LFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 317 VVLSRNIASLGIYPAVDPLDSTSRQLDPLVVGEEHYNVARGVQGTLQRYKELKDIIAILGMDELSEDDKRLVARARKIER 396
Cdd:TIGR01039 321 TVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQR 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493291288 397 FLSQPFHVAEVFNGVPGKFVPLKETIRGFKGILEGEYDHIPEQAFYMAGSIDEVVERAKQM 457
Cdd:TIGR01039 401 FLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
3-457 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 789.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 3 TGKIVQIIGAVIDVEFPQDAVPKVYDALKVESG--------LTLEVQQQLGGGVVRCIALGSSDGLKRGLKVENTNKAIE 74
Cdd:CHL00060 16 LGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRdtagqeinVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 75 VPVGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKT 154
Cdd:CHL00060 96 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 155 VNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMKDSNVLD-------KVSLVYGQMNEPPGNRLRVALTGLTMAEK 227
Cdd:CHL00060 176 VLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 228 FRDEGR-DVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSP 306
Cdd:CHL00060 256 FRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 307 ATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRQLDPLVVGEEHYNVARGVQGTLQRYKELKDIIAILGMDELSEDDKR 386
Cdd:CHL00060 336 ATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRL 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493291288 387 LVARARKIERFLSQPFHVAEVFNGVPGKFVPLKETIRGFKGILEGEYDHIPEQAFYMAGSIDEVVERAKQM 457
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 ... |
74-344 |
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: 562.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 74 EVPVGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGK 153
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 154 TVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMKDSNV-----LDKVSLVYGQMNEPPGNRLRVALTGLTMAEKF 228
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVinldgLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 229 RD-EGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPA 307
Cdd:cd01133 161 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPA 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 493291288 308 TTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRQLDP 344
Cdd:cd01133 241 TTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
4-449 |
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: 555.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 4 GKIVQIIGAVIDVEFPQDaVPKVYDALKV--ESGLTLEVQQQLGGGVVRCIALGSSDGLKRGLKVENTNKAIEVPVGTKT 81
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGE-LPAIHSVLRAgrEGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 82 LGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKTVNMMELI 161
Cdd:TIGR03305 80 LSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 162 RNIAIEHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRD-EGRDVLFFVD 240
Cdd:TIGR03305 160 HNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDdEKQDVLLLID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 241 NIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDSTVVLS 320
Cdd:TIGR03305 240 NIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSASLVLS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 321 RNIASLGIYPAVDPLDSTSRQLDPLVVGEEHYNVARGVQGTLQRYKELKDIIAILGMDELSEDDKRLVARARKIERFLSQ 400
Cdd:TIGR03305 320 RKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLERFLTQ 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 493291288 401 PFHVAEVFNGVPGKFVPLKETIRGFKGILEGEYDHIPEQAFYMAGSIDE 449
Cdd:TIGR03305 400 PFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDE 448
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
75-340 |
4.41e-124 |
|
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: 361.77 E-value: 4.41e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 75 VPVGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKT 154
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 155 VNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRD 234
Cdd:cd19476 82 VLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 235 VLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT--GSITSVQAVYVPADDLTDPSPATTFAH 312
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDggGSITAIPAVSTPGDDLTDPIPDNTFAI 241
|
250 260
....*....|....*....|....*...
gi 493291288 313 LDSTVVLSRNIASLGIYPAVDPLDSTSR 340
Cdd:cd19476 242 LDGQIVLSRELARKGIYPAINVLDSTSR 269
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
127-339 |
1.35e-92 |
|
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: 278.86 E-value: 1.35e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 127 GIKVIDLVAPFAKGGKVGLFGGAGVGKTVNMMELIRNIAiehSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQ 206
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQAS---ADVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 207 MNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITST--K 284
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVkgK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493291288 285 TGSITSVQAVYVPADDLTDPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTS 339
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 ... |
346-453 |
1.48e-75 |
|
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: 231.60 E-value: 1.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 346 VVGEEHYNVARGVQGTLQRYKELKDIIAILGMDELSEDDKRLVARARKIERFLSQPFHVAEVFNGVPGKFVPLKETIRGF 425
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 493291288 426 KGILEGEYDHIPEQAFYMAGSIDEVVER 453
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
3-429 |
3.30e-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: 228.76 E-value: 3.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 3 TGKIVQIIGAVIDVEFPQdavPKVYDALKVESGLTLEVQQQ---LGGGVVRCIALGSSDGLKRGLKVENTNKAIEVPVGT 79
Cdd:COG1157 20 SGRVTRVVGLLIEAVGPD---ASIGELCEIETADGRPVLAEvvgFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 80 KTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKTVNMME 159
Cdd:COG1157 97 GLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 160 LIRNIA--IehsgySVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLF 237
Cdd:COG1157 177 IARNTEadV-----NVIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 238 FVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDSTV 317
Cdd:COG1157 252 LMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILDGHI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 318 VLSRNIASLGIYPAVDPLDSTSRqLDPLVVGEEHYNVARGVQGTLQRYKELKDIIAI----LGMDElsEDDkRLVARARK 393
Cdd:COG1157 332 VLSRKLAERGHYPAIDVLASISR-VMPDIVSPEHRALARRLRRLLARYEENEDLIRIgayqPGSDP--ELD-EAIALIPA 407
|
410 420 430
....*....|....*....|....*....|....*.
