|
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: 1034.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 1 MNSGKVVQVIGPVIDVEFAPGKLPDIYNAVVIRTEDQENkdfeidLTLEAAQHLGNNTVRCVAMSSTDGLVRGMKVIDTG 80
Cdd:COG0055 3 MNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEGGGE------LVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 81 KPISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAG 160
Cdd:COG0055 77 APISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 161 VGKTVLIQELIRNIAHEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQMNEPPGARQRIGLTGLTIAEYFRD 240
Cdd:COG0055 157 VGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 241 VQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTKQGSITSVQAVYVPADDLTDPAPATT 320
Cdd:COG0055 237 EEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 321 FAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILDPDIVGEEHYEVAIKVQEVLQTYKELQDIIAILGMDELSDEDKITVA 400
Cdd:COG0055 317 FAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1180564254 401 RARKIQRFFSQPFFVAEQFTGFPGKYVPVKETIRGFKEILEGKHDDLPEHAFLFVGTIDEAVEKAKK 467
Cdd:COG0055 397 RARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKK 463
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
2-467 |
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: 905.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 2 NSGKVVQVIGPVIDVEFAPGKLPDIYNAVVIRTEdqenkdFEIDLTLEAAQHLGNNTVRCVAMSSTDGLVRGMKVIDTGK 81
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNR------AESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 82 PISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAGV 161
Cdd:TIGR01039 75 PISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 162 GKTVLIQELIRNIAHEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQMNEPPGARQRIGLTGLTIAEYFRDV 241
Cdd:TIGR01039 155 GKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 242 QKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTKQGSITSVQAVYVPADDLTDPAPATTF 321
Cdd:TIGR01039 235 QGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 322 AHLDAQTVLNRAITEQGIYPAVDPLDSNSRILDPDIVGEEHYEVAIKVQEVLQTYKELQDIIAILGMDELSDEDKITVAR 401
Cdd:TIGR01039 315 AHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVER 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1180564254 402 ARKIQRFFSQPFFVAEQFTGFPGKYVPVKETIRGFKEILEGKHDDLPEHAFLFVGTIDEAVEKAKK 467
Cdd:TIGR01039 395 ARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKK 460
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
2-467 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 864.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 2 NSGKVVQVIGPVIDVEFAPGKLPDIYNAVVIrtEDQENKDFEIDLTLEAAQHLGNNTVRCVAMSSTDGLVRGMKVIDTGK 81
Cdd:CHL00060 15 NLGRITQIIGPVLDVAFPPGKMPNIYNALVV--KGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 82 PISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAGV 161
Cdd:CHL00060 93 PLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 162 GKTVLIQELIRNIAHEHGGYSVFAGVGERTREGNDLWHEMQDSGVID-------KTALVFGQMNEPPGARQRIGLTGLTI 234
Cdd:CHL00060 173 GKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 235 AEYFRDVQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTKQGSITSVQAVYVPADDLTD 314
Cdd:CHL00060 253 AEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 315 PAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILDPDIVGEEHYEVAIKVQEVLQTYKELQDIIAILGMDELSDE 394
Cdd:CHL00060 333 PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180564254 395 DKITVARARKIQRFFSQPFFVAEQFTGFPGKYVPVKETIRGFKEILEGKHDDLPEHAFLFVGTIDEAVEKAKK 467
Cdd:CHL00060 413 DRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAAN 485
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
84-355 |
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: 591.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 84 SVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAGVGK 163
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 164 TVLIQELIRNIAHEHGGYSVFAGVGERTREGNDLWHEMQDSGVI-----DKTALVFGQMNEPPGARQRIGLTGLTIAEYF 238
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVInldglSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 239 RDVQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTKQGSITSVQAVYVPADDLTDPAPA 318
Cdd:cd01133 161 RDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPA 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1180564254 319 TTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILDP 355
Cdd:cd01133 241 TTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
4-461 |
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: 590.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 4 GKVVQVIGPVIDVEFaPGKLPDIYNAVVIRTEDqenkdfeiDLTLEAAQHLGNNTVRCVAMSSTDGLVRGMKVIDTGKPI 83
Cdd:TIGR03305 1 GHVVAVRGSIVDVRF-DGELPAIHSVLRAGREG--------EVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 84 SVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAGVGK 163
Cdd:TIGR03305 72 KAPVGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 164 TVLIQELIRNIAHEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQMNEPPGARQRIGLTGLTIAEYFRDVQK 243
Cdd:TIGR03305 152 TVLLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 244 QDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTKQGSITSVQAVYVPADDLTDPAPATTFAH 323
Cdd:TIGR03305 232 QDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSH 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 324 LDAQTVLNRAITEQGIYPAVDPLDSNSRILDPDIVGEEHYEVAIKVQEVLQTYKELQDIIAILGMDELSDEDKITVARAR 403
Cdd:TIGR03305 312 LSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRAR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1180564254 404 KIQRFFSQPFFVAEQFTGFPGKYVPVKETIRGFKEILEGKHDDLPEHAFLFVGTIDEA 461
Cdd:TIGR03305 392 RLERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
84-352 |
2.64e-131 |
|
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: 380.26 E-value: 2.64e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 84 SVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAGVGK 163
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 164 TVLIQELIRNIAHEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQMNEPPGARQRIGLTGLTIAEYFRDvQK 243
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRD-NG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 244 QDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTK--QGSITSVQAVYVPADDLTDPAPATTF 321
Cdd:cd19476 160 QHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDPIPDNTF 239
|
250 260 270
....*....|....*....|....*....|.
