|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-467 |
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: 989.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 1 MSSGKIAQVIGPVVDVLFAAGEkLPEINNALVVYKNDERKtkIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPI 80
Cdd:COG0055 3 MNTGKIVQVIGPVVDVEFPEGE-LPAIYNALEVENEGGGE--LVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 81 SVPVGKETLGRVFNVLGDTIDLEAPFtEDAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVG 160
Cdd:COG0055 80 SVPVGEATLGRIFNVLGEPIDGKGPI-EAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 161 KTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVE 240
Cdd:COG0055 159 KTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 241 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIYVPADDYTDPAPATAFA 320
Cdd:COG0055 239 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 321 HLDSTTNLERKLVQLGIYPAVDPLASSSRALAPEIVGEEHYAVAAEVKRVLQRYHELQDIIAILGMDELSDEEKTLVARA 400
Cdd:COG0055 319 HLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 906780787 401 RRIQFFLSQNFNVAEQFTGQPGSYVPVAETVRGFKEILDGKYDHLPEDAFRGVGSIEDVIAKAEKMG 467
Cdd:COG0055 399 RKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLK 465
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
2-466 |
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: 867.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 2 SSGKIAQVIGPVVDVLFAAGEkLPEINNALVVYKNDERKtkIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPIS 81
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGE-LPRIYNALKVQNRAESE--LTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 82 VPVGKETLGRVFNVLGDTIDLEAPFTEDaERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGK 161
Cdd:TIGR01039 78 VPVGKETLGRIFNVLGEPIDEKGPIPAK-ERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 162 TVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEG 241
Cdd:TIGR01039 157 TVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 242 QDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIYVPADDYTDPAPATAFAH 321
Cdd:TIGR01039 237 QDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 322 LDSTTNLERKLVQLGIYPAVDPLASSSRALAPEIVGEEHYAVAAEVKRVLQRYHELQDIIAILGMDELSDEEKTLVARAR 401
Cdd:TIGR01039 317 LDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERAR 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 906780787 402 RIQFFLSQNFNVAEQFTGQPGSYVPVAETVRGFKEILDGKYDHLPEDAFRGVGSIEDVIAKAEKM 466
Cdd:TIGR01039 397 RIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
2-466 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 804.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 2 SSGKIAQVIGPVVDVLFAAGeKLPEINNALVVYKNDE--RKTKIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRP 79
Cdd:CHL00060 15 NLGRITQIIGPVLDVAFPPG-KMPNIYNALVVKGRDTagQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 80 ISVPVGKETLGRVFNVLGDTIDLEAPFtEDAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGV 159
Cdd:CHL00060 94 LSVPVGGATLGRIFNVLGEPVDNLGPV-DTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 160 GKTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYWEMKESGVIE-------KTAMVFGQMNEPPGARMRVALTGLTI 232
Cdd:CHL00060 173 GKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 233 AEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIYVPADDYTD 312
Cdd:CHL00060 253 AEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 313 PAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRALAPEIVGEEHYAVAAEVKRVLQRYHELQDIIAILGMDELSDE 392
Cdd:CHL00060 333 PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 906780787 393 EKTLVARARRIQFFLSQNFNVAEQFTGQPGSYVPVAETVRGFKEILDGKYDHLPEDAFRGVGSIEDVIAKAEKM 466
Cdd:CHL00060 413 DRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANL 486
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
4-458 |
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: 576.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 4 GKIAQVIGPVVDVLFAagEKLPEINNALVVYKNDErktkIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPISVP 83
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFD--GELPAIHSVLRAGREGE----VVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 84 VGKETLGRVFNVLGDTIDLEAPFTeDAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTV 163
Cdd:TIGR03305 75 VGKPTLSRMFDVFGNTIDRREPPK-DVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 164 LIQELIHNIAQEHGGISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQD 243
Cdd:TIGR03305 154 LLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 244 VLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIYVPADDYTDPAPATAFAHLD 323
Cdd:TIGR03305 234 VLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 324 STTNLERKLVQLGIYPAVDPLASSSRALAPEIVGEEHYAVAAEVKRVLQRYHELQDIIAILGMDELSDEEKTLVARARRI 403
Cdd:TIGR03305 314 ASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 906780787 404 QFFLSQNFNVAEQFTGQPGSYVPVAETVRGFKEILDGKYDHLPEDAFRGVGSIED 458
Cdd:TIGR03305 394 ERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDE 448
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
81-353 |
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: 569.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 81 SVPVGKETLGRVFNVLGDTIDlEAPFTEDAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVG 160
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPID-ERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 161 KTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYWEMKESGVI-----EKTAMVFGQMNEPPGARMRVALTGLTIAEY 235
Cdd:cd01133 80 KTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVInldglSKVALVYGQMNEPPGARARVALTGLTMAEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 236 FRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIYVPADDYTDPAP 315
Cdd:cd01133 160 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAP 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 906780787 316 ATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRALAP 353
Cdd:cd01133 240 ATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
81-350 |
4.18e-124 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 362.16 E-value: 4.18e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 81 SVPVGKETLGRVFNVLGDTIDLEAPFTEDaERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVG 160
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTK-QRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 161 KTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvE 240
Cdd:cd19476 80 KTVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRD-N 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 241 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTK--KGSVTSIQAIYVPADDYTDPAPATA 318
Cdd:cd19476 159 GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 906780787 319 FAHLDSTTNLERKLVQLGIYPAVDPLASSSRA 350
