|
Name |
Accession |
Description |
Interval |
E-value |
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
1-488 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 1113.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 1 MEVSALEKKNLGRIAQIIGPVLDVAFSTGKMPNIYNALVVKGRDTSGHTMNVICEVQQLLGNNQVRAVAMSATDGLMRGM 80
Cdd:CHL00060 6 PGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 81 DVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQLETKLSIFETGIKVVDLLAPYRRGGKIG 160
Cdd:CHL00060 86 EVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 161 LFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRV 240
Cdd:CHL00060 166 LFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 241 GLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKKGSITSIQAVYV 320
Cdd:CHL00060 246 GLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 321 PADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILG 400
Cdd:CHL00060 326 PADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 401 LDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLSETIRGFKLILSGELDGLPEQAFYLVGNIDEATTKATN 480
Cdd:CHL00060 406 LDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAAN 485
|
....*...
gi 62902810 481 LEMENKLK 488
Cdd:CHL00060 486 LEVESKLK 493
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
7-485 |
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: 947.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 7 EKKNLGRIAQIIGPVLDVAFSTGKMPNIYNALVVKGRDTsghtMNVICEVQQLLGNNQVRAVAMSATDGLMRGMDVIDTG 86
Cdd:COG0055 1 MAMNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEGG----GELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 87 APLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQLETKLSIFETGIKVVDLLAPYRRGGKIGLFGGAG 166
Cdd:COG0055 77 APISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 167 VGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALT 246
Cdd:COG0055 157 VGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 247 MAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKKGSITSIQAVYVPADDLT 326
Cdd:COG0055 230 MAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 327 DPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSE 406
Cdd:COG0055 310 DPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSE 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62902810 407 EDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLSETIRGFKLILSGELDGLPEQAFYLVGNIDEATTKATNLEMEN 485
Cdd:COG0055 390 EDKLTVARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAEA 468
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
10-481 |
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: 839.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 10 NLGRIAQIIGPVLDVAFSTGKMPNIYNALVVKGRDTSghtmNVICEVQQLLGNNQVRAVAMSATDGLMRGMDVIDTGAPL 89
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNRAES----ELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 90 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQLETKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 169
Cdd:TIGR01039 77 SVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 170 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAE 249
Cdd:TIGR01039 157 TVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 250 YFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKKGSITSIQAVYVPADDLTDPA 329
Cdd:TIGR01039 230 YFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 330 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDR 409
Cdd:TIGR01039 310 PATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDK 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62902810 410 LTVARARKIERFLSQPFFVAEVFTGSPGKYVGLSETIRGFKLILSGELDGLPEQAFYLVGNIDEATTKATNL 481
Cdd:TIGR01039 390 LTVERARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
12-474 |
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: 581.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 12 GRIAQIIGPVLDVAFStGKMPNIYNALvvkgrdTSGHTMNVICEVQQLLGNNQVRAVAMSATDGLMRGMDVIDTGAPLSV 91
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFD-GELPAIHSVL------RAGREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 92 PVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQLETKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 171
Cdd:TIGR03305 74 PVGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 172 LIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEqniaeskVALVYGQMNEPPGARMRVGLTALTMAEYF 251
Cdd:TIGR03305 154 LLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDN-------TVMVFGQMNEPPGARFRVGHTALTMAEYF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 252 RDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKKGSITSIQAVYVPADDLTDPAPA 331
Cdd:TIGR03305 227 RDDEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 332 TTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLT 411
Cdd:TIGR03305 307 HTFSHLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRV 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62902810 412 VARARKIERFLSQPFFVAEVFTGSPGKYVGLSETIRGFKLILSGELDGLPEQAFYLVGNIDEA 474
Cdd:TIGR03305 387 VNRARRLERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
90-368 |
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: 580.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 90 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQLETKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 169
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 170 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEqnIAESKVALVYGQMNEPPGARMRVGLTALTMAE 249
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINL--DGLSKVALVYGQMNEPPGARARVALTGLTMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 250 YFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKKGSITSIQAVYVPADDLTDPA 329
Cdd:cd01133 159 YFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPA 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 62902810 330 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP 368
Cdd:cd01133 239 PATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
90-365 |
2.18e-134 |
|
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: 389.12 E-value: 2.18e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 90 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQLETKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 169
