|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-474 |
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: 971.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 1 MSQGKVVQIIGAVVDVEFPRDQVPQVYDALKID---GTDITLEVQQQLGDGIVRTIALGSTEGLKRGLQARNTGEGIKVP 77
Cdd:COG0055 3 MNTGKIVQVIGPVVDVEFPEGELPAIYNALEVEnegGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 78 VGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVN 157
Cdd:COG0055 83 VGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 158 MLELINNIATQHAGLSVFAGVGERTREGNDFYHEMQEAGVVKidnlpesKVAMVYGQMNEPPGNRLRVALTGLTMAEYFR 237
Cdd:COG0055 163 IMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTMAEYFR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 238 DEKdengkGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERITSTKTGSITSIQAVYVPADDYTD 317
Cdd:COG0055 236 DEE-----GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 318 PSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLDPLVIGQEHYDVARRVQGTLQRYKELKDIIAILGMDELSEE 397
Cdd:COG0055 311 PAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEE 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494142616 398 DKQAVSRARKCERFFSQPFHVAEVFTGSPGKYVSLAETIRGFKMIVDGDVDHIPEQAFYMVGGIDDAIKKAEEMGAK 474
Cdd:COG0055 391 DKLTVARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAE 467
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
4-471 |
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: 849.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 4 GKVVQIIGAVVDVEFPRDQVPQVYDALKIDGT---DITLEVQQQLGDGIVRTIALGSTEGLKRGLQARNTGEGIKVPVGK 80
Cdd:TIGR01039 3 GKVVQVIGPVVDVEFEQGELPRIYNALKVQNRaesELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 81 ATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVNMLE 160
Cdd:TIGR01039 83 ETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 161 LINNIATQHAGLSVFAGVGERTREGNDFYHEMQEAGVVKidnlpesKVAMVYGQMNEPPGNRLRVALTGLTMAEYFRDEK 240
Cdd:TIGR01039 163 LINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 241 dengkGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERITSTKTGSITSIQAVYVPADDYTDPSP 320
Cdd:TIGR01039 236 -----GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 321 ATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLDPLVIGQEHYDVARRVQGTLQRYKELKDIIAILGMDELSEEDKQ 400
Cdd:TIGR01039 311 ATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKL 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494142616 401 AVSRARKCERFFSQPFHVAEVFTGSPGKYVSLAETIRGFKMIVDGDVDHIPEQAFYMVGGIDDAIKKAEEM 471
Cdd:TIGR01039 391 TVERARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
2-476 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 807.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 2 SQGKVVQIIGAVVDVEFPRDQVPQVYDALKIDGTD-------ITLEVQQQLGDGIVRTIALGSTEGLKRGLQARNTGEGI 74
Cdd:CHL00060 15 NLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDtagqeinVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 75 KVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGK 154
Cdd:CHL00060 95 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 155 TVNMLELINNIATQHAGLSVFAGVGERTREGNDFYHEMQEAGVVKIDNLPESKVAMVYGQMNEPPGNRLRVALTGLTMAE 234
Cdd:CHL00060 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 235 YFRDEKDEngkgkDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERITSTKTGSITSIQAVYVPADD 314
Cdd:CHL00060 255 YFRDVNKQ-----DVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 315 YTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLDPLVIGQEHYDVARRVQGTLQRYKELKDIIAILGMDEL 394
Cdd:CHL00060 330 LTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDEL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 395 SEEDKQAVSRARKCERFFSQPFHVAEVFTGSPGKYVSLAETIRGFKMIVDGDVDHIPEQAFYMVGGIDDAIKKAEEMGAK 474
Cdd:CHL00060 410 SEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLEVE 489
|
..
gi 494142616 475 KA 476
Cdd:CHL00060 490 SK 491
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
4-464 |
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: 569.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 4 GKVVQIIGAVVDVEFPRdQVPQVYDALKI-DGTDITLEVQQQLGDGIVRTIALGSTEGLKRGLQARNTGEGIKVPVGKAT 82
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDG-ELPAIHSVLRAgREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 83 LGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVNMLELI 162
Cdd:TIGR03305 80 LSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 163 NNIATQHAGLSVFAGVGERTREGNDFYHEMQEAGVvkIDNLpeskvAMVYGQMNEPPGNRLRVALTGLTMAEYFRDEKde 242
Cdd:TIGR03305 160 HNMVGQHQGVSIFCGIGERCREGEELYREMKEAGV--LDNT-----VMVFGQMNEPPGARFRVGHTALTMAEYFRDDE-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 243 ngkGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERITSTKTGSITSIQAVYVPADDYTDPSPAT 322
Cdd:TIGR03305 231 ---KQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 323 TFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLDPLVIGQEHYDVARRVQGTLQRYKELKDIIAILGMDELSEEDKQAV 402
Cdd:TIGR03305 308 TFSHLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVV 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494142616 403 SRARKCERFFSQPFHVAEVFTGSPGKYVSLAETIRGFKMIVDGDVDHIPEQAFYMVGGIDDA 464
Cdd:TIGR03305 388 NRARRLERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
75-358 |
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: 553.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 75 KVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGK 154
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 155 TVNMLELINNIATQHAGLSVFAGVGERTREGNDFYHEMQEAGVvkIDNLPESKVAMVYGQMNEPPGNRLRVALTGLTMAE 234
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGV--INLDGLSKVALVYGQMNEPPGARARVALTGLTMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 235 YFRDEKdengkGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERITSTKTGSITSIQAVYVPADD 314
Cdd:cd01133 159 YFRDEE-----GQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADD 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 494142616 315 YTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLDP 358
Cdd:cd01133 234 LTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
75-354 |
1.42e-118 |
|
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: 348.29 E-value: 1.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 75 KVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGK 154
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 155 TVNMLELINNIATQHAGLSVFAGVGERTREGNDFYHEMQEAGVvkidnlpESKVAMVYGQMNEPPGNRLRVALTGLTMAE 234
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGA-------MERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 235 YFRDEkdengkGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERITSTKT--GSITSIQAVYVPA 312
Cdd:cd19476 154 YFRDN------GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDggGSITAIPAVSTPG 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 494142616 313 DDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSR 354
Cdd:cd19476 228 DDLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSR 269
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
128-353 |
3.32e-91 |
|
