|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
2-467 |
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: 984.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 2 TGRIVAVIGAVVDVQFDEG-LPPILNALEVQ-GRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVG 79
Cdd:COG0055 5 TGKIVQVIGPVVDVEFPEGeLPAIYNALEVEnEGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 80 PETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIM 159
Cdd:COG0055 85 EATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 160 ELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINlkdatsKVALVYGQMNEPPGARARVALTGLTVAEYFRDQE 239
Cdd:COG0055 165 ELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD------KTALVFGQMNEPPGARLRVALTALTMAEYFRDEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 240 GQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFA 319
Cdd:COG0055 239 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 320 HLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRA 399
Cdd:COG0055 319 HLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 306991568 400 RKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAE 467
Cdd:COG0055 399 RKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKA 466
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
1-465 |
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: 875.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 1 TTGRIVAVIGAVVDVQFDEG-LPPILNALEVQGR-ETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPV 78
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGeLPRIYNALKVQNRaESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 79 GPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLI 158
Cdd:TIGR01039 81 GKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 159 MELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINlkdatsKVALVYGQMNEPPGARARVALTGLTVAEYFRDQ 238
Cdd:TIGR01039 161 QELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 239 EGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTF 318
Cdd:TIGR01039 235 QGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 319 AHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSR 398
Cdd:TIGR01039 315 AHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVER 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 306991568 399 ARKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKL 465
Cdd:TIGR01039 395 ARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| 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: 840.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 2 TGRIVAVIGAVVDVQFDEG-LPPILNALEVQGRET-----RLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIR 75
Cdd:CHL00060 16 LGRITQIIGPVLDVAFPPGkMPNIYNALVVKGRDTagqeiNVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 76 IPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKT 155
Cdd:CHL00060 96 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 156 VLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKD-ATSKVALVYGQMNEPPGARARVALTGLTVAEY 234
Cdd:CHL00060 176 VLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNiAESKVALVYGQMNEPPGARMRVGLTALTMAEY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 235 FRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAP 314
Cdd:CHL00060 256 FRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 315 ATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKL 394
Cdd:CHL00060 336 ATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRL 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 306991568 395 TVSRARKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAE 467
Cdd:CHL00060 416 TVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLEV 488
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
75-352 |
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: 617.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 75 RIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGK 154
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 155 TVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLkDATSKVALVYGQMNEPPGARARVALTGLTVAEY 234
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINL-DGLSKVALVYGQMNEPPGARARVALTGLTMAEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 235 FRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAP 314
Cdd:cd01133 160 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAP 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 306991568 315 ATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDP 352
Cdd:cd01133 240 ATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
3-458 |
0e+00 |
|
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 beta subunit of this apparent second ATP synthase.
Pssm-ID: 132348 [Multi-domain] Cd Length: 449 Bit Score: 585.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 3 GRIVAVIGAVVDVQFDEGLPPILNALEVqGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPET 82
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGELPAIHSVLRA-GREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 83 LGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELI 162
Cdd:TIGR03305 80 LSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 163 NNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINlkdatsKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQD 242
Cdd:TIGR03305 160 HNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLD------NTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 243 VLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLD 322
Cdd:TIGR03305 234 VLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 323 ATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKI 402
Cdd:TIGR03305 314 ASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 306991568 403 QRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEA 458
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 ... |
75-349 |
1.52e-142 |
|
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: 408.77 E-value: 1.52e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 75 RIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGK 154
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 155 TVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGvinlkdATSKVALVYGQMNEPPGARARVALTGLTVAEY 234
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSG------AMERTVVVANTANDPPGARMRVPYTGLTIAEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 235 FRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTK--KGSITSVQAIYVPADDLTDP 312
Cdd:cd19476 155 FRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDP 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 306991568 313 APATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRI 349
Cdd:cd19476 234 IPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
128-347 |
