|
Name |
Accession |
Description |
Interval |
E-value |
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
6-489 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 1099.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 6 TTSGSEVSAVEKKNPGRIVKIIGPVLDVAFPPGKMPNIYNALVVQGRDN--EQTNVTCEVQQLLGNNRVRAVAMSDTDGL 83
Cdd:CHL00060 2 NPTGPGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTagQEINVTCEVQQLLGNNRVRAVAMSATDGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 84 MRGMEVIDTRAPISVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRG 163
Cdd:CHL00060 82 MRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 164 GKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYLEMKESGVINEENIAESKVALVYGQMNEPPGA 243
Cdd:CHL00060 162 GKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 244 RMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQ 323
Cdd:CHL00060 242 RMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 324 AVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDII 403
Cdd:CHL00060 322 AVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDII 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 404 AILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATA 483
Cdd:CHL00060 402 AILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATA 481
|
....*.
gi 21633283 484 KAMNLK 489
Cdd:CHL00060 482 KAANLE 487
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
16-489 |
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: 948.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 16 EKKNPGRIVKIIGPVLDVAFPPGKMPNIYNALVVqgRDNEQTNVTCEVQQLLGNNRVRAVAMSDTDGLMRGMEVIDTRAP 95
Cdd:COG0055 1 MAMNTGKIVQVIGPVVDVEFPEGELPAIYNALEV--ENEGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 96 ISVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 175
Cdd:COG0055 79 ISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 176 KTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYLEMKESGVINeeniaesKVALVYGQMNEPPGARMRVGLTALTMA 255
Cdd:COG0055 159 KTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTMA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 256 EYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDP 335
Cdd:COG0055 232 EYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 336 APATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEED 415
Cdd:COG0055 312 APATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEED 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21633283 416 RLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNLK 489
Cdd:COG0055 392 KLTVARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLK 465
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
19-488 |
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: 838.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 19 NPGRIVKIIGPVLDVAFPPGKMPNIYNALVVQGRdnEQTNVTCEVQQLLGNNRVRAVAMSDTDGLMRGMEVIDTRAPISV 98
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNR--AESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 99 PVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 178
Cdd:TIGR01039 79 PVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 179 LIMELINNIAKAHGGVSVFGGVGERTREGNDLYLEMKESGVINeeniaesKVALVYGQMNEPPGARMRVGLTALTMAEYF 258
Cdd:TIGR01039 159 LIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAEYF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 259 RDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPA 338
Cdd:TIGR01039 232 RDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 339 TTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLT 418
Cdd:TIGR01039 312 TTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLT 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 419 VARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNL 488
Cdd:TIGR01039 392 VERARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
97-375 |
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: 578.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 97 SVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 176
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 177 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYLEMKESGVINEENIaeSKVALVYGQMNEPPGARMRVGLTALTMAE 256
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGL--SKVALVYGQMNEPPGARARVALTGLTMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 257 YFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 336
Cdd:cd01133 159 YFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPA 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 21633283 337 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP 375
Cdd:cd01133 239 PATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
21-481 |
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: 578.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 21 GRIVKIIGPVLDVAFPpGKMPNIYNALvvqgRDNEQTNVTCEVQQLLGNNRVRAVAMSDTDGLMRGMEVIDTRAPISVPV 100
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFD-GELPAIHSVL----RAGREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 101 GGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLI 180
Cdd:TIGR03305 76 GKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 181 MELINNIAKAHGGVSVFGGVGERTREGNDLYLEMKESGVINEeniaeskVALVYGQMNEPPGARMRVGLTALTMAEYFRD 260
Cdd:TIGR03305 156 TEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDN-------TVMVFGQMNEPPGARFRVGHTALTMAEYFRD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 261 VNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATT 340
Cdd:TIGR03305 229 DEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 341 FAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVA 420
Cdd:TIGR03305 309 FSHLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVN 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21633283 421 RARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEA 481
Cdd:TIGR03305 389 RARRLERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
97-372 |
7.41e-132 |
|
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: 382.57 E-value: 7.41e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 97 SVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 176
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 177 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYLEMKESGvineeniAESKVALVYGQMNEPPGARMRVGLTALTMAE 256
