|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
60-526 |
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: 987.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 60 TGRIVAVIGAVVDVQFDEG-LPPILNALEVQ-GRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVG 137
Cdd:COG0055 5 TGKIVQVIGPVVDVEFPEGeLPAIYNALEVEnEGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 138 PETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIM 217
Cdd:COG0055 85 EATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 218 ELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINlkdatsKVALVYGQMNEPPGARARVALTGLTVAEYFRDQE 297
Cdd:COG0055 165 ELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD------KTALVFGQMNEPPGARLRVALTALTMAEYFRDEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 298 GQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFA 377
Cdd:COG0055 239 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 378 HLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRA 457
Cdd:COG0055 319 HLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2W6G_D 458 RKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEE 526
Cdd:COG0055 399 RKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAE 467
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
59-523 |
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: 877.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 59 TTGRIVAVIGAVVDVQFDEG-LPPILNALEVQGR-ETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPV 136
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGeLPRIYNALKVQNRaESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 137 GPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLI 216
Cdd:TIGR01039 81 GKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 217 MELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINlkdatsKVALVYGQMNEPPGARARVALTGLTVAEYFRDQ 296
Cdd:TIGR01039 161 QELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 297 EGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTF 376
Cdd:TIGR01039 235 QGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 377 AHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSR 456
Cdd:TIGR01039 315 AHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVER 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
2W6G_D 457 ARKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKL 523
Cdd:TIGR01039 395 ARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
60-526 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 842.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 60 TGRIVAVIGAVVDVQFDEG-LPPILNALEVQGRET-----RLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIR 133
Cdd:CHL00060 16 LGRITQIIGPVLDVAFPPGkMPNIYNALVVKGRDTagqeiNVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 134 IPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKT 213
Cdd:CHL00060 96 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 214 VLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKD-ATSKVALVYGQMNEPPGARARVALTGLTVAEY 292
Cdd:CHL00060 176 VLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNiAESKVALVYGQMNEPPGARMRVGLTALTMAEY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 293 FRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAP 372
Cdd:CHL00060 256 FRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 373 ATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKL 452
Cdd:CHL00060 336 ATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRL 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2W6G_D 453 TVSRARKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEE 526
Cdd:CHL00060 416 TVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLEVE 489
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
133-410 |
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: 616.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 133 RIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGK 212
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 213 TVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLkDATSKVALVYGQMNEPPGARARVALTGLTVAEY 292
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINL-DGLSKVALVYGQMNEPPGARARVALTGLTMAEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 293 FRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAP 372
Cdd:cd01133 160 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAP 239
|
250 260 270
....*....|....*....|....*....|....*...
2W6G_D 373 ATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDP 410
Cdd:cd01133 240 ATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
61-516 |
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: 584.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 61 GRIVAVIGAVVDVQFDEGLPPILNALEVqGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPET 140
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGELPAIHSVLRA-GREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 141 LGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELI 220
Cdd:TIGR03305 80 LSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 221 NNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINlkdatsKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQD 300
Cdd:TIGR03305 160 HNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLD------NTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 301 VLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLD 380
Cdd:TIGR03305 234 VLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 381 ATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKI 460
Cdd:TIGR03305 314 ASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
2W6G_D 461 QRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEA 516
Cdd:TIGR03305 394 ERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
133-407 |
2.25e-140 |
|
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: 405.69 E-value: 2.25e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 133 RIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGK 212
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 213 TVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGvinlkdATSKVALVYGQMNEPPGARARVALTGLTVAEY 292
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSG------AMERTVVVANTANDPPGARMRVPYTGLTIAEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 293 FRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTK--KGSITSVQAIYVPADDLTDP 370
Cdd:cd19476 155 FRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDP 233
|
250 260 270
....*....|....*....|....*....|....*..
2W6G_D 371 APATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRI 407
Cdd:cd19476 234 IPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
186-405 |
6.91e-93 |
|
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: 281.94 E-value: 6.91e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 186 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKahgGYSVFAGVGERTREGNDLYHEMIESGVInlkdatSKV 265
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL------KRT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 266 ALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQER 345
Cdd:pfam00006 72 VVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
2W6G_D 346 ITTT--KKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTS 405
Cdd:pfam00006 151 AGRVkgKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
412-519 |
1.91e-77 |
|
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic.