6.92e-94 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 282.71 E-value: 6.92e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 128 GIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKahgGYSVFAGVGERTREGNDLYHEMIESGVInlkdatSKV 207
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL------KRT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 208 ALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQER 287
Cdd:pfam00006 72 VVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 306991568 288 ITTT--KKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTS 347
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 ... |
354-461 |
2.69e-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: 236.22 E-value: 2.69e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 354 IVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGF 433
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 306991568 434 QQILAGEYDHLPEQAFYMVGPIEEAVAK 461
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
2-437 |
8.66e-68 |
|
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: 222.98 E-value: 8.66e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 2 TGRIVAVIGAVVDVqfdEGLPPILNAL-EVQGRETRLVL-EVaqhLG--ESTVRTIAMDGTEGLVRGQKVLDSGAPIRIP 77
Cdd:COG1157 20 SGRVTRVVGLLIEA---VGPDASIGELcEIETADGRPVLaEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRPLSVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 78 VGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVL 157
Cdd:COG1157 94 VGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 158 IMELINNvAKAHggYSVFAGVGERTREGNdlyhEMIES--GVINLKD-----ATSkvalvygqmNEPPGARARVALTGLT 230
Cdd:COG1157 174 LGMIARN-TEAD--VNVIALIGERGREVR----EFIEDdlGEEGLARsvvvvATS---------DEPPLMRLRAAYTATA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 231 VAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITsvqAIY---VPAD 307
Cdd:COG1157 238 IAEYFRDQ-GKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSIT---AFYtvlVEGD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 308 DLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI----L 383
Cdd:COG1157 314 DMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLLARYEENEDLIRIgayqP 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 306991568 384 GMDELSEEdklTVSRARKIQRFLSQPfqVAEVftghlgklVPLKETIKGFQQIL 437
Cdd:COG1157 393 GSDPELDE---AIALIPAIEAFLRQG--MDER--------VSFEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
75-349 |
6.04e-60 |
|
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: 197.01 E-value: 6.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 75 RIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGK 154
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 155 TVLIMELINNVAKAhggYSVFAGVGERTREGNdlyhEMIEsGVINlKDATSKVALVYGQMNEPPGARARVALTGLTVAEY 234
Cdd:cd01136 81 STLLGMIARNTDAD---VNVIALIGERGREVR----EFIE-KDLG-EEGLKRSVLVVATSDESPLLRVRAAYTATAIAEY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 235 FRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAP 314
Cdd:cd01136 152 FRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIA 230
|
250 260 270
....*....|....*....|....*....|....*
gi 306991568 315 ATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRI 349
Cdd:cd01136 231 DEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
59-438 |
1.39e-57 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 196.06 E-value: 1.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 59 EGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPY 138
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTC 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 139 AKGGKIGLFGGAGVGKTVLiMELINNVAKAHggYSVFAGVGERTREgndlYHEMIESgviNLKDATSKVALVYGQMNEPP 218
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKSTL-MGMIVKGCLAP--IKVVALIGERGRE----IPEFIEK---NLGGDLENTVIVVATSDDSP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 219 GARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTK-KGSIT 297
Cdd:PRK08472 225 LMRKYGAFCAMSVAEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSIT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 298 SVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDpNIVGSEHYDVARGVQKILQDYKSLQ 377
Cdd:PRK08472 304 AFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENE 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 306991568 378 DIIAI----LGMD-ELSEedklTVSRARKIQRFLSQPFQvaevftghlgKLVPLKETIKGFQQILA 438
Cdd:PRK08472 383 VLIRIgayqKGNDkELDE----AISKKEFMEQFLKQNPN----------ELFPFEQTFEQLEEILR 434
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
56-437 |
2.90e-54 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 187.71 E-value: 2.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 56 DGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDErGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLL 135
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 136 APYAKGGKIGLFGGAGVGKTVLIMELinnVAKAHGGYSVFAGVGERTREgndlYHEMIESGVInlKDATSKVALVYGQMN 215
Cdd:PRK06820 158 LSCGEGQRIGIFAAAGVGKSTLLGML---CADSAADVMVLALIGERGRE----VREFLEQVLT--PEARARTVVVVATSD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 216 EPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGS 295
Cdd:PRK06820 229 RPALERLKGLSTATTIAEYFRDR-GKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGS 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 296 ITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKS 375
Cdd:PRK06820 308 ITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQE 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 306991568 376 LQDIIAI----LGMDELSEEdklTVSRARKIQRFLSQpfqvaevftgHLGKLVPLKETIKGFQQIL 437
Cdd:PRK06820 387 IELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ----------DHSETAHLETTLEHLAQVV 439
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
1-409 |
4.17e-52 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 181.89 E-value: 4.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 1 TTGRIVAVIGAVVDVQfdeGLPPILNAL-EVQGRETRLvLEVAQHLGEStvRTIAM----DGTEGLVRGQKVLDSGAPIR 75
Cdd:PRK09099 24 RTGKVVEVIGTLLRVS---GLDVTLGELcELRQRDGTL-LQRAEVVGFS--RDVALlspfGELGGLSRGTRVIGLGRPLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 76 IPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKT 155
Cdd:PRK09099 98 VPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 156 VLIMELINNvakAHGGYSVFAGVGERTREgndlYHEMIEsgVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYF 235
Cdd:PRK09099 178 TLMGMFARG---TQCDVNVIALIGERGRE----VREFIE--LILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 236 RDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPA 315
Cdd:PRK09099 249 RDR-GLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 316 TTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI----LGMDELSEE 391
Cdd:PRK09099 328 EVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE 406
|
410
....*....|....*...