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSG-------AMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 257 YFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK--EGSITSIQAVYVPADDLTD 334
Cdd:cd19476 154 YFRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTD 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 21633283 335 PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTM 372
Cdd:cd19476 233 PIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
150-370 |
2.36e-86 |
|
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: 264.22 E-value: 2.36e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 150 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKahgGVSVFGGVGERTREGNDLYLEMKESGVIneeniaeSK 229
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-------KR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 230 VALVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQE 309
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21633283 310 RITSTKE--GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 370
Cdd:pfam00006 150 RAGRVKGkgGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 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 ... |
377-484 |
2.18e-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: 237.38 E-value: 2.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 377 IVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGF 456
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 21633283 457 QLILSGELDGLPEQAFYLVGNIDEATAK 484
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
21-460 |
3.59e-66 |
|
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: 219.52 E-value: 3.59e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 21 GRIVKIIGPVLDVAFPPGKMpniyNALV-VQGRDNEqtNVTCEVqqlLG--NNRVRAVAMSDTDGLMRGMEVIDTRAPIS 97
Cdd:COG1157 21 GRVTRVVGLLIEAVGPDASI----GELCeIETADGR--PVLAEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 98 VPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQ---LDTKLsifETGIKVVDLLAPYRRGGKIGLFGGAGV 174
Cdd:COG1157 92 VPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLErarITEPL---DTGVRAIDGLLTVGRGQRIGIFAGSGV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 175 GKTVLIMELINN----------IAkahggvsvfggvgERTREGNDlYLEMkesgVINEENIAESKValVYGQMNEPPGAR 244
Cdd:COG1157 169 GKSTLLGMIARNteadvnvialIG-------------ERGREVRE-FIED----DLGEEGLARSVV--VVATSDEPPLMR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 245 MRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQA 324
Cdd:COG1157 229 LRAAYTATAIAEYFRDQG-KNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 325 VYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMlqPRIVGEEHYETAQRVKQTLQRYKELQDII 403
Cdd:COG1157 308 VLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISrVM--PDIVSPEHRALARRLRRLLARYEENEDLI 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21633283 404 AIlG---------LDElseedrlTVARARKIERFLSQpffvaevftgSPGKYVGLAETIRGFQLIL 460
Cdd:COG1157 386 RI-GayqpgsdpeLDE-------AIALIPAIEAFLRQ----------GMDERVSFEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
97-370 |
1.55e-53 |
|
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: 180.83 E-value: 1.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 97 SVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 176
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 177 TVLIMELINNiAKAhgGVSVFGGVGERTREGNDlYLEmkesGVINEENIaeSKVALVYGQMNEPPGARMRVGLTALTMAE 256
Cdd:cd01136 81 STLLGMIARN-TDA--DVNVIALIGERGREVRE-FIE----KDLGEEGL--KRSVLVVATSDESPLLRVRAAYTATAIAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 257 YFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 336
Cdd:cd01136 151 YFRD-QGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPI 229
|
250 260 270
....*....|....*....|....*....|....
gi 21633283 337 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 370
Cdd:cd01136 230 ADEVRSILDGHIVLSRRLAERGHYPAIDVLASIS 263
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
66-431 |
3.01e-47 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 169.22 E-value: 3.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 66 LLGNNRVRA--VAM----------SDTDGLMRGMEVIDTRAPISVPVGGSTLGRIFNVLGQPVDNlGPVDTNTTSPIHRS 133
Cdd:PRK06820 55 RIEPQGMLAevVSIeqemallspfASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 134 APAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELInniAKAHGGVSVFGGVGERTREGNDlYLE 213
Cdd:PRK06820 134 PPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLC---ADSAADVMVLALIGERGREVRE-FLE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 214 MkesgVINEEniAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSA 293
Cdd:PRK06820 210 Q----VLTPE--ARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRG-KKVLLMADSLTRYARAAREIGLAAGEPPAA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 294 VGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTML 373
Cdd:PRK06820 283 GSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21633283 374 qPRIVGEEHYETAQRVKQTLQRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQ 431
Cdd:PRK06820 363 -PQIVSAGQLAMAQKLRRMLACYQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
77-431 |
2.76e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 166.85 E-value: 2.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 77 MSDTDGLMRGMEVIDTRAPISVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQ---LDTKLSifeTGIKV 153
Cdd:PRK06936 76 LGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSrrlIETPLS---LGVRV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 154 VDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFGGVGERTREgndlYLEMKESGvINEENIAESkvALV 233
Cdd:PRK06936 153 IDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIESD-LGEEGLRKA--VLV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 234 YGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS 313
Cdd:PRK06936 223 VATSDRPSMERAKAGFVATSIAEYFRD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 314 TKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQRVKQTL 393
Cdd:PRK06936 302 SDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELL 380
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 21633283 394 QRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQ 431
Cdd:PRK06936 381 AKYEEVELLLQIgeyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
21-466 |