gi 493291288 394 IERFLSQPFHVAevfngvpgkfVPLKETIRGFKGIL 429
Cdd:COG1157 408 IEAFLRQGMDER----------VSFEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
74-340 |
2.01e-62 |
|
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: 203.18 E-value: 2.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 74 EVPVGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGK 153
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 154 TVNMMELIRNIAiehSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGR 233
Cdd:cd01136 81 STLLGMIARNTD---ADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 234 DVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHL 313
Cdd:cd01136 158 KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSIL 237
|
250 260
....*....|....*....|....*..
gi 493291288 314 DSTVVLSRNIASLGIYPAVDPLDSTSR 340
Cdd:cd01136 238 DGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
54-402 |
1.15e-54 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 187.89 E-value: 1.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 54 LGSSDGLKRGLKVENTNKAIEVPVGTKTLGRIMNVLGE------PIDEAGPIGEEErwTIHRAAPSYEEQANSTELLETG 127
Cdd:PRK08149 61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKiverfdAPPTVGPISEER--VIDVAPPSYAERRPIREPLITG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 128 IKVIDLVAPFAKGGKVGLFGGAGVGKTVNMmelirNIAIEHSGYSVF--AGVGERTREGNDFYHEMKDSNVLDKVSLVYG 205
Cdd:PRK08149 139 VRAIDGLLTCGVGQRMGIFASAGCGKTSLM-----NMLIEHSEADVFviGLIGERGREVTEFVESLRASSRREKCVLVYA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 206 QMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT 285
Cdd:PRK08149 214 TSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 286 GSITSVQAVYVPADDLTDPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRQLDPlVVGEEHYNVARGVQGTLQRY 365
Cdd:PRK08149 294 GSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQ-VTDPKHRQLAAAFRKLLTRL 372
|
330 340 350
....*....|....*....|....*....|....*....
gi 493291288 366 KELKDIIAiLGMDELSE--DDKRLVARARKIERFLSQPF 402
Cdd:PRK08149 373 EELQLFID-LGEYRRGEnaDNDRAMDKRPALEAFLKQDV 410
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
58-430 |
8.35e-53 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 183.35 E-value: 8.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 58 DGLKRGLKVENTNKAIEVPVGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPF 137
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTC 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 138 AKGGKVGLFGGAGVGKTVNMMELIRNiaiEHSGYSVFAGVGERTREGNDFYHEMKDSNvLDKVSLVYGQMNEPPGNRLRV 217
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKSTLMGMIVKG---CLAPIKVVALIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSPLMRKYG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 218 ALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT-GSITSVQAVYV 296
Cdd:PRK08472 231 AFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGkGSITAFFTVLV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 297 PADDLTDPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRQLDPlVVGEEHYNVARGVQGTLQRYKELKDIIAI-- 374
Cdd:PRK08472 311 EGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMND-IISPEHKLAARKFKRLYSLLKENEVLIRIga 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 493291288 375 --LGMD-ELSEddkrLVARARKIERFLSQPfhvaevfngvPGKFVPLKETIRGFKGILE 430
Cdd:PRK08472 390 yqKGNDkELDE----AISKKEFMEQFLKQN----------PNELFPFEQTFEQLEEILR 434
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
56-400 |
4.31e-49 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 173.46 E-value: 4.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 56 SSDGLKRGLKVENTNKAIEVPVGTKTLGRIMNVLGEPIDEAGPIGEEERwTIHRAAPSYEEQANSTELLETGIKVIDLVA 135
Cdd:PRK06820 80 SSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWR-ELDCPPPSPLTRQPIEQMLTTGIRAIDGIL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 136 PFAKGGKVGLFGGAGVGKTVnmmeLIRNIAiEHSGYSV--FAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGN 213
Cdd:PRK06820 159 SCGEGQRIGIFAAAGVGKST----LLGMLC-ADSAADVmvLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 214 RLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQA 293
Cdd:PRK06820 234 RLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 294 VYVPADDLTDPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRQLdPLVVGEEHYNVARGVQGTLQRYKELKDIIA 373
Cdd:PRK06820 314 VLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIELLVR 392
|
330 340 350
....*....|....*....|....*....|.