gi 306991568 392 dklTVSRARKIQRFLSQP 409
Cdd:PRK09099 407 ---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
64-351 |
3.85e-51 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 179.42 E-value: 3.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 64 GQKVLDSGaPIRIPVGPETLGRIMNVIGEPIDERGPIKT-KQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGG 142
Cdd:PRK06002 88 GDAVFRKG-PLRIRPDPSWKGRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQ 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 143 KIGLFGGAGVGKTVLIMELinnvAKAHGGYSV-FAGVGERTREgndlYHEMIESgviNLKDATSKVALVYGQMNEPPGAR 221
Cdd:PRK06002 167 RIGIFAGSGVGKSTLLAML----ARADAFDTVvIALVGERGRE----VREFLED---TLADNLKKAVAVVATSDESPMMR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 222 ARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI--TTTKKGSITSV 299
Cdd:PRK06002 236 RLAPLTATAIAEYFRDR-GENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGI 314
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 306991568 300 QAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMD 351
Cdd:PRK06002 315 FSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLAR 366
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
60-382 |
3.31e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 176.81 E-value: 3.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 60 GLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYA 139
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 140 KGGKIGLFGGAGVGKTVLI-MELINNVAKAhggySVFAGVGERTREgndlYHEMIESgvINLKDATSKVALVYGQMNEPP 218
Cdd:PRK08972 161 KGQRMGLFAGSGVGKSVLLgMMTRGTTADV----IVVGLVGERGRE----VKEFIEE--ILGEEGRARSVVVAAPADTSP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 219 GARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITT--TKKGSI 296
Cdd:PRK08972 231 LMRLKGCETATTIAEYFRDQ-GLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNggPGQGSI 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 297 TSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSL 376
Cdd:PRK08972 310 TAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQN 388
|
....*.
gi 306991568 377 QDIIAI 382
Cdd:PRK08972 389 RDLISI 394
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
59-408 |
3.88e-50 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 176.48 E-value: 3.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 59 EGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPY 138
Cdd:PRK06936 80 YGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 139 AKGGKIGLFGGAGVGKTVLIMELINNvakAHGGYSVFAGVGERTREgndlYHEMIESgviNL-KDATSKVALVYGQMNEP 217
Cdd:PRK06936 160 GEGQRMGIFAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIES---DLgEEGLRKAVLVVATSDRP 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 218 PGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSIT 297
Cdd:PRK06936 230 SMERAKAGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSIT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 298 SVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDpNIVGSEHYDVARGVQKILQDYKSLQ 377
Cdd:PRK06936 309 ALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVE 387
|
330 340 350
....*....|....*....|....*....|....*
gi 306991568 378 DIIAI----LGMDELSEEdklTVSRARKIQRFLSQ 408
Cdd:PRK06936 388 LLLQIgeyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
64-382 |
8.05e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 170.29 E-value: 8.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 64 GQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGK 143
Cdd:PRK07721 81 GCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 144 IGLFGGAGVGKTVLiMELINNVAKAHggYSVFAGVGERTREgndlYHEMIES--GVINLKdatsKVALVYGQMNEPPGAR 221
Cdd:PRK07721 161 VGIFAGSGVGKSTL-MGMIARNTSAD--LNVIALIGERGRE----VREFIERdlGPEGLK----RSIVVVATSDQPALMR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 222 ARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQA 301
Cdd:PRK07721 230 IKGAYTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 302 IYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIA 381
Cdd:PRK07721 309 VLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLIN 387
|
.