Cdd:cd19476 239 FAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
135-348 |
3.49e-97 |
|
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: 291.18 E-value: 3.49e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 135 GIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQehgGISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQ 214
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 215 MNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITST-- 292
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVkg 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 906780787 293 KKGSVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSS 348
Cdd:pfam00006 157 KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
57-438 |
1.24e-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: 219.90 E-value: 1.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 57 RTIAM--ESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFtEDAERQPIHKKAPTFDELSTSSEILET 134
Cdd:COG1157 65 RVLLMplGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPL-PGEERRPLDAPPPNPLERARITEPLDT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 135 GIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTRE-----GNDLYWE-MKESGVIEKT 208
Cdd:COG1157 144 GVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARNTEAD---VNVIALIGERGREvrefiEDDLGEEgLARSVVVVAT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 209 AmvfgqmNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQER 288
Cdd:COG1157 221 S------DEPPLMRLRAAYTATAIAEYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLER 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 289 ITSTKKGSVTsiqAIY---VPADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRaLAPEIVGEEHYAVAA 365
Cdd:COG1157 294 AGNGGKGSIT---AFYtvlVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISR-VMPDIVSPEHRALAR 369
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 906780787 366 EVKRVLQRYHELQDIIAI----LGMDELSDEEktlVARARRIQFFLSQNfnvaeqftgqPGSYVPVAETVRGFKEIL 438
Cdd:COG1157 370 RLRRLLARYEENEDLIRIgayqPGSDPELDEA---IALIPAIEAFLRQG----------MDERVSFEESLAQLAELL 433
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
355-462 |
5.04e-65 |
|
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: 204.63 E-value: 5.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 355 IVGEEHYAVAAEVKRVLQRYHELQDIIAILGMDELSDEEKTLVARARRIQFFLSQNFNVAEQFTGQPGSYVPVAETVRGF 434
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 906780787 435 KEILDGKYDHLPEDAFRGVGSIEDVIAK 462
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
81-349 |
8.24e-56 |
|
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: 186.61 E-value: 8.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 81 SVPVGKETLGRVFNVLGDTIDLEAPFTEDaERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVG 160
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEP-ERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 161 KTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvE 240
Cdd:cd01136 80 KSTLLGMIARNTDAD---VNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRD-Q 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 241 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIYVPADDYTDPAPATAFA 320
Cdd:cd01136 156 GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRS 235
|
250 260
....*....|....*....|....*....
gi 906780787 321 HLDSTTNLERKLVQLGIYPAVDPLASSSR 349
Cdd:cd01136 236 ILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
62-412 |
2.76e-53 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 185.02 E-value: 2.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 62 ESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPftEDAERQPIHKKAPTFDELSTSSEILETGIKVIDL 141
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPP--LTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 142 LAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGA 221
Cdd:PRK06820 157 ILSCGEGQRIGIFAAAGVGKSTLLGMLCADSAAD---VMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 222 RMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQ 301
Cdd:PRK06820 234 RLKGLSTATTIAEYFRD-RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFY 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 302 AIYVPADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRALaPEIVGEEHYAVAAEVKRVLQRYHELQDII 381
Cdd:PRK06820 313 TVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIELLV 391
|
330 340 350
....*....|....*....|....*....|....*
gi 906780787 382 AI----LGMDELSDEEktlVARARRIQFFLSQNFN 412
Cdd:PRK06820 392 RVgeyqAGEDLQADEA---LQRYPAICAFLQQDHS 423
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
66-409 |
3.62e-50 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 176.48 E-value: 3.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 66 GLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDlEAPFTEDAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPY 145
Cdd:PRK06936 81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFD-GGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 146 LKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGND-LYWEMKESGvIEKTAMVFGQMNEPPGARMR 224
Cdd:PRK06936 160 GEGQRMGIFAAAGGGKSTLLASLIRSAEVD---VTVLALIGERGREVREfIESDLGEEG-LRKAVLVVATSDRPSMERAK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 225 VALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIY 304
Cdd:PRK06936 236 AGFVATSIAEYFRD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 305 VPADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRALApEIVGEEHYAVAAEVKRVLQRYHELQDIIAI- 383
Cdd:PRK06936 315 VEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIg 393
|
330 340
....*....|....*....|....*....
gi 906780787 384 ---LGMDELSDEEktlVARARRIQFFLSQ 409
Cdd:PRK06936 394 eyqKGQDKEADQA---IERIGAIRGFLRQ 419
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
63-417 |
1.89e-48 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 171.72 E-value: 1.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 63 STDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLG---DTIDLEAPFTEDAERQPIHKKAPTFDELSTSSEILETGIKVI 139
Cdd:PRK08149 63 NAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGkivERFDAPPTVGPISEERVIDVAPPSYAERRPIREPLITGVRAI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 140 DLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPP 219
Cdd:PRK08149 143 DGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEAD---VFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 220 GARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTS 299
Cdd:PRK08149 220 VDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 300 IQAIYVPADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRaLAPEIVGEEHYAVAAEVKRVLQRYHELQD 379