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 170 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGvineqniAESKVALVYGQMNEPPGARMRVGLTALTMAE 249
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSG-------AMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 250 YFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK--KGSITSIQAVYVPADDLTD 327
Cdd:cd19476 154 YFRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTD 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 62902810 328 PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTM 365
Cdd:cd19476 233 PIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
143-363 |
1.01e-86 |
|
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: 264.99 E-value: 1.01e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 143 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKahgGVSVFGGVGERTREGNDLYMEMKESGVIneqniaeSK 222
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-------KR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 223 VALVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQE 302
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62902810 303 RITST--KKGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 363
Cdd:pfam00006 150 RAGRVkgKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 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 ... |
370-477 |
6.68e-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: 235.84 E-value: 6.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 370 IVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLSETIRGF 449
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 62902810 450 KLILSGELDGLPEQAFYLVGNIDEATTK 477
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
12-425 |
3.89e-62 |
|
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: 208.73 E-value: 3.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 12 GRIAQIIGPVLDVA---FSTGKMPNIYNAlvvkgrdtSGHTmnVICEVqqlLGNNQVRAVAM--SATDGLMRGMDVIDTG 86
Cdd:COG1157 21 GRVTRVVGLLIEAVgpdASIGELCEIETA--------DGRP--VLAEV---VGFRGDRVLLMplGDLEGISPGARVVPTG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 87 APLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQ---LETKLsifETGIKVVDLLAPYRRGGKIGLFG 163
Cdd:COG1157 88 RPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLErarITEPL---DTGVRAIDGLLTVGRGQRIGIFA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 164 GAGVGKTVLIMELINN----------IAkahggvsvfggvgERTREGNDlYME-------MKESGVIneqnIAESkvalv 226
Cdd:COG1157 165 GSGVGKSTLLGMIARNteadvnvialIG-------------ERGREVRE-FIEddlgeegLARSVVV----VATS----- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 227 ygqmNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS 306
Cdd:COG1157 222 ----DEPPLMRLRAAYTATAIAEYFRDQG-KNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 307 TKKGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMlqPRIVGEEHYETAQRVKQT 385
Cdd:COG1157 297 GGKGSITAFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISrVM--PDIVSPEHRALARRLRRL 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 62902810 386 LQRYKELQDIIAIlG---------LDElseedrlTVARARKIERFLSQP 425
Cdd:COG1157 375 LARYEENEDLIRI-GayqpgsdpeLDE-------AIALIPAIEAFLRQG 415
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
90-363 |
1.08e-53 |
|
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: 181.22 E-value: 1.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 90 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQLETKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 169
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 170 TVLIMELINNiAKAhgGVSVFGGVGERTREGNDlYMEmkesGVINEQNIaeSKVALVYGQMNEPPGARMRVGLTALTMAE 249
Cdd:cd01136 81 STLLGMIARN-TDA--DVNVIALIGERGREVRE-FIE----KDLGEEGL--KRSVLVVATSDESPLLRVRAAYTATAIAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 250 YFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKKGSITSIQAVYVPADDLTDPA 329
Cdd:cd01136 151 YFRD-QGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPI 229
|
250 260 270
....*....|....*....|....*....|....
gi 62902810 330 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 363
Cdd:cd01136 230 ADEVRSILDGHIVLSRRLAERGHYPAIDVLASIS 263
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
71-424 |
3.20e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 171.92 E-value: 3.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 71 SATDGLMRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPVDNlGPVDTRTTSPIHKSAPAFIQLETKLSIFETGIKVVDLL 150
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 151 APYRRGGKIGLFGGAGVGKTVLIMELInniAKAHGGVSVFGGVGERTREGNDLYmemkesgvinEQNI---AESKVALVY 227
Cdd:PRK06820 158 LSCGEGQRIGIFAAAGVGKSTLLGMLC---ADSAADVMVLALIGERGREVREFL----------EQVLtpeARARTVVVV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 228 GQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITST 307
Cdd:PRK06820 225 ATSDRPALERLKGLSTATTIAEYFRDRG-KKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNS 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 308 KKGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQRVKQTLQ 387
Cdd:PRK06820 304 DRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLA 382
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 62902810 388 RYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQ 424
Cdd:PRK06820 383 CYQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
75-424 |
1.75e-47 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 169.93 E-value: 1.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 75 GLMRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQ---LETKLSifeTGIKVVDLLA 151
Cdd:PRK06936 81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSrrlIETPLS---LGVRVIDGLL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 152 PYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFGGVGERTREgndlYMEMKESGvINEQNIAESkvALVYGQMN 231
Cdd:PRK06936 158 TCGEGQRMGIFAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIESD-LGEEGLRKA--VLVVATSD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 232 EPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKKGS 311
Cdd:PRK06936 228 RPSMERAKAGFVATSIAEYFRD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGS 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 312 ITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQRVKQTLQRYKE 391
Cdd:PRK06936 307 ITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEE 385
|
330 340 350
....*....|....*....|....*....|....*..