gi 1180564254 322 AHLDAQTVLNRAITEQGIYPAVDPLDSNSRI 352
Cdd:cd19476 240 AILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
137-350 |
5.80e-100 |
|
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: 298.12 E-value: 5.80e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 137 GIKVIDLLAPYSKGGKVGLFGGAGVGKTVLIQELIRNIAHehgGYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQ 216
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 217 MNEPPGARQRIGLTGLTIAEYFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITST-- 294
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVkg 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1180564254 295 KQGSITSVQAVYVPADDLTDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNS 350
Cdd:pfam00006 157 KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
3-440 |
3.83e-77 |
|
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: 247.25 E-value: 3.83e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 3 SGKVVQVIGPVIDVEFAPGKLPDIynaVVIRTEDQENKDFEIdltleaaqhLG--NNTVRCVAMSSTDGLVRGMKVIDTG 80
Cdd:COG1157 20 SGRVTRVVGLLIEAVGPDASIGEL---CEIETADGRPVLAEV---------VGfrGDRVLLMPLGDLEGISPGARVVPTG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 81 KPISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAG 160
Cdd:COG1157 88 RPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 161 VGKTVLIQELIRNIAHEhggYSVFAGVGERTRE-----GNDLWHE-MQDSGVIDKTAlvfgqmNEPPGARQRIGLTGLTI 234
Cdd:COG1157 168 VGKSTLLGMIARNTEAD---VNVIALIGERGREvrefiEDDLGEEgLARSVVVVATS------DEPPLMRLRAAYTATAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 235 AEYFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTKQGSITSVQAVYVPADDLTD 314
Cdd:COG1157 239 AEYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMND 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 315 PAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILdPDIVGEEHYEVAIKVQEVLQTYKELQDIIAI----LGMDE 390
Cdd:COG1157 318 PIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLLARYEENEDLIRIgayqPGSDP 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1180564254 391 LSDEdkiTVARARKIQRFFSQPffvaeqftgfPGKYVPVKETIRGFKEIL 440
Cdd:COG1157 397 ELDE---AIALIPAIEAFLRQG----------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 ... |
357-464 |
1.89e-74 |
|
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: 228.90 E-value: 1.89e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 357 IVGEEHYEVAIKVQEVLQTYKELQDIIAILGMDELSDEDKITVARARKIQRFFSQPFFVAEQFTGFPGKYVPVKETIRGF 436
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 1180564254 437 KEILEGKHDDLPEHAFLFVGTIDEAVEK 464
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
84-352 |
1.28e-62 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 204.33 E-value: 1.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 84 SVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAGVGK 163
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 164 TVLIQELIRNIAHEhggYSVFAGVGERTREGND-LWHEMQDSGvIDKTALVFGQMNEPPGARQRIGLTGLTIAEYFRDvQ 242
Cdd:cd01136 81 STLLGMIARNTDAD---VNVIALIGERGREVREfIEKDLGEEG-LKRSVLVVATSDESPLLRVRAAYTATAIAEYFRD-Q 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 243 KQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTKQGSITSVQAVYVPADDLTDPAPATTFA 322
Cdd:cd01136 156 GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRS 235
|
250 260 270
....*....|....*....|....*....|
gi 1180564254 323 HLDAQTVLNRAITEQGIYPAVDPLDSNSRI 352
Cdd:cd01136 236 ILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
65-411 |
1.63e-55 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 190.80 E-value: 1.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 65 SSTDGLVRGMKVIDTGKPISVPVGEGTLGRILNVTGDAIDERGPvkADDSW-SIHRPAPSFEEQNPATEILETGIKVIDL 143
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPP--LTGQWrELDCPPPSPLTRQPIEQMLTTGIRAIDG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 144 LAPYSKGGKVGLFGGAGVGKTVLIQELIrniAHEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQMNEPPGA 223
Cdd:PRK06820 157 ILSCGEGQRIGIFAAAGVGKSTLLGMLC---ADSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 224 RQRIGLTGLTIAEYFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTKQGSITSVQ 303
Cdd:PRK06820 234 RLKGLSTATTIAEYFRD-RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFY 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 304 AVYVPADDLTDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILdPDIVGEEHYEVAIKVQEVLQTYKELQDII 383
Cdd:PRK06820 313 TVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIELLV 391
|
330 340 350
....*....|....*....|....*....|..