Cdd:PRK08149 299 FYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSR-VFGQVTDPKHRQLAAAFRKLLTRLEELQL 377
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 906780787 380 IIAiLGMDELSDEEKTLVARARRIQF--FLSQNFNVAEQF 417
Cdd:PRK08149 378 FID-LGEYRRGENADNDRAMDKRPALeaFLKQDVAEKSSF 416
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
42-438 |
9.55e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 169.87 E-value: 9.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 42 KIVLEVALELGDGMVRTIAMES--------TDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFtEDAERQ 113
Cdd:PRK08472 44 KIESSDNGKECLGMVVVIEKEQfgispfsfIEGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAI-DYERYA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 114 PIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHN-IAQehggISVFAGVGERTRE- 191
Cdd:PRK08472 123 PIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGcLAP----IKVVALIGERGREi 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 192 --------GNDLywemkesgviEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSA 263
Cdd:PRK08472 199 pefieknlGGDL----------ENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKN-QGLDVLFIMDSVTRFAMAQREIGL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 264 LLGRMPSAVGYQPTLATEMGQLQERITSTK-KGSVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVD 342
Cdd:PRK08472 268 ALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPIN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 343 PLASSSRaLAPEIVGEEHYAVAAEVKRVLQRYHELQDIIAI----LGMDELSDEEktlVARARRIQFFLSQNFNvaEQFt 418
Cdd:PRK08472 348 ILNSASR-VMNDIISPEHKLAARKFKRLYSLLKENEVLIRIgayqKGNDKELDEA---ISKKEFMEQFLKQNPN--ELF- 420
|
410 420
....*....|....*....|
gi 906780787 419 gqpgsyvPVAETVRGFKEIL 438
Cdd:PRK08472 421 -------PFEQTFEQLEEIL 433
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
42-409 |
6.01e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 167.85 E-value: 6.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 42 KIVLEV-ALELGDGMVrtIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEApftEDAERQPIHKKAP 120
Cdd:PRK06793 52 NVLCEViAIEKENNML--LPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEA---ENIPLQKIKLDAP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 121 TFDELSTS--SEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGND-LYW 197
Cdd:PRK06793 127 PIHAFEREeiTDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKAD---INVISLVGERGREVKDfIRK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 198 EMKESGvIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAvGYQPT 277
Cdd:PRK06793 204 ELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 278 LATEMGQLQERITSTKKGSVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRALApEIVG 357
Cdd:PRK06793 281 MESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVS 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 906780787 358 EEHYAVAAEVKRVLQRYHElQDIIAILGMDELSDEEKTLVARARRIQF---FLSQ 409
Cdd:PRK06793 360 PNHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAYIFECKNKVEGintFLKQ 413
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
4-383 |
8.03e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 164.90 E-value: 8.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 4 GKIAQVIGPVVDvlfaagEKLPE--INNALVVYKNDERKTKIVLEVaLELGDGMVRTIAMESTDGLTRGMEVLDTGRPIS 81
Cdd:PRK07721 20 GKVSRVIGLMIE------SKGPEssIGDVCYIHTKGGGDKAIKAEV-VGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 82 VPVGKETLGRVFNVLGDTIDLE------APFTEDA------ERQPIhkkaptfdelstsSEILETGIKVIDLLAPYLKGG 149
Cdd:PRK07721 93 VKVGSGLIGQVLDALGEPLDGSalpkglAPVSTDQdppnplKRPPI-------------REPMEVGVRAIDSLLTVGKGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 150 KVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGND-LYWEMKESGvIEKTAMVFGQMNEPPGARMRVALT 228
Cdd:PRK07721 160 RVGIFAGSGVGKSTLMGMIARNTSAD---LNVIALIGERGREVREfIERDLGPEG-LKRSIVVVATSDQPALMRIKGAYT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 229 GLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIYVPAD 308
Cdd:PRK07721 236 ATAIAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGD 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 906780787 309 DYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRALaPEIVGEEHYAVAAEVKRVLQRYHELQDIIAI 383
Cdd:PRK07721 315 DMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
90-385 |
1.59e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 164.40 E-value: 1.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 90 GRVFNVLGDTIDLEAPFTEDAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELi 169
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 170 hniAQEHGGISV-FAGVGERTREGNdlywEMKE---SGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVL 245
Cdd:PRK06002 186 ---ARADAFDTVvIALVGERGREVR----EFLEdtlADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRD-RGENVL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 246 LFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI--TSTKKGSVTSIQAIYVPADDYTDPAPATAFAHLD 323
Cdd:PRK06002 258 LIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLD 337
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 906780787 324 STTNLERKLVQLGIYPAVDPLASSSRaLAPEIVGEEHYAVAAEVKRVLQRYHELQDIIAILG 385
Cdd:PRK06002 338 GHIVLDRAIAEQGRYPAVDPLASISR-LARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
62-441 |
4.32e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 160.25 E-value: 4.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 62 ESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEDaerQPIHKKAPTFDELSTS--SEILETGIKVI 139
Cdd:PRK08972 77 EELRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTD---QRASRHSPPINPLSRRpiTEPLDVGVRAI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 140 DLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYWE-MKESGViEKTAMVFGQMNEP 218
Cdd:PRK08972 154 NAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEiLGEEGR-ARSVVVAAPADTS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 219 PGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI--TSTKKGS 296
Cdd:PRK08972 230 PLMRLKGCETATTIAEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAgnGGPGQGS 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 297 VTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRaLAPEIVGEEHYAVAAEVKRVLQRYHE 376
Cdd:PRK08972 309 ITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISR-VMPMVISEEHLEAMRRVKQVYSLYQQ 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 906780787 377 LQDIIAILGMDELSDEEKTLVARAR-RIQFFLSQNFNVAeqftgqpgsyVPVAETVRGFKEILDGK 441
Cdd:PRK08972 388 NRDLISIGAYKQGSDPRIDNAIRLQpAMNAFLQQTMKEA----------VPYDMSVNMLKQLAAQC 443
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
54-409 |