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: 276.16 E-value: 3.32e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 128 GIKVIDLVCPFAKGGKVGLFGGAGVGKTVnmleLINNIATQ-HAGLSVFAGVGERTREGNDFYHEMQEAGVVKidnlpes 206
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTV----LAGMIARQaSADVVVYALIGERGREVREFIEELLGSGALK------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 207 KVAMVYGQMNEPPGNRLRVALTGLTMAEYFRDekdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADE 286
Cdd:pfam00006 70 RTVVVVATSDEPPLARYRAPYTALTIAEYFRD------QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494142616 287 MGVLQERITST--KTGSITSIQAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTS 353
Cdd:pfam00006 144 LARLLERAGRVkgKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 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 ... |
360-467 |
7.07e-75 |
|
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: 230.44 E-value: 7.07e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 360 VIGQEHYDVARRVQGTLQRYKELKDIIAILGMDELSEEDKQAVSRARKCERFFSQPFHVAEVFTGSPGKYVSLAETIRGF 439
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 494142616 440 KMIVDGDVDHIPEQAFYMVGGIDDAIKK 467
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
4-443 |
1.01e-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: 220.29 E-value: 1.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 4 GKVVQIIGAVVDVEFPRDQVPQVYDALKIDGTDITLEVqqqLG--DGIVRTIALGSTEGLKRGLQARNTGEGIKVPVGKA 81
Cdd:COG1157 21 GRVTRVVGLLIEAVGPDASIGELCEIETADGRPVLAEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 82 TLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVnmleL 161
Cdd:COG1157 98 LLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKST----L 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 162 INNIA--TQhAGLSVFAGVGERTREGNDFY-HEMQEAG----VVkidnlpeskvamVYGQMNEPPGNRLRVALTGLTMAE 234
Cdd:COG1157 174 LGMIArnTE-ADVNVIALIGERGREVREFIeDDLGEEGlarsVV------------VVATSDEPPLMRLRAAYTATAIAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 235 YFRDekdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERITSTKTGSITSIQAVYVPADD 314
Cdd:COG1157 241 YFRD------QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 315 YTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRqLDPLVIGQEHYDVARRVQGTLQRYKELKDIIAI----LG 390
Cdd:COG1157 315 MNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISR-VMPDIVSPEHRALARRLRRLLARYEENEDLIRIgayqPG 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 494142616 391 MDElsEEDkQAVSRARKCERFFSQPFHVAevftgspgkyVSLAETIRGFKMIV 443
Cdd:COG1157 394 SDP--ELD-EAIALIPAIEAFLRQGMDER----------VSFEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
75-354 |
1.32e-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: 196.63 E-value: 1.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 75 KVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGK 154
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 155 TVNMLELINNIAtqhAGLSVFAGVGERTREGNDFY-HEMQEAGVvkidnlpeSKVAMVYGQMNEPPGNRLRVALTGLTMA 233
Cdd:cd01136 81 STLLGMIARNTD---ADVNVIALIGERGREVREFIeKDLGEEGL--------KRSVLVVATSDESPLLRVRAAYTATAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 234 EYFRDEkdengkGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERITSTKTGSITSIQAVYVPAD 313
Cdd:cd01136 150 EYFRDQ------GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGD 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 494142616 314 DYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSR 354
Cdd:cd01136 224 DFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
55-416 |
2.15e-50 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 177.11 E-value: 2.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 55 LGSTEGLKRGLQARNTGEGIKVPVGKATLGRIMDVLGNPIDE-VGPINAE---DHWVIHREAPSYDEQAAANDLLETGIK 130
Cdd:PRK08149 61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERfDAPPTVGpisEERVIDVAPPSYAERRPIREPLITGVR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 131 VID--LVCpfAKGGKVGLFGGAGVGKTVNMLELINNIAtqhAGLSVFAGVGERTREGNDFYHEMQEAGvvkidnlPESKV 208
Cdd:PRK08149 141 AIDglLTC--GVGQRMGIFASAGCGKTSLMNMLIEHSE---ADVFVIGLIGERGREVTEFVESLRASS-------RREKC 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 209 AMVYGQMNEPPGNRLRVALTGLTMAEYFRDEkdengkGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMG 288
Cdd:PRK08149 209 VLVYATSDFSSVDRCNAALVATTVAEYFRDQ------GKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLP 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 289 VLQERITSTKTGSITSIQAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRqldplVIGQ----E 364
Cdd:PRK08149 283 RLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSR-----VFGQvtdpK 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 494142616 365 HYDVARRVQGTLQRYKELKDIIAiLGMDELSE--EDKQAVSRARKCERFFSQPF 416
Cdd:PRK08149 358 HRQLAAAFRKLLTRLEELQLFID-LGEYRRGEnaDNDRAMDKRPALEAFLKQDV 410
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
59-443 |
4.08e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 174.10 E-value: 4.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 59 EGLKRGLQARNTGEGIKVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVID--LVC 136
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDglLTC 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 137 pfAKGGKVGLFGGAGVGKTVNMLELINNiatQHAGLSVFAGVGERTREGNDFYHEmqeagvvKIDNLPESKVAMVyGQMN 216
Cdd:PRK08472 155 --GKGQKLGIFAGSGVGKSTLMGMIVKG---CLAPIKVVALIGERGREIPEFIEK-------NLGGDLENTVIVV-ATSD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 217 EPPGNRLRVALTGLTMAEYFRDekdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERITS 296
Cdd:PRK08472 222 DSPLMRKYGAFCAMSVAEYFKN------QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 297 TKT-GSITSIQAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLDPlVIGQEHYDVARRVQGT 375
Cdd:PRK08472 296 EEGkGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMND-IISPEHKLAARKFKRL 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494142616 376 LQRYKELKDIIAI----LGMD-ELSEedkqAVSRARKCERFFSQpfhvaevftgSPGKYVSLAETIRGFKMIV 443
Cdd:PRK08472 375 YSLLKENEVLIRIgayqKGNDkELDE----AISKKEFMEQFLKQ----------NPNELFPFEQTFEQLEEIL 433
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
71-388 |
8.87e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 173.35 E-value: 8.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 71 GEGIKVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGA 150
Cdd:PRK08972 92 GEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 151 GVGKTVnMLELINNIATqhAGLSVFAGVGERTREGNDFYHE-MQEAGvvkidnlpESKVAMVYGQMNEPPGNRLRVALTG 229
Cdd:PRK08972 172 GVGKSV-LLGMMTRGTT--ADVIVVGLVGERGREVKEFIEEiLGEEG--------RARSVVVAAPADTSPLMRLKGCETA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 230 LTMAEYFRDekdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERIT--STKTGSITSIQA 307
Cdd:PRK08972 241 TTIAEYFRD------QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPGQGSITAFYT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 308 VYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLdPLVIGQEHYDVARRVQGTLQRYKELKDIIA 387
Cdd:PRK08972 315 VLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLIS 393
|
.