gi 493291288 374 I----LGMDeLSEDDKrlVARARKIERFLSQ 400
Cdd:PRK06820 393 VgeyqAGED-LQADEA--LQRYPAICAFLQQ 420
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
83-376 |
1.18e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 172.49 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 83 GRIMNVLGEPIDEAGPIGE-EERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKTVNMMELI 161
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 162 RNIAIEHSgysVFAGVGERTREGNDFYHEMKDSNvLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDN 241
Cdd:PRK06002 187 RADAFDTV---VIALVGERGREVREFLEDTLADN-LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDS 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 242 IYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDSTVVL 319
Cdd:PRK06002 263 VTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVL 342
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 493291288 320 SRNIASLGIYPAVDPLDSTSRQLDPLVVGEEHYNVARgVQGTLQRYKELKDIIAILG 376
Cdd:PRK06002 343 DRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSR-LKSMIARFEETRDLRLIGG 398
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
4-409 |
2.02e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 171.86 E-value: 2.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 4 GKIVQIIGAVIDVEFPQDAVPKVYDALKVESGLTL--EV---QQQlgggVVRCIALGSSDGLKRGLKVENTNKAIEVPVG 78
Cdd:PRK06936 25 GRVTQVTGTILKAVVPGVRIGELCYLRNPDNSLSLqaEVigfAQH----QALLTPLGEMYGISSNTEVSPTGTMHQVGVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 79 TKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKTVNMM 158
Cdd:PRK06936 101 EHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 159 ELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFF 238
Cdd:PRK06936 181 SLIRSAEVD---VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 239 VDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDSTVV 318
Cdd:PRK06936 258 MDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSILDGHII 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 319 LSRNIASLGIYPAVDPLDSTSRQLDPlVVGEEHYNVARGVQGTLQRYKELKDIIAI----LGMDELSEDdkrLVARARKI 394
Cdd:PRK06936 338 LSRKLAAANHYPAIDVLRSASRVMNQ-IVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKEADQ---AIERIGAI 413
|
410
....*....|....*
gi 493291288 395 ERFLSQPFHVAEVFN 409
Cdd:PRK06936 414 RGFLRQGTHELSHFN 428
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
59-374 |
4.49e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 171.04 E-value: 4.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 59 GLKRGLKVENTNKAIEVPVGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFA 138
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 139 KGGKVGLFGGAGVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVA 218
Cdd:PRK08972 161 KGQRMGLFAGSGVGKSVLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGC 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 219 LTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAVYV 296
Cdd:PRK08972 238 ETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAgnGGPGQGSITAFYTVLT 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493291288 297 PADDLTDPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRQLdPLVVGEEHYNVARGVQGTLQRYKELKDIIAI 374
Cdd:PRK08972 318 EGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
4-400 |
1.49e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 166.69 E-value: 1.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 4 GKIVQIIGAVIDVEFPQDAVpKVYDALKVESGLTLEVQQQL---GGGVVRCIALGSSDGLKRGLKVENTNKAIEVPVGTK 80
Cdd:PRK08927 19 GRVVAVRGLLVEVAGPIHAL-SVGARIVVETRGGRPVPCEVvgfRGDRALLMPFGPLEGVRRGCRAVIANAAAAVRPSRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 81 TLGRIMNVLGEPIDEAGPIGE-EERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKTVNMME 159
Cdd:PRK08927 98 WLGRVVNALGEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 160 LIRNIAIEhsgYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFV 239
Cdd:PRK08927 178 LARNADAD---VSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 240 DNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDSTV 317
Cdd:PRK08927 255 DSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 318 VLSRNIASLGIYPAVDPLDSTSRQLdPLVVGEEHYNVARGVQGTLQRYKELKDIIAI----LGMDelSEDDkRLVARARK 393
Cdd:PRK08927 335 VMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRLgayrAGSD--PEVD-EAIRLNPA 410
|
....*..
gi 493291288 394 IERFLSQ 400
Cdd:PRK08927 411 LEAFLRQ 417
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
4-374 |
2.61e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 163.35 E-value: 2.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 4 GKIVQIIGAVIDVEFPQDAVPKVYdALKVESGLTLEVQQQLGGGVVRCIALGSSDGLKR---GLKVENTNKAIEVPVGTK 80
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESSIGDVC-YIHTKGGGDKAIKAEVVGFKDEHVLLMPYTEVAEiapGCLVEATGKPLEVKVGSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 81 TLGRIMNVLGEPID-EAGPIGEEErWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKTVNMME 159
Cdd:PRK07721 99 LIGQVLDALGEPLDgSALPKGLAP-VSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 160 LIRNIAIEhsgYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFV 239
Cdd:PRK07721 178 IARNTSAD---LNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 240 DNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDSTVVL 319
Cdd:PRK07721 255 DSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVL 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 493291288 320 SRNIASLGIYPAVDPLDSTSRQLdPLVVGEEHYNVARGVQGTLQRYKELKDIIAI 374
Cdd:PRK07721 335 DRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
2-401 |
3.69e-45 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 163.02 E-value: 3.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 2 ATGKIVQIIGAVIDVEFPQDAVPKVYDaLKVESGLTLEVQQQLGggVVRCIAL----GSSDGLKRGLKVENTNKAIEVPV 77
Cdd:PRK09099 24 RTGKVVEVIGTLLRVSGLDVTLGELCE-LRQRDGTLLQRAEVVG--FSRDVALlspfGELGGLSRGTRVIGLGRPLSVPV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 78 GTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKTVNM 157
Cdd:PRK09099 101 GPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 158 MELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLF 237
Cdd:PRK09099 181 GMFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 238 FVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDSTV 317
Cdd:PRK09099 258 MMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 318 VLSRNIASLGIYPAVDPLDSTSRQLdPLVVGEEHYNVARGVQGTLQRYKELKDIIAI----LGMDELSEDdkrLVARARK 393
Cdd:PRK09099 338 ILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE---AIAKIDA 413
|
....*...
gi 493291288 394 IERFLSQP 401
Cdd:PRK09099 414 IRDFLSQR 421
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
59-400 |
2.06e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 160.83 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 59 GLKRGLKVENTNKAIEVPVGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFA 138
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 139 KGGKVGLFGGAGVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVA 218
Cdd:PRK07196 154 KGQRVGLMAGSGVGKSVLLGMITRYTQAD---VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKAT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 219 LTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPT-------LAEEMGvlqeriTSTKTGSITSV 291
Cdd:PRK07196 231 ELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSafsiiprLAESAG------NSSGNGTMTAI 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 292 QAVYVPADDLTDPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRQLDPlVVGEEHYNVARGVQGTLQRYKELKDI 371
Cdd:PRK07196 305 YTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQ-VIGSQQAKAASLLKQCYADYMAIKPL 383
|
330 340 350
....*....|....*....|....*....|...