gi 62902810 392 LQDIIAI----LGLDELSEEdrlTVARARKIERFLSQ 424
Cdd:PRK06936 386 VELLLQIgeyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
53-426 |
2.63e-47 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 169.02 E-value: 2.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 53 ICEVQQLLGNNQVRAVA--------------MSATDGLMRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDT- 117
Cdd:PRK08149 30 ICEIRAGWHSNEVIARAqvvgfqrertilslIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTv 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 118 ---RTTSPIHKSAPAFIQLETKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFGGVG 194
Cdd:PRK08149 110 gpiSEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 195 ERTREGNDLYMEMKESGvineqniAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGS 274
Cdd:PRK08149 187 ERGREVTEFVESLRASS-------RREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQG-KRVVLFIDSMTRYARALR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 275 EVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKKGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYP 354
Cdd:PRK08149 259 DVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYP 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62902810 355 AVDPLDSTSTMLQpRIVGEEHYETAQRVKQTLQRYKELQDIIAiLG---LDELSEEDRlTVARARKIERFLSQPF 426
Cdd:PRK08149 339 AIDVLKSVSRVFG-QVTDPKHRQLAAAFRKLLTRLEELQLFID-LGeyrRGENADNDR-AMDKRPALEAFLKQDV 410
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
28-425 |
4.47e-46 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 166.10 E-value: 4.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 28 TGKMPNIYNALV-VKGRDTsghTMNVICEVQQ----LLGNNQV----RAVAM----SATDGLMRGMDVIDTGAPLSVPVG 94
Cdd:PRK09099 25 TGKVVEVIGTLLrVSGLDV---TLGELCELRQrdgtLLQRAEVvgfsRDVALlspfGELGGLSRGTRVIGLGRPLSVPVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 95 GATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQLETKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIM 174
Cdd:PRK09099 102 PALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 175 EL-------INNIAkahggvsvfgGVGERTREGNDlYMEMkesgVINEQNIAESKValVYGQMNEPPGARMRVGLTALTM 247
Cdd:PRK09099 182 MFargtqcdVNVIA----------LIGERGREVRE-FIEL----ILGEDGMARSVV--VCATSDRSSIERAKAAYVATAI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 248 AEYFRDVNEQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKKGSITSIQAVYVPADDLTD 327
Cdd:PRK09099 245 AEYFRDRGLR-VLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 328 PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQRVKQTLQRYKELQDIIAI----LGLDE 403
Cdd:PRK09099 324 PIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDP 402
|
410 420
....*....|....*....|..
gi 62902810 404 LSEEdrlTVARARKIERFLSQP 425
Cdd:PRK09099 403 VADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
4-424 |
1.13e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 162.16 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 4 SALEKKNL----GRIAQIIGPVLDVafsTGKMPNIYNALVVKGRDTSGHTMNVICEVQQllgnNQVRAVAMSATDGLMRG 79
Cdd:PRK08472 8 NKLQKFNLsprfGSITKISPTIIEA---DGLNPSVGDIVKIESSDNGKECLGMVVVIEK----EQFGISPFSFIEGFKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 80 MDVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQLETKLSIFETGIKVVDLLAPYRRGGKI 159
Cdd:PRK08472 81 DKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 160 GLFGGAGVGKTVLiMELINNIAKAhgGVSVFGGVGERTRE---------GNDLymemkESGVINEQNIAESKVALVYGqm 230
Cdd:PRK08472 161 GIFAGSGVGKSTL-MGMIVKGCLA--PIKVVALIGERGREipefieknlGGDL-----ENTVIVVATSDDSPLMRKYG-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 231 neppgarmrvGLTALTMAEYFRDVNEqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK-K 309
Cdd:PRK08472 231 ----------AFCAMSVAEYFKNQGL-DVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 310 GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQRVKQTLQRY 389
Cdd:PRK08472 300 GSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLL 378
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 62902810 390 KELQDIIAI----LGLD-ELSEedrlTVARARKIERFLSQ 424
Cdd:PRK08472 379 KENEVLIRIgayqKGNDkELDE----AISKKEFMEQFLKQ 414
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
2-424 |
6.53e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 160.14 E-value: 6.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 2 EVSALEKKNL-GRIAQIIGPVLDVAFSTGKMpNIYNALVVKGRDTSGhtmnVICEVqqlLGNNQVRAVAM--SATDGLMR 78
Cdd:PRK08927 8 AIGDIDTLVIyGRVVAVRGLLVEVAGPIHAL-SVGARIVVETRGGRP----VPCEV---VGFRGDRALLMpfGPLEGVRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 79 GMDVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTS-PIHKSAP---AFIQLETKLsifETGIKVVDLLAPYR 154
Cdd:PRK08927 80 GCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPyPLRAPPPpahSRARVGEPL---DLGVRALNTFLTCC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 155 RGGKIGLFGGAGVGKTVLIMELINNIAKAhggVSVFGGVGERTREGNDLYMEmkesgVINEQNIAESKValVYGQMNEPP 234
Cdd:PRK08927 157 RGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREVQEFLQD-----DLGPEGLARSVV--VVATSDEPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 235 GARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI--TSTKKGSI 312
Cdd:PRK08927 227 LMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 313 TSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMlqPRIVGEEHYETAQRVKQTLQRYKE 391
Cdd:PRK08927 306 TGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSrTM--PGCNDPEENPLVRRARQLMATYAD 383
|
410 420 430
....*....|....*....|....*....|....*..