5.68e-44 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 159.93 E-value: 5.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 54 GMVRTIAMES----TDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEDaERQPIHKKAPTFDELSTSS 129
Cdd:PRK09099 66 GFSRDVALLSpfgeLGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCD-ELVPVIAAPPDPMSRRMVE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 130 EILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYWEMKESGVIEKTA 209
Cdd:PRK09099 145 APLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 210 MVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI 289
Cdd:PRK09099 222 VVCATSDRSSIERAKAAYVATAIAEYFRD-RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 290 TSTKKGSVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRALaPEIVGEEHYAVAAEVKR 369
Cdd:PRK09099 301 GMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQ 379
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 906780787 370 VLQRYHELQDIIAI----LGMDELSDEEktlVARARRIQFFLSQ 409
Cdd:PRK09099 380 LLAKHREVETLLQVgeyrAGSDPVADEA---IAKIDAIRDFLSQ 420
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
57-410 |
2.37e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 158.22 E-value: 2.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 57 RTIAM--ESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEDAERQPIHKKAPTFDELSTSSEILET 134
Cdd:PRK08927 65 RALLMpfGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPYPLRAPPPPAHSRARVGEPLDL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 135 GIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTRE-----GNDLYWE-MKESGVIEKT 208
Cdd:PRK08927 145 GVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREvqeflQDDLGPEgLARSVVVVAT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 209 AmvfgqmNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQER 288
Cdd:PRK08927 222 S------DEPALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLER 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 289 I--TSTKKGSVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRALaPEIVGEEHYAVAAE 366
Cdd:PRK08927 295 AgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRR 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 906780787 367 VKRVLQRYHELQDIIAI----LGMDELSDEEktlVARARRIQFFLSQN 410
Cdd:PRK08927 374 ARQLMATYADMEELIRLgayrAGSDPEVDEA---IRLNPALEAFLRQG 418
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
63-392 |
8.82e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 156.65 E-value: 8.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 63 STDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTID-----------LEAPFTEDAERQPIhkkaptfdelstsSEI 131
Cdd:PRK07594 72 STIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDgrelpdvcwkdYDAMPPPAMVRQPI-------------TQP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 132 LETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIhniAQEHGGISVFAGVGERTREGNDLYWEMKESGVIEKTAMV 211
Cdd:PRK07594 139 LMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLC---NAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 212 FGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITS 291
Cdd:PRK07594 216 VATSDRPALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGM 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 292 TKKGSVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRALaPEIVGEEHYAVAAEVKRVL 371
Cdd:PRK07594 295 GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCL 373
|
330 340
....*....|....*....|....*
gi 906780787 372 QRYHELQDIIAI----LGMDELSDE 392
Cdd:PRK07594 374 ALYQEVELLIRIgeyqRGVDTDTDK 398
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
63-412 |
9.18e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 156.81 E-value: 9.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 63 STDGLTRGMEVL---DTGRpisVPVGKETLGRVFNVLGDTIDLEAPFTEDAErqpIHKKAPTFDELSTS--SEILETGIK 137
Cdd:PRK05688 84 SVAGIAPGARVVplaDTGR---LPMGMSMLGRVLDGAGRALDGKGPMKAEDW---VPMDGPTINPLNRHpiSEPLDVGIR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 138 VIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNE 217
Cdd:PRK05688 158 SINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEAD---IIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 218 PPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKK--G 295
Cdd:PRK05688 235 APLMRLRAAMYCTRIAEYFRD-KGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPggG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 296 SVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRALaPEIVGEEHYAVAAEVKRVLQRYH 375
Cdd:PRK05688 314 SITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQ 392
|
330 340 350
....*....|....*....|....*....|....*...
gi 906780787 376 ELQDIIAILGMDELSDEEKTL-VARARRIQFFLSQNFN 412
Cdd:PRK05688 393 QSRDLISVGAYVAGGDPETDLaIARFPHLVQFLRQGLR 430
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
66-410 |
4.20e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 154.66 E-value: 4.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 66 GLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEDAerqPIHKKAPTFDELSTSS--EILETGIKVIDLLA 143
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGST---PLQQQLPQIHPLQRRAvdTPLDVGVNAINGLL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 144 PYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARM 223
Cdd:PRK07196 151 TIGKGQRVGLMAGSGVGKSVLLGMITRYTQAD---VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRI 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 224 RVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI-TSTKKGSVTSIQA 302
Cdd:PRK07196 228 KATELCHAIATYYRD-KGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMTAIYT 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 303 IYVPADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRALApEIVGEEHYAVAAEVKRVLQRYHELQDIIA 382
Cdd:PRK07196 307 VLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAIKPLIP 385
|
330 340 350
....*....|....*....|....*....|..
gi 906780787 383 ----ILGMDELSDEEktlVARARRIQFFLSQN 410
Cdd:PRK07196 386 lggyVAGADPMADQA---VHYYPAITQFLRQE 414
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
67-439 |
2.78e-36 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 138.88 E-value: 2.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 67 LTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEdAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYL 146
Cdd:PRK05922 77 VALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPK-THLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 147 KGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDlYWEMKESGVIE-KTAMVFGQMNEPPGARMRV 225
Cdd:PRK05922 156 KGQRIGVFSEPGSGKSSLLSTIAKGSKST---INVIALIGERGREVRE-YIEQHKEGLAAqRTIIIASPAHETAPTKVIA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 226 ALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAI-Y 304