gi 1180564254 384 AI----LGMDELSDEdkiTVARARKIQRFFSQ 411
Cdd:PRK06820 392 RVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
4-385 |
3.93e-54 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 187.24 E-value: 3.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 4 GKVVQVIGPVIDvefAPGKLPDIYNAVVIRTEDQENKDFeidltleAAQHLGNNTVRCVAM--SSTDGLVRGMKVIDTGK 81
Cdd:PRK07721 20 GKVSRVIGLMIE---SKGPESSIGDVCYIHTKGGGDKAI-------KAEVVGFKDEHVLLMpyTEVAEIAPGCLVEATGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 82 PISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAGV 161
Cdd:PRK07721 90 PLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 162 GKTVLIQELIRNIAHEhggYSVFAGVGERTRE-----GNDLWHEMqdsgvIDKTALVFGQMNEPPGARQRIGLTGLTIAE 236
Cdd:PRK07721 170 GKSTLMGMIARNTSAD---LNVIALIGERGREvrefiERDLGPEG-----LKRSIVVVATSDQPALMRIKGAYTATAIAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 237 YFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTKQGSITSVQAVYVPADDLTDPA 316
Cdd:PRK07721 242 YFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPI 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1180564254 317 PATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILdPDIVGEEHYEVAIKVQEVLQTYKELQDIIAI 385
Cdd:PRK07721 321 ADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
69-385 |
5.33e-54 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 186.83 E-value: 5.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 69 GLVRGMKVIDTGKPISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYS 148
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 149 KGGKVGLFGGAGVGKTVLIQELIRNIAHEhggYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQMNEPPGARQRIG 228
Cdd:PRK08972 161 KGQRMGLFAGSGVGKSVLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGC 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 229 LTGLTIAEYFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERIT--STKQGSITSVQAVY 306
Cdd:PRK08972 238 ETATTIAEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPGQGSITAFYTVL 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1180564254 307 VPADDLTDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILdPDIVGEEHYEVAIKVQEVLQTYKELQDIIAI 385
Cdd:PRK08972 317 TEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
83-441 |
1.99e-53 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 185.27 E-value: 1.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 83 ISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAGVG 162
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 163 KTVLIQELIRNiahEHGGYSVFAGVGERTREGNDLWHEmQDSGVIDKTALVFGQMNEPPGARQRIGLTGLTIAEYFRDvQ 242
Cdd:PRK08472 170 KSTLMGMIVKG---CLAPIKVVALIGERGREIPEFIEK-NLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKN-Q 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 243 KQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTK-QGSITSVQAVYVPADDLTDPAPATTF 321
Cdd:PRK08472 245 GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTVLVEGDDMSDPIADQSR 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 322 AHLDAQTVLNRAITEQGIYPAVDPLDSNSRILDpDIVGEEHYEVAIKVQEVLQTYKELQDIIAI----LGMDELSDEdki 397
Cdd:PRK08472 325 SILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIRIgayqKGNDKELDE--- 400
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1180564254 398 TVARARKIQRFFSQPffvaeqftgfPGKYVPVKETIRGFKEILE 441
Cdd:PRK08472 401 AISKKEFMEQFLKQN----------PNELFPFEQTFEQLEEILR 434
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
69-411 |
1.14e-52 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 183.42 E-value: 1.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 69 GLVRGMKVIDTGKPISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYS 148
Cdd:PRK06936 81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 149 KGGKVGLFGGAGVGKTVLIQELIRNIAHEhggYSVFAGVGERTREGND-LWHEMQDSGvIDKTALVFGQMNEPPGARQRI 227
Cdd:PRK06936 161 EGQRMGIFAAAGGGKSTLLASLIRSAEVD---VTVLALIGERGREVREfIESDLGEEG-LRKAVLVVATSDRPSMERAKA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 228 GLTGLTIAEYFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTKQGSITSVQAVYV 307
Cdd:PRK06936 237 GFVATSIAEYFRD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 308 PADDLTDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILDpDIVGEEHYEVAIKVQEVLQTYKELQDIIAI-- 385
Cdd:PRK06936 316 EGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIge 394
|
330 340
....*....|....*....|....*...
gi 1180564254 386 --LGMDELSDEdkiTVARARKIQRFFSQ 411
Cdd:PRK06936 395 yqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
51-413 |
8.44e-51 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 177.88 E-value: 8.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 51 AQHLGNNTVRCV--AMSSTDGLVRGMKVIDTGKPISVPVGEGTLGRILNVTGdAIDER--GPVKAD---DSWSIHRPAPS 123
Cdd:PRK08149 46 AQVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTG-KIVERfdAPPTVGpisEERVIDVAPPS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 124 FEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAGVGKTVLIQELIrniahEHGGYSVF--AGVGERTREGNDLWHEM 201
Cdd:PRK08149 125 YAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLI-----EHSEADVFviGLIGERGREVTEFVESL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 202 QDSGVIDKTALVFGQMNEPPGARQRIGLTGLTIAEYFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLA 281
Cdd:PRK08149 200 RASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 282 TEMGNLQERITSTKQGSITSVQAVYVPADDLTDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILDpDIVGEE 361
Cdd:PRK08149 279 DSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVTDPK 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1180564254 362 HYEVAIKVQEVLQTYKELQDIIAI----LGMDELSDedkITVARARKIQRFFSQPF 413
Cdd:PRK08149 358 HRQLAAAFRKLLTRLEELQLFIDLgeyrRGENADND---RAMDKRPALEAFLKQDV 410
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
93-387 |
2.62e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 177.11 E-value: 2.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 93 GRILNVTGDAIDERGPVKA-DDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAGVGKTVLIQELI 171
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 172 RNIAHEHggySVFAGVGERTREGNDLWHE-MQDSgvIDKTALVFGQMNEPPGARQRIGLTGLTIAEYFRDvQKQDVLLFI 250
Cdd:PRK06002 187 RADAFDT---VVIALVGERGREVREFLEDtLADN--LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRD-RGENVLLIV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 251 DNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERI--TSTKQGSITSVQAVYVPADDLTDPAPATTFAHLDAQT 328
Cdd:PRK06002 261 DSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHI 340
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1180564254 329 VLNRAITEQGIYPAVDPLDSNSRILDPDIVGEEHYEVAiKVQEVLQTYKELQDIIAILG 387
Cdd:PRK06002 341 VLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVS-RLKSMIARFEETRDLRLIGG 398
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
3-412 |
6.53e-50 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 176.11 E-value: 6.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 3 SGKVVQVIGPVIDVEFAPGKLPDIYNavvIRTEDQEnkdfeidlTLEAAQHLG--NNTVRCVAMSSTDGLVRGMKVIDTG 80
Cdd:PRK09099 25 TGKVVEVIGTLLRVSGLDVTLGELCE---LRQRDGT--------LLQRAEVVGfsRDVALLSPFGELGGLSRGTRVIGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 81 KPISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAG 160
Cdd:PRK09099 94 RPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 161 VGKTVLIQELIRNIAHEhggYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQMNEPPGARQRIGLTGLTIAEYFRD 240
Cdd:PRK09099 174 VGKSTLMGMFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 241 vQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTKQGSITSVQAVYVPADDLTDPAPATT 320
Cdd:PRK09099 251 -RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 321 FAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILdPDIVGEEHYEVAIKVQEVLQTYKELQDIIAI----LGMDELSDEdk 396
Cdd:PRK09099 330 RGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE-- 406
|
410
....*....|....*.