gi 494142616 388 I 388
Cdd:PRK08972 394 I 394
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
57-414 |
1.85e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 172.31 E-value: 1.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 57 STEGLKRGLQARNTGEGIKVPVGKATLGRIMDVLGNPIDEVGPinAEDHW-VIHREAPSYDEQAAANDLLETGIKVIDLV 135
Cdd:PRK06820 80 SSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPP--LTGQWrELDCPPPSPLTRQPIEQMLTTGIRAIDGI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 136 CPFAKGGKVGLFGGAGVGKTVnMLELInnIATQHAGLSVFAGVGERTREGNDF--YHEMQEAgvvkidnlpESKVAMVYG 213
Cdd:PRK06820 158 LSCGEGQRIGIFAAAGVGKST-LLGML--CADSAADVMVLALIGERGREVREFleQVLTPEA---------RARTVVVVA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 214 QMNEPPGNRLRVALTGLTMAEYFRDekdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQER 293
Cdd:PRK06820 226 TSDRPALERLKGLSTATTIAEYFRD------RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLER 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 294 ITSTKTGSITSIQAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLDPLViGQEHYDVARRVQ 373
Cdd:PRK06820 300 TGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIV-SAGQLAMAQKLR 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 494142616 374 GTLQRYKELKDIIAI----LGMDELSEEdkqAVSRARKCERFFSQ 414
Cdd:PRK06820 379 RMLACYQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
3-388 |
1.29e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 167.24 E-value: 1.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 3 QGKVVQIIGAVVDVEFPRDQVPQVydaLKIDGTDITLEVQQQLgDGIVRTIAL----GSTEGLKRGLQARNTGEGIKVPV 78
Cdd:PRK06936 24 RGRVTQVTGTILKAVVPGVRIGEL---CYLRNPDNSLSLQAEV-IGFAQHQALltplGEMYGISSNTEVSPTGTMHQVGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 79 GKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVNM 158
Cdd:PRK06936 100 GEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 159 LELINNIAtqhAGLSVFAGVGERTREGNDFY-HEMQEAGVvkidnlpeSKVAMVYGQMNEPPGNRLRVALTGLTMAEYFR 237
Cdd:PRK06936 180 ASLIRSAE---VDVTVLALIGERGREVREFIeSDLGEEGL--------RKAVLVVATSDRPSMERAKAGFVATSIAEYFR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 238 DEkdengkGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERITSTKTGSITSIQAVYVPADDYTD 317
Cdd:PRK06936 249 DQ------GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTE 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494142616 318 PSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLDPLViGQEHYDVARRVQGTLQRYKELKDIIAI 388
Cdd:PRK06936 323 PVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIV-SKEHKTWAGRLRELLAKYEEVELLLQI 392
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
84-390 |
2.51e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 164.02 E-value: 2.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 84 GRIMDVLGNPIDEVGPINAEDHWV-IHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGKT--VNMLe 160
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKStlLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 161 linniaTQHAGLS--VFAGVGERTREGNDFYHEmqeagvVKIDNLpeSKVAMVYGQMNEPPGNRLRVALTGLTMAEYFRD 238
Cdd:PRK06002 186 ------ARADAFDtvVIALVGERGREVREFLED------TLADNL--KKAVAVVATSDESPMMRRLAPLTATAIAEYFRD 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 239 ekdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERI--TSTKTGSITSIQAVYVPADDYT 316
Cdd:PRK06002 252 ------RGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHN 325
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494142616 317 DPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRqLDPLVIGQEHYDVARRVQGTLQRYKELKDIIAILG 390
Cdd:PRK06002 326 DPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISR-LARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGG 398
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
4-415 |
4.51e-45 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 163.40 E-value: 4.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 4 GKVVQIIGAVvdvefprdqvpqvydaLKIDGTDITL----EVQQQLGD--------GIVRTIAL----GSTEGLKRGLQA 67
Cdd:PRK09099 26 GKVVEVIGTL----------------LRVSGLDVTLgelcELRQRDGTllqraevvGFSRDVALlspfGELGGLSRGTRV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 68 RNTGEGIKVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLF 147
Cdd:PRK09099 90 IGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 148 GGAGVGKTVNMLELINNIATQhagLSVFAGVGERTREGNDFY-HEMQEAGVvkidnlpeSKVAMVYGQMNEPPGNRLRVA 226
Cdd:PRK09099 170 APAGVGKSTLMGMFARGTQCD---VNVIALIGERGREVREFIeLILGEDGM--------ARSVVVCATSDRSSIERAKAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 227 LTGLTMAEYFRDekdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERITSTKTGSITSIQ 306
Cdd:PRK09099 239 YVATAIAEYFRD------RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 307 AVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLdPLVIGQEHYDVARRVQGTLQRYKELKDII 386
Cdd:PRK09099 313 TVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLL 391
|
410 420 430
....*....|....*....|....*....|...