gi 306991568 382 I 382
Cdd:PRK07721 388 I 388
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
3-438 |
1.20e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 164.90 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 3 GRIVAVIGAVVDVqfdEGLP-PILNALEVQGRETRLVLEV-AQHLGESTVRTIAM--DGTEGLVRGQKVLDSGAPIRIPV 78
Cdd:PRK05688 29 GRLLRMVGLTLEA---EGLRaAVGSRCLVINDDSYHPVQVeAEVMGFSGDKVFLMpvGSVAGIAPGARVVPLADTGRLPM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 79 GPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLi 158
Cdd:PRK05688 106 GMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVL- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 159 MELINNVAKAHggYSVFAGVGERTREgndlYHEMIESgvINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQ 238
Cdd:PRK05688 185 LGMMTRFTEAD--IIVVGLIGERGRE----VKEFIEH--ILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 239 eGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKG--SITSVQAIYVPADDLTDPAPAT 316
Cdd:PRK05688 257 -GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITAFYTVLSEGDDQQDPIADS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 317 TFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI----LGMDelsEED 392
Cdd:PRK05688 336 ARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLISVgayvAGGD---PET 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 306991568 393 KLTVSRARKIQRFLSQpfqvaevftgHLGKLVPLKETIKGFQQILA 438
Cdd:PRK05688 412 DLAIARFPHLVQFLRQ----------GLRENVSLAQSREQLAAIFA 447
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
1-382 |
2.91e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 163.61 E-value: 2.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 1 TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVL-EVaqhLGESTVRTIAM--DGTEGLVRGQKVLDSGAPIRIP 77
Cdd:PRK08927 17 IYGRVVAVRGLLVEVAGPIHALSVGARIVVETRGGRPVPcEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 78 VGPETLGRIMNVIGEPIDERGPI-KTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTV 156
Cdd:PRK08927 94 PSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 157 LIMELINNVAKAhggYSVFAGVGERTRE-----GNDLYHEMIESGVINLkdATSkvalvygqmNEPPGARARVALTGLTV 231
Cdd:PRK08927 174 LLSMLARNADAD---VSVIGLIGERGREvqeflQDDLGPEGLARSVVVV--ATS---------DEPALMRRQAAYLTLAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 232 AEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERIT--TTKKGSITSVQAIYVPADDL 309
Cdd:PRK08927 240 AEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGpgPIGEGTITGLFTVLVDGDDH 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 306991568 310 TDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQDIIAI 382
Cdd:PRK08927 319 NEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
58-408 |
8.18e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 162.07 E-value: 8.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 58 TEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDErgPIKTKQFAAIHAEAPEFVEMSVEQ--EILVTGIKVVDLL 135
Cdd:PRK06793 73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIHAFEREEitDVFETGIKSIDSM 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 136 APYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHggYSVFAGVGERTREGND-LYHEMIESGVinlkdatSKVALVYGQM 214
Cdd:PRK06793 151 LTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKAD--INVISLVGERGREVKDfIRKELGEEGM-------RKSVVVVATS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 215 NEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAvGYQPTLATDMGTMQERITTTKKG 294
Cdd:PRK06793 221 DESHLMQLRAAKLATSIAEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 295 SITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDpNIVGSEHYDVARGVQKILQDYK 374
Cdd:PRK06793 299 SITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKILSIYK 377
|
330 340 350
....*....|....*....|....*....|....*..
gi 306991568 375 SlQDIIAILGMDELSEEDKLTVSRARK---IQRFLSQ 408
Cdd:PRK06793 378 E-NELYFKLGTIQENAENAYIFECKNKvegINTFLKQ 413
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
58-382 |
8.83e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 156.65 E-value: 8.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 58 TEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERgPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAP 137
Cdd:PRK07594 73 TIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVAT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 138 YAKGGKIGLFGGAGVGKTVLIMELINnvaKAHGGYSVFAGVGERTREgndlYHEMIESGVInlKDATSKVALVYGQMNEP 217
Cdd:PRK07594 152 CGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFIDFTLS--EETRKRCVIVVATSDRP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 218 PGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSIT 297
Cdd:PRK07594 223 ALERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSIT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 298 SVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVGSEHYDVARGVQKILQDYKSLQ 377
Cdd:PRK07594 302 AFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVE 380
|
....*
gi 306991568 378 DIIAI 382
Cdd:PRK07594 381 LLIRI 385
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
38-416 |
1.05e-41 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 153.61 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 38 VLEVAQHLGESTVRTI--AMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEpIDER--GPIKTKQFA---AIHA 110
Cdd:PRK08149 42 VIARAQVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGK-IVERfdAPPTVGPISeerVIDV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 111 EAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvakAHGGYSVFAGVGERTREGNDLYH 190