gi 1180564254 397 iTVARARKIQRFFSQP 412
Cdd:PRK09099 407 -AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
66-411 |
7.50e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 170.68 E-value: 7.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 66 STDGLVRGMKVIDTGKPISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLA 145
Cdd:PRK05688 84 SVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 146 PYSKGGKVGLFGGAGVGKTVLIQELIRNIAHEhggYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQMNEPPGARQ 225
Cdd:PRK05688 164 TVGRGQRLGLFAGTGVGKSVLLGMMTRFTEAD---IIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 226 RIGLTGLTIAEYFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTKQG--SITSVQ 303
Cdd:PRK05688 241 RAAMYCTRIAEYFRD-KGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITAFY 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 304 AVYVPADDLTDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILdPDIVGEEHYEVAIKVQEVLQTYKELQDII 383
Cdd:PRK05688 320 TVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLI 398
|
330 340
....*....|....*....|....*....
gi 1180564254 384 AILGMDELSD-EDKITVARARKIQRFFSQ 411
Cdd:PRK05688 399 SVGAYVAGGDpETDLAIARFPHLVQFLRQ 427
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
4-385 |
7.50e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 167.85 E-value: 7.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 4 GKVVQVIGPVIDVEfAPGKLPDIYNAVVIRTEDQENKDFEIdltleaaqhLGNNTVRCVAM--SSTDGLVRGMKVIDTGK 81
Cdd:PRK08927 19 GRVVAVRGLLVEVA-GPIHALSVGARIVVETRGGRPVPCEV---------VGFRGDRALLMpfGPLEGVRRGCRAVIANA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 82 PISVPVGEGTLGRILNVTGDAIDERGPV-KADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAG 160
Cdd:PRK08927 89 AAAVRPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 161 VGKTVLIQELIRNIAHEhggYSVFAGVGERTRE-----GNDLWHE-MQDSGVIDKTAlvfgqmNEPPGARQRIGLTGLTI 234
Cdd:PRK08927 169 VGKSVLLSMLARNADAD---VSVIGLIGERGREvqeflQDDLGPEgLARSVVVVATS------DEPALMRRQAAYLTLAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 235 AEYFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERI--TSTKQGSITSVQAVYVPADDL 312
Cdd:PRK08927 240 AEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDH 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180564254 313 TDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILdPDIVGEEHYEVAIKVQEVLQTYKELQDIIAI 385
Cdd:PRK08927 319 NEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
67-378 |
7.71e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 164.77 E-value: 7.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 67 TDGLVRGMKVIDTGKPISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAP 146
Cdd:PRK06793 73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLT 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 147 YSKGGKVGLFGGAGVGKTVLIQELIRNIAHEhggYSVFAGVGERTREGND-LWHEMQDSGvIDKTALVFGQMNEPPGARQ 225
Cdd:PRK06793 153 IGIGQKIGIFAGSGVGKSTLLGMIAKNAKAD---INVISLVGERGREVKDfIRKELGEEG-MRKSVVVVATSDESHLMQL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 226 RIGLTGLTIAEYFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAvGYQPTLATEMGNLQERITSTKQGSITSVQAV 305
Cdd:PRK06793 229 RAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKGSITGIYTV 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180564254 306 YVPADDLTDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILDpDIVGEEHYEVAIKVQEVLQTYKE 378
Cdd:PRK06793 307 LVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKILSIYKE 378
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
65-394 |
1.70e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 161.27 E-value: 1.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 65 SSTDGLVRGMKVIDTGKPISVPVGEGTLGRILNVTGDAIDER----GPVKADDSwsihRPAPSFEEQnPATEILETGIKV 140
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRelpdVCWKDYDA----MPPPAMVRQ-PITQPLMTGIRA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 141 IDLLAPYSKGGKVGLFGGAGVGKTVLIQELIrniAHEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQMNEP 220
Cdd:PRK07594 146 IDSVATCGEGQRVGIFSAPGVGKSTLLAMLC---NAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 221 PGARQRIGLTGLTIAEYFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTKQGSIT 300
Cdd:PRK07594 223 ALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSIT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 301 SVQAVYVPADDLTDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILdPDIVGEEHYEVAIKVQEVLQTYKELQ 380
Cdd:PRK07594 302 AFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVE 380
|
330
....*....|....*...