gi 62902810 392 LQDIIAI----LGLDelSEEDRlTVARARKIERFLSQ 424
Cdd:PRK08927 384 MEELIRLgayrAGSD--PEVDE-AIRLNPALEAFLRQ 417
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
75-398 |
1.01e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 159.87 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 75 GLMRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHksAPAFIQLETKlSIFE---TGIKVVDLLA 151
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRR-PITEpldVGVRAINAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 152 PYRRGGKIGLFGGAGVGKTVLI-MELINNIAKAhggvSVFGGVGERTREGNDLYMEmkesgVINEQNIAESKValVYGQM 230
Cdd:PRK08972 158 TVGKGQRMGLFAGSGVGKSVLLgMMTRGTTADV----IVVGLVGERGREVKEFIEE-----ILGEEGRARSVV--VAAPA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 231 NEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERIT--STK 308
Cdd:PRK08972 227 DTSPLMRLKGCETATTIAEYFRDQG-LNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 309 KGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQRVKQTLQR 388
Cdd:PRK08972 306 QGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSL 384
|
330
....*....|
gi 62902810 389 YKELQDIIAI 398
Cdd:PRK08972 385 YQQNRDLISI 394
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
99-400 |
2.10e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 156.31 E-value: 2.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 99 GRIFNVLGEPVDNLGPVDTRTTS-PIHKSAPAFIQLETKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELi 177
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPmSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 178 nniAKA-HGGVSVFGGVGERTREgndlYMEMKEsGVINEqniAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNE 256
Cdd:PRK06002 186 ---ARAdAFDTVVIALVGERGRE----VREFLE-DTLAD---NLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 257 qDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI--TSTKKGSITSIQAVYVPADDLTDPAPATTF 334
Cdd:PRK06002 255 -NVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIR 333
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62902810 335 AHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHyETAQRVKQTLQRYKELQDIIAILG 400
Cdd:PRK06002 334 GTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQR-KLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
44-424 |
3.76e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 155.66 E-value: 3.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 44 DTSGHTMNVICEVQQLLGNnQVRAVAMSATDGLMRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPV-------- 115
Cdd:PRK05688 57 DDSYHPVQVEAEVMGFSGD-KVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMkaedwvpm 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 116 DTRTTSPIHK---SAPafiqletklsiFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLiMELINNIAKAHGGVSVFGG 192
Cdd:PRK05688 136 DGPTINPLNRhpiSEP-----------LDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVL-LGMMTRFTEADIIVVGLIG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 193 vgERTREgndlymeMKE--SGVINEQNIAESKValVYGQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFV 270
Cdd:PRK05688 204 --ERGRE-------VKEfiEHILGEEGLKRSVV--VASPADDAPLMRLRAAMYCTRIAEYFRDKG-KNVLLLMDSLTRFA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 271 QAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKKG--SITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLA 348
Cdd:PRK05688 272 QAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 349 AKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQRVKQTLQRYKELQDIIAI----LGLDelsEEDRLTVARARKIERFLSQ 424
Cdd:PRK05688 352 EEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLISVgayvAGGD---PETDLAIARFPHLVQFLRQ 427
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
85-398 |
6.58e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 154.88 E-value: 6.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 85 TGAPLSVPVGGATLGRIFNVLGEPVDN------LGPVDTRTTSPIHKSAPafiQLETKLSIfetGIKVVDLLAPYRRGGK 158
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLDGsalpkgLAPVSTDQDPPNPLKRP---PIREPMEV---GVRAIDSLLTVGKGQR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 159 IGLFGGAGVGKTVLIMEL-------INNIAkahggvsvfgGVGERTREGNDlYMEmKESGvinEQNIAESKValVYGQMN 231
Cdd:PRK07721 161 VGIFAGSGVGKSTLMGMIarntsadLNVIA----------LIGERGREVRE-FIE-RDLG---PEGLKRSIV--VVATSD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 232 EPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKKGS 311
Cdd:PRK07721 224 QPALMRIKGAYTATAIAEYFRDQG-LNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 312 ITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQRVKQTLQRYKE 391
Cdd:PRK07721 303 ITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQN 381
|
....*..