Cdd:PRK05922 232 GRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlH 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 305 VP--ADDYTDPAPATAFAHLdSTTNLERKLVQlgiyPAVDPLASSSRAlAPEIVGEEHYAVAAEVKRVLQRYHELQDIIA 382
Cdd:PRK05922 311 YPnhPDIFTDYLKSLLDGHF-FLTPQGKALAS----PPIDILTSLSRS-ARQLALPHHYAAAEELRSLLKAYHEALDIIQ 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 906780787 383 ILGMDELSDEEktlVARARRIqfflsqnFNVAEQFTGQP-GSYVPVAETVRGFKEILD 439
Cdd:PRK05922 385 LGAYVPGQDAH---LDRAVKL-------LPSIKQFLSQPlSSYCALHNTLKQLEALLK 432
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
5-412 |
4.50e-36 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 138.81 E-value: 4.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 5 KIAQVIGPVVDVLFAAGEKLPEINNalVVYKNDERKTKIVLEValelGDGMVRTIAMESTDGL-TRGMEVLDTGRPISVP 83
Cdd:PRK04196 6 TVSEIKGPLLFVEGVEGVAYGEIVE--IELPNGEKRRGQVLEV----SEDKAVVQVFEGTTGLdLKDTKVRFTGEPLKLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 84 VGKETLGRVFNVLGDTID-LEAPFTEDaeRQPIHKKA--PTFDElsTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGvg 160
Cdd:PRK04196 80 VSEDMLGRIFDGLGRPIDgGPEIIPEK--RLDINGAPinPVARE--YPEEFIQTGISAIDGLNTLVRGQKLPIFSGSG-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 161 ktvliqeLIHN-----IAQ-------EHGGISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARM---RV 225
Cdd:PRK04196 154 -------LPHNelaaqIARqakvlgeEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERIltpRM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 226 AltgLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQER--ITSTKKGSVTSIQAI 303
Cdd:PRK04196 227 A---LTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPIL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 304 YVPADDYTDPAPatafahlDST---TN----LERKLVQLGIYPAVDPLASSSRaLAPEIVG-----EEHYAVAAEVKRVL 371
Cdd:PRK04196 304 TMPDDDITHPIP-------DLTgyiTEgqivLSRELHRKGIYPPIDVLPSLSR-LMKDGIGegktrEDHKDVANQLYAAY 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 906780787 372 QRYHELQDIIAILGMDELSDEEKTLVARARRI-QFFLSQNFN 412
Cdd:PRK04196 376 ARGKDLRELAAIVGEEALSERDRKYLKFADAFeREFVNQGFD 417
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
16-409 |
9.10e-36 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 137.61 E-value: 9.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 16 VLFAAGEKLPEINNALVvykndERKT-KIVLEVALEL----GDGMVrTIAMESTDGLTRGMEVLdtGRPIS--------- 81
Cdd:PRK07960 38 VLEATGLQLPLGATCVI-----ERQNgSETHEVESEVvgfnGQRLF-LMPLEEVEGILPGARVY--ARNISgeglqsgkq 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 82 VPVGKETLGRVFNVLGDTID-LEAPftEDAERQPIHkkAPTFDELSTS--SEILETGIKVIDLLAPYLKGGKVGLFGGAG 158
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDgLPAP--DTGETGALI--TPPFNPLQRTpiEHVLDTGVRAINALLTVGRGQRMGLFAGSG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 159 VGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRD 238
Cdd:PRK07960 186 VGKSVLLGMMARYTQAD---VIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 239 vEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITS--TKKGSVTSIQAIYVPADDYTDPAPA 316
Cdd:PRK07960 263 -RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIAD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 317 TAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRALApEIVGEEHYAVAAEVKRVLQRYHELQDIIAI----LGMDELSDE 392
Cdd:PRK07960 342 SARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALIDEQHYARVRQFKQLLSSFQRNRDLVSVgayaKGSDPMLDK 420
|
410
....*....|....*..
gi 906780787 393 EKTLVArarRIQFFLSQ 409
Cdd:PRK07960 421 AIALWP---QLEAFLQQ 434
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
2-80 |
5.68e-32 |
|
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: 116.85 E-value: 5.68e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 906780787 2 SSGKIAQVIGPVVDVLFAAGEkLPEINNALVVykNDERKTKIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPI 80
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGE-LPPIYNALEV--KGDDGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
79-349 |
1.17e-31 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 122.72 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 79 PISVPVGKETLGRVFNVLGDTIDLEAPFTEDAER----QPIHKKAPTFDElstssEILETGIKVIDLLAPYLKGGKVGLF 154
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLdingPPINPVARIYPE-----EMIQTGISAIDVMNTLVRGQKLPIF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 155 GGAGvgktvliqeLIHN-----IA-------QEHGGISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGAR 222
Cdd:cd01135 76 SGSG---------LPHNelaaqIArqagvvgSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIER 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 223 MRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQER--ITSTKKGSVTSI 300
Cdd:cd01135 147 IITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQI 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 906780787 301 QAIYVPADDYTDPAPatafahlDST---TN----LERKLVQLGIYPAVDPLASSSR 349
Cdd:cd01135 227 PILTMPNDDITHPIP-------DLTgyiTEgqiyLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
47-466 |
1.92e-31 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 126.18 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 47 VALELGDGMVRTIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPfTEDAERQPIHKKAPTFDELS 126
Cdd:PRK13343 62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGP-LQATARRPLERPAPAIIERD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 127 TSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIhnIAQEHGG-ISVFAGVGERTREGNDLYWEMKESGVI 205
Cdd:PRK13343 141 FVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAI--INQKDSDvICVYVAIGQKASAVARVIETLREHGAL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 206 EKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQL 285
Cdd:PRK13343 219 EYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 286 QERIT--STKK--GSVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRalapeiVG--EE 359
Cdd:PRK13343 298 LERAAklSPELggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR------VGgkAQ 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 360 HYAVAAEVKRV---LQRYHELQdIIAILGMDeLSDEEKTLVARARRIQFFLSQN----FNVAEQ----FTGQPGSY--VP 426
Cdd:PRK13343 372 HPAIRKESGRLrldYAQFLELE-AFTRFGGL-LDAGTQKQITRGRRLRELLKQPrfspLSVEEQiallYALNEGLLdaVP 449
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 906780787 427 VAEtVRGFKEILDGKYDHLPEDAFRGVGSIEDVIAKAEKM 466
Cdd:PRK13343 450 LAN-IQAFEERLLEKLDARFAALSLALESPRELDEAWLAA 488
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
79-349 |
9.93e-31 |
|
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: 119.99 E-value: 9.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 79 PISVPVGKETLGRVF----NVLGDTIDLEAPFTE---DAERQPIHKKAPTFDELsTSSEILETGIKVIDLLAPYLKGGKV 151
