|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-458 |
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: 990.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 1 MSSGRIVQIIGAVIDVEFPRDAVPSIYEALKV---QGVETTLEVQQQLGDGVVRSIAMGSTEGLKRGLNVDSTGAAISVP 77
Cdd:COG0055 3 MNTGKIVQVIGPVVDVEFPEGELPAIYNALEVeneGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 78 VGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVN 157
Cdd:COG0055 83 VGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 158 MMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRD-EGRDV 236
Cdd:COG0055 163 IMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 237 LLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSIQAVYVPADDLTDPSPATTFAHLDA 316
Cdd:COG0055 243 LLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 317 TVVLSRDIASLGIYPAVDPLDSTSRQLDPLVIGQDHYDTARGVQYVLQRYKELKDIIAILGMDELSEADKLLVARARKIQ 396
Cdd:COG0055 323 TTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKIQ 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600747 397 RFLSQPFFVAEVFTGSPGKYVSLKDTIAGFKGILNGDYDHLPEQAFYMVGGIEEAVEKAKKL 458
Cdd:COG0055 403 RFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKL 464
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
2-458 |
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: 887.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 2 SSGRIVQIIGAVIDVEFPRDAVPSIYEALKVQ---GVETTLEVQQQLGDGVVRSIAMGSTEGLKRGLNVDSTGAAISVPV 78
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQnraESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 79 GKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVNM 158
Cdd:TIGR01039 81 GKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 159 MELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRDE-GRDVL 237
Cdd:TIGR01039 161 QELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 238 LFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSIQAVYVPADDLTDPSPATTFAHLDAT 317
Cdd:TIGR01039 241 LFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 318 VVLSRDIASLGIYPAVDPLDSTSRQLDPLVIGQDHYDTARGVQYVLQRYKELKDIIAILGMDELSEADKLLVARARKIQR 397
Cdd:TIGR01039 321 TVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQR 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600747 398 FLSQPFFVAEVFTGSPGKYVSLKDTIAGFKGILNGDYDHLPEQAFYMVGGIEEAVEKAKKL 458
Cdd:TIGR01039 401 FLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
2-458 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 818.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 2 SSGRIVQIIGAVIDVEFPRDAVPSIYEALKVQGVET-------TLEVQQQLGDGVVRSIAMGSTEGLKRGLNVDSTGAAI 74
Cdd:CHL00060 15 NLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTagqeinvTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 75 SVPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGK 154
Cdd:CHL00060 95 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 155 TVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMKDSNVLD-------KVALVYGQMNEPPGNRLRVALTGLTMAE 227
Cdd:CHL00060 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 228 KFRDEGR-DVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSIQAVYVPADDLTDPS 306
Cdd:CHL00060 255 YFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 307 PATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSRQLDPLVIGQDHYDTARGVQYVLQRYKELKDIIAILGMDELSEADK 386
Cdd:CHL00060 335 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDR 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600747 387 LLVARARKIQRFLSQPFFVAEVFTGSPGKYVSLKDTIAGFKGILNGDYDHLPEQAFYMVGGIEEAVEKAKKL 458
Cdd:CHL00060 415 LTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANL 486
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
4-451 |
0e+00 |
|
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 beta subunit of this apparent second ATP synthase.
Pssm-ID: 132348 [Multi-domain] Cd Length: 449 Bit Score: 564.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 4 GRIVQIIGAVIDVEFPRDaVPSIYEALKVQG-VETTLEVQQQLGDGVVRSIAMGSTEGLKRGLNVDSTGAAISVPVGKAT 82
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGE-LPAIHSVLRAGReGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 83 LGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVNMMELI 162
Cdd:TIGR03305 80 LSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 163 RNIAIEHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRD-EGRDVLLFID 241
Cdd:TIGR03305 160 HNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDdEKQDVLLLID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 242 NIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSIQAVYVPADDLTDPSPATTFAHLDATVVLS 321
Cdd:TIGR03305 240 NIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSASLVLS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 322 RDIASLGIYPAVDPLDSTSRQLDPLVIGQDHYDTARGVQYVLQRYKELKDIIAILGMDELSEADKLLVARARKIQRFLSQ 401
Cdd:TIGR03305 320 RKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLERFLTQ 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 15600747 402 PFFVAEVFTGSPGKYVSLKDTIAGFKGILNGDYDHLPEQAFYMVGGIEEA 451
Cdd:TIGR03305 400 PFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
75-345 |
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: 563.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 75 SVPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGK 154
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 155 TVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMKDSNV-----LDKVALVYGQMNEPPGNRLRVALTGLTMAEKF 229
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVinldgLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 230 RD-EGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSIQAVYVPADDLTDPSPA 308
Cdd:cd01133 161 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPA 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 15600747 309 TTFAHLDATVVLSRDIASLGIYPAVDPLDSTSRQLDP 345
Cdd:cd01133 241 TTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
75-341 |
8.85e-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: 366.01 E-value: 8.85e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 75 SVPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGK 154
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 155 TVNMMELIRNIAIEHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRDEGR 234
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 235 DVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTK--KGSITSIQAVYVPADDLTDPSPATTFA 312
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDPIPDNTFA 240
|
250 260
....*....|....*....|....*....