2.00e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 164.38 E-value: 2.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 21 GRIVKIIGPVLDVAFPPGKMpNIYNALVVQGRDNEQtnVTCEVqqlLGNNRVRAVAM--SDTDGLMRGMEVIDTRAPISV 98
Cdd:PRK08927 19 GRVVAVRGLLVEVAGPIHAL-SVGARIVVETRGGRP--VPCEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 99 PVGGSTLGRIFNVLGQPVDNLGPVDTNTTS-PIHRSAP---AFIQLDTKLsifETGIKVVDLLAPYRRGGKIGLFGGAGV 174
Cdd:PRK08927 93 RPSRAWLGRVVNALGEPIDGKGPLPQGPVPyPLRAPPPpahSRARVGEPL---DLGVRALNTFLTCCRGQRMGIFAGSGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 175 GKTVLIMELINNIAKAhggVSVFGGVGERTREGNDlYLEmkesGVINEENIAESKValVYGQMNEPPGARMRVGLTALTM 254
Cdd:PRK08927 170 GKSVLLSMLARNADAD---VSVIGLIGERGREVQE-FLQ----DDLGPEGLARSVV--VVATSDEPALMRRQAAYLTLAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 255 AEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI--TSTKEGSITSIQAVYVPADDL 332
Cdd:PRK08927 240 AEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 333 TDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMlqPRIVGEEHYETAQRVKQTLQRYKELQDIIAI----LG 407
Cdd:PRK08927 319 NEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSrTM--PGCNDPEENPLVRRARQLMATYADMEELIRLgayrAG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 21633283 408 LDelSEEDRlTVARARKIERFLSQpffvaevftgSPGKYVGLAETIRGFQLILSGELDG 466
Cdd:PRK08927 397 SD--PEVDE-AIRLNPALEAFLRQ----------GKDEATSLAEGYARLAQILGGPETE 442
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
25-433 |
2.72e-45 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 163.63 E-value: 2.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 25 KIIGPVLDVAFPP---GKMPNIYnalvvqgRDNEQTNVTCEVQqLLGNNRVRAV--AMSDTDGLMRGMEVIDTRAPISVP 99
Cdd:PRK08149 12 RIQGPIIEAELPDvaiGEICEIR-------AGWHSNEVIARAQ-VVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 100 VGGSTLGRIFNVLGQPVDNLG---PVDTNTTS-PIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 175
Cdd:PRK08149 84 VGEALLGAVLDPTGKIVERFDappTVGPISEErVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 176 KTVLIMELINNiakAHGGVSVFGGVGERTREGNDLYLEMKESGvineeniAESKVALVYGQMNEPPGARMRVGLTALTMA 255
Cdd:PRK08149 164 KTSLMNMLIEH---SEADVFVIGLIGERGREVTEFVESLRASS-------RREKCVLVYATSDFSSVDRCNAALVATTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 256 EYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDP 335
Cdd:PRK08149 234 EYFRDQG-KRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 336 APATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQRVKQTLQRYKELQDIIAiLG---LDELS 412
Cdd:PRK08149 313 IGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVTDPKHRQLAAAFRKLLTRLEELQLFID-LGeyrRGENA 390
|
410 420
....*....|....*....|.
gi 21633283 413 EEDRlTVARARKIERFLSQPF 433
Cdd:PRK08149 391 DNDR-AMDKRPALEAFLKQDV 410
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
81-432 |
9.89e-45 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 162.63 E-value: 9.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 81 DGLMRGMEVIDTRAPISVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQ---LDTKLSifeTGIKVVDLL 157
Cdd:PRK09099 81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSrrmVEAPLP---TGVRIVDGL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 158 APYRRGGKIGLFGGAGVGKTVLIMEL-------INNIAkahggvsvfgGVGERTREGNDlYLEMkesgVINEENIAESKV 230
Cdd:PRK09099 158 MTLGEGQRMGIFAPAGVGKSTLMGMFargtqcdVNVIA----------LIGERGREVRE-FIEL----ILGEDGMARSVV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 231 alVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER 310
Cdd:PRK09099 223 --VCATSDRSSIERAKAAYVATAIAEYFRDRGLR-VLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLER 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 311 ITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQRVK 390
Cdd:PRK09099 300 AGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLR 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 21633283 391 QTLQRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQP 432
Cdd:PRK09099 379 QLLAKHREVETLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
82-405 |
1.62e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 162.18 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 82 GLMRGMEVIDTRAPISVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHrsAPAFIQLDTKlSIFE---TGIKVVDLLA 158
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRR-PITEpldVGVRAINAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 159 PYRRGGKIGLFGGAGVGKTVLI-MELINNIAKAhggvSVFGGVGERTREGNDLYLEmkesgVINEENIAESKValVYGQM 237
Cdd:PRK08972 158 TVGKGQRMGLFAGSGVGKSVLLgMMTRGTTADV----IVVGLVGERGREVKEFIEE-----ILGEEGRARSVV--VAAPA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 238 NEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERIT--STK 315
Cdd:PRK08972 227 DTSPLMRLKGCETATTIAEYFRDQG-LNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 316 EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQRVKQTLQR 395
Cdd:PRK08972 306 QGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSL 384
|
330
....*....|
gi 21633283 396 YKELQDIIAI 405
Cdd:PRK08972 385 YQQNRDLISI 394
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
21-431 |
9.05e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 160.28 E-value: 9.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 21 GRIVKIIGPVLDVAFPPGKMPNiyNALVVQGRDNEQTNVTCEVQQLLGNnRVRAVAMSDTDGLMRGMEVIDTRAPISVPV 100
Cdd:PRK05688 29 GRLLRMVGLTLEAEGLRAAVGS--RCLVINDDSYHPVQVEAEVMGFSGD-KVFLMPVGSVAGIAPGARVVPLADTGRLPM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 101 GGSTLGRIFNVLGQPVDNLGPV--------DTNTTSPIHRsAPAFIQLDTklsifetGIKVVDLLAPYRRGGKIGLFGGA 172
Cdd:PRK05688 106 GMSMLGRVLDGAGRALDGKGPMkaedwvpmDGPTINPLNR-HPISEPLDV-------GIRSINGLLTVGRGQRLGLFAGT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 173 GVGKTVLiMELINNIAKAHGGVSVFGGvgERTREgndlyleMKE--SGVINEENIAESKValVYGQMNEPPGARMRVGLT 250
Cdd:PRK05688 178 GVGKSVL-LGMMTRFTEADIIVVGLIG--ERGRE-------VKEfiEHILGEEGLKRSVV--VASPADDAPLMRLRAAMY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 251 ALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEG--SITSIQAVYVP 328
Cdd:PRK05688 246 CTRIAEYFRDKG-KNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITAFYTVLSE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 329 ADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQRVKQTLQRYKELQDIIAI--- 405
Cdd:PRK05688 325 GDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLISVgay 403
|
410 420
....*....|....*....|....*..