gi 494142616 387 AI----LGMDELSEEdkqAVSRARKCERFFSQP 415
Cdd:PRK09099 392 QVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
4-388 |
1.17e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 159.50 E-value: 1.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 4 GKVVQIIGAVVDVEFPRDQVPQV-YDALKIDGTD-ITLEVQQQLGDGI-------VRTIALGS-TEGlkrglqarnTGEG 73
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESSIGDVcYIHTKGGGDKaIKAEVVGFKDEHVllmpyteVAEIAPGClVEA---------TGKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 74 IKVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVG 153
Cdd:PRK07721 91 LEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 154 KTVnmleLINNIATQ-HAGLSVFAGVGERTREGNDFyhemqeagvVKIDNLPE--SKVAMVYGQMNEPPGNRLRVALTGL 230
Cdd:PRK07721 171 KST----LMGMIARNtSADLNVIALIGERGREVREF---------IERDLGPEglKRSIVVVATSDQPALMRIKGAYTAT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 231 TMAEYFRDekdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERITSTKTGSITSIQAVYV 310
Cdd:PRK07721 238 AIAEYFRD------QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLV 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494142616 311 PADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLdPLVIGQEHYDVARRVQGTLQRYKELKDIIAI 388
Cdd:PRK07721 312 DGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
4-388 |
5.57e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 157.45 E-value: 5.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 4 GKVVQIIGAVVDVEFPRDQVpQVYDALKI---DGTDITLEVqqqLGDGIVRTIAL--GSTEGLKRGLQARNTGEGIKVPV 78
Cdd:PRK08927 19 GRVVAVRGLLVEVAGPIHAL-SVGARIVVetrGGRPVPCEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVRP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 79 GKATLGRIMDVLGNPIDEVGPI-NAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVN 157
Cdd:PRK08927 95 SRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 158 MLELINNIAtqhAGLSVFAGVGERTREGNDFYHE-MQEAGvvkidnLPESKVamVYGQMNEPPGNRLRVALTGLTMAEYF 236
Cdd:PRK08927 175 LSMLARNAD---ADVSVIGLIGERGREVQEFLQDdLGPEG------LARSVV--VVATSDEPALMRRQAAYLTLAIAEYF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 237 RDEkdengkGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERI--TSTKTGSITSIQAVYVPADD 314
Cdd:PRK08927 244 RDQ------GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDD 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494142616 315 YTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLdPLVIGQEHYDVARRVQGTLQRYKELKDIIAI 388
Cdd:PRK08927 318 HNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
78-414 |
3.52e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 155.05 E-value: 3.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 78 VGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVn 157
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSV- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 158 MLELINNiATQhAGLSVFAGVGERTREGNDFY-HEMQEAGVvkidnlpeSKVAMVYGQMNEPPGNRLRVALTGLTMAEYF 236
Cdd:PRK07196 171 LLGMITR-YTQ-ADVVVVGLIGERGREVKEFIeHSLQAAGM--------AKSVVVAAPADESPLMRIKATELCHAIATYY 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 237 RDekdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERI-TSTKTGSITSIQAVYVPADDY 315
Cdd:PRK07196 241 RD------KGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMTAIYTVLAEGDDQ 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 316 TDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLDPlVIGQEHYDVARRVQGTLQRYKELKDIIA----ILGM 391
Cdd:PRK07196 315 QDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQ-VIGSQQAKAASLLKQCYADYMAIKPLIPlggyVAGA 393
|
330 340
....*....|....*....|...
gi 494142616 392 DELSEedkQAVSRARKCERFFSQ 414
Cdd:PRK07196 394 DPMAD---QAVHYYPAITQFLRQ 413
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
55-388 |
7.06e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 154.89 E-value: 7.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 55 LGSTEGLKRGLQARNTGEGIKVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDL 134
Cdd:PRK05688 82 VGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSING 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 135 VCPFAKGGKVGLFGGAGVGKTVnMLELINNIATqhAGLSVFAGVGERTREGNDFY-HEMQEAGVvkidnlpeSKVAMVYG 213
Cdd:PRK05688 162 LLTVGRGQRLGLFAGTGVGKSV-LLGMMTRFTE--ADIIVVGLIGERGREVKEFIeHILGEEGL--------KRSVVVAS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 214 QMNEPPGNRLRVALTGLTMAEYFRDekdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQER 293
Cdd:PRK05688 231 PADDAPLMRLRAAMYCTRIAEYFRD------KGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVER 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 294 ITSTKTG--SITSIQAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLdPLVIGQEHYDVARR 371
Cdd:PRK05688 305 AGNAEPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQR 383
|
330
....*....|....*..
gi 494142616 372 VQGTLQRYKELKDIIAI 388
Cdd:PRK05688 384 FKQLWSRYQQSRDLISV 400
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
56-388 |
5.14e-41 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 152.03 E-value: 5.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 56 GSTEGLKRGLQARNTGEGIKVPVGKATLGRIMDVLGNPIDevgpiNAEDHWVIHRE-----APSYDEQAAANDLLeTGIK 130
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLD-----GRELPDVCWKDydampPPAMVRQPITQPLM-TGIR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 131 VIDLVCPFAKGGKVGLFGGAGVGKTVnMLELINNiaTQHAGLSVFAGVGERTREGNDFYHEMqeagvvkIDNLPESKVAM 210
Cdd:PRK07594 145 AIDSVATCGEGQRVGIFSAPGVGKST-LLAMLCN--APDADSNVLVLIGERGREVREFIDFT-------LSEETRKRCVI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 211 VYGQMNEPPGNRLRVALTGLTMAEYFRDEkdengkGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVL 290
Cdd:PRK07594 215 VVATSDRPALERVRALFVATTIAEFFRDN------GKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 291 QERITSTKTGSITSIQAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLdPLVIGQEHYDVAR 370
Cdd:PRK07594 289 LERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAA 367
|
330
....*....|....*...