Pssm-ID: 349745 [Multi-domain] Cd Length: 108 Bit Score: 238.53 E-value: 1.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 412 IVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGF 491
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
2W6G_D 492 QQILAGEYDHLPEQAFYMVGPIEEAVAK 519
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
60-495 |
1.28e-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: 221.44 E-value: 1.28e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 60 TGRIVAVIGAVVDVqfdEGLPPILNAL-EVQGRETRLVL-EVaqhLG--ESTVRTIAMDGTEGLVRGQKVLDSGAPIRIP 135
Cdd:COG1157 20 SGRVTRVVGLLIEA---VGPDASIGELcEIETADGRPVLaEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRPLSVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 136 VGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVL 215
Cdd:COG1157 94 VGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 216 IMELINNvAKAHggYSVFAGVGERTREGNdlyhEMIES--GVINLKD-----ATSkvalvygqmNEPPGARARVALTGLT 288
Cdd:COG1157 174 LGMIARN-TEAD--VNVIALIGERGREVR----EFIEDdlGEEGLARsvvvvATS---------DEPPLMRLRAAYTATA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 289 VAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITsvqAIY---VPAD 365
Cdd:COG1157 238 IAEYFRDQ-GKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSIT---AFYtvlVEGD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 366 DLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI----L 441
Cdd:COG1157 314 DMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLLARYEENEDLIRIgayqP 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
2W6G_D 442 GMDELSEEdklTVSRARKIQRFLSQPfqVAEVftghlgklVPLKETIKGFQQIL 495
Cdd:COG1157 393 GSDPELDE---AIALIPAIEAFLRQG--MDER--------VSFEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
133-407 |
6.31e-59 |
|
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: 196.24 E-value: 6.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 133 RIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGK 212
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 213 TVLIMELINNVAKAhggYSVFAGVGERTREGNdlyhEMIEsGVINlKDATSKVALVYGQMNEPPGARARVALTGLTVAEY 292
Cdd:cd01136 81 STLLGMIARNTDAD---VNVIALIGERGREVR----EFIE-KDLG-EEGLKRSVLVVATSDESPLLRVRAAYTATAIAEY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 293 FRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAP 372
Cdd:cd01136 152 FRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIA 230
|
250 260 270
....*....|....*....|....*....|....*
2W6G_D 373 ATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRI 407
Cdd:cd01136 231 DEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
117-496 |
3.12e-57 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 196.83 E-value: 3.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 117 EGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPY 196
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTC 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 197 AKGGKIGLFGGAGVGKTVLiMELINNVAKAHggYSVFAGVGERTREgndlYHEMIESgviNLKDATSKVALVYGQMNEPP 276
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKSTL-MGMIVKGCLAP--IKVVALIGERGRE----IPEFIEK---NLGGDLENTVIVVATSDDSP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 277 GARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTK-KGSIT 355
Cdd:PRK08472 225 LMRKYGAFCAMSVAEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSIT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 356 SVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDpNIVGSEHYDVARGVQKILQDYKSLQ 435
Cdd:PRK08472 304 AFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENE 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
2W6G_D 436 DIIAI----LGMD-ELSEedklTVSRARKIQRFLSQPFQvaevftghlgKLVPLKETIKGFQQILA 496
Cdd:PRK08472 383 VLIRIgayqKGNDkELDE----AISKKEFMEQFLKQNPN----------ELFPFEQTFEQLEEILR 434
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
114-495 |
7.58e-53 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 185.40 E-value: 7.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 114 DGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDErGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLL 193
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 194 APYAKGGKIGLFGGAGVGKTVLIMELinnVAKAHGGYSVFAGVGERTREgndlYHEMIESGVInlKDATSKVALVYGQMN 273
Cdd:PRK06820 158 LSCGEGQRIGIFAAAGVGKSTLLGML---CADSAADVMVLALIGERGRE----VREFLEQVLT--PEARARTVVVVATSD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 274 EPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGS 353
Cdd:PRK06820 229 RPALERLKGLSTATTIAEYFRDR-GKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGS 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 354 ITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKS 433
Cdd:PRK06820 308 ITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQE 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
2W6G_D 434 LQDIIAI----LGMDELSEEdklTVSRARKIQRFLSQpfqvaevftgHLGKLVPLKETIKGFQQIL 495
Cdd:PRK06820 387 IELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ----------DHSETAHLETTLEHLAQVV 439
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
56-467 |
1.61e-51 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 181.89 E-value: 1.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 56 AGATTGRIVAVIGAVVDVQfdeGLPPILNAL-EVQGRETRLvLEVAQHLGEStvRTIAM----DGTEGLVRGQKVLDSGA 130
Cdd:PRK09099 21 AVRRTGKVVEVIGTLLRVS---GLDVTLGELcELRQRDGTL-LQRAEVVGFS--RDVALlspfGELGGLSRGTRVIGLGR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 131 PIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGV 210
Cdd:PRK09099 95 PLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 211 GKTVLIMELINNvakAHGGYSVFAGVGERTREgndlYHEMIEsgVINLKDATSKVALVYGQMNEPPGARARVALTGLTVA 290
Cdd:PRK09099 175 GKSTLMGMFARG---TQCDVNVIALIGERGRE----VREFIE--LILGEDGMARSVVVCATSDRSSIERAKAAYVATAIA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 291 EYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDP 370
Cdd:PRK09099 246 EYFRDR-GLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 371 APATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI----LGMDEL 446
Cdd:PRK09099 325 IAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPV 403
|
410 420
....*....|....*....|.