gi 15600747 313 HLDATVVLSRDIASLGIYPAVDPLDSTSR 341
Cdd:cd19476 241 ILDGQIVLSRELARKGIYPAINVLDSTSR 269
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
128-340 |
2.51e-94 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 283.48 E-value: 2.51e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 128 GIKVIDLVCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAiehSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQ 207
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQAS---ADVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 208 MNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITST--K 285
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVkgK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600747 286 KGSITSIQAVYVPADDLTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTS 340
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 ... |
347-454 |
4.04e-77 |
|
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: 235.45 E-value: 4.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 347 VIGQDHYDTARGVQYVLQRYKELKDIIAILGMDELSEADKLLVARARKIQRFLSQPFFVAEVFTGSPGKYVSLKDTIAGF 426
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 15600747 427 KGILNGDYDHLPEQAFYMVGGIEEAVEK 454
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
3-430 |
1.13e-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: 230.30 E-value: 1.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 3 SGRIVQIIGAVIDVEFPRDAVPSIYEALKVQGVETTLEVqqqLG--DGVVRSIAMGSTEGLKRGLNVDSTGAAISVPVGK 80
Cdd:COG1157 20 SGRVTRVVGLLIEAVGPDASIGELCEIETADGRPVLAEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 81 ATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVNMME 160
Cdd:COG1157 97 GLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 161 LIRNIAIEhsgYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFI 240
Cdd:COG1157 177 IARNTEAD---VNVIALIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLM 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 241 DNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSIQAVYVPADDLTDPSPATTFAHLDATVVL 320
Cdd:COG1157 254 DSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILDGHIVL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 321 SRDIASLGIYPAVDPLDSTSRqLDPLVIGQDHYDTARGVQYVLQRYKELKDIIAI----LGMD-ELSEAdkllVARARKI 395
Cdd:COG1157 334 SRKLAERGHYPAIDVLASISR-VMPDIVSPEHRALARRLRRLLARYEENEDLIRIgayqPGSDpELDEA----IALIPAI 408
|
410 420 430
....*....|....*....|....*....|....*
gi 15600747 396 QRFLSQpffvaevftgSPGKYVSLKDTIAGFKGIL 430
Cdd:COG1157 409 EAFLRQ----------GMDERVSFEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
75-341 |
4.92e-63 |
|
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: 205.10 E-value: 4.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 75 SVPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGK 154
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 155 TVNMMELIRNIAiehSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRDEGR 234
Cdd:cd01136 81 STLLGMIARNTD---ADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 235 DVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSIQAVYVPADDLTDPSPATTFAHL 314
Cdd:cd01136 158 KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSIL 237
|
250 260
....*....|....*....|....*..
gi 15600747 315 DATVVLSRDIASLGIYPAVDPLDSTSR 341
Cdd:cd01136 238 DGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
9-403 |
2.36e-55 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 189.82 E-value: 2.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 9 IIGAVIDVEFPRDAVPSIYEALKVQGVETTLEVQQQLGDGVVRSI--AMGSTEGLKRGLNVDSTGAAISVPVGKATLGRI 86
Cdd:PRK08149 13 IQGPIIEAELPDVAIGEICEIRAGWHSNEVIARAQVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 87 MDVLGN------PIDEAGPIGEEErwGIHREAPSYADQAGGNELLETGIKVID--LVCpfAKGGKVGLFGGAGVGKTVNM 158
Cdd:PRK08149 93 LDPTGKiverfdAPPTVGPISEER--VIDVAPPSYAERRPIREPLITGVRAIDglLTC--GVGQRMGIFASAGCGKTSLM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 159 melirNIAIEHSGYSVF--AGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDV 236
Cdd:PRK08149 169 -----NMLIEHSEADVFviGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 237 LLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSIQAVYVPADDLTDPSPATTFAHLDA 316
Cdd:PRK08149 244 VLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 317 TVVLSRDIASLGIYPAVDPLDSTSRqldplVIGQ----DHYDTARGVQYVLQRYKELKDIIAiLG---MDELSEADKLLV 389
Cdd:PRK08149 324 HIYLSRKLAAKGHYPAIDVLKSVSR-----VFGQvtdpKHRQLAAAFRKLLTRLEELQLFID-LGeyrRGENADNDRAMD 397
|
410
....*....|....
gi 15600747 390 ARArKIQRFLSQPF 403
Cdd:PRK08149 398 KRP-ALEAFLKQDV 410
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
59-431 |
7.44e-54 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 186.04 E-value: 7.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 59 EGLKRGLNVDSTGAAISVPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIHReAPSYADQAGG-NELLETGIKVID--LV 135
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMK-APIAAMKRGLiDEVFSVGVKSIDglLT 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 136 CpfAKGGKVGLFGGAGVGKTVNMMELIRNiaiEHSGYSVFAGVGERTREGNDFYHEMKDSNvLDKVALVYGQMNEPPGNR 215
Cdd:PRK08472 154 C--GKGQKLGIFAGSGVGKSTLMGMIVKG---CLAPIKVVALIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSPLMR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 216 LRVALTGLTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTK-KGSITSIQA 294
Cdd:PRK08472 228 KYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 295 VYVPADDLTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSRQLDPlVIGQDHYDTARGVQYVLQRYKELKDIIA 374
Cdd:PRK08472 308 VLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMND-IISPEHKLAARKFKRLYSLLKENEVLIR 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600747 375 I----LGMD-ELSEAdkllVARARKIQRFLSQpffvaevftgSPGKYVSLKDTIAGFKGILN 431
Cdd:PRK08472 387 IgayqKGNDkELDEA----ISKKEFMEQFLKQ----------NPNELFPFEQTFEQLEEILR 434
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
4-401 |
6.74e-53 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 183.80 E-value: 6.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 4 GRIVQIIGAVIdvefpRDAVPS--IYEALKVQGVETTLEVQQQLgDGVVRSIA----MGSTEGLKRGLNVDSTGAAISVP 77
Cdd:PRK06936 25 GRVTQVTGTIL-----KAVVPGvrIGELCYLRNPDNSLSLQAEV-IGFAQHQAlltpLGEMYGISSNTEVSPTGTMHQVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 78 VGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVN 157
Cdd:PRK06936 99 VGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 158 MMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVL 237
Cdd:PRK06936 179 LASLIRSAEVD---VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 238 LFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSIQAVYVPADDLTDPSPATTFAHLDAT 317
Cdd:PRK06936 256 LLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSILDGH 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 318 VVLSRDIASLGIYPAVDPLDSTSRQLDPLViGQDHYDTARGVQYVLQRYKELKDIIAI----LGMDelSEADKLLvARAR 393
Cdd:PRK06936 336 IILSRKLAAANHYPAIDVLRSASRVMNQIV-SKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQD--KEADQAI-ERIG 411
|
....*...