gi 1180564254 381 DIIAI----LGMDELSDE 394
Cdd:PRK07594 381 LLIRIgeyqRGVDTDTDK 398
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
69-411 |
7.92e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 159.67 E-value: 7.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 69 GLVRGMKVIDTGKPISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYS 148
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 149 KGGKVGLFGGAGVGKTVLIQELIRniaHEHGGYSVFAGVGERTREGND-LWHEMQDSGvIDKTALVFGQMNEPPGARQRI 227
Cdd:PRK07196 154 KGQRVGLMAGSGVGKSVLLGMITR---YTQADVVVVGLIGERGREVKEfIEHSLQAAG-MAKSVVVAAPADESPLMRIKA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 228 GLTGLTIAEYFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERI-TSTKQGSITSVQAVY 306
Cdd:PRK07196 230 TELCHAIATYYRD-KGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMTAIYTVL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 307 VPADDLTDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILDpDIVGEEHYEVAIKVQEVLQTYKELQDIIA-- 384
Cdd:PRK07196 309 AEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAIKPLIPlg 387
|
330 340
....*....|....*....|....*....
gi 1180564254 385 --ILGMDELSDEdkiTVARARKIQRFFSQ 411
Cdd:PRK07196 388 gyVAGADPMADQ---AVHYYPAITQFLRQ 413
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
2-83 |
1.68e-38 |
|
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: 134.18 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 2 NSGKVVQVIGPVIDVEFAPGKLPDIYNAVVIRTEDqenkdfEIDLTLEAAQHLGNNTVRCVAMSSTDGLVRGMKVIDTGK 81
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDD------GKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGA 74
|
..
gi 1180564254 82 PI 83
Cdd:cd18115 75 PI 76
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
51-352 |
6.93e-36 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 138.89 E-value: 6.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 51 AQHLGNNTVRCVAMSSTDGLVRGMKVIDTGKPISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPA 130
Cdd:PRK13343 63 AFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 131 TEILETGIKVIDLLAPYSKGGKVGLFGGAGVGKTVLIQELIRNiAHEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKT 210
Cdd:PRK13343 143 TEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN-QKDSDVICVYVAIGQKASAVARVIETLREHGALEYT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 211 ALVFGQMNEPPGARQRIGLTGLTIAEYFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQER 290
Cdd:PRK13343 222 TVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLER 300
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1180564254 291 IT--STKQ--GSITSVQAVYVPADDLTDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRI 352
Cdd:PRK13343 301 AAklSPELggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRV 366
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
5-413 |
2.77e-35 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 136.49 E-value: 2.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 5 KVVQVIGPVIDVEfapgKLPDI-YNAVV-IRTEDQENKD---FEIDLTLEAAQHLGnntvrcvamsSTDGL-VRGMKVID 78
Cdd:PRK04196 6 TVSEIKGPLLFVE----GVEGVaYGEIVeIELPNGEKRRgqvLEVSEDKAVVQVFE----------GTTGLdLKDTKVRF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 79 TGKPISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPApsfeeQNPAT-----EILETGIKVIDLLAPYSKGGKV 153
Cdd:PRK04196 72 TGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAP-----INPVAreypeEFIQTGISAIDGLNTLVRGQKL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 154 GLFGGAGVGKTVLIQELIRNIA---HEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQMNEPPGARQRIGLT 230
Cdd:PRK04196 147 PIFSGSGLPHNELAAQIARQAKvlgEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 231 GLTIAEYFRDVQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQER--ITSTKQGSITSVQAVYVP 308
Cdd:PRK04196 227 ALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 309 ADDLTDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILDpDIVG-----EEHYEVAIKVQEVLQTYKELQDII 383
Cdd:PRK04196 307 DDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMK-DGIGegktrEDHKDVANQLYAAYARGKDLRELA 385
|
410 420 430
....*....|....*....|....*....|.