2W6G_D 447 SEEdklTVSRARKIQRFLSQP 467
Cdd:PRK09099 404 ADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
122-409 |
8.02e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 177.50 E-value: 8.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 122 GQKVLDSGaPIRIPVGPETLGRIMNVIGEPIDERGPIKT-KQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGG 200
Cdd:PRK06002 88 GDAVFRKG-PLRIRPDPSWKGRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQ 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 201 KIGLFGGAGVGKTVLIMELinnvAKAHGGYSV-FAGVGERTREgndlYHEMIESgviNLKDATSKVALVYGQMNEPPGAR 279
Cdd:PRK06002 167 RIGIFAGSGVGKSTLLAML----ARADAFDTVvIALVGERGRE----VREFLED---TLADNLKKAVAVVATSDESPMMR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 280 ARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI--TTTKKGSITSV 357
Cdd:PRK06002 236 RLAPLTATAIAEYFRDR-GENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGI 314
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
2W6G_D 358 QAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMD 409
Cdd:PRK06002 315 FSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLAR 366
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
118-440 |
3.30e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 175.66 E-value: 3.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 118 GLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYA 197
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 198 KGGKIGLFGGAGVGKTVLI-MELINNVAKAhggySVFAGVGERTREgndlYHEMIESgvINLKDATSKVALVYGQMNEPP 276
Cdd:PRK08972 161 KGQRMGLFAGSGVGKSVLLgMMTRGTTADV----IVVGLVGERGRE----VKEFIEE--ILGEEGRARSVVVAAPADTSP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 277 GARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITT--TKKGSI 354
Cdd:PRK08972 231 LMRLKGCETATTIAEYFRDQ-GLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNggPGQGSI 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 355 TSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSL 434
Cdd:PRK08972 310 TAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQN 388
|
....*.
2W6G_D 435 QDIIAI 440
Cdd:PRK08972 389 RDLISI 394
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
117-466 |
3.81e-49 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 175.33 E-value: 3.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 117 EGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPY 196
Cdd:PRK06936 80 YGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 197 AKGGKIGLFGGAGVGKTVLIMELINNvakAHGGYSVFAGVGERTREgndlYHEMIESgviNL-KDATSKVALVYGQMNEP 275
Cdd:PRK06936 160 GEGQRMGIFAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIES---DLgEEGLRKAVLVVATSDRP 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 276 PGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSIT 355
Cdd:PRK06936 230 SMERAKAGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSIT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 356 SVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDpNIVGSEHYDVARGVQKILQDYKSLQ 435
Cdd:PRK06936 309 ALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVE 387
|
330 340 350
....*....|....*....|....*....|....*
2W6G_D 436 DIIAI----LGMDELSEEdklTVSRARKIQRFLSQ 466
Cdd:PRK06936 388 LLLQIgeyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
122-440 |
2.75e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 170.29 E-value: 2.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 122 GQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGK 201
Cdd:PRK07721 81 GCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 202 IGLFGGAGVGKTVLiMELINNVAKAHggYSVFAGVGERTREgndlYHEMIES--GVINLKdatsKVALVYGQMNEPPGAR 279
Cdd:PRK07721 161 VGIFAGSGVGKSTL-MGMIARNTSAD--LNVIALIGERGRE----VREFIERdlGPEGLK----RSIVVVATSDQPALMR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 280 ARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQA 359
Cdd:PRK07721 230 IKGAYTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 360 IYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIA 439
Cdd:PRK07721 309 VLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLIN 387
|
.