gi 15600747 394 KIQRFLSQ 401
Cdd:PRK06936 412 AIRGFLRQ 419
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
57-401 |
1.20e-49 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 175.00 E-value: 1.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 57 STEGLKRGLNVDSTGAAISVPVGKATLGRIMDVLGNPIDEAGPIGEEERwGIHREAPSYADQAGGNELLETGIKVIDLVC 136
Cdd:PRK06820 80 SSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWR-ELDCPPPSPLTRQPIEQMLTTGIRAIDGIL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 137 PFAKGGKVGLFGGAGVGKTVnmmeLIRNIAiEHSGYSV--FAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGN 214
Cdd:PRK06820 159 SCGEGQRIGIFAAAGVGKST----LLGMLC-ADSAADVmvLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 215 RLRVALTGLTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSIQA 294
Cdd:PRK06820 234 RLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 295 VYVPADDLTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSRQLDPLViGQDHYDTARGVQYVLQRYKELKDIIA 374
Cdd:PRK06820 314 VLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIV-SAGQLAMAQKLRRMLACYQEIELLVR 392
|
330 340 350
....*....|....*....|....*....|.
gi 15600747 375 I----LGMDelSEADKLLvARARKIQRFLSQ 401
Cdd:PRK06820 393 VgeyqAGED--LQADEAL-QRYPAICAFLQQ 420
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
76-375 |
1.54e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 174.89 E-value: 1.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 76 VPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGKT 155
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 156 VNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRD 235
Cdd:PRK08972 177 VLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLN 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 236 VLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKKGSITSIQAVYVPADDLTDPSPATTFAH 313
Cdd:PRK08972 254 VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAgnGGPGQGSITAFYTVLTEGDDLQDPIADASRAI 333
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600747 314 LDATVVLSRDIASLGIYPAVDPLDSTSRQLdPLVIGQDHYDTARGVQYVLQRYKELKDIIAI 375
Cdd:PRK08972 334 LDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
3-402 |
4.22e-46 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 165.71 E-value: 4.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 3 SGRIVQIIGAVIdvefprdavpsiyealKVQGVETTL----EVQQQLGD--------GVVRSIAM----GSTEGLKRGLN 66
Cdd:PRK09099 25 TGKVVEVIGTLL----------------RVSGLDVTLgelcELRQRDGTllqraevvGFSRDVALlspfGELGGLSRGTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 67 VDSTGAAISVPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGL 146
Cdd:PRK09099 89 VIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 147 FGGAGVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMA 226
Cdd:PRK09099 169 FAPAGVGKSTLMGMFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 227 EKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSIQAVYVPADDLTDPS 306
Cdd:PRK09099 246 EYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 307 PATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSRQLdPLVIGQDHYDTARGVQYVLQRYKELKDIIAI----LGMDELS 382
Cdd:PRK09099 326 AEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVA 404
|
410 420
....*....|....*....|
gi 15600747 383 EAdklLVARARKIQRFLSQP 402
Cdd:PRK09099 405 DE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
50-375 |
4.59e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 165.28 E-value: 4.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 50 VRSIAMGSTeglkrglnVDSTGAAISVPVGKATLGRIMDVLGNPID-EAGPIGEEErWGIHREAPSYADQAGGNELLETG 128
Cdd:PRK07721 75 VAEIAPGCL--------VEATGKPLEVKVGSGLIGQVLDALGEPLDgSALPKGLAP-VSTDQDPPNPLKRPPIREPMEVG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 129 IKVIDLVCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQM 208
Cdd:PRK07721 146 VRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTSAD---LNVIALIGERGREVREFIERDLGPEGLKRSIVVVATS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 209 NEPPGNRLRVALTGLTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGS 288
Cdd:PRK07721 223 DQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 289 ITSIQAVYVPADDLTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSRQLdPLVIGQDHYDTARGVQYVLQRYKE 368
Cdd:PRK07721 303 ITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQN 381
|
....*..
gi 15600747 369 LKDIIAI 375
Cdd:PRK07721 382 SEDLINI 388
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
84-377 |
1.10e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 164.79 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 84 GRIMDVLGNPIDEAGPIGE-EERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVNMMELI 162
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 163 RNIAIEHSgysVFAGVGERTREGNDFYHEMKDSNvLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFIDN 242
Cdd:PRK06002 187 RADAFDTV---VIALVGERGREVREFLEDTLADN-LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDS 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 243 IYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKKGSITSIQAVYVPADDLTDPSPATTFAHLDATVVL 320
Cdd:PRK06002 263 VTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVL 342
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600747 321 SRDIASLGIYPAVDPLDSTSRqLDPLVIGQDHYDTARGVQYVLQRYKELKDIIAILG 377
Cdd:PRK06002 343 DRAIAEQGRYPAVDPLASISR-LARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
4-401 |
6.14e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 162.46 E-value: 6.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 4 GRIVQIIGAVIDVEFPRDAVpSIYEALKVQGVETTLEVQQQLGDGVVRSIAM--GSTEGLKRGLNVDSTGAAISVPVGKA 81
Cdd:PRK08927 19 GRVVAVRGLLVEVAGPIHAL-SVGARIVVETRGGRPVPCEVVGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVRPSRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 82 TLGRIMDVLGNPIDEAGPIGE-EERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVNMME 160
Cdd:PRK08927 98 WLGRVVNALGEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 161 LIRNIAIEhsgYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFI 240
Cdd:PRK08927 178 LARNADAD---VSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 241 DNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKKGSITSIQAVYVPADDLTDPSPATTFAHLDATV 318
Cdd:PRK08927 255 DSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 319 VLSRDIASLGIYPAVDPLDSTSRQLdPLVIGQDHYDTARGVQYVLQRYKELKDIIAI----LGMD-ELSEAdkllVARAR 393
Cdd:PRK08927 335 VMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRLgayrAGSDpEVDEA----IRLNP 409
|
....*...