gi 21633283 406 -LGLDelsEEDRLTVARARKIERFLSQ 431
Cdd:PRK05688 404 vAGGD---PETDLAIARFPHLVQFLRQ 427
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
96-431 |
1.12e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 156.77 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 96 ISVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 175
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 176 KTVLiMELINNIAKAhgGVSVFGGVGERTRE---------GNDLylemkESGVINEENIAESKVALVYGqmneppgarmr 246
Cdd:PRK08472 170 KSTL-MGMIVKGCLA--PIKVVALIGERGREipefieknlGGDL-----ENTVIVVATSDDSPLMRKYG----------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 247 vGLTALTMAEYFRDVNEqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK-EGSITSIQAV 325
Cdd:PRK08472 231 -AFCAMSVAEYFKNQGL-DVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 326 YVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQRVKQTLQRYKELQDIIAI 405
Cdd:PRK08472 309 LVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIRI 387
|
330 340 350
....*....|....*....|....*....|.
gi 21633283 406 ----LGLD-ELSEedrlTVARARKIERFLSQ 431
Cdd:PRK08472 388 gayqKGNDkELDE----AISKKEFMEQFLKQ 414
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
106-407 |
4.84e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 155.54 E-value: 4.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 106 GRIFNVLGQPVDNLGPVDTNTTS-PIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELi 184
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPmSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 185 nniAKA-HGGVSVFGGVGERTREGNDLYlemkesgvinEENIAE--SKVALVYGQMNEPPGARMRVGLTALTMAEYFRDV 261
Cdd:PRK06002 186 ---ARAdAFDTVVIALVGERGREVREFL----------EDTLADnlKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDR 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 262 NEqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE--GSITSIQAVYVPADDLTDPAPAT 339
Cdd:PRK06002 253 GE-NVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEggGSITGIFSVLVDGDDHNDPVADS 331
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21633283 340 TFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHyETAQRVKQTLQRYKELQDIIAILG 407
Cdd:PRK06002 332 IRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQR-KLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
56-431 |
2.49e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 150.51 E-value: 2.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 56 QTNVTCEVQQLLGNNRVrAVAMSDTDGLMRGMEVIDTRAPISVPVGGSTLGRIFN----VLGQPVDNLG----PVDTntt 127
Cdd:PRK06793 50 EHNVLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSangeVLNEEAENIPlqkiKLDA--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 128 SPIHrsapAFIQLDTKlSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGvgERTREG 207
Cdd:PRK06793 126 PPIH----AFEREEIT-DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKADINVISLVG--ERGREV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 208 NDLYleMKESGvinEENIAESKValVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALL 287
Cdd:PRK06793 198 KDFI--RKELG---EEGMRKSVV--VVATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 288 GRMPSAvGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLD 367
Cdd:PRK06793 270 KELPIG-GKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLD 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21633283 368 STSTMLQpRIVGEEHYETAQRVKQTLQRYKElQDIIAILGLDELSEEDRLTVARARKIE---RFLSQ 431
Cdd:PRK06793 349 SVSRIME-EIVSPNHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAYIFECKNKVEginTFLKQ 413
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
92-405 |
5.38e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 149.49 E-value: 5.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 92 TRAPISVPVGGSTLGRIFNVLGQPVDN------LGPVDTNTTSPIHRSAPAFIQldtklsIFETGIKVVDLLAPYRRGGK 165
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLDGsalpkgLAPVSTDQDPPNPLKRPPIRE------PMEVGVRAIDSLLTVGKGQR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 166 IGLFGGAGVGKTVLIMEL-------INNIAkahggvsvfgGVGERTREGNDlYLEmKESGvinEENIAESKValVYGQMN 238
Cdd:PRK07721 161 VGIFAGSGVGKSTLMGMIarntsadLNVIA----------LIGERGREVRE-FIE-RDLG---PEGLKRSIV--VVATSD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 239 EPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGS 318
Cdd:PRK07721 224 QPALMRIKGAYTATAIAEYFRDQG-LNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 319 ITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQRVKQTLQRYKE 398
Cdd:PRK07721 303 ITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQN 381
|
....*..