gi 493291288 372 IA----ILGMDELSEddkRLVARARKIERFLSQ 400
Cdd:PRK07196 384 IPlggyVAGADPMAD---QAVHYYPAITQFLRQ 413
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
57-400 |
7.14e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 156.68 E-value: 7.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 57 SDGLKRGLKVENTNKAIEVPVGTKTLGRIMNVLGEPIDEagPIGEEERWTIHRAAPSYE--EQANSTELLETGIKVIDLV 134
Cdd:PRK06793 73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIHafEREEITDVFETGIKSIDSM 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 135 APFAKGGKVGLFGGAGVGKTVNMMELIRNiaiEHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNR 214
Cdd:PRK06793 151 LTIGIGQKIGIFAGSGVGKSTLLGMIAKN---AKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 215 LRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPsaVGYQPTLAEE-MGVLQERITSTKTGSITSVQA 293
Cdd:PRK06793 228 LRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP--IGGKTLLMESyMKKLLERSGKTQKGSITGIYT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 294 VYVPADDLTDPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRQLDPlVVGEEHYNVARGVQGTLQRYKElKDIIA 373
Cdd:PRK06793 306 VLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEE-IVSPNHWQLANEMRKILSIYKE-NELYF 383
|
330 340 350
....*....|....*....|....*....|
gi 493291288 374 ILGMDELSEDDKRLVARARKIE---RFLSQ 400
Cdd:PRK06793 384 KLGTIQENAENAYIFECKNKVEginTFLKQ 413
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
46-374 |
3.77e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 154.89 E-value: 3.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 46 GGVVRCIALGSSDGLKRGLKVENTNKAIEVPVGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLE 125
Cdd:PRK05688 74 GDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 126 TGIKVIDLVAPFAKGGKVGLFGGAGVGKTV--NMMELIRNIAIehsgySVFAGVGERTREGNDFYHEMKDSNVLDKVSLV 203
Cdd:PRK05688 154 VGIRSINGLLTVGRGQRLGLFAGTGVGKSVllGMMTRFTEADI-----IVVGLIGERGREVKEFIEHILGEEGLKRSVVV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 204 YGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITST 283
Cdd:PRK05688 229 ASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 284 KT--GSITSVQAVYVPADDLTDPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRQLdPLVVGEEHYNVARGVQGT 361
Cdd:PRK05688 309 EPggGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQL 387
|
330
....*....|...
gi 493291288 362 LQRYKELKDIIAI 374
Cdd:PRK05688 388 WSRYQQSRDLISV 400
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
55-374 |
5.21e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 154.34 E-value: 5.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 55 GSSDGLKRGLKVENTNKAIEVPVGTKTLGRIMNVLGEPIDeaGPIGEEERWTIHRAAPSYE-EQANSTELLETGIKVIDL 133
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLD--GRELPDVCWKDYDAMPPPAmVRQPITQPLMTGIRAIDS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 134 VAPFAKGGKVGLFGGAGVGKTVNMMELIrniAIEHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGN 213
Cdd:PRK07594 149 VATCGEGQRVGIFSAPGVGKSTLLAMLC---NAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 214 RLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQA 293
Cdd:PRK07594 226 RVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 294 VYVPADDLTDPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRQLdPLVVGEEHYNVARGVQGTLQRYKELKDIIA 373
Cdd:PRK07594 306 VLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVELLIR 384
|
.
gi 493291288 374 I 374
Cdd:PRK07594 385 I 385
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
62-400 |
1.59e-34 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 134.14 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 62 RGLKVENTNKAIEVPVGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGG 141
Cdd:PRK07960 97 RNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 142 KVGLFGGAGVGKTVNMMELIRniaIEHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTG 221
Cdd:PRK07960 177 RMGLFAGSGVGKSVLLGMMAR---YTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 222 LTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITS--TKTGSITSVQAVYVPAD 299
Cdd:PRK07960 254 TRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 300 DLTDPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRQLDPLvVGEEHYNVARGVQGTLQRYKELKDIIAI----L 375
Cdd:PRK07960 334 DQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAL-IDEQHYARVRQFKQLLSSFQRNRDLVSVgayaK 412
|
330 340
....*....|....*....|....*
gi 493291288 376 GMDELSEddkRLVARARKIERFLSQ 400
Cdd:PRK07960 413 GSDPMLD---KAIALWPQLEAFLQQ 434
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
54-403 |
4.16e-34 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 133.03 E-value: 4.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 54 LGSSDGLK-RGLKVENTNKAIEVPVGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAA--PSYEEQANstELLETGIKV 130
Cdd:PRK04196 56 FEGTTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVAREYPE--EFIQTGISA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 131 IDLVAPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYS---VFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQM 207
Cdd:PRK04196 134 IDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQAKVLGEEENfavVFAAMGITFEEANFFMEDFEETGALERSVVFLNLA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 208 NEPPGNRL---RVAltgLTMAE--KFrDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQER--I 280
Cdd:PRK04196 214 DDPAIERIltpRMA---LTAAEylAF-EKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 281 TSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRQLDpLVVG-----EEHYNVA 355
Cdd:PRK04196 290 IKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMK-DGIGegktrEDHKDVA 368
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 493291288 356 RGVQGTLQRYKELKDIIAILGMDELSEDDKRLVARARKIE-RFLSQPFH 403
Cdd:PRK04196 369 NQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFErEFVNQGFD 417
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
10-436 |