gi 15600747 394 KIQRFLSQ 401
Cdd:PRK08927 410 ALEAFLRQ 417
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
55-401 |
1.50e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 158.74 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 55 MGSTEGLKRGLNVDSTGAAISVPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDL 134
Cdd:PRK05688 82 VGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSING 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 135 VCPFAKGGKVGLFGGAGVGKTV--NMMELIRNIAIehsgySVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPP 212
Cdd:PRK05688 162 LLTVGRGQRLGLFAGTGVGKSVllGMMTRFTEADI-----IVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAP 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 213 GNRLRVALTGLTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKK--GSIT 290
Cdd:PRK05688 237 LMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPggGSIT 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 291 SIQAVYVPADDLTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSRQLdPLVIGQDHYDTARGVQYVLQRYKELK 370
Cdd:PRK05688 317 AFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSR 395
|
330 340 350
....*....|....*....|....*....|....*
gi 15600747 371 DIIAI----LGMDelSEADkLLVARARKIQRFLSQ 401
Cdd:PRK05688 396 DLISVgayvAGGD--PETD-LAIARFPHLVQFLRQ 427
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
58-401 |
6.45e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 156.68 E-value: 6.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 58 TEGLKRGLNVDSTGAAISVPVGKATLGRIMDVLGNPIDEagPIGEEERWGIHREAPSYA--DQAGGNELLETGIKVIDLV 135
Cdd:PRK06793 73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIHafEREEITDVFETGIKSIDSM 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 136 CPFAKGGKVGLFGGAGVGKTVNMMELIRNiaiEHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNR 215
Cdd:PRK06793 151 LTIGIGQKIGIFAGSGVGKSTLLGMIAKN---AKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 216 LRVALTGLTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPsaVGYQPTLAEE-MGVLQERITSTKKGSITSIQA 294
Cdd:PRK06793 228 LRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP--IGGKTLLMESyMKKLLERSGKTQKGSITGIYT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 295 VYVPADDLTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSRQLDPLViGQDHYDTARGVQYVLQRYKElKDIIA 374
Cdd:PRK06793 306 VLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIV-SPNHWQLANEMRKILSIYKE-NELYF 383
|
330 340 350
....*....|....*....|....*....|
gi 15600747 375 ILGMDELSEADKLLVARARK---IQRFLSQ 401
Cdd:PRK06793 384 KLGTIQENAENAYIFECKNKvegINTFLKQ 413
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
40-375 |
1.84e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 155.50 E-value: 1.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 40 EVQQQLGDGVVRSiAMGSTEGLKRGLNVDSTGAAISVPVGKATLGRIMDVLGNPIDeagpiGEEERWGIHRE-----APS 114
Cdd:PRK07594 56 EVVGINGSKALLS-PFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLD-----GRELPDVCWKDydampPPA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 115 YADQAGGNELLeTGIKVIDLVCPFAKGGKVGLFGGAGVGKTVNMMELIrniAIEHSGYSVFAGVGERTREGNDFYHEMKD 194
Cdd:PRK07594 130 MVRQPITQPLM-TGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLC---NAPDADSNVLVLIGERGREVREFIDFTLS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 195 SNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEM 274
Cdd:PRK07594 206 EETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSAL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 275 GVLQERITSTKKGSITSIQAVYVPADDLTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSRQLdPLVIGQDHYD 354
Cdd:PRK07594 286 PRLLERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQ 364
|
330 340
....*....|....*....|.
gi 15600747 355 TARGVQYVLQRYKELKDIIAI 375
Cdd:PRK07594 365 LAAILRRCLALYQEVELLIRI 385
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
78-401 |
1.80e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 150.04 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 78 VGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVN 157
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 158 MMELIRNIAIEhsgYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVL 237
Cdd:PRK07196 172 LGMITRYTQAD---VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 238 LFIDNIYRYTLAGTEVSALLGRMPSAVGYQPT-------LAEEMGvlqeriTSTKKGSITSIQAVYVPADDLTDPSPATT 310
Cdd:PRK07196 249 LLVDSLTRYAMAQREIALSLGEPPATKGYPPSafsiiprLAESAG------NSSGNGTMTAIYTVLAEGDDQQDPIVDCA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 311 FAHLDATVVLSRDIASLGIYPAVDPLDSTSRQLDPlVIGQDHYDTARGVQYVLQRYKELKDIIAILGMdeLSEADKLL-- 388
Cdd:PRK07196 323 RAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQ-VIGSQQAKAASLLKQCYADYMAIKPLIPLGGY--VAGADPMAdq 399
|
330
....*....|....