gi 21633283 399 LQDIIAI 405
Cdd:PRK07721 382 SEDLINI 388
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
19-96 |
5.12e-37 |
|
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: 130.71 E-value: 5.12e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21633283 19 NPGRIVKIIGPVLDVAFPPGKMPNIYNALVVQGRDNEqtNVTCEVQQLLGNNRVRAVAMSDTDGLMRGMEVIDTRAPI 96
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDDGK--KLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
82-450 |
2.89e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 136.56 E-value: 2.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 82 GLMRGMEVIDTRAPISVPVGGSTLGRIFNVLGQPVDNLGPVDTNTtsPIHRSAPAFIQLDTKL--SIFETGIKVVDLLAP 159
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGST--PLQQQLPQIHPLQRRAvdTPLDVGVNAINGLLT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 160 YRRGGKIGLFGGAGVGKTVLiMELINNIAKAHGGVSVFGGvgERTREGNDLYlemkeSGVINEENIAESkvALVYGQMNE 239
Cdd:PRK07196 152 IGKGQRVGLMAGSGVGKSVL-LGMITRYTQADVVVVGLIG--ERGREVKEFI-----EHSLQAAGMAKS--VVVAAPADE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 240 PPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI-TSTKEGS 318
Cdd:PRK07196 222 SPLMRIKATELCHAIATYYRDKG-HDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGT 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 319 ITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQRVKQTLQRYKE 398
Cdd:PRK07196 301 MTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMA 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 21633283 399 LQDIIA----ILGLDELSEEdrlTVARARKIERFLSQPFFVAEVFTGSPGKYVGLA 450
Cdd:PRK07196 380 IKPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQEVGHPALFSASVEQLTGMF 432
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
80-405 |
5.74e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 135.47 E-value: 5.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 80 TDGLMRGMEVIDTRAPISVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQLDTKLSIFeTGIKVVDLLAP 159
Cdd:PRK07594 73 TIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRELPDVCWKDYDAMPPPAMVRQPITQPLM-TGIRAIDSVAT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 160 YRRGGKIGLFGGAGVGKTVLIMELINniaKAHGGVSVFGGVGERTREGNDlYLEMkesgVINEEniAESKVALVYGQMNE 239
Cdd:PRK07594 152 CGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGREVRE-FIDF----TLSEE--TRKRCVIVVATSDR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 240 PPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSI 319
Cdd:PRK07594 222 PALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSI 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 320 TSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQRVKQTLQRYKEL 399
Cdd:PRK07594 301 TAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEV 379
|
....*.
gi 21633283 400 QDIIAI 405
Cdd:PRK07594 380 ELLIRI 385
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
98-434 |
3.10e-33 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 131.06 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 98 VPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIhrSAPAF--IQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 175
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGAL--ITPPFnpLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 176 KTVLiMELINNIAKAHGGVSVFGGvgERTREGNDlYLEmkesGVINEENIAESKValVYGQMNEPPGARMRVGLTALTMA 255
Cdd:PRK07960 188 KSVL-LGMMARYTQADVIVVGLIG--ERGREVKD-FIE----NILGAEGRARSVV--IAAPADVSPLLRMQGAAYATRIA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 256 EYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS--TKEGSITSIQAVYVPADDLT 333
Cdd:PRK07960 258 EDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQ 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 334 DPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQRVKQTLQRYKELQDIIAI----LGLD 409
Cdd:PRK07960 337 DPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALIDEQHYARVRQFKQLLSSFQRNRDLVSVgayaKGSD 415
|
330 340
....*....|....*....|....*
gi 21633283 410 ELSEEdrlTVARARKIERFLSQPFF 434
Cdd:PRK07960 416 PMLDK---AIALWPQLEAFLQQGIF 437
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
75-463 |
2.79e-31 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 125.40 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 75 VAMSDTDGLMRGMEVIDTRAPISVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQLDTKLSIFETGIKVV 154
Cdd:PRK05922 69 MSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 155 DLLAPYRRGGKIGLFGGAGVGKTvlimELINNIAK-AHGGVSVFGGVGERTREGNDlYLEMKESGvineenIAESKVALV 233
Cdd:PRK05922 149 DAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVRE-YIEQHKEG------LAAQRTIII 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 234 YGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS 313
Cdd:PRK05922 218 ASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 314 TKEGSITSIQAV-YVP--ADDLTDPAPATTFAHLDATTVlSRGLAAkgiyPAVDPLDSTSTMLQpRIVGEEHYETAQRVK 390
Cdd:PRK05922 297 NDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSRSAR-QLALPHHYAAAEELR 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21633283 391 QTLQRYKELQDIIAiLGLDELSEEDRLTvaRARK----IERFLSQPFfvaevftgspGKYVGLAETIRGFQLILSGE 463
Cdd:PRK05922 371 SLLKAYHEALDIIQ-LGAYVPGQDAHLD--RAVKllpsIKQFLSQPL----------SSYCALHNTLKQLEALLKHE 434
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
67-434 |