4.35e-33 |
|
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: 130.59 E-value: 4.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 10 IGAVIDVefpQDAVPKVYDALKVESGLTLE-------VQQQLGGGVVRCIALGSSDGLKRGLKVENTNKAIEVPVGTKTL 82
Cdd:TIGR00962 27 VGTVVSV---GDGIARVYGLENVMSGELIEfeggvqgIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 83 GRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKTVNMMELIR 162
Cdd:TIGR00962 104 GRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTII 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 163 NIAIEHSgYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNI 242
Cdd:TIGR00962 184 NQKDSDV-YCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDNGKHALIIYDDL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 243 YRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTK----TGSITSVQAVYVPADDLTDPSPATTFAHLDSTVV 318
Cdd:TIGR00962 263 SKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNdekgGGSLTALPIIETQAGDVSAYIPTNVISITDGQIF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 319 LSRNIASLGIYPAVDPLDSTSRqldplVVGEEHYNVARGVQGTLQ----RYKELkDIIAILGMDeLSEDDKRLVARARKI 394
Cdd:TIGR00962 343 LESDLFNSGIRPAINVGLSVSR-----VGGAAQIKAMKQVAGSLRlelaQYREL-EAFSQFASD-LDEATKKQLERGQRV 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 493291288 395 ERFLSQ----PFHVAE----VFNGVPG--KFVPLKEtIRGFKgilEGEYDHI 436
Cdd:TIGR00962 416 VELLKQpqykPLSVEEqvviLFAGTKGylDDIPVDK-IRKFE---QALLAYL 463
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
74-340 |
1.03e-31 |
|
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: 122.72 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 74 EVPVGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGK 153
Cdd:cd01135 3 KLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLPH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 154 TVNMMELIRNIAIEHSGYS---VFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFR- 229
Cdd:cd01135 83 NELAAQIARQAGVVGSEENfaiVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYLAy 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 230 DEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQER--ITSTKTGSITSVQAVYVPADDLTDPSPA 307
Cdd:cd01135 163 EKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMPNDDITHPIPD 242
|
250 260 270
....*....|....*....|....*....|...
gi 493291288 308 TTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSR 340
Cdd:cd01135 243 LTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
2-73 |
2.60e-31 |
|
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: 114.92 E-value: 2.60e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493291288 2 ATGKIVQIIGAVIDVEFPQDAVPKVYDALKVESG----LTLEVQQQLGGGVVRCIALGSSDGLKRGLKVENTNKAI 73
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDdgkkLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
49-401 |
1.53e-29 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 120.79 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 49 VRCIALGSSDGLKRGLKVENTNKAIEVPVGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGI 128
Cdd:PRK13343 71 VGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 129 KVIDLVAPFAKGGKVGLFGGAGVGKTVNMMELIrnIAIEHSG-YSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQM 207
Cdd:PRK13343 151 KVVDALIPIGRGQRELIIGDRQTGKTAIAIDAI--INQKDSDvICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 208 NEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERIT----ST 283
Cdd:PRK13343 229 SDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAklspEL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 284 KTGSITSVQAVYVPADDLTDPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRqldplVVGEEHYNVARGVQGTLQ 363
Cdd:PRK13343 309 GGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR-----VGGKAQHPAIRKESGRLR 383
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 493291288 364 ----RYKELKdIIAILGMDeLSEDDKRLVARARKIERFLSQP 401
Cdd:PRK13343 384 ldyaQFLELE-AFTRFGGL-LDAGTQKQITRGRRLRELLKQP 423
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
75-402 |
4.96e-29 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 118.47 E-value: 4.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 75 VPVGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKT 154
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 155 vnmmELIRNIAI-EHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGR 233
Cdd:PRK05922 172 ----SLLSTIAKgSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGH 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 234 DVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAV-YVP--ADDLTDPSPATtf 310
Cdd:PRK05922 248 RVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSL-- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 311 ahLDSTVVLSRNIASLGiYPAVDPLDSTSRQLDPLVVgEEHYNVARGVQGTLQRYKELKDIIAI----LGMDELSEDDKR 386
Cdd:PRK05922 326 --LDGHFFLTPQGKALA-SPPIDILTSLSRSARQLAL-PHHYAAAEELRSLLKAYHEALDIIQLgayvPGQDAHLDRAVK 401
|
330
....*....|....*.
gi 493291288 387 LVArarKIERFLSQPF 402
Cdd:PRK05922 402 LLP---SIKQFLSQPL 414
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
104-340 |
5.89e-25 |
|
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: 103.81 E-value: 5.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 104 RWTIHRAAPsYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKTVnmmelirniaIEH--SGYS-----VFAG 176
Cdd:cd01134 41 RWPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTV----------ISQslSKWSnsdvvIYVG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 177 VGER----TREGNDFYH---EMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAG 249
Cdd:cd01134 110 CGERgnemAEVLEEFPElkdPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 250 TEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKT-------GSITSVQAVYVPADDLTDPSPATT------FAHLDST 316
Cdd:cd01134 190 REISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRClgspgreGSVTIVGAVSPPGGDFSEPVTQATlrivqvFWGLDKK 269
|
250 260
....*....|....*....|....