gi 15600747 389 -VARARKIQRFLSQ 401
Cdd:PRK07196 400 aVHYYPAITQFLRQ 413
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
56-403 |
3.59e-36 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 138.81 E-value: 3.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 56 GSTEGLK-RGLNVDSTGAAISVPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIH--------REAPSyadqaggnELLE 126
Cdd:PRK04196 57 EGTTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINgapinpvaREYPE--------EFIQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 127 TGIKVID----LVcpfaKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYS---VFAGVGERTREGNDFYHEMKDSNVLD 199
Cdd:PRK04196 129 TGISAIDglntLV----RGQKLPIFSGSGLPHNELAAQIARQAKVLGEEENfavVFAAMGITFEEANFFMEDFEETGALE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 200 KVALVYGQMNEPPGNRL---RVAltgLTMAE--KFrDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEM 274
Cdd:PRK04196 205 RSVVFLNLADDPAIERIltpRMA---LTAAEylAF-EKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 275 GVLQER--ITSTKKGSITSIQAVYVPADDLTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSRQLDpLVIG--- 349
Cdd:PRK04196 281 ATIYERagRIKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMK-DGIGegk 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600747 350 --QDHYDTARGVQYVLQRYKELKDIIAILGMDELSEADKLLVARARKI-QRFLSQPF 403
Cdd:PRK04196 360 trEDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFeREFVNQGF 416
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
63-375 |
1.49e-35 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 136.84 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 63 RGLNVDSTGAAISVPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGG 142
Cdd:PRK07960 97 RNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 143 KVGLFGGAGVGKTVNMMELIRniaIEHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTG 222
Cdd:PRK07960 177 RMGLFAGSGVGKSVLLGMMAR---YTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 223 LTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITS--TKKGSITSIQAVYVPAD 300
Cdd:PRK07960 254 TRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGD 333
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600747 301 DLTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSRQLDPLvIGQDHYDTARGVQYVLQRYKELKDIIAI 375
Cdd:PRK07960 334 DQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAL-IDEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
76-349 |
1.67e-34 |
|
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: 130.03 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 76 VPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIH--------REAPSyadqaggnELLETGIKVIDLVCPFAKGGKVGLF 147
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINgppinpvaRIYPE--------EMIQTGISAIDVMNTLVRGQKLPIF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 148 GGAGVGKTVNMMELIRNIAIEHSGYS---VFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLT 224
Cdd:cd01135 76 SGSGLPHNELAAQIARQAGVVGSEENfaiVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 225 MAEKFR-DEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQER--ITSTKKGSITSIQAVYVPADD 301
Cdd:cd01135 156 TAEYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMPNDD 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15600747 302 LTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSRqLDPLVIG 349
Cdd:cd01135 236 ITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR-LMKSGIG 282
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
10-402 |
1.73e-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: 131.74 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 10 IGAVIDVEfprDAVPSIY--------EALKVQGveTTLEVQQQLGDGVVRSIAMGSTEGLKRGLNVDSTGAAISVPVGKA 81
Cdd:TIGR00962 27 VGTVVSVG---DGIARVYglenvmsgELIEFEG--GVQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 82 TLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVNMMEL 161
Cdd:TIGR00962 102 LLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 162 IRNIAIEHSgYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFID 241
Cdd:TIGR00962 182 IINQKDSDV-YCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDNGKHALIIYD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 242 NIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTK----KGSITSIQAVYVPADDLTDPSPATTFAHLDAT 317
Cdd:TIGR00962 261 DLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNdekgGGSLTALPIIETQAGDVSAYIPTNVISITDGQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 318 VVLSRDIASLGIYPAVDPLDSTSR-----QLDplVIGQdhydTARGVQYVLQRYKELkDIIAILGMDeLSEADKLLVARA 392
Cdd:TIGR00962 341 IFLESDLFNSGIRPAINVGLSVSRvggaaQIK--AMKQ----VAGSLRLELAQYREL-EAFSQFASD-LDEATKKQLERG 412
|
410
....*....|
gi 15600747 393 RKIQRFLSQP 402
Cdd:TIGR00962 413 QRVVELLKQP 422
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
75-431 |
1.94e-32 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 128.10 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 75 SVPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGK 154
Cdd:PRK05922 91 SLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 155 TvnmmELIRNIAI-EHSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRDEG 233
Cdd:PRK05922 171 S----SLLSTIAKgSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 234 RDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKKGSITSIQAV-YVP--ADDLTDPSPATt 310
Cdd:PRK05922 247 HRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSL- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 311 fahLDATVVLSRDIASLGiYPAVDPLDSTSRQLDPLVIGQdHYDTARGVQYVLQRYKELKDIIAI----LGMD-ELSEAD 385
Cdd:PRK05922 326 ---LDGHFFLTPQGKALA-SPPIDILTSLSRSARQLALPH-HYAAAEELRSLLKAYHEALDIIQLgayvPGQDaHLDRAV 400
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 15600747 386 KLLVArarkIQRFLSQPFfvaevftgspGKYVSLKDTIAGFKGILN 431
Cdd:PRK05922 401 KLLPS----IKQFLSQPL----------SSYCALHNTLKQLEALLK 432
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
2-74 |
1.14e-30 |
|
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: 113.00 E-value: 1.14e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600747 2 SSGRIVQIIGAVIDVEFPRDAVPSIYEALKVQGVET---TLEVQQQLGDGVVRSIAMGSTEGLKRGLNVDSTGAAI 74
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDDGkklVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
53-341 |
1.33e-29 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 120.79 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 53 IAMGSTEGLKRGLNVDSTGAAISVPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVI 132
Cdd:PRK13343 74 VLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 133 DLVCPFAKGGKVGLFGGAGVGKTVNMMELIrnIAIEHSG-YSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEP 211
Cdd:PRK13343 154 DALIPIGRGQRELIIGDRQTGKTAIAIDAI--INQKDSDvICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 212 PGNRLRVALTGLTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERIT--STKK--G 287
Cdd:PRK13343 232 PGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAklSPELggG 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15600747 288 SITSIQAVYVPADDLTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSR 341
Cdd:PRK13343 312 SLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
75-341 |
7.96e-26 |
|