gi 494142616 371 RVQGTLQRYKELKDIIAI 388
Cdd:PRK07594 368 ILRRCLALYQEVELLIRI 385
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
70-398 |
3.54e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 141.65 E-value: 3.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 70 TGEGIKVPVGKATLGRIMDVLGNPIDEvgPINAEDHWVIHREAPSYD--EQAAANDLLETGIKVIDLVCPFAKGGKVGLF 147
Cdd:PRK06793 85 IAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIHafEREEITDVFETGIKSIDSMLTIGIGQKIGIF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 148 GGAGVGKTVnMLELINNIATqhAGLSVFAGVGERTREGNDFYH-EMQEAGVvkidnlpeSKVAMVYGQMNEPPGNRLRVA 226
Cdd:PRK06793 163 AGSGVGKST-LLGMIAKNAK--ADINVISLVGERGREVKDFIRkELGEEGM--------RKSVVVVATSDESHLMQLRAA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 227 LTGLTMAEYFRDEkdengkGKDVLFFVDNIYRYTLAGTEVSALLGRMPsaVGYQPTLADE-MGVLQERITSTKTGSITSI 305
Cdd:PRK06793 232 KLATSIAEYFRDQ------GNNVLLMMDSVTRFADARRSVDIAVKELP--IGGKTLLMESyMKKLLERSGKTQKGSITGI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 306 QAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLDPLViGQEHYDVARRVQGTLQRYKElKDI 385
Cdd:PRK06793 304 YTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIV-SPNHWQLANEMRKILSIYKE-NEL 381
|
330
....*....|...
gi 494142616 386 IAILGMDELSEED 398
Cdd:PRK06793 382 YFKLGTIQENAEN 394
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
55-417 |
9.64e-36 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 138.04 E-value: 9.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 55 LGSTEGLK-RGLQARNTGEGIKVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIH--------REAPSydeqaaanDLL 125
Cdd:PRK04196 56 FEGTTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINgapinpvaREYPE--------EFI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 126 ETGIKVID----LVcpfaKGGKVGLFGGAGVgkTVNMLELinNIATQHAGLS-------VFAGVGERTREGNDFYHEMQE 194
Cdd:PRK04196 128 QTGISAIDglntLV----RGQKLPIFSGSGL--PHNELAA--QIARQAKVLGeeenfavVFAAMGITFEEANFFMEDFEE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 195 AGVVkidnlpeSKVAMVYGQMNEPPGNRL---RVAltgLTMAEYFRDEKDengkgKDVLFFVDNIYRYTLAGTEVSALLG 271
Cdd:PRK04196 200 TGAL-------ERSVVFLNLADDPAIERIltpRMA---LTAAEYLAFEKG-----MHVLVILTDMTNYCEALREISAARE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 272 RMPSAVGYQPTLADEMGVLQER--ITSTKTGSITSIQAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPL 349
Cdd:PRK04196 265 EVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVL 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494142616 350 ASTSRQLDpLVIG-----QEHYDVARRVQGTLQRYKELKDIIAILGMDELSEEDKQAVSRARKCE-RFFSQPFH 417
Cdd:PRK04196 345 PSLSRLMK-DGIGegktrEDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFErEFVNQGFD 417
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
63-388 |
3.29e-34 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 133.76 E-value: 3.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 63 RGLQARNTGEGIKVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGG 142
Cdd:PRK07960 97 RNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 143 KVGLFGGAGVGKTVnmleLINNIA--TQhAGLSVFAGVGERTREGNDFyhemqeagvvkIDNL--PE--SKVAMVYGQMN 216
Cdd:PRK07960 177 RMGLFAGSGVGKSV----LLGMMAryTQ-ADVIVVGLIGERGREVKDF-----------IENIlgAEgrARSVVIAAPAD 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 217 EPPGNRLRVALTGLTMAEYFRDekdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERITS 296
Cdd:PRK07960 241 VSPLLRMQGAAYATRIAEDFRD------RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGN 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 297 --TKTGSITSIQAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLDPLvIGQEHYDVARRVQG 374
Cdd:PRK07960 315 giSGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAL-IDEQHYARVRQFKQ 393
|
330
....*....|....
gi 494142616 375 TLQRYKELKDIIAI 388
Cdd:PRK07960 394 LLSSFQRNRDLVSV 407
|
|
| 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 |
1.63e-32 |
|
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic.