Cdd:PRK08149 121 APPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFVE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 191 EMIESGvinlkdATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSA 270
Cdd:PRK08149 198 SLRASS------RREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQ-GKRVVLFIDSMTRYARALRDVALAAGELPAR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 271 VGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIM 350
Cdd:PRK08149 271 RGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVF 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 306991568 351 DpNIVGSEHYDVARGVQKILQDYKSLQDIIAiLGMDELSE--EDKLTVSRARKIQRFLSQPFQVAEVF 416
Cdd:PRK08149 351 G-QVTDPKHRQLAAAFRKLLTRLEELQLFID-LGEYRRGEnaDNDRAMDKRPALEAFLKQDVAEKSSF 416
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
60-426 |
8.79e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 145.80 E-value: 8.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 60 GLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYA 139
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 140 KGGKIGLFGGAGVGKTVLiMELINNVAKAHggYSVFAGVGERTREGNDLY-HEMIESGVinlkdatSKVALVYGQMNEPP 218
Cdd:PRK07196 154 KGQRVGLMAGSGVGKSVL-LGMITRYTQAD--VVVVGLIGERGREVKEFIeHSLQAAGM-------AKSVVVAAPADESP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 219 GARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTK-KGSIT 297
Cdd:PRK07196 224 LMRIKATELCHAIATYYRDK-GHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSgNGTMT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 298 SVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDpNIVGSEHYDVARGVQKILQDYKSLQ 377
Cdd:PRK07196 303 AIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAIK 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 306991568 378 DIIA----ILGMDELSEEdklTVSRARKIQRFLSQPFQVAEVFTGHLGKLVPL 426
Cdd:PRK07196 382 PLIPlggyVAGADPMADQ---AVHYYPAITQFLRQEVGHPALFSASVEQLTGM 431
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
12-410 |
1.85e-37 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 142.66 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 12 VVDVQFDEglppiLNALEVQGRETRL--VLEVaqhlGESTVRTIAMDGTEGL-VRGQKVLDSGAPIRIPVGPETLGRIMN 88
Cdd:PRK04196 20 VEGVAYGE-----IVEIELPNGEKRRgqVLEV----SEDKAVVQVFEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 89 VIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKA 168
Cdd:PRK04196 91 GLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQ-AKV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 169 HGGYS----VFAGVGERTREGNDLYHEMIESGVINlkdatsKVALVYGQMNEPPGAR---ARVAltgLTVAEYFRDQEGQ 241
Cdd:PRK04196 170 LGEEEnfavVFAAMGITFEEANFFMEDFEETGALE------RSVVFLNLADDPAIERiltPRMA---LTAAEYLAFEKGM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 242 DVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQER--ITTTKKGSITSVQAIYVPADDLTDPAPATTFA 319
Cdd:PRK04196 241 HVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIPDLTGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 320 HLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNI----VGSEHYDV--------ARGVQkilqdyksLQDIIAILGMDE 387
Cdd:PRK04196 321 ITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIgegkTREDHKDVanqlyaayARGKD--------LRELAAIVGEEA 392
|
410 420
....*....|....*....|....
gi 306991568 388 LSEEDKLTVSRARKI-QRFLSQPF 410
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 ... |
73-354 |
5.74e-37 |
|
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: 5.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 73 PIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGV 152
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 153 GKTVLIMELINNVAKAHGGYS---VFAGVGERTREGNDLYHEMIESGVINlkdatsKVALVYGQMNEPPGARARVALTGL 229
Cdd:cd01135 81 PHNELAAQIARQAGVVGSEENfaiVFAAMGVTMEEARFFKDDFEETGALE------RVVLFLNLANDPTIERIITPRMAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 230 TVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQER--ITTTKKGSITSVQAIYVPAD 307
Cdd:cd01135 155 TTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMPND 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 306991568 308 DLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNI 354
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 ... |
2-74 |
5.98e-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: 127.63 E-value: 5.98e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306991568 2 TGRIVAVIGAVVDVQFDEG-LPPILNALEVQGRET-RLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPI 74
Cdd:cd18115 2 TGKIVQVIGPVVDVEFPEGeLPPIYNALEVKGDDGkKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
55-382 |
1.40e-33 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 131.83 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 55 MDGTEGLVRGQKVL-------DSGAPIRIPVGPETLGRIMNVIGEPID--------ERGPIKTKQFAAIHAEAPEfvems 119
Cdd:PRK07960 82 LEEVEGILPGARVYarnisgeGLQSGKQLPLGPALLGRVLDGSGKPLDglpapdtgETGALITPPFNPLQRTPIE----- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 120 veqEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLImeliNNVAKAHGGYSVFAG-VGERTREGNDLyhemIESgvI 198
Cdd:PRK07960 157 ---HVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLL----GMMARYTQADVIVVGlIGERGREVKDF----IEN--I 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 199 NLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLA 278
Cdd:PRK07960 224 LGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDR-GQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVF 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 279 TDMGTMQERITT--TKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMdPNIVG 356
Cdd:PRK07960 303 AKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAM-TALID 381
|
330 340
....*....|....*....|....*.