gi 62902810 392 LQDIIAI 398
Cdd:PRK07721 382 SEDLINI 388
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
51-424 |
6.76e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 154.75 E-value: 6.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 51 NVICEVQQLLGNNQVrAVAMSATDGLMRGMDVIDTGAPLSVPVGGATLGRIFN----VLGEPVDNLG----PVDTrttSP 122
Cdd:PRK06793 52 NVLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSangeVLNEEAENIPlqkiKLDA---PP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 123 IHksapAFIQLETKlSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGvgERTREGND 202
Cdd:PRK06793 128 IH----AFEREEIT-DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKADINVISLVG--ERGREVKD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 203 -LYMEMKESGVineqniaeSKVALVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLG 281
Cdd:PRK06793 200 fIRKELGEEGM--------RKSVVVVATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 282 RMPSAvGYQPTLSTEMGSLQERITSTKKGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDS 361
Cdd:PRK06793 271 ELPIG-GKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDS 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62902810 362 TSTMLQpRIVGEEHYETAQRVKQTLQRYKElQDIIAILGLDELSEEDRLTVARARKIE---RFLSQ 424
Cdd:PRK06793 350 VSRIME-EIVSPNHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAYIFECKNKVEginTFLKQ 413
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
10-89 |
5.41e-37 |
|
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: 130.71 E-value: 5.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 10 NLGRIAQIIGPVLDVAFSTGKMPNIYNALVVKGRDTsghtMNVICEVQQLLGNNQVRAVAMSATDGLMRGMDVIDTGAPL 89
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDDG----KKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
75-424 |
5.85e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 135.40 E-value: 5.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 75 GLMRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTtsPIHKSAPAFIQLETKL--SIFETGIKVVDLLAP 152
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGST--PLQQQLPQIHPLQRRAvdTPLDVGVNAINGLLT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 153 YRRGGKIGLFGGAGVGKTVLiMELINNIAKAHGGVSVFGGvgERTREGNDLY-MEMKESGVineqniaeSKVALVYGQMN 231
Cdd:PRK07196 152 IGKGQRVGLMAGSGVGKSVL-LGMITRYTQADVVVVGLIG--ERGREVKEFIeHSLQAAGM--------AKSVVVAAPAD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 232 EPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI-TSTKKG 310
Cdd:PRK07196 221 ESPLMRIKATELCHAIATYYRDKG-HDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 311 SITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQRVKQTLQRYK 390
Cdd:PRK07196 300 TMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYM 378
|
330 340 350
....*....|....*....|....*....|....*...
gi 62902810 391 ELQDIIA----ILGLDELSEEdrlTVARARKIERFLSQ 424
Cdd:PRK07196 379 AIKPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQ 413
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
71-398 |
8.71e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 135.08 E-value: 8.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 71 SATDGLMRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPVDNL----GPVDTRTTSPihksAPAFIQLETKLSIFeTGIKV 146
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRelpdVCWKDYDAMP----PPAMVRQPITQPLM-TGIRA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 147 VDLLAPYRRGGKIGLFGGAGVGKTVLIMELINniaKAHGGVSVFGGVGERTREgndlYMEMKESGVINEqniAESKVALV 226
Cdd:PRK07594 146 IDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFIDFTLSEE---TRKRCVIV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 227 YGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS 306
Cdd:PRK07594 216 VATSDRPALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGM 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 307 TKKGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQRVKQTL 386
Cdd:PRK07594 295 GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCL 373
|
330
....*....|..