Pssm-ID: 349739 [Multi-domain] Cd Length: 76 Bit Score: 118.39 E-value: 1.63e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494142616 2 SQGKVVQIIGAVVDVEFPRDQVPQVYDALKI---DGTDITLEVQQQLGDGIVRTIALGSTEGLKRGLQARNTGEGI 74
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVkgdDGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
75-362 |
4.09e-31 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 121.18 E-value: 4.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 75 KVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIH--------REAPSydeqaaanDLLETGIKVIDLVCPFAKGGKVGL 146
Cdd:cd01135 3 KLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINgppinpvaRIYPE--------EMIQTGISAIDVMNTLVRGQKLPI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 147 FGGAGvgktvnmlELINNIATQ---HAGLS--------VFAGVGERTREGNDFYHEMQEAGVVkidnlpeSKVAMVYGQM 215
Cdd:cd01135 75 FSGSG--------LPHNELAAQiarQAGVVgseenfaiVFAAMGVTMEEARFFKDDFEETGAL-------ERVVLFLNLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 216 NEPPGNRLRVALTGLTMAEYFRDEkdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQER-- 293
Cdd:cd01135 140 NDPTIERIITPRMALTTAEYLAYE-----KGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERag 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494142616 294 ITSTKTGSITSIQAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRqLDPLVIG 362
Cdd:cd01135 215 RVEGRKGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR-LMKSGIG 282
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
50-415 |
2.41e-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: 2.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 50 VRTIALGSTEGLKRGLQARNTGEGIKVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGI 129
Cdd:TIGR00962 70 VGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 130 KVIDLVCPFAKGGKVGLFGGAGVGKTVNMLELINNIATQHAgLSVFAGVGERTREGNDFYHEMQEAGVVKidnlpesKVA 209
Cdd:TIGR00962 150 KAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIINQKDSDV-YCIYVAIGQKASTVAQVVRKLEEHGAMA-------YTI 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 210 MVYGQMNEPPGNRLRVALTGLTMAEYFRDekdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGY---------- 279
Cdd:TIGR00962 222 VVAATASDSASLQYLAPYTGCTMGEYFRD------NGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFpgdvfylhsr 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 280 ----QPTLADEMGvlqeritstkTGSITSIQAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRq 355
Cdd:TIGR00962 296 llerAAKLNDEKG----------GGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSR- 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494142616 356 ldplVIGQEHYDVARRVQGTLQ----RYKELkDIIAILGMDeLSEEDKQAVSRARKCERFFSQP 415
Cdd:TIGR00962 365 ----VGGAAQIKAMKQVAGSLRlelaQYREL-EAFSQFASD-LDEATKKQLERGQRVVELLKQP 422
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
76-444 |
5.68e-28 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 115.39 E-value: 5.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 76 VPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGKT 155
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 156 vnmlELINNIAT-QHAGLSVFAGVGERTREGNDFYHEMQEAgvvkidnLPESKVAMVYGQMNEPPGNRLRVALTGLTMAE 234
Cdd:PRK05922 172 ----SLLSTIAKgSKSTINVIALIGERGREVREYIEQHKEG-------LAAQRTIIIASPAHETAPTKVIAGRAAMTIAE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 235 YFRDEkdengkGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERITSTKTGSITSIQAV-YVP-- 311
Cdd:PRK05922 241 YFRDQ------GHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnh 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 312 ADDYTDPSPATtfahLDSTVALSRDIASLGiYPAVDPLASTSRQLDPLVIgQEHYDVARRVQGTLQRYKELKDIIAILGM 391
Cdd:PRK05922 315 PDIFTDYLKSL----LDGHFFLTPQGKALA-SPPIDILTSLSRSARQLAL-PHHYAAAEELRSLLKAYHEALDIIQLGAY 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 494142616 392 DELSEED-KQAVSRARKCERFFSQPFhvaevftgspGKYVSLAETIRGFKMIVD 444
Cdd:PRK05922 389 VPGQDAHlDRAVKLLPSIKQFLSQPL----------SSYCALHNTLKQLEALLK 432
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
53-354 |
1.72e-23 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 103.07 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 53 IALGSTEGLKRGLQARNTGEGIKVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVI 132
Cdd:PRK13343 74 VLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 133 DLVCPFAKGGKVGLFGGAGVGKTVNMLELINNiatQHAG--LSVFAGVGERTregndfyhemqeAGVVK-IDNL-----P 204
Cdd:PRK13343 154 DALIPIGRGQRELIIGDRQTGKTAIAIDAIIN---QKDSdvICVYVAIGQKA------------SAVARvIETLrehgaL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 205 ESKVAMVyGQMNEPPGNRLRVALTGLTMAEYFRDekdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYqPtlA 284
Cdd:PRK13343 219 EYTTVVV-AEASDPPGLQYLAPFAGCAIAEYFRD------QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAY-P--G 288
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494142616 285 DEMGV---LQERIT----STKTGSITSIQAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSR 354
Cdd:PRK13343 289 DIFYLhsrLLERAAklspELGGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
41-417 |
4.01e-23 |
|
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: 101.72 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 41 VQQQLGDGIVRTIALGSTEGLK---------RGLQARN-----TGEGIKVPVGKATLGRIMDVLGNPIDEVGPINAEDHW 106
Cdd:TIGR01040 27 VNLTLPDGTVRSGQVLEVSGNKavvqvfegtSGIDAKKttcefTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 107 VIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGKtvnmleliNNIATQ---HAGLS---------- 173
Cdd:TIGR01040 107 DINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPH--------NEIAAQicrQAGLVklptkdvhdg 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 174 -------VFAGVGERTREGNDFYHEMQEAGVVKidnlpesKVAMVYGQMNEPPGNRLRVALTGLTMAEYFRDEkdengKG 246
Cdd:TIGR01040 179 hednfaiVFAAMGVNMETARFFKQDFEENGSME-------RVCLFLNLANDPTIERIITPRLALTTAEYLAYQ-----CE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 247 KDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERI--TSTKTGSITSIQAVYVPADDYTDPSPATTF 324
Cdd:TIGR01040 247 KHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 325 AHLDSTVALSRDIASLGIYPAVDPLASTSRqLDPLVIGQ-----EHYDVARRVQGTLQRYKELKDIIAILGMDELSEEDK 399
Cdd:TIGR01040 327 YITEGQIYVDRQLHNRQIYPPINVLPSLSR-LMKSAIGEgmtrkDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDL 405
|
410
....*....|....*....