Cdd:cd01134 1 PLSVELGPGLLGSIFdgiqRPLEVIAETGSIFIPrgvNVQRWPVRQPRPVKEKL-PPNVPLLTGQRVLDTLFPVAKGGTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 152 GLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERtreGND----------LYWEMKESGVIEKTAMVFGQMNEPPGA 221
Cdd:cd01134 80 AIPGPFGCGKTVISQSLSKWSNSD---VVIYVGCGER---GNEmaevleefpeLKDPITGESLMERTVLIANTSNMPVAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 222 RMRVALTGLTIAEYFRDVeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI-------TSTKK 294
Cdd:cd01134 154 REASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSPGRE 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 906780787 295 GSVTSIQAIYVPADDYTDP-APAT-----AFAHLDsttnleRKLVQLGIYPAVDPLASSSR 349
Cdd:cd01134 233 GSVTIVGAVSPPGGDFSEPvTQATlrivqVFWGLD------KKLAQRRHFPSINWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
80-410 |
1.22e-29 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 121.81 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 80 ISVPVGKEtlGRVFNVLGD---TID-----LEAPFTEDAERQPIHK----KAPTFDELSTSSEILETGIKVIDLLAPYLK 147
Cdd:PRK04192 149 IMVPPGVS--GTVKEIVSEgdyTVDdtiavLEDEDGEGVELTMMQKwpvrRPRPYKEKLPPVEPLITGQRVIDTFFPVAK 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 148 GGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERtreGNdlywEMKE------------SG--VIEKTAMVFG 213
Cdd:PRK04192 227 GGTAAIPGPFGSGKTVTQHQLAKWADAD---IVIYVGCGER---GN----EMTEvleefpelidpkTGrpLMERTVLIAN 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 214 QMNEPPGARMRVALTGLTIAEYFRDVeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQER----I 289
Cdd:PRK04192 297 TSNMPVAAREASIYTGITIAEYYRDM-GYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvK 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 290 T-STKKGSVTSIQAIYVPADDYTDP-APAT-----AFAHLDsttnleRKLVQLGIYPAVDPLASSSR---ALAP---EIV 356
Cdd:PRK04192 376 TlGGEEGSVTIIGAVSPPGGDFSEPvTQNTlrivkVFWALD------AELADRRHFPAINWLTSYSLyldQVAPwweENV 449
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 906780787 357 GEEHYAVAAEVKRVLQRYHELQDIIAILGMDELSDEEKTLVARARRIQF-FLSQN 410
Cdd:PRK04192 450 DPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIREdFLQQN 504
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
168-453 |
5.05e-23 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 102.79 E-value: 5.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 168 LIHNIAQEH-------GGISVFAGVGERTREGNDLYWEMKE-------SGVIEKTAMVFGQMNEPPGARMRVALTGLTIA 233
Cdd:PRK14698 666 LLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIA 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 234 EYFRDVeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI-------TSTKKGSVTSIQAIYVP 306
Cdd:PRK14698 746 EYFRDM-GYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPP 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 307 ADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRALAP------EIVGEEHYAVAAEVKRVLQRYHELQDI 380
Cdd:PRK14698 825 GGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEI 904
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 906780787 381 IAILGMDELSDEEKT--LVARARRIQFFLSQNFNVAEqftgqpgSYVPVAETVRGFKEILDgKYDHLPEDAFRGV 453
Cdd:PRK14698 905 VRIVGPDALPERERAilLVARMLREDYLQQDAFDEVD-------TYCPPEKQVTMMRVLLN-FYDKTMDAISRGV 971
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
6-394 |
3.85e-22 |
|
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: 98.64 E-value: 3.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 6 IAQVIGPVVDVLFAAGEKLPEINNaLVVYKNDERKTKiVLEVAlelGDGMVRTIaMESTDGLTRGMEVLD-TGRPISVPV 84
Cdd:TIGR01040 5 VSGVNGPLVILDNVKFPRFAEIVN-LTLPDGTVRSGQ-VLEVS---GNKAVVQV-FEGTSGIDAKKTTCEfTGDILRTPV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 85 GKETLGRVFNVLGDTIDLEAP-FTE---DAERQPIHKKAPTFDElstssEILETGIKVIDLLAPYLKGGKVGLFGGAG-- 158
Cdd:TIGR01040 79 SEDMLGRVFNGSGKPIDKGPPvLAEdylDINGQPINPYARIYPE-----EMIQTGISAIDVMNSIARGQKIPIFSAAGlp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 159 -----------VGKTVLIQELIHNIAQEHGGIsVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVAL 227
Cdd:TIGR01040 154 hneiaaqicrqAGLVKLPTKDVHDGHEDNFAI-VFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 228 TGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI--TSTKKGSVTSIQAIYV 305
Cdd:TIGR01040 233 LALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 306 PADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRaLAPEIVGE-----EHYAVAAEVKRVLQRYHELQDI 380
Cdd:TIGR01040 313 PNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSR-LMKSAIGEgmtrkDHSDVSNQLYACYAIGKDVQAM 391
|
410
....*....|....
gi 906780787 381 IAILGMDELSDEEK 394
Cdd:TIGR01040 392 KAVVGEEALSSEDL 405
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
80-349 |
7.14e-22 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 94.93 E-value: 7.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 80 ISVPVGKETLGRVFNVLGDTIDLEAPFTEDaERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGV 159
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTK-ERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 160 GKTVLIQELIHNiAQEHGGISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDv 239
Cdd:cd01132 81 GKTAIAIDTIIN-QKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRD- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 240 EGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKK----GSVTSIQAIYVPADDYTDPAP 315
Cdd:cd01132 159 NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSLTALPIIETQAGDVSAYIP 238
|
250 260 270
....*....|....*....|....*....|....
gi 906780787 316 ATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSR 349
Cdd:cd01132 239 TNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
5-315 |
9.18e-19 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 88.17 E-value: 9.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 5 KIAQVIGPVVDVLfAAGEKLPEInnALVVYKNDERKTKIVL----EVALELGDGmvrtiamesTDGLTRGMEVLDTGRPI 80
Cdd:PRK02118 7 KITDITGNVITVE-AEGVGYGEL--ATVERKDGSSLAQVIRldgdKVTLQVFGG---------TRGISTGDEVVFLGRPM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 81 SVPVGKETLGRVFNVLGDTIDLEApfteDAERQPIHKKAPTFDELS--TSSEILETGIKVIDLLAPYLKGGKVGLFGGAG 158
Cdd:PRK02118 75 QVTYSESLLGRRFNGSGKPIDGGP----ELEGEPIEIGGPSVNPVKriVPREMIRTGIPMIDVFNTLVESQKIPIFSVSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 159 VGktvlIQELIHNIA-QEHGGISVFAGVGERtregNDLYW----EMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIA 233
Cdd:PRK02118 151 EP----YNALLARIAlQAEADIIILGGMGLT----FDDYLffkdTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 234 EYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKK-GSVTSIQAIYVPADDYTD 312
Cdd:PRK02118 223 EKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEDgGSITIIAVTTMPGDDVTH 302
|
...