2W6G_D 440 I 440
Cdd:PRK07721 388 I 388
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
48-496 |
3.57e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 164.90 E-value: 3.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 48 AQASPSPKAGATTGRIVAVIGAVVDVqfdEGLP-PILNALEVQGRETRLVLEV-AQHLGESTVRTIAM--DGTEGLVRGQ 123
Cdd:PRK05688 16 AEAISLPAQPVVEGRLLRMVGLTLEA---EGLRaAVGSRCLVINDDSYHPVQVeAEVMGFSGDKVFLMpvGSVAGIAPGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 124 KVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIG 203
Cdd:PRK05688 93 RVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 204 LFGGAGVGKTVLiMELINNVAKAHggYSVFAGVGERTREgndlYHEMIESgvINLKDATSKVALVYGQMNEPPGARARVA 283
Cdd:PRK05688 173 LFAGTGVGKSVL-LGMMTRFTEAD--IIVVGLIGERGRE----VKEFIEH--ILGEEGLKRSVVVASPADDAPLMRLRAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 284 LTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKG--SITSVQAIY 361
Cdd:PRK05688 244 MYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITAFYTVL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 362 VPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI- 440
Cdd:PRK05688 323 SEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLISVg 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
2W6G_D 441 ---LGMDelsEEDKLTVSRARKIQRFLSQpfqvaevftgHLGKLVPLKETIKGFQQILA 496
Cdd:PRK05688 402 ayvAGGD---PETDLAIARFPHLVQFLRQ----------GLRENVSLAQSREQLAAIFA 447
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
116-466 |
6.01e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 163.99 E-value: 6.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 116 TEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDErgPIKTKQFAAIHAEAPEFVEMSVEQ--EILVTGIKVVDLL 193
Cdd:PRK06793 73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIHAFEREEitDVFETGIKSIDSM 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 194 APYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHggYSVFAGVGERTREGND-LYHEMIESGVinlkdatSKVALVYGQM 272
Cdd:PRK06793 151 LTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKAD--INVISLVGERGREVKDfIRKELGEEGM-------RKSVVVVATS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 273 NEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAvGYQPTLATDMGTMQERITTTKKG 352
Cdd:PRK06793 221 DESHLMQLRAAKLATSIAEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 353 SITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDpNIVGSEHYDVARGVQKILQDYK 432
Cdd:PRK06793 299 SITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKILSIYK 377
|
330 340 350
....*....|....*....|....*....|....*..
2W6G_D 433 SlQDIIAILGMDELSEEDKLTVSRARK---IQRFLSQ 466
Cdd:PRK06793 378 E-NELYFKLGTIQENAENAYIFECKNKvegINTFLKQ 413
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
59-440 |
4.11e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 161.69 E-value: 4.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 59 TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVL-EVaqhLGESTVRTIAM--DGTEGLVRGQKVLDSGAPIRIP 135
Cdd:PRK08927 17 IYGRVVAVRGLLVEVAGPIHALSVGARIVVETRGGRPVPcEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 136 VGPETLGRIMNVIGEPIDERGPI-KTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTV 214
Cdd:PRK08927 94 PSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 215 LIMELINNVAKAhggYSVFAGVGERTRE-----GNDLYHEMIESGVINLkdATSkvalvygqmNEPPGARARVALTGLTV 289
Cdd:PRK08927 174 LLSMLARNADAD---VSVIGLIGERGREvqeflQDDLGPEGLARSVVVV--ATS---------DEPALMRRQAAYLTLAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 290 AEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERIT--TTKKGSITSVQAIYVPADDL 367
Cdd:PRK08927 240 AEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGpgPIGEGTITGLFTVLVDGDDH 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2W6G_D 368 TDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI 440
Cdd:PRK08927 319 NEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
116-440 |
8.82e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 155.11 E-value: 8.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 116 TEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERgPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAP 195
Cdd:PRK07594 73 TIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVAT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 196 YAKGGKIGLFGGAGVGKTVLIMELINnvaKAHGGYSVFAGVGERTREgndlYHEMIESGVInlKDATSKVALVYGQMNEP 275
Cdd:PRK07594 152 CGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFIDFTLS--EETRKRCVIVVATSDRP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 276 PGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSIT 355
Cdd:PRK07594 223 ALERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSIT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 356 SVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQ 435
Cdd:PRK07594 302 AFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVE 380
|
....*
2W6G_D 436 DIIAI 440
Cdd:PRK07594 381 LLIRI 385
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
96-474 |
4.26e-41 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 153.23 E-value: 4.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 96 VLEVAQHLGESTVRTI--AMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEpIDER--GPIKTKQFA---AIHA 168
Cdd:PRK08149 42 VIARAQVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGK-IVERfdAPPTVGPISeerVIDV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 169 EAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvakAHGGYSVFAGVGERTREGNDLYH 248