gi 62902810 387 QRYKELQDIIAI 398
Cdd:PRK07594 374 ALYQEVELLIRI 385
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
91-427 |
6.73e-33 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 130.29 E-value: 6.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 91 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIhkSAPAFIQLE-TKLS-IFETGIKVVDLLAPYRRGGKIGLFGGAGVG 168
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGAL--ITPPFNPLQrTPIEhVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 169 KTVLiMELINNIAKAHGGVSVFGGvgERTREGNDlYMEmkesGVINEQNIAESKValVYGQMNEPPGARMRVGLTALTMA 248
Cdd:PRK07960 188 KSVL-LGMMARYTQADVIVVGLIG--ERGREVKD-FIE----NILGAEGRARSVV--IAAPADVSPLLRMQGAAYATRIA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 249 EYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS--TKKGSITSIQAVYVPADDLT 326
Cdd:PRK07960 258 EDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQ 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 327 DPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQRVKQTLQRYKELQDIIAI----LGLD 402
Cdd:PRK07960 337 DPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALIDEQHYARVRQFKQLLSSFQRNRDLVSVgayaKGSD 415
|
330 340
....*....|....*....|....*
gi 62902810 403 ELSEEdrlTVARARKIERFLSQPFF 427
Cdd:PRK07960 416 PMLDK---AIALWPQLEAFLQQGIF 437
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
62-456 |
4.36e-30 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 121.93 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 62 NNQVRAVAMSATDGLMRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQLETKLSIFE 141
Cdd:PRK05922 63 NRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 142 TGIKVVDLLAPYRRGGKIGLFGGAGVGKTvlimELINNIAK-AHGGVSVFGGVGERTREGNDlYMEMKESGvineqnIAE 220
Cdd:PRK05922 143 TGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVRE-YIEQHKEG------LAA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 221 SKVALVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSL 300
Cdd:PRK05922 212 QRTIIIASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 301 QERITSTKKGSITSIQAV-YVP--ADDLTDPAPATTFAHLDATTVlSRGLAAkgiyPAVDPLDSTSTMLQpRIVGEEHYE 377
Cdd:PRK05922 291 TERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSRSAR-QLALPHHYA 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 378 TAQRVKQTLQRYKELQDIIAiLGLDELSEEDRLTvaRARK----IERFLSQPFfvaevftgspGKYVGLSETIRGFKLIL 453
Cdd:PRK05922 365 AAEELRSLLKAYHEALDIIQ-LGAYVPGQDAHLD--RAVKllpsIKQFLSQPL----------SSYCALHNTLKQLEALL 431
|
...
gi 62902810 454 SGE 456
Cdd:PRK05922 432 KHE 434
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
73-426 |
4.53e-28 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 116.46 E-value: 4.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 73 TDGLM-RGMDVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSA--PA-------FIQletklsifeT 142
Cdd:PRK04196 59 TTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVareypeeFIQ---------T 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 143 GIKVVDLLAPYRRGGKIGLFGGAGvgktvlimeLINNIAKAHGGVSVFGGVGE------------RTREGNDLYMEMKES 210
Cdd:PRK04196 130 GISAIDGLNTLVRGQKLPIFSGSG---------LPHNELAAQIARQAKVLGEEenfavvfaamgiTFEEANFFMEDFEET 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 211 GVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQ 290
Cdd:PRK04196 201 GALE-------RSVVFLNLADDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 291 PTLSTEMGSLQER--ITSTKKGSITSIQAVYVPADDLTDPAPattfahlDAT-------TVLSRGLAAKGIYPAVDPLDS 361
Cdd:PRK04196 274 GYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegqIVLSRELHRKGIYPPIDVLPS 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62902810 362 TSTMLQPRIvG-----EEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQPF 426
Cdd:PRK04196 347 LSRLMKDGI-GegktrEDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFErEFVNQGF 416
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
88-367 |
5.37e-26 |
|
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: 106.92 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 88 PLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSA--PA-------FIQletklsifeTGIKVVDLLAPYRRGGK 158
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPinPVariypeeMIQ---------TGISAIDVMNTLVRGQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 159 IGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGERTREGNDLYMEMKESgviNEQNIAESKVALVYGQMNEPPGARM 238
Cdd:cd01135 72 LPIFSGSGLPHNELAAQIARQ-AGVVGSEENFAIVFAAMGVTMEEARFFKDD---FEETGALERVVLFLNLANDPTIERI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 239 RVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER--ITSTKKGSITSIQ 316
Cdd:cd01135 148 ITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIP 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 62902810 317 AVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ 367
Cdd:cd01135 228 ILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMK 278
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
60-427 |
1.08e-25 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 109.62 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 60 LGNNQVRAVAMSATDGLMRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQLETKLSI 139