gi 906780787 313 PAP 315
Cdd:PRK02118 303 PVP 305
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-77 |
2.45e-17 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 76.04 E-value: 2.45e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 906780787 6 IAQVIGPVVDVLFAAGeKLPEINNALVVYKNDerKTKIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTG 77
Cdd:pfam02874 1 IVQVIGPVVDVEFGIG-RLPGLLNALEVELVE--FGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
53-377 |
3.81e-17 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 83.94 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 53 DGMVRTIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDL------EAPFTEDAERQPIHKKAPTFDELS 126
Cdd:PTZ00185 88 DGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPVglltrsRALLESEQTLGKVDAGAPNIVSRS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 127 TSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHN-------IAQEHGGISVFAGVGERTREGNDLYWEM 199
Cdd:PTZ00185 168 PVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSNVARIHRLL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 200 KESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLA 279
Cdd:PTZ00185 248 RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVF 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 280 TEMGQLQER--ITSTKK--GSVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLVQLGIYPAVDPLASSSRaLAPEI 355
Cdd:PTZ00185 327 YLHSRLLERaaMLSPGKggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR-VGSSA 405
|
330 340
....*....|....*....|..
gi 906780787 356 VGEEHYAVAAEVKRVLQRYHEL 377
Cdd:PTZ00185 406 QNVAMKAVAGKLKGILAEYRKL 427
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
44-269 |
6.04e-17 |
|
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: 83.16 E-value: 6.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 44 VLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEDaERQPIHKKAPTFD 123
Cdd:COG0056 59 VYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAE-ERRPVERPAPGVI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 124 ELSTSSEILETGIKVIDLLAPylkggkVG------LFGGAGVGKTVLIQELIhnIAQEHGG-ISVFAGVGERT----REG 192
Cdd:COG0056 138 DRQPVHEPLQTGIKAIDAMIP------IGrgqrelIIGDRQTGKTAIAIDTI--INQKGKDvICIYVAIGQKAstvaQVV 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 906780787 193 NDLywemKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 269
Cdd:COG0056 210 ETL----EEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMD-QGKDVLIVYDDLSKHAVAYRELSLLLRRPP 281
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
360-420 |
3.18e-16 |
|
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: 72.86 E-value: 3.18e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 906780787 360 HYAVAAEVKRVLQRYHELQDIIAILGMDELSDEEKTLVARARRIQFFLSQNFNVAEQFTGQ 420
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDT 61
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
44-269 |
1.44e-15 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 78.95 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 44 VLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFtEDAERQPIHKKAPTFD 123
Cdd:PRK09281 59 VYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPI-EATETRPVERKAPGVI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 124 ELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIhnIAQEHGGI-----------SVFAGVGErtreg 192
Cdd:PRK09281 138 DRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTI--INQKGKDViciyvaigqkaSTVAQVVR----- 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 906780787 193 ndlywEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 269
Cdd:PRK09281 211 -----KLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
65-269 |
7.65e-13 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 70.38 E-value: 7.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 65 DGLT--RGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEDAERqPIHKKAPTFDELSTSSEILETGIKVIDLL 142
Cdd:CHL00059 57 DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESR-LIESPAPGIISRRSVYEPLQTGLIAIDSM 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 143 APYLKGGKVGLFGGAGVGKTVLIQELIHNiAQEHGGISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGAR 222
Cdd:CHL00059 136 IPIGRGQRELIIGDRQTGKTAVATDTILN-QKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQ 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 906780787 223 MRVALTGLTIAEYFRdVEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 269
Cdd:CHL00059 215 YLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
66-349 |
7.62e-12 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 66.65 E-value: 7.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 66 GLTRGMEVLDTGRPISvpvGKETLGRVFNVLGDTIDLEAPFTEDAERQPIHKKAPTFDELSTSSEILetgiKVIDLLAPY 145
Cdd:PRK12608 58 NLRTGDVVEGVARPRE---RYRVLVRVDSVNGTDPEKLARRPHFDDLTPLHPRERLRLETGSDDLSM----RVVDLVAPI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 146 LKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAG-VGERTREGNDlyweMKESgvieKTAMVFGQMNEPPGARmR 224
Cdd:PRK12608 131 GKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTD----MRRS----VKGEVYASTFDRPPDE-H 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 225 VALTGLTIAEYFRDVE-GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAvgyqpTLATEMGQLQERITSTKK-----GSVT 298
Cdd:PRK12608 202 IRVAELVLERAKRLVEqGKDVVILLDSLTRLARAYNNEVESSGRTLSG-----GVDARALQRPKRLFGAARnieegGSLT 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 906780787 299 SIQAIYVP----ADDYTdpapataFAHLDSTTNLE----RKLVQLGIYPAVDPLASSSR 349
Cdd:PRK12608 277 IIATALVDtgsrMDEVI-------FEEFKGTGNMEivldRELADKRVFPAIDIAKSGTR 328
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
137-349 |
3.04e-08 |
|
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: 54.52 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 137 KVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAG-VGERTREGNDlyweMKESGVIEKTAMVFgqm 215
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRSVKGEVVASTF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 216 NEPPGARMRVALTGLTIAEyfRDVE-GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAvGYQPTLAtemgQLQERITSTKK 294
Cdd:cd01128 78 DEPPERHVQVAEMVIEKAK--RLVEhGKDVVILLDSITRLARAYNTVVPSSGKTLSG-GVDANAL----HKPKRFFGAAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 906780787 295 -----GSVTSIQAIYVPADDYTDPApatAFAHLDSTTNLE----RKLVQLGIYPAVDPLASSSR 349
Cdd:cd01128 151 nieegGSLTIIATALVDTGSRMDEV---IFEEFKGTGNMElvldRKLAEKRIFPAIDILKSGTR 211
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
4-78 |
6.79e-07 |
|
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: 46.54 E-value: 6.79e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 906780787 4 GKIAQVIGPVVDvlfAAGEKLPEINNALVVYKNDERKTKIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGR 78
Cdd:cd01426 2 GRVIRVNGPLVE---AELEGEVAIGEVCEIERGDGNNETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
125-388 |
3.52e-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: 49.30 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 125 LSTSSEILETgiKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAG-VGERTREGNDlyweMKESG 203
Cdd:TIGR00767 147 LETSTEDLST--RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVELIVLlIDERPEEVTD----MQRSV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 204 VIEKTAMVFgqmNEPPGARMRVAltGLTIAEYFRDVE-GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAvGYQPTLAtem 282
Cdd:TIGR00767 221 KGEVVASTF---DEPASRHVQVA--EMVIEKAKRLVEhKKDVVILLDSITRLARAYNTVTPASGKVLSG-GVDANAL--- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 283 gQLQERITSTKK-----GSVTSIQAIYVPADDYTDpapATAFAHLDSTTNLE----RKLVQLGIYPAVDPLASSSRalAP 353
Cdd:TIGR00767 292 -HRPKRFFGAARnieegGSLTIIATALIDTGSRMD---EVIFEEFKGTGNMElhldRKLADRRIFPAIDIKKSGTR--KE 365
|
250 260 270
....*....|....*....|....*....|....*.