gi 494142616 400 QAVSRARKCER-FFSQPFH 417
Cdd:TIGR01040 406 LYLEFLDKFEKnFIAQGPY 424
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
76-354 |
5.29e-23 |
|
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: 98.42 E-value: 5.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 76 VPVGKATLGRIMDVLGNPIDEV----GP-----INAEdHWVIHREAPsYDEQAAANDLLETGIKVIDLVCPFAKGGKVGL 146
Cdd:cd01134 4 VELGPGLLGSIFDGIQRPLEVIaetgSIfiprgVNVQ-RWPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 147 FGGAGVGKTVnmlelinniaTQHAgLS--------VFAGVGERtreGNdfyhEMQEAgvvkIDNLPESKV---------- 208
Cdd:cd01134 82 PGPFGCGKTV----------ISQS-LSkwsnsdvvIYVGCGER---GN----EMAEV----LEEFPELKDpitgeslmer 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 209 -AMVYGQMNEPPGNRLRVALTGLTMAEYFRDekdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEM 287
Cdd:cd01134 140 tVLIANTSNMPVAAREASIYTGITIAEYFRD------MGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARL 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494142616 288 GVLQERITSTKT-------GSITSIQAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSR 354
Cdd:cd01134 214 AEFYERAGRVRClgspgreGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
157-439 |
2.68e-21 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 97.40 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 157 NMLELINNIATQH-------AGLSVFAGVGERTREGNDFYHEMQEAGVVKIDNLPESKVAMVYGQMNEPPGNRLRVALTG 229
Cdd:PRK14698 662 NMPTLLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTG 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 230 LTMAEYFRDekdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERI-------TSTKTGSI 302
Cdd:PRK14698 742 ITIAEYFRD------MGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSV 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 303 TSIQAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSRQLDPLV------IGQEHYDVARRVQGTL 376
Cdd:PRK14698 816 SVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKdwwhknVDPEWKAMRDKAMELL 895
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494142616 377 QRYKELKDIIAILGMDELSEEDKQAVSRARKCERFFSQPFHVAEVFT-GSPGKYVSLAETIRGF 439
Cdd:PRK14698 896 QKEAELQEIVRIVGPDALPERERAILLVARMLREDYLQQDAFDEVDTyCPPEKQVTMMRVLLNF 959
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
5-410 |
2.30e-20 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 93.17 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 5 KVVQIIGAVVDV--EFPR-DQVPQVYDA--------LKIDGTDITLEVqqqlgdgivrtiaLGSTEGLKRGLQARNTGEG 73
Cdd:PRK02118 7 KITDITGNVITVeaEGVGyGELATVERKdgsslaqvIRLDGDKVTLQV-------------FGGTRGISTGDEVVFLGRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 74 IKVPVGKATLGRIMDVLGNPIDEvGPINAEDHWVIhrEAPSYD--EQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAg 151
Cdd:PRK02118 74 MQVTYSESLLGRRFNGSGKPIDG-GPELEGEPIEI--GGPSVNpvKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVS- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 152 vGKTVNmlELINNIATQ-HAGLSVFAGVGERTREGNDFYHEMQEAGVVkidnlpeSKVAMVYGQMNEPPGNRLRVALTGL 230
Cdd:PRK02118 150 -GEPYN--ALLARIALQaEADIIILGGMGLTFDDYLFFKDTFENAGAL-------DRTVMFIHTASDPPVECLLVPDMAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 231 TMAEYFRDEkdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQERITSTK-TGSITSIQAVY 309
Cdd:PRK02118 220 AVAEKFALE-----GKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEdGGSITIIAVTT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 310 VPADDYTDPSPATTFAHLDSTVALSRDiaslgiypAVDPLASTSRqLDPLVIGQEHYDVARRVQGTLQR-YKELKDIIAI 388
Cdd:PRK02118 295 MPGDDVTHPVPDNTGYITEGQFYLRRG--------RIDPFGSLSR-LKQLVIGKKTREDHGDLMNAMIRlYADSREAKEK 365
|
410 420
....*....|....*....|...
gi 494142616 389 LGMD-ELSEEDKQAVSRARKCER 410
Cdd:PRK02118 366 MAMGfKLSNWDEKLLKFSELFES 388
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
110-399 |
5.71e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 92.92 E-value: 5.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 110 REAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVnmlelinniaTQHAgLS--------VFAGVGER 181
Cdd:PRK04192 196 RRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTV----------TQHQ-LAkwadadivIYVGCGER 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 182 treGNdfyhEMQEAgvvkIDNLPEskvamvygqMNEP-PGNRL--R-----------VA------LTGLTMAEYFRDekd 241
Cdd:PRK04192 265 ---GN----EMTEV----LEEFPE---------LIDPkTGRPLmeRtvliantsnmpVAareasiYTGITIAEYYRD--- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 242 engKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLADEMGVLQER----IT-STKTGSITSIQAVYVPADDYT 316
Cdd:PRK04192 322 ---MGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTIIGAVSPPGGDFS 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 317 DP-SPAT-----TFAHLDSTVALSRDiaslgiYPAVDPLASTSRQLDPL------VIGQEHYDVARRVQGTLQRYKELKD 384
Cdd:PRK04192 399 EPvTQNTlrivkVFWALDAELADRRH------FPAINWLTSYSLYLDQVapwweeNVDPDWRELRDEAMDLLQREAELQE 472
|
330
....*....|....*
gi 494142616 385 IIAILGMDELSEEDK 399
Cdd:PRK04192 473 IVRLVGPDALPEEDR 487
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
74-354 |
1.67e-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: 88.38 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 74 IKVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVG 153
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 154 KTVNMLELINNIATQHAgLSVFAGVGERTREGNDFYHEMQEAGVVKidnlpesKVAMVYGQMNEPPGNRLRVALTGLTMA 233
Cdd:cd01132 82 KTAIAIDTIINQKGKKV-YCIYVAIGQKRSTVAQIVKTLEEHGAME-------YTIVVAATASDPAPLQYLAPYAGCAMG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 234 EYFRDekdengKGKDVLFFVDNIYRYTLAGTEVSALLGR------MPSAVGY--------QPTLADEMGvlqeritstkT 299
Cdd:cd01132 154 EYFRD------NGKHALIIYDDLSKQAVAYRQMSLLLRRppgreaYPGDVFYlhsrllerAAKLSDELG----------G 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 494142616 300 GSITSIQAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVDPLASTSR 354
Cdd:cd01132 218 GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
55-274 |
7.62e-18 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 85.89 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 55 LGSTEGLKRGLQARNTGEGIKVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDL 134
Cdd:PRK09281 76 LGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 135 VCPFAKGGKVGLFGGAGVGKTVNMLELINNiatQHAG--LSVFAGVGERtregndfyhemqEAGVVKIDNLPESKVAMVY 212
Cdd:PRK09281 156 MIPIGRGQRELIIGDRQTGKTAIAIDTIIN---QKGKdvICIYVAIGQK------------ASTVAQVVRKLEEHGAMEY 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494142616 213 -----GQMNEPPGNRLRVALTGLTMAEYFRDekdengKGKDVLFFVDNI------YRytlagtEVSALLGRMP 274
Cdd:PRK09281 221 tivvaATASDPAPLQYLAPYAGCAMGEYFMD------NGKDALIVYDDLskqavaYR------QLSLLLRRPP 281
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
365-428 |
9.58e-18 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 77.48 E-value: 9.58e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494142616 365 HYDVARRVQGTLQRYKELKDIIAILGMDELSEEDKQAVSRARKCERFFSQPFHVAEVFTGSPGK 428
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEK 64
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
55-274 |
1.59e-17 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 85.09 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 55 LGSTEGLKRGLQARNTGEGIKVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDLLETGIKVIDL 134
Cdd:COG0056 76 LGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 135 VCPFAKGGKVGLFGGAGVGKTVNMLELINNiatQHAG--LSVFAGVGERtregndfyhemqeagvvkidnlpESKVAMV- 211
Cdd:COG0056 156 MIPIGRGQRELIIGDRQTGKTAIAIDTIIN---QKGKdvICIYVAIGQK-----------------------ASTVAQVv 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 212 -----YGQM----------NEPPGNRLRVALTGLTMAEYFRDekdengKGKDVLFFVDNI------YRytlagtEVSALL 270
Cdd:COG0056 210 etleeHGAMeytivvaataSDPAPLQYIAPYAGCAMGEYFMD------QGKDVLIVYDDLskhavaYR------ELSLLL 277
|
....