Cdd:PRK08149 121 APPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFVE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 249 EMIESGvinlkdATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSA 328
Cdd:PRK08149 198 SLRASS------RREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQ-GKRVVLFIDSMTRYARALRDVALAAGELPAR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 329 VGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIM 408
Cdd:PRK08149 271 RGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVF 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2W6G_D 409 DpNIVGSEHYDVARGVQKILQDYKSLQDIIAiLGMDELSE--EDKLTVSRARKIQRFLSQPFQVAEVF 474
Cdd:PRK08149 351 G-QVTDPKHRQLAAAFRKLLTRLEELQLFID-LGEYRRGEnaDNDRAMDKRPALEAFLKQDVAEKSSF 416
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
118-484 |
1.55e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 143.49 E-value: 1.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 118 GLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYA 197
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 198 KGGKIGLFGGAGVGKTVLiMELINNVAKAHggYSVFAGVGERTREGNDLY-HEMIESGVinlkdatSKVALVYGQMNEPP 276
Cdd:PRK07196 154 KGQRVGLMAGSGVGKSVL-LGMITRYTQAD--VVVVGLIGERGREVKEFIeHSLQAAGM-------AKSVVVAAPADESP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 277 GARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTK-KGSIT 355
Cdd:PRK07196 224 LMRIKATELCHAIATYYRDK-GHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSgNGTMT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 356 SVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDpNIVGSEHYDVARGVQKILQDYKSLQ 435
Cdd:PRK07196 303 AIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAIK 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
2W6G_D 436 DIIA----ILGMDELSEEdklTVSRARKIQRFLSQPFQVAEVFTGHLGKLVPL 484
Cdd:PRK07196 382 PLIPlggyVAGADPMADQ---AVHYYPAITQFLRQEVGHPALFSASVEQLTGM 431
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
70-468 |
2.41e-37 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 143.43 E-value: 2.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 70 VVDVQFDEglppiLNALEVQGRETRL--VLEVaqhlGESTVRTIAMDGTEGL-VRGQKVLDSGAPIRIPVGPETLGRIMN 146
Cdd:PRK04196 20 VEGVAYGE-----IVEIELPNGEKRRgqVLEV----SEDKAVVQVFEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 147 VIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKA 226
Cdd:PRK04196 91 GLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQ-AKV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 227 HGGYS----VFAGVGERTREGNDLYHEMIESGVINlkdatsKVALVYGQMNEPPGAR---ARVAltgLTVAEYFRDQEGQ 299
Cdd:PRK04196 170 LGEEEnfavVFAAMGITFEEANFFMEDFEETGALE------RSVVFLNLADDPAIERiltPRMA---LTAAEYLAFEKGM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 300 DVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQER--ITTTKKGSITSVQAIYVPADDLTDPAPATTFA 377
Cdd:PRK04196 241 HVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIPDLTGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 378 HLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNI----VGSEHYDV--------ARGVQkilqdyksLQDIIAILGMDE 445
Cdd:PRK04196 321 ITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIgegkTREDHKDVanqlyaayARGKD--------LRELAAIVGEEA 392
|
410 420
....*....|....*....|....
2W6G_D 446 LSEEDKLTVSRARKI-QRFLSQPF 468
Cdd:PRK04196 393 LSERDRKYLKFADAFeREFVNQGF 416
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
131-412 |
1.39e-36 |
|
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: 136.97 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 131 PIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGV 210
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 211 GKTVLIMELINNVAKAHGGYS---VFAGVGERTREGNDLYHEMIESGVINlkdatsKVALVYGQMNEPPGARARVALTGL 287
Cdd:cd01135 81 PHNELAAQIARQAGVVGSEENfaiVFAAMGVTMEEARFFKDDFEETGALE------RVVLFLNLANDPTIERIITPRMAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 288 TVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQER--ITTTKKGSITSVQAIYVPAD 365
Cdd:cd01135 155 TTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMPND 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
2W6G_D 366 DLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNI 412
Cdd:cd01135 235 DITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGI 281
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
60-132 |
6.11e-36 |
|
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: 128.40 E-value: 6.11e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2W6G_D 60 TGRIVAVIGAVVDVQFDEG-LPPILNALEVQGRET-RLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPI 132
Cdd:cd18115 2 TGKIVQVIGPVVDVEFPEGeLPPIYNALEVKGDDGkKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
113-440 |
7.60e-33 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 130.67 E-value: 7.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 113 MDGTEGLVRGQKVL-------DSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVT 185
Cdd:PRK07960 82 LEEVEGILPGARVYarnisgeGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 186 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVLImeliNNVAKAHGGYSVFAG-VGERTREGNDLyhemIESgvINLKDATSK 264
Cdd:PRK07960 162 GVRAINALLTVGRGQRMGLFAGSGVGKSVLL----GMMARYTQADVIVVGlIGERGREVKDF----IEN--ILGAEGRAR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 265 VALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQE 344
Cdd:PRK07960 232 SVVIAAPADVSPLLRMQGAAYATRIAEDFRDR-GQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 345 RITT--TKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVAR 422
Cdd:PRK07960 311 RAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAM-TALIDEQHYARVR 389
|
330
....*....|....*...