gi 1180564254 384 AILGMDELSDEDKITVARARKI-QRFFSQPF 413
Cdd:PRK04196 386 AIVGEEALSERDRKYLKFADAFeREFVNQGF 416
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
82-351 |
2.07e-32 |
|
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: 124.61 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 82 PISVPVGEGTLGRILnvtgDAIDERGPVKADDS------------WSIHRPAPsFEEQNPATEILETGIKVIDLLAPYSK 149
Cdd:cd01134 1 PLSVELGPGLLGSIF----DGIQRPLEVIAETGsifiprgvnvqrWPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 150 GGKVGLFGGAGVGKTVLIQELIRNIAHEhggYSVFAGVGERtreGND----------LWHEMQDSGVIDKTALVFGQMNE 219
Cdd:cd01134 76 GGTAAIPGPFGCGKTVISQSLSKWSNSD---VVIYVGCGER---GNEmaevleefpeLKDPITGESLMERTVLIANTSNM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 220 PPGARQRIGLTGLTIAEYFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERI-------T 292
Cdd:cd01134 150 PVAAREASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgS 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1180564254 293 STKQGSITSVQAVYVPADDLTDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSR 351
Cdd:cd01134 229 PGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
85-385 |
3.76e-32 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 127.59 E-value: 3.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 85 VPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAGVGKT 164
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKS 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 165 VLIQELIRniaHEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQMNEPPGARQRIGLTGLTIAEYFRDvQKQ 244
Cdd:PRK07960 190 VLLGMMAR---YTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRD-RGQ 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 245 DVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITS--TKQGSITSVQAVYVPADDLTDPAPATTFA 322
Cdd:PRK07960 266 HVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARA 345
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1180564254 323 HLDAQTVLNRAITEQGIYPAVDPLDSNSRILdPDIVGEEHYEVAIKVQEVLQTYKELQDIIAI 385
Cdd:PRK07960 346 ILDGHIVLSRRLAEAGHYPAIDIEASISRAM-TALIDEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
82-354 |
4.17e-32 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 123.87 E-value: 4.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 82 PISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPApsfeeQNPAT-----EILETGIKVIDLLAPYSKGGKVGLF 156
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPP-----INPVAriypeEMIQTGISAIDVMNTLVRGQKLPIF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 157 GGAGVGKTVLIQELIRN---IAHEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQMNEPPGARQRIGLTGLT 233
Cdd:cd01135 76 SGSGLPHNELAAQIARQagvVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 234 IAEYFRDVQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQER--ITSTKQGSITSVQAVYVPADD 311
Cdd:cd01135 156 TAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMPNDD 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1180564254 312 LTDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILD 354
Cdd:cd01135 236 ITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMK 278
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
56-413 |
8.89e-32 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 126.17 E-value: 8.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 56 NNTVRCVAMSSTDGLVRGMKVIDTGKPISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILE 135
Cdd:PRK05922 63 NRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 136 TGIKVIDLLAPYSKGGKVGLFGGAGVGKTVLIQELIRNiahEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFG 215
Cdd:PRK05922 143 TGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKG---SKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIAS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 216 QMNEPPGARQRIGLTGLTIAEYFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTK 295
Cdd:PRK05922 220 PAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 296 QGSITSVQAV-YVP--ADDLTDPAPATTFAHLdaqtvlnrAITEQG---IYPAVDPLDSNSRILDpDIVGEEHYEVAIKV 369
Cdd:PRK05922 299 KGSITALYAIlHYPnhPDIFTDYLKSLLDGHF--------FLTPQGkalASPPIDILTSLSRSAR-QLALPHHYAAAEEL 369
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1180564254 370 QEVLQTYKELQDIIAILGMDELSDEDkitVARARK----IQRFFSQPF 413
Cdd:PRK05922 370 RSLLKAYHEALDIIQLGAYVPGQDAH---LDRAVKllpsIKQFLSQPL 414
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
115-411 |
7.22e-31 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 125.28 E-value: 7.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 115 WSIHRPAPsFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAGVGKTVLIQELIRniahehggYS-----VFAGVGE 189
Cdd:PRK04192 193 WPVRRPRP-YKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQLAK--------WAdadivIYVGCGE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 190 RtreGNdlwhEMQD------------SG--VIDKTALVFGQMNEPPGARQRIGLTGLTIAEYFRDvQKQDVLLFIDNIFR 255
Cdd:PRK04192 264 R---GN----EMTEvleefpelidpkTGrpLMERTVLIANTSNMPVAAREASIYTGITIAEYYRD-MGYDVLLMADSTSR 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 256 FTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQER----IT-STKQGSITSVQAVYVPADDLTDPAPATT------FAHL 324
Cdd:PRK04192 336 WAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTIIGAVSPPGGDFSEPVTQNTlrivkvFWAL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 325 DAqtvlNRAitEQGIYPAVDPLDSNSRILD------PDIVGEEHYEVAIKVQEVLQTYKELQDIIAILGMDELSDEDKIT 398
Cdd:PRK04192 416 DA----ELA--DRRHFPAINWLTSYSLYLDqvapwwEENVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLI 489
|
330
....*....|...
gi 1180564254 399 VARARKIQRFFSQ 411
Cdd:PRK04192 490 LEVARLIREDFLQ 502
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
83-352 |
4.14e-26 |
|
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: 106.87 E-value: 4.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 83 ISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAGVG 162
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 163 KTVLIQELIRNiAHEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQMNEPPGARQRIGLTGLTIAEYFRDvQ 242
Cdd:cd01132 82 KTAIAIDTIIN-QKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRD-N 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 243 KQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTKQ----GSITSVQAVYVPADDLTDPAPA 318
Cdd:cd01132 160 GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSLTALPIIETQAGDVSAYIPT 239
|
250 260 270
....*....|....*....|....*....|....
gi 1180564254 319 TTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRI 352
Cdd:cd01132 240 NVISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
79-409 |
1.85e-25 |
|
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: 108.66 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 79 TGKPISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIH-RPAPSFEEQNPaTEILETGIKVIDLLAPYSKGGKVGLFG 157
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINgQPINPYARIYP-EEMIQTGISAIDVMNSIARGQKIPIFS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 158 GAGVGKTVLIQELIRNIA------------HEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQMNEPPGARQ 225
Cdd:TIGR01040 149 AAGLPHNEIAAQICRQAGlvklptkdvhdgHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 226 RIGLTGLTIAEYFRDVQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERI--TSTKQGSITSVQ 303
Cdd:TIGR01040 229 ITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIP 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 304 AVYVPADDLTDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRILDPDIvGE-----EHYEVAIKVQEVLQTYKE 378
Cdd:TIGR01040 309 ILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHSDVSNQLYACYAIGKD 387
|
330 340 350
....*....|....*....|....*....|.