gi 306991568 357 SEHYDVARGVQKILQDYKSLQDIIAI 382
Cdd:PRK07960 382 EQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
38-442 |
2.77e-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: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 38 VLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVE 117
Cdd:TIGR00962 58 VQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 118 -MSVEQEiLVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHGGYSVFAGVGERTREGNDLYHEMIESG 196
Cdd:TIGR00962 138 rKSVHEP-LQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIIN-QKDSDVYCIYVAIGQKASTVAQVVRKLEEHG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 197 vinlkdATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPT 276
Cdd:TIGR00962 216 ------AMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDN-GKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGD 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 277 LATDMGTMQERITTTK----KGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRimdp 352
Cdd:TIGR00962 289 VFYLHSRLLERAAKLNdekgGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSR---- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 353 niVGSEHY-----DVARGVQKILQDYKSLqDIIAILGMDeLSEEDKLTVSRARKIQRFLSQPF--------QVAEVFTGH 419
Cdd:TIGR00962 365 --VGGAAQikamkQVAGSLRLELAQYREL-EAFSQFASD-LDEATKKQLERGQRVVELLKQPQykplsveeQVVILFAGT 440
|
410 420
....*....|....*....|....*
gi 306991568 420 LGKL--VPLKEtIKGFQQILAGEYD 442
Cdd:TIGR00962 441 KGYLddIPVDK-IRKFEQALLAYLD 464
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
64-440 |
5.11e-29 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 118.47 E-value: 5.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 64 GQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGK 143
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 144 IGLFGGAGVGKTvlimELINNVAK-AHGGYSVFAGVGERTREGNDlYHEMIESGVinlkdATSKVALVYGQMNEPPGARA 222
Cdd:PRK05922 160 IGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVRE-YIEQHKEGL-----AAQRTIIIASPAHETAPTKV 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 223 RVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAI 302
Cdd:PRK05922 230 IAGRAAMTIAEYFRDQ-GHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 303 -YVP--ADDLTDPAPATTFAHLDATTVlSRAIAElgiyPAVDPLDSTSRiMDPNIVGSEHYDVARGVQKILQDYKSLQDI 379
Cdd:PRK05922 309 lHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSR-SARQLALPHHYAAAEELRSLLKAYHEALDI 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306991568 380 IAiLGMDELSEEDKLtvSRARK----IQRFLSQPfqvaevftghLGKLVPLKETIKGFQQILAGE 440
Cdd:PRK05922 383 IQ-LGAYVPGQDAHL--DRAVKllpsIKQFLSQP----------LSSYCALHNTLKQLEALLKHE 434
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
3-349 |
7.29e-28 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 115.78 E-value: 7.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 3 GRIVAV------IGAVVDVQFDEglppilnALEVQGRETRLVLevaqHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRI 76
Cdd:PRK13343 29 GRVESVgdgiafVSGLPDAALDE-------LLRFEGGSRGFAF----NLEEELVGAVLLDDTADILAGTEVRRTGRVLEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 77 PVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTV 156
Cdd:PRK13343 98 PVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 157 LIMELINNvAKAHGGYSVFAGVGERTregndlyhemieSGVIN----LK--DATSKVALVYGQMNEPPGARARVALTGLT 230
Cdd:PRK13343 178 IAIDAIIN-QKDSDVICVYVAIGQKA------------SAVARvietLRehGALEYTTVVVAEASDPPGLQYLAPFAGCA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 231 VAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKK----GSITSVQAIYVPA 306
Cdd:PRK13343 245 IAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPelggGSLTALPIIETLA 323
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 306991568 307 DDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRI 349
Cdd:PRK13343 324 GELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRV 366
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
38-417 |
4.39e-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: 110.20 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 38 VLEVAQHLGESTVrtiaMDGTEGL-VRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFV 116
Cdd:TIGR01040 41 VLEVSGNKAVVQV----FEGTSGIdAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 117 EMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNV-------AKAHGGYS-----VFAGVGERTRE 184
Cdd:TIGR01040 117 ARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvklptKDVHDGHEdnfaiVFAAMGVNMET 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 185 GNDLYHEMIESGvinlkdATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALL 264
Cdd:TIGR01040 197 ARFFKQDFEENG------SMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 265 GRIPSAVGYQPTLATDMGTMQERI--TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDP 342
Cdd:TIGR01040 271 EEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 343 LDSTSRIMDPNI----VGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQR-FLSQ-PFQVAEVF 416
Cdd:TIGR01040 351 LPSLSRLMKSAIgegmTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQgPYENRTIF 430
|
.