1.78e-28 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 118.09 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 67 LGNNRVRAVAMSDTDGLMRGMEVIDTRAPISVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQLDTKLSI 146
Cdd:PRK13343 66 LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 147 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGNDLY-----LEMKESGVIN 221
Cdd:PRK13343 146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN------------------QKDSDVIcvyvaIGQKASAVAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 222 -----EENIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGY 296
Cdd:PRK13343 208 vietlREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAY 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 297 QPTLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTStm 372
Cdd:PRK13343 287 PGDIFYLHSRLLERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVS-- 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21633283 373 lqpRIVGEEHY----ETAQRVKQTLQRYKELQdIIAILGLDeLSEEDRLTVARARKIERFLSQPFF 434
Cdd:PRK13343 365 ---RVGGKAQHpairKESGRLRLDYAQFLELE-AFTRFGGL-LDAGTQKQITRGRRLRELLKQPRF 425
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
79-433 |
1.53e-26 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 111.84 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 79 DTDGLM-RGMEVIDTRAPISVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSA--PA-------FIQldtklsife 148
Cdd:PRK04196 58 GTTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVareypeeFIQ--------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 149 TGIKVVDLLAPYRRGGKIGLFGGAGvgktvlimeLINNIAKAHGGVSVFGGVGE------------RTREGNDLYLEMKE 216
Cdd:PRK04196 129 TGISAIDGLNTLVRGQKLPIFSGSG---------LPHNELAAQIARQAKVLGEEenfavvfaamgiTFEEANFFMEDFEE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 217 SGVINeeniaesKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGY 296
Cdd:PRK04196 200 TGALE-------RSVVFLNLADDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGY 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 297 QPTLSTEMGSLQER--ITSTKEGSITSIQAVYVPADDLTDPAPattfahlDAT-------TVLSRGLAAKGIYPAVDPLD 367
Cdd:PRK04196 273 PGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegqIVLSRELHRKGIYPPIDVLP 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21633283 368 STSTMLQPRIvG-----EEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQPF 433
Cdd:PRK04196 346 SLSRLMKDGI-GegktrEDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFErEFVNQGF 416
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
95-374 |
2.95e-25 |
|
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: 105.00 E-value: 2.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 95 PISVPVGGSTLGRIFNVLGQPVDNLGPV------DTNTTS--PIHRSAPA-FIQldtklsifeTGIKVVDLLAPYRRGGK 165
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPIlpedylDINGPPinPVARIYPEeMIQ---------TGISAIDVMNTLVRGQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 166 IGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGERTREGNDLYLEMKESgviNEENIAESKVALVYGQMNEPPGARM 245
Cdd:cd01135 72 LPIFSGSGLPHNELAAQIARQ-AGVVGSEENFAIVFAAMGVTMEEARFFKDD---FEETGALERVVLFLNLANDPTIERI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 246 RVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER--ITSTKEGSITSIQ 323
Cdd:cd01135 148 ITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIP 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 21633283 324 AVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ 374
Cdd:cd01135 228 ILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMK 278
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
250-431 |
1.24e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 94.85 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 250 TALTMAEYFRDvneQ--DVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER----IT-STKEGSITSI 322
Cdd:PRK04192 311 TGITIAEYYRD---MgyDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTII 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 323 QAVYVPADDLTDPapaTTFAHLDATTV---LSRGLAAKGIYPAVDPLDSTS---TMLQP---RIVGEEHYETAQRVKQTL 393
Cdd:PRK04192 388 GAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAINWLTSYSlylDQVAPwweENVDPDWRELRDEAMDLL 464
|
170 180 190
....*....|....*....|....*....|....*....
gi 21633283 394 QRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 431
Cdd:PRK04192 465 QREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
96-431 |
2.20e-20 |
|
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: 93.63 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 96 ISVPVGGSTLGRIFNVLGQPVDNLGPV------DTNTtSPIHRSAPAFIQldtklSIFETGIKVVDLLAPYRRGGKIGLF 169
Cdd:TIGR01040 74 LRTPVSEDMLGRVFNGSGKPIDKGPPVlaedylDING-QPINPYARIYPE-----EMIQTGISAIDVMNSIARGQKIPIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 170 GGAGVGKTvlimELINNIAKAHGGVSVFGGVGERTREGN------DLYLEMKESGVIN---EENIAESKVALVYGQMNEP 240
Cdd:TIGR01040 148 SAAGLPHN----EIAAQICRQAGLVKLPTKDVHDGHEDNfaivfaAMGVNMETARFFKqdfEENGSMERVCLFLNLANDP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 241 PGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI--TSTKEGS 318
Cdd:TIGR01040 224 TIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGS 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 319 ITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIvGE-----EHYETAQRVKQTL 393
Cdd:TIGR01040 304 ITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHSDVSNQLYACY 382
|
330 340 350
....*....|....*....|....*....|....*....