gi 1180564254 379 LQDIIAILGMDELSDEDKITVARARKIQRFF 409
Cdd:TIGR01040 388 VQAMKAVVGEEALSSEDLLYLEFLDKFEKNF 418
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-80 |
7.19e-22 |
|
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: 88.76 E-value: 7.19e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1180564254 6 VVQVIGPVIDVEFAPGKLPDIYNAVVIRTEDQENkdfeidLTLEAAQHLGNNTVRCVAMSSTDGLVRGMKVIDTG 80
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVEFGS------LVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
183-411 |
4.23e-21 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 96.63 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 183 VFAGVGERTREGNDLWHE---MQDSG----VIDKTALVFGQMNEPPGARQRIGLTGLTIAEYFRDVqKQDVLLFIDNIFR 255
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEfpkLKDPKtgkpLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVALMADSTSR 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 256 FTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERI-------TSTKQGSITSVQAVYVPADDLTDPAPATTFAHLDAQT 328
Cdd:PRK14698 765 WAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFW 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 329 VLNRAITEQGIYPAVDPLDSNSRILDP------DIVGEEHYEVAIKVQEVLQTYKELQDIIAILGMDELSDEDKITVARA 402
Cdd:PRK14698 845 ALDADLARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAILLVA 924
|
....*....
gi 1180564254 403 RKIQRFFSQ 411
Cdd:PRK14698 925 RMLREDYLQ 933
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
42-352 |
6.67e-19 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 88.87 E-value: 6.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 42 FEiDLTLEAAQHLGNNTVRCVAMSSTDGLVRGMKVIDTGKPISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPA 121
Cdd:CHL00059 34 FE-DGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 122 PSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAGVGKTVLIQELIRNIAHEhGGYSVFAGVGERTREGNDLWHEM 201
Cdd:CHL00059 113 PGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQ-NVICVYVAIGQKASSVAQVVTTL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 202 QDSGVIDKTALVFGQMNEpPGARQRIG-LTGLTIAEYFRdVQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTL 280
Cdd:CHL00059 192 QERGAMEYTIVVAETADS-PATLQYLApYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDV 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1180564254 281 ATEMGNLQERI----TSTKQGSITSVQAVYVPADDLTDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRI 352
Cdd:CHL00059 270 FYLHSRLLERAaklsSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRV 345
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
51-271 |
8.15e-19 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 88.97 E-value: 8.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 51 AQHLGNNTVRCVAMSSTDGLVRGMKVIDTGKPISVPVGEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPSFEEQNPA 130
Cdd:PRK09281 63 ALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 131 TEILETGIKVIDLLAPYSKGGKVGLFGGAGVGKTVLIQELIRNiAHEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKT 210
Cdd:PRK09281 143 HEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN-QKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYT 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1180564254 211 ALVFGQMNEPPGArQRIG-LTGLTIAEYFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMP 271
Cdd:PRK09281 222 IVVAATASDPAPL-QYLApYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
67-352 |
3.96e-18 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 86.24 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 67 TDGLVRGMKVIDTGKPISVPVGEGTLGRILNVTGDAIDeRGPVKADDSWSIHrpAPSFeeqNPATEIL-----ETGIKVI 141
Cdd:PRK02118 58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPID-GGPELEGEPIEIG--GPSV---NPVKRIVpremiRTGIPMI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 142 DLLAPYSKGGKVGLFGGAGVGKTVLiqeLIRNIAHEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQMNEPP 221
Cdd:PRK02118 132 DVFNTLVESQKIPIFSVSGEPYNAL---LARIALQAEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 222 GARQRIGLTGLTIAEYFRDVQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTKQ-GSIT 300
Cdd:PRK02118 209 VECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEDgGSIT 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1180564254 301 SVQAVYVPADDLTDPAPATTfahldaqtvlnRAITEQGIY---PAVDPLDSNSRI 352
Cdd:PRK02118 289 IIAVTTMPGDDVTHPVPDNT-----------GYITEGQFYlrrGRIDPFGSLSRL 332
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
362-431 |
4.17e-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: 78.25 E-value: 4.17e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 362 HYEVAIKVQEVLQTYKELQDIIAILGMDELSDEDKITVARARKIQRFFSQPFFVAEQFTGFPGKYVPVKE 431
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
4-379 |
8.27e-15 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 76.62 E-value: 8.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 4 GKVVQVIGPVIDVEFAPGKLPDIYNAVVIRTEDQENKDFEIDLTLEAAQHLGnntvrCVAMSSTDGLVRGMKVIDTGKPI 83
Cdd:PTZ00185 41 GYVHSIDGTIATLIPAPGNPGVAYNTIIMIQVSPTTFAAGLVFNLEKDGRIG-----IILMDNITEVQSGQKVMATGKLL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 84 SVPVGEGTLGRILNVTGDAID------ERGPVKADDSW-SIHRPAPSFEEQNPATEILETGIKVIDLLAPYSKGGKVGLF 156
Cdd:PTZ00185 116 YIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQTLgKVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 157 GGAGVGKTVLIQELIRN-------IAHEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKTALVFGQMNEPPGARQRIGL 229