gi 493291288 317 VVLSRNiaslgiYPAVDPLDSTSR 340
Cdd:cd01134 270 LAQRRH------FPSINWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
104-430 |
4.95e-22 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 98.70 E-value: 4.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 104 RWTIHRAAPsYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKTVnmmeLIRNIAiehsGYS-----VFAGVG 178
Cdd:PRK04192 192 KWPVRRPRP-YKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTV----TQHQLA----KWAdadivIYVGCG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 179 ERtreGNdfyhEMKDsnVLdkvslvygqmNEPP-------GNRL--R-----------VA------LTGLTMAEKFRDEG 232
Cdd:PRK04192 263 ER---GN----EMTE--VL----------EEFPelidpktGRPLmeRtvliantsnmpVAareasiYTGITIAEYYRDMG 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 233 RDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLA-------EEMGVLqeRITSTKTGSITSVQAVYVPADDLTDPS 305
Cdd:PRK04192 324 YDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLAsrlaefyERAGRV--KTLGGEEGSVTIIGAVSPPGGDFSEPV 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 306 PATTFAhldstVV-----LSRNIASLGIYPAVDPLDSTSRQLDplVVGEE-HYNVARG-------VQGTLQRYKELKDII 372
Cdd:PRK04192 402 TQNTLR-----IVkvfwaLDAELADRRHFPAINWLTSYSLYLD--QVAPWwEENVDPDwrelrdeAMDLLQREAELQEIV 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 373 AILGMDELSEDDKRLVARARKI-ERFLSQ-PFHvaEVfngvpGKFVPLKETIRGFKGILE 430
Cdd:PRK04192 475 RLVGPDALPEEDRLILEVARLIrEDFLQQnAFD--PV-----DTYCPPEKQYEMLKLILT 527
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
73-340 |
7.06e-22 |
|
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: 94.93 E-value: 7.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 73 IEVPVGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVG 152
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 153 KTVNMMELIrniaIEHSG---YSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFR 229
Cdd:cd01132 82 KTAIAIDTI----INQKGkkvYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 230 DEGRDVLFFVDNIYRYTLAGTEVSALLGR------MPSAVGY-QPTLAEEMGVLQERItstKTGSITSVQAVYVPADDLT 302
Cdd:cd01132 158 DNGKHALIIYDDLSKQAVAYRQMSLLLRRppgreaYPGDVFYlHSRLLERAAKLSDEL---GGGSLTALPIIETQAGDVS 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 493291288 303 DPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSR 340
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 ... |
65-403 |
1.12e-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: 97.10 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 65 KVENTNKAIEVPVGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVG 144
Cdd:TIGR01040 66 TCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 145 LFGGAGVGKTVNMMELIRNIAI-------EHSGYS-----VFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPG 212
Cdd:TIGR01040 146 IFSAAGLPHNEIAAQICRQAGLvklptkdVHDGHEdnfaiVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 213 NRLRVALTGLTMAEKFRDE-GRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKTGSIT 289
Cdd:TIGR01040 226 ERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSIT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 290 SVQAVYVPADDLTDPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRqLDPLVVGE-----EHYNVARGVQGTLQR 364
Cdd:TIGR01040 306 QIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSR-LMKSAIGEgmtrkDHSDVSNQLYACYAI 384
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 493291288 365 YKELKDIIAILGMDELSEDDKRLVARARKIER-FLSQPFH 403
Cdd:TIGR01040 385 GKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQGPY 424
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
5-396 |
2.39e-20 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 92.79 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 5 KIVQIIGAVIDVEfpqdAVPKVYDAL---KVESGLTLEVQQQLGGGVVRCIALGSSDGLKRGLKVENTNKAIEVPVGTKT 81
Cdd:PRK02118 7 KITDITGNVITVE----AEGVGYGELatvERKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 82 LGRIMNVLGEPIDeAGPIGEEERWTIhrAAPSYE--EQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAgvGKTVNmmE 159
Cdd:PRK02118 83 LGRRFNGSGKPID-GGPELEGEPIEI--GGPSVNpvKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVS--GEPYN--A 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 160 LIRNIAIE-HSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFR-DEGRDVLF 237
Cdd:PRK02118 156 LLARIALQaEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 238 FVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTK-TGSITSVQAVYVPADDLTDPSPATTFAHLDST 316
Cdd:PRK02118 236 LLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEdGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 317 VVLSRNiaslgiypAVDPLDSTSRqLDPLVVG----EEHynvaRGVQGTLQR-YKELKDIIAILGMD-ELSEDDKRLVAR 390
Cdd:PRK02118 316 FYLRRG--------RIDPFGSLSR-LKQLVIGkktrEDH----GDLMNAMIRlYADSREAKEKMAMGfKLSNWDEKLLKF 382
|
....*.