gi 21633283 394 QRYKELQDIIAILGLDELSEEDRLTVARARKIER-FLSQ 431
Cdd:TIGR01040 383 AIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
23-92 |
2.64e-20 |
|
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: 84.52 E-value: 2.64e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 23 IVKIIGPVLDVAFPPGKMPNIYNALVVQGRDNEqtNVTCEVQQLLGNNRVRAVAMSDTDGLMRGMEVIDT 92
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVEFG--SLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRT 68
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
95-370 |
3.78e-19 |
|
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: 87.63 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 95 PISVPVGGSTLGRIFNVLGQPVDNLGPVD--------TNTTSPIHRSAPAFIQLDTKLsIFETGIKVVDLLAPYRRGGKI 166
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAETGsifiprgvNVQRWPVRQPRPVKEKLPPNV-PLLTGQRVLDTLFPVAKGGTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 167 GLFGGAGVGKTVlimeLINNIAK-AHGGVSVFGGVGERtreGNdlylEMKEsgVINE----------ENIAEsKVALVYG 235
Cdd:cd01134 80 AIPGPFGCGKTV----ISQSLSKwSNSDVVIYVGCGER---GN----EMAE--VLEEfpelkdpitgESLME-RTVLIAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 236 QMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI---- 311
Cdd:cd01134 146 TSNMPVAAREASIYTGITIAEYFRDMG-YNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvr 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21633283 312 ---TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 370
Cdd:cd01134 225 clgSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYS 286
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
382-445 |
1.23e-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: 79.80 E-value: 1.23e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21633283 382 HYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGK 445
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEK 64
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
202-443 |
3.87e-18 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 87.77 E-value: 3.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 202 ERTREGNDLYLEMKESGVINEENIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGS 281
Cdd:PRK14698 692 ERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMG-YDVALMADSTSRWAEALR 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 282 EVSALLGRMPSAVGYQPTLSTEMGSLQERI-------TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGL 354
Cdd:PRK14698 771 EISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 355 AAKGIYPAVDPLDSTSTMLQP------RIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ER 427
Cdd:PRK14698 851 ARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAILLVARMLrED 930
|
250
....*....|....*.
gi 21633283 428 FLSQPFFvAEVFTGSP 443
Cdd:PRK14698 931 YLQQDAF-DEVDTYCP 945
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-370 |
4.73e-17 |
|
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: 81.07 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 96 ISVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 175
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 176 KTVLIMELINNiakahggvsvfggvgertREGNDLY-----LEMKESGVINEENIAESKVALVY-----GQMNEPPGARM 245
Cdd:cd01132 82 KTAIAIDTIIN------------------QKGKKVYciyvaIGQKRSTVAQIVKTLEEHGAMEYtivvaATASDPAPLQY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 246 RVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE----GSITS 321
Cdd:cd01132 144 LAPYAGCAMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSLTA 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 21633283 322 IQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 370
Cdd:cd01132 223 LPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVS 271
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
72-163 |
1.85e-15 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 78.57 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 72 VRAVAMSDTDGLMRGMEVIDTRAPISVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQldtKLSIFE--- 148
Cdd:PRK09281 71 VGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID---RKSVHEplq 147
|
90
....*....|....*
gi 21633283 149 TGIKVVDLLAPYRRG 163
Cdd:PRK09281 148 TGIKAIDAMIPIGRG 162
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
80-340 |
2.05e-13 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 71.99 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 80 TDGLMRGMEVIDTRAPISVPVGGSTLGRIFNVLGQPVDNlGP------VDTNTTS--PIHRSAPAfiqldtklSIFETGI 151
Cdd:PRK02118 58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GPelegepIEIGGPSvnPVKRIVPR--------EMIRTGI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 152 KVVDLLAPYRRGGKIGLFGGAGVGKTVLIMElINNIAKAHGGVSVFGGVGertregNDLYLEMKESgviNEENIAESKVA 231
Cdd:PRK02118 129 PMIDVFNTLVESQKIPIFSVSGEPYNALLAR-IALQAEADIIILGGMGLT------FDDYLFFKDT---FENAGALDRTV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 232 LVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI 311
Cdd:PRK02118 199 MFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKA 278
|
250 260 270
....*....|....*....|....*....|
gi 21633283 312 TSTKE-GSITSIQAVYVPADDLTDPAPATT 340
Cdd:PRK02118 279 VDFEDgGSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
67-364 |
3.95e-11 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 64.98 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 67 LGNNRVRAVAMSDTDGLMRGMEVIDTRAPISVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIqldTKLSI 146
Cdd:CHL00059 45 LESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGII---SRRSV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 147 FE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGND---LYLEM--KESG 218
Cdd:CHL00059 122 YEplqTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN------------------QKGQNvicVYVAIgqKASS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 219 VINEENIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRdVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSA 293