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: 106.50 E-value: 7.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 75 SVPVGKATLGRIMDVLGNPIDEagpIGEEE-----------RWGIHREAPsYADQAGGNELLETGIKVIDLVCPFAKGGK 143
Cdd:cd01134 3 SVELGPGLLGSIFDGIQRPLEV---IAETGsifiprgvnvqRWPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 144 VGLFGGAGVGKTVnmmelirniaIEH--SGYS-----VFAGVGER----TREGNDFYH---EMKDSNVLDKVALVYGQMN 209
Cdd:cd01134 79 AAIPGPFGCGKTV----------ISQslSKWSnsdvvIYVGCGERgnemAEVLEEFPElkdPITGESLMERTVLIANTSN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 210 EPPGNRLRVALTGLTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI-------T 282
Cdd:cd01134 149 MPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgS 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600747 283 STKKGSITSIQAVYVPADDLTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSR 341
Cdd:cd01134 229 PGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
74-341 |
1.50e-24 |
|
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: 102.64 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 74 ISVPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVG 153
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 154 KTVNMMELIrniaIEHSG---YSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFR 230
Cdd:cd01132 82 KTAIAIDTI----INQKGkkvYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 231 DEGRDVLLFIDNIYRYTLAGTEVSALLGR------MPSAVGY-QPTLAEEMGVLQERItstKKGSITSIQAVYVPADDLT 303
Cdd:cd01132 158 DNGKHALIIYDDLSKQAVAYRQMSLLLRRppgreaYPGDVFYlHSRLLERAAKLSDEL---GGGSLTALPIIETQAGDVS 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 15600747 304 DPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSR 341
Cdd:cd01132 235 AYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
1-401 |
1.69e-22 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 100.24 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 1 MSSGRIVQIIGAVIDVEFPRDAvpSIYEALKVQGVETTLEVQQQLGDGVVrsIAM-GSTEGLKRGLNVDSTGAAISVPVG 79
Cdd:PRK04192 2 MTKGKIVRVSGPLVVAEGMGGA--RMYEVVRVGEEGLIGEIIRIEGDKAT--IQVyEETSGIKPGEPVEFTGEPLSVELG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 80 KATLGRIMDVLGNPIDE--------------AGPIGEEERW------------------GI--------HR--------- 110
Cdd:PRK04192 78 PGLLGSIFDGIQRPLDElaeksgdflergvyVPALDREKKWeftptvkvgdkveagdilGTvqetpsieHKimvppgvsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 111 ------EAPSY--------ADQAGGN-------------------------ELLETGIKVIDLVCPFAKGGKVGLFGGAG 151
Cdd:PRK04192 158 tvkeivSEGDYtvddtiavLEDEDGEgveltmmqkwpvrrprpykeklppvEPLITGQRVIDTFFPVAKGGTAAIPGPFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 152 VGKTVnmmeLIRNIAiehsGYS-----VFAGVGERtreGNdfyhEMKDsnVLdkvalvygqmNEPP-------GNRL--R 217
Cdd:PRK04192 238 SGKTV----TQHQLA----KWAdadivIYVGCGER---GN----EMTE--VL----------EEFPelidpktGRPLmeR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 218 -----------VA------LTGLTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLA-------EE 273
Cdd:PRK04192 291 tvliantsnmpVAareasiYTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLAsrlaefyER 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 274 MGVLqeRITSTKKGSITSIQAVYVPADDLTDPspaTTFAHLDATVV---LSRDIASLGIYPAVDPLDSTSRQLDPL---- 346
Cdd:PRK04192 371 AGRV--KTLGGEEGSVTIIGAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAINWLTSYSLYLDQVapww 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600747 347 --VIGQDHYDTARGVQYVLQRYKELKDIIAILGMDELSEADKLLVARARKI-QRFLSQ 401
Cdd:PRK04192 446 eeNVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
55-261 |
4.47e-21 |
|
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: 95.49 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 55 MGSTEGLKRGLNVDSTGAAISVPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDL 134
Cdd:COG0056 76 LGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 135 VCPFAKGGKVGLFGGAGVGKTVnmmelirnIAIE------HSG-YSVFAGVGErtregndfyhemKDSNVLDKVALV--Y 205
Cdd:COG0056 156 MIPIGRGQRELIIGDRQTGKTA--------IAIDtiinqkGKDvICIYVAIGQ------------KASTVAQVVETLeeH 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600747 206 GQM----------NEPPGNRLRVALTGLTMAEKFRDEGRDVLLFIDNI------YRytlagtEVSALLGRMP 261
Cdd:COG0056 216 GAMeytivvaataSDPAPLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLskhavaYR------ELSLLLRRPP 281
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
157-426 |
5.87e-21 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 96.24 E-value: 5.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 157 NMMELIRNIAIEH-------SGYSVFAGVGERTREGNDFYHE---MKDSN----VLDKVALVYGQMNEPPGNRLRVALTG 222
Cdd:PRK14698 662 NMPTLLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEfpkLKDPKtgkpLMERTVLIANTSNMPVAAREASIYTG 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 223 LTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERI-------TSTKKGSITSIQAV 295
Cdd:PRK14698 742 ITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAV 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 296 YVPADDLTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSRQLDPLvigQDHYDTARGVQY---------VLQRY 366
Cdd:PRK14698 822 SPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAV---KDWWHKNVDPEWkamrdkameLLQKE 898
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600747 367 KELKDIIAILGMDELSEADK--LLVARARKiQRFLSQPFFVAEVFTGSPGKYVSLKDTIAGF 426
Cdd:PRK14698 899 AELQEIVRIVGPDALPERERaiLLVARMLR-EDYLQQDAFDEVDTYCPPEKQVTMMRVLLNF 959
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
41-401 |
6.20e-21 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 94.79 E-value: 6.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 41 VQQQLGDGVVRSIAMGSTEGLK--------------RGLNVDSTGAAISVPVGKATLGRIMDVLGNPIDEAGPIGEEERW 106
Cdd:TIGR01040 27 VNLTLPDGTVRSGQVLEVSGNKavvqvfegtsgidaKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 107 GIHREAPSYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAI-------EHSGYS-----V 174
Cdd:TIGR01040 107 DINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvklptkdVHDGHEdnfaiV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 175 FAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRDE-GRDVLLFIDNIYRYTLAGTEV 253
Cdd:TIGR01040 187 FAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 254 SALLGRMPSAVGYQPTLAEEMGVLQERI--TSTKKGSITSIQAVYVPADDLTDPSPATTFAHLDATVVLSRDIASLGIYP 331
Cdd:TIGR01040 267 SAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYP 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600747 332 AVDPLDSTSRqLDPLVIGQ-----DHYDTARGVQYVLQRYKELKDIIAILGMDELSEADKLLVARARKIQR-FLSQ 401
Cdd:TIGR01040 347 PINVLPSLSR-LMKSAIGEgmtrkDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
48-261 |
1.42e-20 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 93.98 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 48 GVVrsiAMGSTEGLKRGLNVDSTGAAISVPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLET 127
Cdd:PRK09281 72 GAV---ILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 128 GIKVIDLVCPFAKGGKVGLFGGAGVGKTVnmmelirnIAIE------HSG-YSVFAGVGErtregndfyhemKDSNvldk 200
Cdd:PRK09281 149 GIKAIDAMIPIGRGQRELIIGDRQTGKTA--------IAIDtiinqkGKDvICIYVAIGQ------------KAST---- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 201 VALV------YGQM----------NEPPGNRLRVALTGLTMAEKFRDEGRDVLLFIDNI------YRytlagtEVSALLG 258
Cdd:PRK09281 205 VAQVvrkleeHGAMeytivvaataSDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLskqavaYR------QLSLLLR 278
|
...