gi 494142616 271 GRMP 274
Cdd:COG0056 278 RRPP 281
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-71 |
1.65e-16 |
|
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: 73.73 E-value: 1.65e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494142616 6 VVQIIGAVVDVEFPRDQVPQVYDALKIDGTD---ITLEVQQQLGDGIVRTIALGSTEGLKRGLQARNTG 71
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVEfgsLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
47-382 |
1.17e-13 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 73.15 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 47 DGIVRTIALGSTEGLKRGLQARNTGEGIKVPVGKATLGRIMDVLGNPIdEVGPINAEDHWV--------IHREAPSYDEQ 118
Cdd:PTZ00185 88 DGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEV-PVGLLTRSRALLeseqtlgkVDAGAPNIVSR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 119 AAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGKT-------VNMLELINNIATQHAGLSVFAGVGERTREGNDFYHE 191
Cdd:PTZ00185 167 SPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsiavstiINQVRINQQILSKNAVISIYVSIGQRCSNVARIHRL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 192 MQEAGVVKIDNLPESKVAmvygqmnEPPGNRLRVALTGLTMAEYFRDekdengKGKDVLFFVDNIYRYTLAGTEVSALLG 271
Cdd:PTZ00185 247 LRSYGALRYTTVMAATAA-------EPAGLQYLAPYSGVTMGEYFMN------RGRHCLCVYDDLSKQAVAYRQISLLLR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 272 RMPSAVGYQPTLADEMGVLQERITSTKT----GSITSIQAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYPAVD 347
Cdd:PTZ00185 314 RPPGREAYPGDVFYLHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVN 393
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 494142616 348 PLASTSRqldplvIGQEHYD-----VARRVQGTLQRYKEL 382
Cdd:PTZ00185 394 IGLSVSR------VGSSAQNvamkaVAGKLKGILAEYRKL 427
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
45-354 |
2.19e-13 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 71.92 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 45 LGDGivRTIALGSTeglkrglqARNTGEGIKVPVGKATLGRIMDVLGNPIDEVGPINAEDHWVIHREAPSYDEQAAANDL 124
Cdd:CHL00059 55 MGDG--LMIQEGSS--------VKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 125 LETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVNMLELINNIATQHaGLSVFAGVGERTregndfyhemqeAGVVKIDNLP 204
Cdd:CHL00059 125 LQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQN-VICVYVAIGQKA------------SSVAQVVTTL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 205 ESKVAMVY-----GQMNEPPGNRLRVALTGLTMAEYFRDekdengKGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGY 279
Cdd:CHL00059 192 QERGAMEYtivvaETADSPATLQYLAPYTGAALAEYFMY------RGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 280 qP---------------TLADEMGvlqeritstkTGSITSIQAVYVPADDYTDPSPATTFAHLDSTVALSRDIASLGIYP 344
Cdd:CHL00059 266 -PgdvfylhsrlleraaKLSSQLG----------EGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRP 334
|
330
....*....|
gi 494142616 345 AVDPLASTSR 354
Cdd:CHL00059 335 AINVGISVSR 344
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
18-194 |
1.02e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 45.01 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 18 FPRDQ----VPQVYDALKIDGTDITLEVQQQlgDGIVRTIALGSteglkrGLQarntGEGIKVP-VGKATLGRIMDVLGN 92
Cdd:PRK14698 112 LPRDKkwhfIPKVKVGDKVVGGDIIGEVPET--SIITHKIMVPP------GIE----GEIVEIAdEGEYTIEEVIAKVKT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494142616 93 PIDEVGPINAEDHWVIHREAPsYDEQAAANDLLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVNMLELinnIATQHAGL 172
Cdd:PRK14698 180 PSGEIKELKMYQRWPVRVKRP-YKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDGDTL---ILTKEFGL 255
|
170 180
....*....|....*....|....*....
gi 494142616 173 -------SVFAGVGERTREGNDFYHEMQE 194
Cdd:PRK14698 256 ikikdlyEILDGKGKKTVEGNEEWTELEE 284
|
|
| ATP-synt_V_A-type_beta_C |
cd18112 |
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 ... |
380-412 |
5.28e-03 |
|
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349747 [Multi-domain] Cd Length: 95 Bit Score: 36.26 E-value: 5.28e-03
10 20 30
....*....|....*....|....*....|...
gi 494142616 380 KELKDIIAILGMDELSEEDKQAVSRARKCERFF 412
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFEREF 54
|
|
| |