Cdd:CHL00059 184 VAQVVTTLQERGAMEYtivvaETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGR 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 294 VGY--------------QPTLSTEMGslqeritstkEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGI 359
Cdd:CHL00059 263 EAYpgdvfylhsrllerAAKLSSQLG----------EGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGI 332
|
....*
gi 21633283 360 YPAVD 364
Cdd:CHL00059 333 RPAIN 337
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
21-364 |
3.22e-08 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 56.20 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 21 GRIVKIIGPVLDVAFPPGKMPNIYNAlVVQGRDNEQTNVTCEVQQLLGNNRVRAVAMSDTDGLMRGMEVIDTRAPISVPV 100
Cdd:PTZ00185 41 GYVHSIDGTIATLIPAPGNPGVAYNT-IIMIQVSPTTFAAGLVFNLEKDGRIGIILMDNITEVQSGQKVMATGKLLYIPV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 101 GGSTLGRIFNVLGQPV---------------DNLGPVDTNTTSPIHRSAPAFIQLdtklsifeTGIKVVDLLAPYRRGGK 165
Cdd:PTZ00185 120 GAGVLGKVVNPLGHEVpvglltrsralleseQTLGKVDAGAPNIVSRSPVNYNLL--------TGFKAVDTMIPIGRGQR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 166 IGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGErtregndLYLEMKE--SGVINEENIAESKVALVY-----GQMN 238
Cdd:PTZ00185 192 ELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVIS-------IYVSIGQrcSNVARIHRLLRSYGALRYttvmaATAA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 239 EPPGARMRVGLTALTMAEYFRDVNEQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE-- 316
Cdd:PTZ00185 265 EPAGLQYLAPYSGVTMGEYFMNRGRH-CLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPgk 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 21633283 317 --GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 364
Cdd:PTZ00185 344 ggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVN 393
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
21-92 |
8.95e-05 |
|
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: 40.76 E-value: 8.95e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21633283 21 GRIVKIIGPVLDVAFPPGkmPNIYNALVVQ-GRDNEQTNVTCEVQQLLGNnRVRAVAMSDTDGLMRGMEVIDT 92
Cdd:cd01426 2 GRVIRVNGPLVEAELEGE--VAIGEVCEIErGDGNNETVLKAEVIGFRGD-RAILQLFESTRGLSRGALVEPT 71
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
378-432 |
1.05e-04 |
|
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family of ATPases that form part of the Type III secretion system (T3SS) present in Escherichia coli. T3SS is a macromolecular complex that creates a syringe-like apparatus extending from the bacterial cytosol across three membranes to the eukaryotic cytosol. This process is essential for pathogenicity. EscN is a functionally unique ATPase that provides an inner-membrane recognition gate for the T3SS chaperone-virulence effector complexes as well as a potential source of energy for their subsequent secretion.The C-terminal domain of T3SS ATPases mediates binding with multiple contact points along the chaperone.
Pssm-ID: 465691 [Multi-domain] Cd Length: 70 Bit Score: 40.49 E-value: 1.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21633283 378 VGEEHYETAQRVKQTLQRYKELQDIIAIlG---------LDElseedrlTVARARKIERFLSQP 432
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRI-GayqagsdpeIDE-------AIAKRPAINAFLRQG 56
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| ATP-synt_V_A-type_alpha_C |
cd18111 |
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of ... |
387-431 |
2.19e-04 |
|
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of the V1/A1 complex of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349746 [Multi-domain] Cd Length: 105 Bit Score: 40.45 E-value: 2.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 21633283 387 QRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 431
Cdd:cd18111 6 TEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIrEDFLQQ 51
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| 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 ... |
397-431 |
3.18e-04 |
|
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: 39.72 E-value: 3.18e-04
10 20 30
....*....|....*....|....*....|....*.
gi 21633283 397 KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ 431
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFErEFINQ 57
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| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
162-290 |
2.25e-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: 38.51 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21633283 162 RGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVsvfggvgertregndLYLEMKESgvineENIAESKVALVYGQMNEPP 241
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV---------------IYIDGEDI-----LEEVLDQLLLIIVGGKKAS 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 21633283 242 GARMRVGLTALTMAEYFRdvneqDVLLFIDNIFRFVQAGSEVSALLGRM 290
Cdd:smart00382 61 GSGELRLRLALALARKLK-----PDVLILDEITSLLDAEQEALLLLLEE 104
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|
| ATP-synt_flagellum-secretory_path_III_C |
cd18114 |
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the ... |
382-434 |
9.55e-03 |
|
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the 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 flagellum-specific ATPase FliI is the soluble export component that drives flagellar protein export, and it shows extensive similarity to the alpha and beta subunits of FoF1-ATP synthase. Although they both are proton driven rotary molecular devices, 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: 349749 [Multi-domain] Cd Length: 71 Bit Score: 34.89 E-value: 9.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 21633283 382 HYETAQRVKQTLQRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQPFF 434
Cdd:cd18114 1 HYLAARKFRELMSTYQENEDLIRIgaykKGSDPEVDE---AIRLKPQIEAFLKQGLN 54
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