2W6G_D 423 GVQKILQDYKSLQDIIAI 440
Cdd:PRK07960 390 QFKQLLSSFQRNRDLVSV 407
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
96-500 |
4.61e-29 |
|
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273365 [Multi-domain] Cd Length: 501 Bit Score: 120.19 E-value: 4.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 96 VLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVE 175
Cdd:TIGR00962 58 VQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 176 -MSVEQEiLVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHGGYSVFAGVGERTREGNDLYHEMIESG 254
Cdd:TIGR00962 138 rKSVHEP-LQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIIN-QKDSDVYCIYVAIGQKASTVAQVVRKLEEHG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 255 vinlkdATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPT 334
Cdd:TIGR00962 216 ------AMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDN-GKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGD 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 335 LATDMGTMQERITTTK----KGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRimdp 410
Cdd:TIGR00962 289 VFYLHSRLLERAAKLNdekgGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSR---- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 411 niVGSEHY-----DVARGVQKILQDYKSLqDIIAILGMDeLSEEDKLTVSRARKIQRFLSQPF--------QVAEVFTGH 477
Cdd:TIGR00962 365 --VGGAAQikamkQVAGSLRLELAQYREL-EAFSQFASD-LDEATKKQLERGQRVVELLKQPQykplsveeQVVILFAGT 440
|
410 420
....*....|....*....|....*
2W6G_D 478 LGKL--VPLKEtIKGFQQILAGEYD 500
Cdd:TIGR00962 441 KGYLddIPVDK-IRKFEQALLAYLD 464
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
122-498 |
3.39e-28 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 116.93 E-value: 3.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 122 GQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGK 201
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 202 IGLFGGAGVGKTvlimELINNVAK-AHGGYSVFAGVGERTREGNDlYHEMIESGVinlkdATSKVALVYGQMNEPPGARA 280
Cdd:PRK05922 160 IGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVRE-YIEQHKEGL-----AAQRTIIIASPAHETAPTKV 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 281 RVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAI 360
Cdd:PRK05922 230 IAGRAAMTIAEYFRDQ-GHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 361 -YVP--ADDLTDPAPATTFAHLDATTVlSRAIAElgiyPAVDPLDSTSRiMDPNIVGSEHYDVARGVQKILQDYKSLQDI 437
Cdd:PRK05922 309 lHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSR-SARQLALPHHYAAAEELRSLLKAYHEALDI 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
2W6G_D 438 IAiLGMDELSEEDKLtvSRARK----IQRFLSQPfqvaevftghLGKLVPLKETIKGFQQILAGE 498
Cdd:PRK05922 383 IQ-LGAYVPGQDAHL--DRAVKllpsIKQFLSQP----------LSSYCALHNTLKQLEALLKHE 434
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
48-407 |
6.48e-28 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 116.94 E-value: 6.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 48 AQASPSPKAGATtGRIVAV------IGAVVDVQFDEglppilnALEVQGRETRLVLevaqHLGESTVRTIAMDGTEGLVR 121
Cdd:PRK13343 17 ARYEPQPDAREI-GRVESVgdgiafVSGLPDAALDE-------LLRFEGGSRGFAF----NLEEELVGAVLLDDTADILA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 122 GQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGK 201
Cdd:PRK13343 85 GTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 202 IGLFGGAGVGKTVLIMELINNvAKAHGGYSVFAGVGERTregndlyhemieSGVIN----LK--DATSKVALVYGQMNEP 275
Cdd:PRK13343 165 ELIIGDRQTGKTAIAIDAIIN-QKDSDVICVYVAIGQKA------------SAVARvietLRehGALEYTTVVVAEASDP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 276 PGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKK---- 351
Cdd:PRK13343 232 PGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPelgg 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
2W6G_D 352 GSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRI 407
Cdd:PRK13343 311 GSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRV 366
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
96-475 |
6.17e-26 |
|
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: 110.58 E-value: 6.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 96 VLEVAQHLGESTVrtiaMDGTEGL-VRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFV 174
Cdd:TIGR01040 41 VLEVSGNKAVVQV----FEGTSGIdAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 175 EMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNV-------AKAHGGYS-----VFAGVGERTRE 242
Cdd:TIGR01040 117 ARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvklptKDVHDGHEdnfaiVFAAMGVNMET 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 243 GNDLYHEMIESGvinlkdATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALL 322
Cdd:TIGR01040 197 ARFFKQDFEENG------SMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 323 GRIPSAVGYQPTLATDMGTMQERI--TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDP 400
Cdd:TIGR01040 271 EEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 401 LDSTSRIMDPNI----VGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQR-FLSQ-PFQVAEVF 474
Cdd:TIGR01040 351 LPSLSRLMKSAIgegmTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQgPYENRTIF 430
|
.