gi 906780787 354 EI-VGEEHyavaaevkrvLQRYHELQDIIAilGMDE 388
Cdd:TIGR00767 366 ELlLTPEE----------LQKIWVLRKIIS--PMDS 389
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
147-268 |
6.93e-06 |
|
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: 45.83 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 147 KGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGvgertregndlywEMKESGVIEKTAMVFGQMNEPPGARMRVA 226
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------EDILEEVLDQLLLIIVGGKKASGSGELRL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 906780787 227 LTGLTIAEYFRdvegqDVLLFIDNIFRFTQAGSEVSALLGRM 268
Cdd:smart00382 68 RLALALARKLK-----PDVLILDEITSLLDAEQEALLLLLEE 104
|
|
| ATP-synt_V_A-type_alpha_C |
cd18111 |
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of ... |
365-410 |
5.77e-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: 39.29 E-value: 5.77e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 906780787 365 AEVKRVLQRYHELQDIIAILGMDELSDEEK-TL-VARARRiQFFLSQN 410
Cdd:cd18111 6 TEAMEILQEEAELQEIVQLVGPDALPEEDRlTLeVARMIR-EDFLQQN 52
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
356-432 |
1.10e-03 |
|
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family of ATPases that form part of the Type III secretion system (T3SS) present in Escherichia coli. T3SS is a macromolecular complex that creates a syringe-like apparatus extending from the bacterial cytosol across three membranes to the eukaryotic cytosol. This process is essential for pathogenicity. EscN is a functionally unique ATPase that provides an inner-membrane recognition gate for the T3SS chaperone-virulence effector complexes as well as a potential source of energy for their subsequent secretion.The C-terminal domain of T3SS ATPases mediates binding with multiple contact points along the chaperone.
Pssm-ID: 465691 [Multi-domain] Cd Length: 70 Bit Score: 37.41 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 356 VGEEHYAVAAEVKRVLQRYHELQDIIAI----LGMDELSDEektlvARARR--IQFFLSQNfnvaeqftgqPGSYVPVAE 429
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIgayqAGSDPEIDE-----AIAKRpaINAFLRQG----------VDEPVSFEE 65
|
...
gi 906780787 430 TVR 432
Cdd:pfam18269 66 TLA 68
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
117-349 |
1.37e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 40.89 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 117 KKAPTFDELS----TSSEILETGI------KVIDLLAPYLKGGKvGLFggagV-----GKTVLIQELIHNIAQEHGGISV 181
Cdd:PRK09376 128 RNRPLFENLTplypNERLRLETGNpedlstRIIDLIAPIGKGQR-GLI----VappkaGKTVLLQNIANSITTNHPEVHL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 182 FAG-VGERTREGNDlyweMKES---GVIEKTamvfgqMNEPPGARMRVAltGLTIAEYFRDVE-GQDVLLFIDNIFRFTQ 256
Cdd:PRK09376 203 IVLlIDERPEEVTD----MQRSvkgEVVAST------FDEPAERHVQVA--EMVIEKAKRLVEhGKDVVILLDSITRLAR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 257 AGSEVSALLGRM------PSAVgYQPT------LATEMGqlqeritstkkGSVTSIqaiyvpaddytdpapATA------ 318
Cdd:PRK09376 271 AYNTVVPSSGKVlsggvdANAL-HRPKrffgaaRNIEEG-----------GSLTII---------------ATAlidtgs 323
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 906780787 319 ------FAHLDSTTN----LERKLVQLGIYPAVDPLASSSR 349
Cdd:PRK09376 324 rmdeviFEEFKGTGNmelhLDRKLAEKRIFPAIDINRSGTR 364
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
111-201 |
4.05e-03 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 39.62 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 111 ERQPIHKKAPTFDELSTSSEILeTGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIhnIAQEHGGISV------FAG 184
Cdd:PRK14698 191 QRWPVRVKRPYKEKLPPEVPLI-TGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDGDTLI--LTKEFGLIKIkdlyeiLDG 267
|
90
....*....|....*..
gi 906780787 185 VGERTREGNDLYWEMKE 201
Cdd:PRK14698 268 KGKKTVEGNEEWTELEE 284
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
86-208 |
5.15e-03 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 39.19 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906780787 86 KETLGRVFNVLGDTIDLEA----PFTEDAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGK 161
Cdd:PRK07165 77 KEYFGKIIDIDGNIIYPEAqnplSKKFLPNTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGK 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 906780787 162 TVLIQELIhnIAQEHGGIS-VFAGVGERTREGNDLYWEMKESGVIEKT 208
Cdd:PRK07165 157 THIALNTI--INQKNTNVKcIYVAIGQKRENLSRIYETLKEHDALKNT 202
|
|
| |