Cdd:PRK13343 66 LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 140 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESGVIN 214
Cdd:PRK13343 146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN------------------QKDSDVIcvyvaIGQKASAVAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 215 -----EQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGY 289
Cdd:PRK13343 208 vietlREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAY 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 290 QPTLSTEMGSLQERIT--STKK--GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTStm 365
Cdd:PRK13343 287 PGDIFYLHSRLLERAAklSPELggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVS-- 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62902810 366 lqpRIVGEEHY----ETAQRVKQTLQRYKELQdIIAILGLDeLSEEDRLTVARARKIERFLSQPFF 427
Cdd:PRK13343 365 ---RVGGKAQHpairKESGRLRLDYAQFLELE-AFTRFGGL-LDAGTQKQITRGRRLRELLKQPRF 425
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
85-424 |
8.88e-21 |
|
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: 94.79 E-value: 8.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 85 TGAPLSVPVGGATLGRIFNVLGEPVDNLGPV------DTRTtSPIHKSAPAFIQletklSIFETGIKVVDLLAPYRRGGK 158
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVlaedylDING-QPINPYARIYPE-----EMIQTGISAIDVMNSIARGQK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 159 IGLFGGAGVGKTvlimELINNIAKAHGGVSVFGGVGERTREGNdLYMEMKESGViN-----------EQNIAESKVALVY 227
Cdd:TIGR01040 144 IPIFSAAGLPHN----EIAAQICRQAGLVKLPTKDVHDGHEDN-FAIVFAAMGV-NmetarffkqdfEENGSMERVCLFL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 228 GQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI--T 305
Cdd:TIGR01040 218 NLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrV 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 306 STKKGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIvGE-----EHYETAQ 380
Cdd:TIGR01040 298 EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHSDVSN 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 62902810 381 RVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIER-FLSQ 424
Cdd:TIGR01040 377 QLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
88-363 |
2.92e-20 |
|
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: 90.71 E-value: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 88 PLSVPVGGATLGRIFNVLGEPVDNLG----------------PVdtRTTSPIHKSAPAFIQLETklsifetGIKVVDLLA 151
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAetgsifiprgvnvqrwPV--RQPRPVKEKLPPNVPLLT-------GQRVLDTLF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 152 PYRRGGKIGLFGGAGVGKTVlimeLINNIAK-AHGGVSVFGGVGERTREGNDLYMEMKE-SGVINEQNIAEsKVALVYGQ 229
Cdd:cd01134 72 PVAKGGTAAIPGPFGCGKTV----ISQSLSKwSNSDVVIYVGCGERGNEMAEVLEEFPElKDPITGESLME-RTVLIANT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 230 MNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI----- 304
Cdd:cd01134 147 SNMPVAAREASIYTGITIAEYFRDMG-YNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrc 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62902810 305 --TSTKKGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 363
Cdd:cd01134 226 lgSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYS 286
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
243-424 |
4.54e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 93.31 E-value: 4.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 243 TALTMAEYFRDvneQ--DVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER----IT-STKKGSITSI 315
Cdd:PRK04192 311 TGITIAEYYRD---MgyDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTII 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 316 QAVYVPADDLTDPapaTTFAHLDATTV---LSRGLAAKGIYPAVDPLDSTS---TMLQP---RIVGEEHYETAQRVKQTL 386
Cdd:PRK04192 388 GAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAINWLTSYSlylDQVAPwweENVDPDWRELRDEAMDLL 464
|
170 180 190
....*....|....*....|....*....|....*....
gi 62902810 387 QRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 424
Cdd:PRK04192 465 QREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
375-438 |
1.91e-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: 79.41 E-value: 1.91e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62902810 375 HYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGK 438
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEK 64
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
195-436 |
2.03e-18 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 88.54 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 195 ERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGS 274
Cdd:PRK14698 692 ERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMG-YDVALMADSTSRWAEALR 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 275 EVSALLGRMPSAVGYQPTLSTEMGSLQERI-------TSTKKGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGL 347
Cdd:PRK14698 771 EISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 348 AAKGIYPAVDPLDSTSTMLQP------RIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ER 420
Cdd:PRK14698 851 ARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAILLVARMLrED 930
|
250
....*....|....*.