gi 493291288 391 ARKIER 396
Cdd:PRK02118 383 SELFES 388
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
156-400 |
1.79e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 91.62 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 156 NMMELIRNIAIEH-------SGYSVFAGVGERTREGNDFYHE---MKDSN----VLDKVSLVYGQMNEPPGNRLRVALTG 221
Cdd:PRK14698 662 NMPTLLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEfpkLKDPKtgkpLMERTVLIANTSNMPVAAREASIYTG 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 222 LTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI-------TSTKTGSITSVQAV 294
Cdd:PRK14698 742 ITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAV 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 295 YVPADDLTDPSPATTFAHLDSTVVLSRNIASLGIYPAVDPLDSTSRQLDPLV------VGEEHYNVARGVQGTLQRYKEL 368
Cdd:PRK14698 822 SPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKdwwhknVDPEWKAMRDKAMELLQKEAEL 901
|
250 260 270
....*....|....*....|....*....|...
gi 493291288 369 KDIIAILGMDELSEDDKRLVARARKI-ERFLSQ 400
Cdd:PRK14698 902 QEIVRIVGPDALPERERAILLVARMLrEDYLQQ 934
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
49-260 |
3.43e-19 |
|
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: 89.71 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 49 VRCIALGSSDGLKRGLKVENTNKAIEVPVGTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGI 128
Cdd:COG0056 71 VGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 129 KVIDLVAPFAKGGKVGLFGGAGVGKTVnmmelirnIAIE------HSG-YSVFAGVGErtregndfyhemKDSNVldkVS 201
Cdd:COG0056 151 KAIDAMIPIGRGQRELIIGDRQTGKTA--------IAIDtiinqkGKDvICIYVAIGQ------------KASTV---AQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 202 LV-----YGQM----------NEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNI------YRytlagtEVSALLGRMP 260
Cdd:COG0056 208 VVetleeHGAMeytivvaataSDPAPLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLskhavaYR------ELSLLLRRPP 281
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
10-260 |
8.22e-19 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 88.58 E-value: 8.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 10 IGAVIDVefpQDAVPKVYDALKVESGLTLEvqqqLGGGV-----------VRCIALGSSDGLKRGLKVENTNKAIEVPVG 78
Cdd:PRK09281 28 VGTVISV---GDGIARVYGLDNVMAGELLE----FPGGVygialnleednVGAVILGDYEDIKEGDTVKRTGRILEVPVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 79 TKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKTVnmm 158
Cdd:PRK09281 101 EALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTA--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 159 elirnIAIE------HSG-YSVFAGVGErtregndfyhemKDSNVldkVSLV-----YGQM----------NEPPGNRLR 216
Cdd:PRK09281 178 -----IAIDtiinqkGKDvICIYVAIGQ------------KASTV---AQVVrkleeHGAMeytivvaataSDPAPLQYL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 493291288 217 VALTGLTMAEKFRDEGRDVLFFVDNI------YRytlagtEVSALLGRMP 260
Cdd:PRK09281 238 APYAGCAMGEYFMDNGKDALIVYDDLskqavaYR------QLSLLLRRPP 281
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
351-420 |
2.01e-18 |
|
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: 79.03 E-value: 2.01e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 351 HYNVARGVQGTLQRYKELKDIIAILGMDELSEDDKRLVARARKIERFLSQPFHVAEVFNGVPGKFVPLKE 420
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-70 |
2.51e-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: 73.35 E-value: 2.51e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493291288 6 IVQIIGAVIDVEFPQDAVPKVYDALKVE----SGLTLEVQQQLGGGVVRCIALGSSDGLKRGLKVENTN 70
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVElvefGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
34-363 |
2.83e-15 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 78.16 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 34 SGLTLEVQQQlggGVVRCIALGSSDGLKRGLKVENTNKAIEVPVGTKTLGRIMNVLGEPIdeagPIG-----------EE 102
Cdd:PTZ00185 79 AGLVFNLEKD---GRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEV----PVGlltrsrallesEQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 103 ERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKT-------VNMMELIRNIAIEHSGYSVFA 175
Cdd:PTZ00185 152 TLGKVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsiavstiINQVRINQQILSKNAVISIYV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 176 GVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSAL 255
Cdd:PTZ00185 232 SIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 256 LGRMPSAVGYQPTLAEEMGVLQERITSTKT----GSITSVQAVYVPADDLTDPSPATTFAHLDSTVVLSRNIASLGIYPA 331
Cdd:PTZ00185 312 LRRPPGREAYPGDVFYLHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPA 391
|
330 340 350
....*....|....*....|....*....|...
gi 493291288 332 VDPLDSTSRqldplvVGEEHYNVA-RGVQGTLQ 363
Cdd:PTZ00185 392 VNIGLSVSR------VGSSAQNVAmKAVAGKLK 418
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
10-340 |
6.03e-12 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 67.30 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 10 IGAVIDVefpQDAVPKVYDALKVESGLTLEVQQQLGG----------GVVrciALGSSDGLKRGLKVENTNKAIEVPVGT 79
Cdd:CHL00059 7 TGTVLQV---GDGIARIYGLDEVMAGELVEFEDGTIGialnlesnnvGVV---LMGDGLMIQEGSSVKATGKIAQIPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 80 KTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPSYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKTVNMME 159
Cdd:CHL00059 81 AYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 160 LIRNIAIEhSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVSLVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLFFV 239
Cdd:CHL00059 161 TILNQKGQ-NVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 240 DNIYRYTLAGTEVSALLGRMPSAVGY-------QPTLAEEMGVLQERITStktGSITSVQAVYVPADDLTDPSPATTFAH 312
Cdd:CHL00059 240 DDLSKQAQAYRQMSLLLRRPPGREAYpgdvfylHSRLLERAAKLSSQLGE---GSMTALPIVETQAGDVSAYIPTNVISI 316
|
330 340
....*....|....*....|....*...