gi 15600747 259 RMP 261
Cdd:PRK09281 279 RPP 281
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
5-393 |
7.85e-20 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 91.25 E-value: 7.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 5 RIVQIIGAVIDVE-----------FPRDAVPSIYEALKVQGVETTLEVqqqlgdgvvrsiaMGSTEGLKRGLNVDSTGAA 73
Cdd:PRK02118 7 KITDITGNVITVEaegvgygelatVERKDGSSLAQVIRLDGDKVTLQV-------------FGGTRGISTGDEVVFLGRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 74 ISVPVGKATLGRIMDVLGNPIDeAGPIGEEERWGIhrEAPSY--ADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAg 151
Cdd:PRK02118 74 MQVTYSESLLGRRFNGSGKPID-GGPELEGEPIEI--GGPSVnpVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVS- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 152 vGKTVNmmELIRNIAIE-HSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFR 230
Cdd:PRK02118 150 -GEPYN--ALLARIALQaEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 231 -DEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKK-GSITSIQAVYVPADDLTDPSPA 308
Cdd:PRK02118 227 lEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEDgGSITIIAVTTMPGDDVTHPVPD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 309 TTFAHLDATVVLSRDiaslgiypAVDPLDSTSRqLDPLVIG----QDHYDTARGvqyVLQRYKELKDIIAILGMD-ELSE 383
Cdd:PRK02118 307 NTGYITEGQFYLRRG--------RIDPFGSLSR-LKQLVIGkktrEDHGDLMNA---MIRLYADSREAKEKMAMGfKLSN 374
|
410
....*....|
gi 15600747 384 ADKLLVARAR 393
Cdd:PRK02118 375 WDEKLLKFSE 384
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
352-420 |
8.60e-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: 82.88 E-value: 8.60e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600747 352 HYDTARGVQYVLQRYKELKDIIAILGMDELSEADKLLVARARKIQRFLSQPFFVAEVFTGSPGKYVSLK 420
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIK 69
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-71 |
5.20e-17 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 75.27 E-value: 5.20e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600747 6 IVQIIGAVIDVEFPRDAVPSIYEALKVQGVE---TTLEVQQQLGDGVVRSIAMGSTEGLKRGLNVDSTG 71
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVEfgsLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
47-341 |
3.50e-15 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 77.77 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 47 DGVVRSIAMGSTEGLKRGLNVDSTGAAISVPVGKATLGRIMDVLGNPIdeagPIG-----------EEERWGIHREAPSY 115
Cdd:PTZ00185 88 DGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEV----PVGlltrsrallesEQTLGKVDAGAPNI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 116 ADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGKT-------VNMMELIRNIAIEHSGYSVFAGVGERTREGNDF 188
Cdd:PTZ00185 164 VSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsiavstiINQVRINQQILSKNAVISIYVSIGQRCSNVARI 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 189 YHEMKDSNVLDKVALVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGYQP 268
Cdd:PTZ00185 244 HRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPG 323
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600747 269 TLAEEMGVLQER--ITSTKK--GSITSIQAVYVPADDLTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSR 341
Cdd:PTZ00185 324 DVFYLHSRLLERaaMLSPGKggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR 400
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
55-341 |
1.78e-13 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 72.30 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 55 MGSTEGLKRGLNVDSTGAAISVPVGKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPSYADQAGGNELLETGIKVIDL 134
Cdd:CHL00059 55 MGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 135 VCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEhSGYSVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGN 214
Cdd:CHL00059 135 MIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQ-NVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 215 RLRVALTGLTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAVGY-------QPTLAEEMGVLQERITStkkG 287
Cdd:CHL00059 214 QYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYpgdvfylHSRLLERAAKLSSQLGE---G 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15600747 288 SITSIQAVYVPADDLTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSR 341
Cdd:CHL00059 291 SMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR 344
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
60-352 |
3.27e-11 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 64.72 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 60 GLKRGLNVDSTgaaISVPVGKATLGRIMDVLGNPIDEAG---------PIGEEERwgIHREAPSyADQAGgnelletgiK 130
Cdd:PRK12608 58 NLRTGDVVEGV---ARPRERYRVLVRVDSVNGTDPEKLArrphfddltPLHPRER--LRLETGS-DDLSM---------R 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 131 VIDLVCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAG-VGERTREGNDFYHEMKdsnvldkvALVYGQMN 209
Cdd:PRK12608 123 VVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSVK--------GEVYASTF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 210 -EPPGNRLRVALTGLTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAvgyqptlaeemGVLQERITSTKK-- 286
Cdd:PRK12608 195 dRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGRTLSG-----------GVDARALQRPKRlf 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 287 ---------GSITSIQAVYVP----ADDLtdpspatTFAHLDAT----VVLSRDIASLGIYPAVDPLDSTSRQLDPLVIG 349
Cdd:PRK12608 264 gaarnieegGSLTIIATALVDtgsrMDEV-------IFEEFKGTgnmeIVLDRELADKRVFPAIDIAKSGTRREELLLDS 336
|
...