gi 306991568 417 T 417
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, ... |
359-428 |
6.81e-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: 97.13 E-value: 6.81e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 359 HYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHLGKLVPLKE 428
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 ... |
123-348 |
1.34e-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: 103.04 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 123 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnvAKahggYS-----VFAGVGERtreGNdlyhEMIEsgV 197
Cdd:cd01134 58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSL----SK----WSnsdvvIYVGCGER---GN----EMAE--V 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 198 IN----LKDATS------KVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRI 267
Cdd:cd01134 121 LEefpeLKDPITgeslmeRTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEM 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 268 PSAVGYQPTLATDMGTMQERI-------TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAV 340
Cdd:cd01134 200 PAEEGYPAYLGARLAEFYERAgrvrclgSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSI 279
|
....*...
gi 306991568 341 DPLDSTSR 348
Cdd:cd01134 280 NWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
123-408 |
9.03e-24 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 104.09 E-value: 9.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 123 EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinnvAKahggYS-----VFAGVGERtreGNdlyhEMIEsgV 197
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQL----AK----WAdadivIYVGCGER---GN----EMTE--V 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 198 IN----LKDATSKVALvygqM----------NEPPGAR-ARVaLTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSA 262
Cdd:PRK04192 272 LEefpeLIDPKTGRPL----MertvliantsNMPVAAReASI-YTGITIAEYYRDM-GYDVLLMADSTSRWAEALREISG 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 263 LLGRIPSAVGYQPTLATDMGTMQER---ITT--TKKGSITSVQAIYVPADDLTDPapaTTFAHLDATTV---LSRAIAEL 334
Cdd:PRK04192 346 RLEEMPGEEGYPAYLASRLAEFYERagrVKTlgGEEGSVTIIGAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 335 GIYPAVDPLDSTSR-------IMDPNIVG--SEHYDVARgvqKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKI-QR 404
Cdd:PRK04192 423 RHFPAINWLTSYSLyldqvapWWEENVDPdwRELRDEAM---DLLQREAELQEIVRLVGPDALPEEDRLILEVARLIrED 499
|
....
gi 306991568 405 FLSQ 408
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 ... |
76-349 |
1.86e-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: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 76 IPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKT 155
Cdd:cd01132 4 VPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 156 VLIMELINNvAKAHGGYSVFAGVGERTREGNDLYHEMIESGvinlkdATSKVALVYGQMNEPPGARARVALTGLTVAEYF 235
Cdd:cd01132 84 AIAIDTIIN-QKGKKVYCIYVAIGQKRSTVAQIVKTLEEHG------AMEYTIVVAATASDPAPLQYLAPYAGCAMGEYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 236 RDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGY-------QPTLATDMGTMQERItttKKGSITSVQAIYVPADD 308
Cdd:cd01132 157 RDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYpgdvfylHSRLLERAAKLSDEL---GGGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 306991568 309 LTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRI 349
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
38-268 |
7.18e-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: 85.86 E-value: 7.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 38 VLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVE 117
Cdd:COG0056 59 VYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVID 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 118 -MSVeQEILVTGIKVVDLLAPyakggkIG------LFGGAGVGKTVLIMELINNvAKAHGGYSVFAGVGERtregndlyh 190
Cdd:COG0056 139 rQPV-HEPLQTGIKAIDAMIP------IGrgqrelIIGDRQTGKTAIAIDTIIN-QKGKDVICIYVAIGQK--------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 191 emiESGVINLKDATSKvalvYGQM----------NEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEV 260
Cdd:COG0056 202 ---ASTVAQVVETLEE----HGAMeytivvaataSDPAPLQYIAPYAGCAMGEYFMDQ-GKDVLIVYDDLSKHAVAYREL 273
|
....*...