2W6G_D 475 T 475
Cdd:TIGR01040 431 E 431
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
417-486 |
6.05e-25 |
|
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: 97.90 E-value: 6.05e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 417 HYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHLGKLVPLKE 486
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
181-406 |
3.82e-24 |
|
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: 102.27 E-value: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 181 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnvAKahggYS-----VFAGVGERtreGNdlyhEMIEsgV 255
Cdd:cd01134 58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSL----SK----WSnsdvvIYVGCGER---GN----EMAE--V 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 256 IN----LKDATS------KVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRI 325
Cdd:cd01134 121 LEefpeLKDPITgeslmeRTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEM 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 326 PSAVGYQPTLATDMGTMQERI-------TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAV 398
Cdd:cd01134 200 PAEEGYPAYLGARLAEFYERAgrvrclgSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSI 279
|
....*...
2W6G_D 399 DPLDSTSR 406
Cdd:cd01134 280 NWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
181-466 |
8.62e-24 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 105.25 E-value: 8.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 181 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnvAKahggYS-----VFAGVGERtreGNdlyhEMIEsgV 255
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQL----AK----WAdadivIYVGCGER---GN----EMTE--V 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 256 IN----LKDATSKVALvygqM----------NEPPGAR-ARVaLTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSA 320
Cdd:PRK04192 272 LEefpeLIDPKTGRPL----MertvliantsNMPVAAReASI-YTGITIAEYYRDM-GYDVLLMADSTSRWAEALREISG 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 321 LLGRIPSAVGYQPTLATDMGTMQER---ITT--TKKGSITSVQAIYVPADDLTDPapaTTFAHLDATTV---LSRAIAEL 392
Cdd:PRK04192 346 RLEEMPGEEGYPAYLASRLAEFYERagrVKTlgGEEGSVTIIGAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 393 GIYPAVDPLDSTSR-------IMDPNIVG--SEHYDVARgvqKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKI-QR 462
Cdd:PRK04192 423 RHFPAINWLTSYSLyldqvapWWEENVDPdwRELRDEAM---DLLQREAELQEIVRLVGPDALPEEDRLILEVARLIrED 499
|
....
2W6G_D 463 FLSQ 466
Cdd:PRK04192 500 FLQQ 503
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
134-407 |
2.66e-19 |
|
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: 88.00 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 134 IPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKT 213
Cdd:cd01132 4 VPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 214 VLIMELINNvAKAHGGYSVFAGVGERTREGNDLYHEMIESGvinlkdATSKVALVYGQMNEPPGARARVALTGLTVAEYF 293
Cdd:cd01132 84 AIAIDTIIN-QKGKKVYCIYVAIGQKRSTVAQIVKTLEEHG------AMEYTIVVAATASDPAPLQYLAPYAGCAMGEYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 294 RDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGY-------QPTLATDMGTMQERItttKKGSITSVQAIYVPADD 366
Cdd:cd01132 157 RDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYpgdvfylHSRLLERAAKLSDEL---GGGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
2W6G_D 367 LTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRI 407
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
232-466 |
8.46e-18 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 87.00 E-value: 8.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 232 VFAGVGERTREGNDLYHEMIEsgvinLKDATS------KVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFI 305
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPK-----LKDPKTgkplmeRTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVALMA 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 306 DNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI-------TTTKKGSITSVQAIYVPADDLTDPAPATTFAH 378
Cdd:PRK14698 760 DSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRV 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 379 LDATTVLSRAIAELGIYPAVDPLDSTSRIMDP------NIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKL 452
Cdd:PRK14698 840 VKVFWALDADLARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERA 919
|
250
....*....|....*
2W6G_D 453 TVSRARKIQR-FLSQ 466
Cdd:PRK14698 920 ILLVARMLREdYLQQ 934
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
96-326 |
8.80e-18 |
|
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: 86.25 E-value: 8.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 96 VLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVE 175
Cdd:COG0056 59 VYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVID 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 176 -MSVeQEILVTGIKVVDLLAPyakggkIG------LFGGAGVGKTVLIMELINNvAKAHGGYSVFAGVGERtregndlyh 248
Cdd:COG0056 139 rQPV-HEPLQTGIKAIDAMIP------IGrgqrelIIGDRQTGKTAIAIDTIIN-QKGKDVICIYVAIGQK--------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 249 emiESGVINLKDATSKvalvYGQM----------NEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEV 318
Cdd:COG0056 202 ---ASTVAQVVETLEE----HGAMeytivvaataSDPAPLQYIAPYAGCAMGEYFMDQ-GKDVLIVYDDLSKHAVAYREL 273
|
....*...