Cdd:PTZ00185 196 GDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 230 TGLTIAEYFRDvQKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAVGYQPTLATEMGNLQERITSTKQ----GSITSVQAV 305
Cdd:PTZ00185 276 SGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPgkggGSVTALPIV 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1180564254 306 YVPADDLTDPAPATTFAHLDAQTVLNRAITEQGIYPAVDPLDSNSRildpdiVGEEHYEVAI-----KVQEVLQTYKEL 379
Cdd:PTZ00185 355 ETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR------VGSSAQNVAMkavagKLKGILAEYRKL 427
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
4-81 |
8.42e-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: 8.42e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1180564254 4 GKVVQVIGPVIDVEFApgKLPDIYNAVVIRTEDQENkdfEIDLTLEAAQHLGNNTVrCVAMSSTDGLVRGMKVIDTGK 81
Cdd:cd01426 2 GRVIRVNGPLVEAELE--GEVAIGEVCEIERGDGNN---ETVLKAEVIGFRGDRAI-LQLFESTRGLSRGALVEPTGR 73
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
149-270 |
3.32e-05 |
|
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: 43.90 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 149 KGGKVGLFGGAGVGKTVLIQELIRNIAHEHGGYSVFAGVGERTREGNDLWHEMQDSGVIDKTalvfgqmnepPGARQRIg 228
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS----------GELRLRL- 69
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1180564254 229 ltGLTIAEYFRdvqkqDVLLFIDNIFRFTQAGSEVSSLLGRM 270
Cdd:smart00382 70 --ALALARKLK-----PDVLILDEITSLLDAEQEALLLLLEE 104
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
88-203 |
9.87e-05 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 45.01 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 88 GEGTLGRILNVTGDAIDERGPVKADDSWSIHRPAPsFEEQNPATEILETGIKVIDLLAPYSKGGKVGLFGGAGVGKTVLI 167
Cdd:PRK14698 166 GEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRP-YKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDG 244
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1180564254 168 QELIrnIAHEHG------GYSVFAGVGERTREGNDLWHEMQD 203
Cdd:PRK14698 245 DTLI--LTKEFGlikikdLYEILDGKGKKTVEGNEEWTELEE 284
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
139-356 |
3.01e-04 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 42.19 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 139 KVIDLLAPYSKGGKVGLFGGAGVGKTVLIQELIRNIAHEHGGYSVFAG-VGERTREGNDlwheMQDSG---VIDKTalvf 214
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRSVkgeVVAST---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 215 gqMNEPPgaRQRIGLTGLTIAEYFRDV-QKQDVLLFIDNIFRFTQAGSEVSSLLGRMPSAvGYQPTlATEMG-------- 285
Cdd:cd01128 77 --FDEPP--ERHVQVAEMVIEKAKRLVeHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-GVDAN-ALHKPkrffgaar 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 286 NLQEritstkQGSITSVqavyvpADDLTDpapatTFAHLD------------AQTVLNRAITEQGIYPAVDPLDSNSR-- 351
Cdd:cd01128 151 NIEE------GGSLTII------ATALVD-----TGSRMDevifeefkgtgnMELVLDRKLAEKRIFPAIDILKSGTRke 213
|
....*..
gi 1180564254 352 --ILDPD 356
Cdd:cd01128 214 elLLTPE 220
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
139-356 |
5.72e-04 |
|
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: 41.98 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 139 KVIDLLAPYSKGGKVGLFGGAGVGKTVLIQELIRNIAHEHGG-YSVFAGVGERTREGNDlwheMQDSGvidKTALVFGQM 217
Cdd:TIGR00767 157 RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEvELIVLLIDERPEEVTD----MQRSV---KGEVVASTF 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1180564254 218 NEPPgaRQRIGLTGLTIAEYFRDV-QKQDVLLFIDNIFRFTQAGSEVSSLLGRM------PSAVGYQPTLATEMGNLQEr 290
Cdd:TIGR00767 230 DEPA--SRHVQVAEMVIEKAKRLVeHKKDVVILLDSITRLARAYNTVTPASGKVlsggvdANALHRPKRFFGAARNIEE- 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1180564254 291 itstkQGSITSVQAVYVPADDLTDPAPATTFAHL-DAQTVLNRAITEQGIYPAVDPLDSNSR----ILDPD 356
Cdd:TIGR00767 307 -----GGSLTIIATALIDTGSRMDEVIFEEFKGTgNMELHLDRKLADRRIFPAIDIKKSGTRkeelLLTPE 372
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
358-412 |
1.78e-03 |
|
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family of ATPases that form part of the Type III secretion system (T3SS) present in Escherichia coli. T3SS is a macromolecular complex that creates a syringe-like apparatus extending from the bacterial cytosol across three membranes to the eukaryotic cytosol. This process is essential for pathogenicity. EscN is a functionally unique ATPase that provides an inner-membrane recognition gate for the T3SS chaperone-virulence effector complexes as well as a potential source of energy for their subsequent secretion.The C-terminal domain of T3SS ATPases mediates binding with multiple contact points along the chaperone.
Pssm-ID: 465691 [Multi-domain] Cd Length: 70 Bit Score: 37.03 E-value: 1.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1180564254 358 VGEEHYEVAIKVQEVLQTYKELQDIIAI----LGMDELSDEdkiTVARARKIQRFFSQP 412
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIgayqAGSDPEIDE---AIAKRPAINAFLRQG 56
|
|
| 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 ... |
368-401 |
2.18e-03 |
|
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of the V1/A1 complex of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349746 [Multi-domain] Cd Length: 105 Bit Score: 37.75 E-value: 2.18e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1180564254 368 KVQEVLQTYKELQDIIAILGMDELSDEDKIT--VAR 401
Cdd:cd18111 7 EAMEILQEEAELQEIVQLVGPDALPEEDRLTleVAR 42
|
|
| |