gi 306991568 261 SALLGRIP 268
Cdd:COG0056 274 SLLLRRPP 281
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
174-408 |
7.31e-18 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 86.61 E-value: 7.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 174 VFAGVGERTREGNDLYHEMIEsgvinLKDATS------KVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFI 247
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPK-----LKDPKTgkplmeRTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVALMA 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 248 DNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI-------TTTKKGSITSVQAIYVPADDLTDPAPATTFAH 320
Cdd:PRK14698 760 DSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRV 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 321 LDATTVLSRAIAELGIYPAVDPLDSTSRIMDP------NIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKL 394
Cdd:PRK14698 840 VKVFWALDADLARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERA 919
|
250
....*....|....*
gi 306991568 395 TVSRARKIQR-FLSQ 408
Cdd:PRK14698 920 ILLVARMLREdYLQQ 934
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
5-71 |
3.58e-17 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 75.66 E-value: 3.58e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 306991568 5 IVAVIGAVVDVQFDEG-LPPILNALEVQGRET-RLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSG 71
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGrLPGLLNALEVELVEFgSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
57-317 |
4.55e-17 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 83.16 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 57 GTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDeRGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLA 136
Cdd:PRK02118 57 GTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPID-GGPELEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 137 PYAKGGKIGLFGGAGVGKTVLIMELinnVAKAHGGYSVFAGVGERtregNDLYHEMIEsgviNLKD--ATSKVALVYGQM 214
Cdd:PRK02118 136 TLVESQKIPIFSVSGEPYNALLARI---ALQAEADIIILGGMGLT----FDDYLFFKD----TFENagALDRTVMFIHTA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 215 NEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQER-ITTTKK 293
Cdd:PRK02118 205 SDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKaVDFEDG 284
|
250 260
....*....|....*....|....
gi 306991568 294 GSITSVQAIYVPADDLTDPAPATT 317
Cdd:PRK02118 285 GSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
38-268 |
1.53e-16 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 81.65 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 38 VLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVE 117
Cdd:PRK09281 59 VYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 118 -MSVEqEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNvAKAHGGYSVFAGVGERtregndlyhemiESG 196
Cdd:PRK09281 139 rKSVH-EPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN-QKGKDVICIYVAIGQK------------AST 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 197 VINLKDATSKvalvYGQM----------NEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGR 266
Cdd:PRK09281 205 VAQVVRKLEE----HGAMeytivvaataSDPAPLQYLAPYAGCAMGEYFMDN-GKDALIVYDDLSKQAVAYRQLSLLLRR 279
|
..
gi 306991568 267 IP 268
Cdd:PRK09281 280 PP 281
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
53-376 |
2.83e-13 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 72.00 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 53 IAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPID------ERGPIKTKQ-FAAIHAEAPEFVEMSVEQEIL 125
Cdd:PTZ00185 94 ILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQtLGKVDAGAPNIVSRSPVNYNL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 126 VTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINN-------VAKAHGGYSVFAGVGERTREGNDLYHEMIESGVI 198
Cdd:PTZ00185 174 LTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSNVARIHRLLRSYGAL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 199 NLKDATSKVALvygqmnEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLA 278
Cdd:PTZ00185 254 RYTTVMAATAA------EPAGLQYLAPYSGVTMGEYFMNR-GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVF 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 279 TDMGTMQERITTTKK----GSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRimdpni 354
Cdd:PTZ00185 327 YLHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR------ 400
|
330 340
....*....|....*....|....*..
gi 306991568 355 VGSEHYDVA-RGV----QKILQDYKSL 376
Cdd:PTZ00185 401 VGSSAQNVAmKAVagklKGILAEYRKL 427
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
64-268 |
3.30e-11 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 64.98 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 64 GQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGK 143
Cdd:CHL00059 64 GSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 144 IGLFGGAGVGKTVLIMELINNvAKAHGGYSVFAGVGERTREGNDLYHEMIESGvinlkdATSKVALVYGQMNEPPGARAR 223
Cdd:CHL00059 144 ELIIGDRQTGKTAVATDTILN-QKGQNVICVYVAIGQKASSVAQVVTTLQERG------AMEYTIVVAETADSPATLQYL 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 306991568 224 VALTGLTVAEYFRdQEGQDVLLFIDNIFRFTQAGSEVSALLGRIP 268
Cdd:CHL00059 217 APYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
140-266 |
2.36e-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: 41.59 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 140 KGGKIGLFGGAGVGKTVLIMELINNVAKAHGGysVFAGVGERTREGNDLYHEMIESGvinlkdatskvalvygqMNEPPG 219
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG--VIYIDGEDILEEVLDQLLLIIVG-----------------GKKASG 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 306991568 220 ARARVALTGLTVAEYFRDQegqdvLLFIDNIFRFTQAGSEVSALLGR 266
Cdd:smart00382 62 SGELRLRLALALARKLKPD-----VLILDEITSLLDAEQEALLLLLE 103
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
79-194 |
1.62e-03 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 41.16 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306991568 79 GPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPeFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTV-- 156
Cdd:PRK14698 166 GEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRP-YKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVdg 244
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 306991568 157 --LIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIE 194
Cdd:PRK14698 245 dtLILTKEFGLIKIKDLYEILDGKGKKTVEGNEEWTELEE 284
|
|
| |