gi 493291288 313 LDSTVVLSRNIASLGIYPAVDPLDSTSR 340
Cdd:CHL00059 317 TDGQIFLSADLFNAGIRPAINVGISVSR 344
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
59-363 |
4.61e-11 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 64.34 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 59 GLKRGLKVENTNKAIEvpvGTKTLGRIMNVLGEPIDEAG---------PIGEEERwtIHRAAPSYEEQAnstelletgiK 129
Cdd:PRK12608 58 NLRTGDVVEGVARPRE---RYRVLVRVDSVNGTDPEKLArrphfddltPLHPRER--LRLETGSDDLSM----------R 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 130 VIDLVAPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAG-VGERTREGNDFYHEMKdsnvldkvSLVYGQMN 208
Cdd:PRK12608 123 VVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSVK--------GEVYASTF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 209 -EPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLA--------------GTEVSALLGrmPSAVGYQPTLAEEM 273
Cdd:PRK12608 195 dRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAynnevessgrtlsgGVDARALQR--PKRLFGAARNIEEG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 274 GVLQerITST---KTGSitsvqavyvPADDLtdpspatTFAHLDST----VVLSRNIASLGIYPAVDPLDSTSRQLDPLV 346
Cdd:PRK12608 273 GSLT--IIATalvDTGS---------RMDEV-------IFEEFKGTgnmeIVLDRELADKRVFPAIDIAKSGTRREELLL 334
|
330
....*....|....*..
gi 493291288 347 VGEEHYNVaRGVQGTLQ 363
Cdd:PRK12608 335 DSKELEKV-RRLRRALA 350
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
120-379 |
2.38e-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: 46.60 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 120 STELLETgiKVIDLVAPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSG-YSVFAGVGERTREgndfyhemkdsnVLD 198
Cdd:TIGR00767 150 STEDLST--RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEvELIVLLIDERPEE------------VTD 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 199 KVSLVYGQM-----NEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAvGYQPTL---- 269
Cdd:TIGR00767 216 MQRSVKGEVvastfDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLSG-GVDANAlhrp 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 270 ---------AEEMGVLQerITST---KTGSitsvqavyvPADDLtdpspatTFAHLDST----VVLSRNIASLGIYPAVD 333
Cdd:TIGR00767 295 krffgaarnIEEGGSLT--IIATaliDTGS---------RMDEV-------IFEEFKGTgnmeLHLDRKLADRRIFPAID 356
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 493291288 334 PLDSTSRQlDPLVVGEEHynvargvqgtLQRYKELKDIIAilGMDE 379
Cdd:TIGR00767 357 IKKSGTRK-EELLLTPEE----------LQKIWVLRKIIS--PMDS 389
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
129-377 |
3.79e-05 |
|
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: 44.89 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 129 KVIDLVAPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAG-VGERTREGNDfyheMKDSNvldKVSLVYGQM 207
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRSV---KGEVVASTF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 208 NEPPGNRLRVALTGLTMAEKFRDEGRDVLFFVDNIYRYTLAGTEVSALLGRMPSAvGYQPTLA-------------EEMG 274
Cdd:cd01128 78 DEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-GVDANALhkpkrffgaarniEEGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 275 VLQerITST---KTGSitsvqavyvPADDLtdpspatTFAHLDST----VVLSRNIASLGIYPAVDPLDSTSRQlDPLVV 347
Cdd:cd01128 157 SLT--IIATalvDTGS---------RMDEV-------IFEEFKGTgnmeLVLDRKLAEKRIFPAIDILKSGTRK-EELLL 217
|
250 260 270
....*....|....*....|....*....|
gi 493291288 348 GEEHYNVARGVQGTLQRYKELKDIIAILGM 377
Cdd:cd01128 218 TPEELQKIWLLRRILSPMDPIEAMEFLLKK 247
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
78-193 |
3.68e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 43.09 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 78 GTKTLGRIMNVLGEPIDEAGPIGEEERWTIHRAAPsYEEQANSTELLETGIKVIDLVAPFAKGGKVGLFGGAGVGKTVNM 157
Cdd:PRK14698 166 GEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRP-YKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDG 244
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 493291288 158 MELIRN-----IAIEHSgYSVFAGVGERTREGNDFYHEMKD 193
Cdd:PRK14698 245 DTLILTkefglIKIKDL-YEILDGKGKKTVEGNEEWTELEE 284
|
|
| 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 ... |
366-400 |
1.26e-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: 37.80 E-value: 1.26e-03
10 20 30
....*....|....*....|....*....|....*.
gi 493291288 366 KELKDIIAILGMDELSEDDKRLVARARKIE-RFLSQ 400
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFErEFINQ 57
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
139-259 |
5.19e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.35 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493291288 139 KGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGvgertregndfyhEMKDSNVLDKVSLVYGQMNEPPGNRLRVA 218
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------EDILEEVLDQLLLIIVGGKKASGSGELRL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 493291288 219 LTGLTMAEKFRdegRDVLFFvDNIYRYTLAGTEVSALLGRM 259
Cdd:smart00382 68 RLALALARKLK---PDVLIL-DEITSLLDAEQEALLLLLEE 104
|
|
| |