2W6G_D 319 SALLGRIP 326
Cdd:COG0056 274 SLLLRRPP 281
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
63-129 |
1.29e-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: 77.20 E-value: 1.29e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2W6G_D 63 IVAVIGAVVDVQFDEG-LPPILNALEVQGRET-RLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSG 129
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGrLPGLLNALEVELVEFgSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
115-375 |
5.17e-17 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 83.16 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 115 GTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDeRGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLA 194
Cdd:PRK02118 57 GTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPID-GGPELEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 195 PYAKGGKIGLFGGAGVGKTVLIMELinnVAKAHGGYSVFAGVGERtregNDLYHEMIEsgviNLKD--ATSKVALVYGQM 272
Cdd:PRK02118 136 TLVESQKIPIFSVSGEPYNALLARI---ALQAEADIIILGGMGLT----FDDYLFFKD----TFENagALDRTVMFIHTA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 273 NEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQER-ITTTKK 351
Cdd:PRK02118 205 SDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKaVDFEDG 284
|
250 260
....*....|....*....|....
2W6G_D 352 GSITSVQAIYVPADDLTDPAPATT 375
Cdd:PRK02118 285 GSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
96-326 |
1.96e-16 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 82.04 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 96 VLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVE 175
Cdd:PRK09281 59 VYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 176 -MSVEqEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHGGYSVFAGVGERtregndlyhemiESG 254
Cdd:PRK09281 139 rKSVH-EPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN-QKGKDVICIYVAIGQK------------AST 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 255 VINLKDATSKvalvYGQM----------NEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGR 324
Cdd:PRK09281 205 VAQVVRKLEE----HGAMeytivvaataSDPAPLQYLAPYAGCAMGEYFMDN-GKDALIVYDDLSKQAVAYRQLSLLLRR 279
|
..
2W6G_D 325 IP 326
Cdd:PRK09281 280 PP 281
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
111-434 |
5.62e-13 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 71.22 E-value: 5.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 111 IAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPID------ERGPIKTKQ-FAAIHAEAPEFVEMSVEQEIL 183
Cdd:PTZ00185 94 ILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQtLGKVDAGAPNIVSRSPVNYNL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 184 VTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINN-------VAKAHGGYSVFAGVGERTREGNDLYHEMIESGVI 256
Cdd:PTZ00185 174 LTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSNVARIHRLLRSYGAL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 257 NLKDATSKVALvygqmnEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLA 336
Cdd:PTZ00185 254 RYTTVMAATAA------EPAGLQYLAPYSGVTMGEYFMNR-GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVF 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 337 TDMGTMQERITTTKK----GSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRimdpni 412
Cdd:PTZ00185 327 YLHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR------ 400
|
330 340
....*....|....*....|....*..
2W6G_D 413 VGSEHYDVA-RGV----QKILQDYKSL 434
Cdd:PTZ00185 401 VGSSAQNVAmKAVagklKGILAEYRKL 427
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
122-326 |
4.26e-11 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 64.98 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 122 GQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGK 201
Cdd:CHL00059 64 GSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 202 IGLFGGAGVGKTVLIMELINNvAKAHGGYSVFAGVGERTREGNDLYHEMIESGvinlkdATSKVALVYGQMNEPPGARAR 281
Cdd:CHL00059 144 ELIIGDRQTGKTAVATDTILN-QKGQNVICVYVAIGQKASSVAQVVTTLQERG------AMEYTIVVAETADSPATLQYL 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
2W6G_D 282 VALTGLTVAEYFRdQEGQDVLLFIDNIFRFTQAGSEVSALLGRIP 326
Cdd:CHL00059 217 APYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
198-324 |
1.38e-04 |
|
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: 42.36 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 198 KGGKIGLFGGAGVGKTVLIMELINNVAKAHGGysVFAGVGERTREGNDLYHEMIESGvinlkdatskvalvygqMNEPPG 277
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG--VIYIDGEDILEEVLDQLLLIIVG-----------------GKKASG 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
2W6G_D 278 ARARVALTGLTVAEYFRDQegqdvLLFIDNIFRFTQAGSEVSALLGR 324
Cdd:smart00382 62 SGELRLRLALALARKLKPD-----VLILDEITSLLDAEQEALLLLLE 103
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
137-252 |
1.61e-03 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 41.16 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2W6G_D 137 GPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPeFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTV-- 214
Cdd:PRK14698 166 GEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRP-YKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVdg 244
|
90 100 110 120
....*....|....*....|....*....|....*....|
2W6G_D 215 --LIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIE 252
Cdd:PRK14698 245 dtLILTKEFGLIKIKDLYEILDGKGKKTVEGNEEWTELEE 284
|
|
| |