gi 15600747 350 QDH 352
Cdd:PRK12608 337 KEL 339
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
113-394 |
1.08e-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: 50.84 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 113 PSYADQ----AGGNELLETgiKVIDLVCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSG-YSVFAGVGERTREgnd 187
Cdd:TIGR00767 138 PLYPNErlrlETSTEDLST--RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEvELIVLLIDERPEE--- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 188 fyhemkdsnVLDKVALVYGQM-----NEPPGNRLRVALTGLTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPS 262
Cdd:TIGR00767 213 ---------VTDMQRSVKGEVvastfDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 263 AvgyqptlaeemGVLQERITSTKK-----------GSITSIQAVYVPADDLTDpspATTFAHLDAT----VVLSRDIASL 327
Cdd:TIGR00767 284 G-----------GVDANALHRPKRffgaarnieegGSLTIIATALIDTGSRMD---EVIFEEFKGTgnmeLHLDRKLADR 349
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600747 328 GIYPAVDPLDSTSRQlDPLVIGQDHydtargvqyvLQRYKELKDIIAilGMDElSEADKLLVARARK 394
Cdd:TIGR00767 350 RIFPAIDIKKSGTRK-EELLLTPEE----------LQKIWVLRKIIS--PMDS-IEAMEFLISKLKK 402
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
130-378 |
1.87e-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: 46.04 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 130 KVIDLVCPFAKGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAG-VGERTREGNDfyheMKDSnvldkvalVYGQM 208
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRS--------VKGEV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 209 -----NEPPGNRLRVALTGLTMAEKFRDEGRDVLLFIDNIYRYTLAGTEVSALLGRMPSAvGYQPTlaeEMGVLQERITS 283
Cdd:cd01128 73 vastfDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-GVDAN---ALHKPKRFFGA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 284 TKK----GSITSIQAVYVP----ADDLtdpspatTFAHLDAT----VVLSRDIASLGIYPAVDPLDSTSRQlDPLVIGQD 351
Cdd:cd01128 149 ARNieegGSLTIIATALVDtgsrMDEV-------IFEEFKGTgnmeLVLDRKLAEKRIFPAIDILKSGTRK-EELLLTPE 220
|
250 260
....*....|....*....|....*..
gi 15600747 352 HYDTARGVQYVLQRYKELKDIIAILGM 378
Cdd:cd01128 221 ELQKIWLLRRILSPMDPIEAMEFLLKK 247
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
84-341 |
3.28e-05 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 46.12 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 84 GRIMDVLGNPIDEAGPIGEEERWGIHReAPSYADQAGG------NELLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVN 157
Cdd:PRK07165 81 GKIIDIDGNIIYPEAQNPLSKKFLPNT-SSIFNLAHGLmtvktlNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 158 MMELI-----RNIAIehsgysVFAGVGERTREGNDFYHEMKDSNVLDKVALVYGQMNEPPGNRLrVALTGLTMAEKFRDE 232
Cdd:PRK07165 160 ALNTIinqknTNVKC------IYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSPYEQYL-APYVAMAHAENISYN 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 233 gRDVLLFID------NIYRytlagtEVSALLGR------MPSAVGYQPTlaeemgVLQERITSTK-KGSITSIQAVYVPA 299
Cdd:PRK07165 233 -DDVLIVFDdltkhaNIYR------EIALLTNKpvgkeaFPGDMFFAHS------KLLERAGKFKnRKTITALPILQTVD 299
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15600747 300 DDLTDPSPATTFAHLDATVVLSRDIASLGIYPAVDPLDSTSR 341
Cdd:PRK07165 300 NDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSR 341
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
79-194 |
7.73e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 41.93 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 79 GKATLGRIMDVLGNPIDEAGPIGEEERWGIHREAPsYADQAGGNELLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVNM 158
Cdd:PRK14698 166 GEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRP-YKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDG 244
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15600747 159 MELIRN-----IAIEHSgYSVFAGVGERTREGNDFYHEMKD 194
Cdd:PRK14698 245 DTLILTkefglIKIKDL-YEILDGKGKKTVEGNEEWTELEE 284
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
140-260 |
1.27e-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: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600747 140 KGGKVGLFGGAGVGKTVNMMELIRNIAIEHSGYSVFAGvgertregndfyhEMKDSNVLDKVALVYGQMNEPPGNRLRVA 219
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------EDILEEVLDQLLLIIVGGKKASGSGELRL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15600747 220 LTGLTMAEKFRDEgrdvLLFIDNIYRYTLAGTEVSALLGRM 260
Cdd:smart00382 68 RLALALARKLKPD----VLILDEITSLLDAEQEALLLLLEE 104
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
4-72 |
1.99e-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: 36.91 E-value: 1.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600747 4 GRIVQIIGAVIDVEFPRDavPSIYEALKVQ------GVETTLEVQQQLGDGVVRSiAMGSTEGLKRGLNVDSTGA 72
Cdd:cd01426 2 GRVIRVNGPLVEAELEGE--VAIGEVCEIErgdgnnETVLKAEVIGFRGDRAILQ-LFESTRGLSRGALVEPTGR 73
|
|
| |