gi 62902810 421 FLSQPFFvAEVFTGSP 436
Cdd:PRK14698 931 YLQQDAF-DEVDTYCP 945
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
14-86 |
1.91e-17 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 76.43 E-value: 1.91e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62902810 14 IAQIIGPVLDVAFSTGKMPNIYNALVVKGRDTSghtmNVICEVQQLLGNNQVRAVAMSATDGLMRGMDVIDTG 86
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVEFG----SLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
89-363 |
2.61e-17 |
|
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: 81.84 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 89 LSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQLETKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 168
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 169 KTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESGVINEQNIAESKVALVY-----GQMNEPPGARM 238
Cdd:cd01132 82 KTAIAIDTIIN------------------QKGKKVYciyvaIGQKRSTVAQIVKTLEEHGAMEYtivvaATASDPAPLQY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 239 RVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKK----GSITS 314
Cdd:cd01132 144 LAPYAGCAMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSLTA 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 62902810 315 IQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 363
Cdd:cd01132 223 LPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVS 271
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
63-284 |
1.47e-15 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 78.95 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 63 NQVRAVAMSATDGLMRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIQletKLSIFE- 141
Cdd:PRK09281 69 DNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID---RKSVHEp 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 142 --TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESGVIN 214
Cdd:PRK09281 146 lqTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN------------------QKGKDVIciyvaIGQKASTVAQ 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62902810 215 EQNIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMP 284
Cdd:PRK09281 208 VVRKLEEHGAMEYtivvaATASDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
73-333 |
2.42e-12 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 68.52 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 73 TDGLMRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPVDNlGP------VDTRTTS--PIHKSAPAfiqletklSIFETGI 144
Cdd:PRK02118 58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GPelegepIEIGGPSvnPVKRIVPR--------EMIRTGI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 145 KVVDLLAPYRRGGKIGLFGGAGVGKTVLIMElINNIAKAHGGVSVFGGVGertregNDLYMEMKESgviNEQNIAESKVA 224
Cdd:PRK02118 129 PMIDVFNTLVESQKIPIFSVSGEPYNALLAR-IALQAEADIIILGGMGLT------FDDYLFFKDT---FENAGALDRTV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 225 LVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI 304
Cdd:PRK02118 199 MFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKA 278
|
250 260 270
....*....|....*....|....*....|
gi 62902810 305 TSTKK-GSITSIQAVYVPADDLTDPAPATT 333
Cdd:PRK02118 279 VDFEDgGSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
60-357 |
2.59e-11 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 65.75 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 60 LGNNQVRAVAMSatDGLM--RGMDVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIqleTKL 137
Cdd:CHL00059 45 LESNNVGVVLMG--DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGII---SRR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 138 SIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGND---LYMEM--KE 209
Cdd:CHL00059 120 SVYEplqTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN------------------QKGQNvicVYVAIgqKA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 210 SGVINEQNIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRdVNEQDVLLFIDNIFRFVQAGSEVSALLGRMP 284
Cdd:CHL00059 182 SSVAQVVTTLQERGAMEYtivvaETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 285 SAVGY--------------QPTLSTEMGSlqeritstkkGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAK 350
Cdd:CHL00059 261 GREAYpgdvfylhsrllerAAKLSSQLGE----------GSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNA 330
|
....*..
gi 62902810 351 GIYPAVD 357
Cdd:CHL00059 331 GIRPAIN 337
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
56-357 |
2.81e-07 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 53.12 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 56 VQQLLGNNQVRAVAMSATDGLMRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPV---------------DNLGPVDTRTT 120
Cdd:PTZ00185 82 VFNLEKDGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVpvglltrsralleseQTLGKVDAGAP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 121 SPIHKSAPAFIQLetklsifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGErtreg 200
Cdd:PTZ00185 162 NIVSRSPVNYNLL--------TGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVIS----- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 201 ndLYMEMKE--SGVINEQNIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRDVNEQdVLLFIDNIFRFVQAG 273
Cdd:PTZ00185 229 --IYVSIGQrcSNVARIHRLLRSYGALRYttvmaATAAEPAGLQYLAPYSGVTMGEYFMNRGRH-CLCVYDDLSKQAVAY 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 274 SEVSALLGRMPSAVGYQPTLSTEMGSLQER--ITSTKK--GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAA 349
Cdd:PTZ00185 306 RQISLLLRRPPGREAYPGDVFYLHSRLLERaaMLSPGKggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFT 385
|
....*...
gi 62902810 350 KGIYPAVD 357
Cdd:PTZ00185 386 GGQRPAVN 393
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
371-425 |
1.12e-04 |
|
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family of ATPases that form part of the Type III secretion system (T3SS) present in Escherichia coli. T3SS is a macromolecular complex that creates a syringe-like apparatus extending from the bacterial cytosol across three membranes to the eukaryotic cytosol. This process is essential for pathogenicity. EscN is a functionally unique ATPase that provides an inner-membrane recognition gate for the T3SS chaperone-virulence effector complexes as well as a potential source of energy for their subsequent secretion.The C-terminal domain of T3SS ATPases mediates binding with multiple contact points along the chaperone.
Pssm-ID: 465691 [Multi-domain] Cd Length: 70 Bit Score: 40.49 E-value: 1.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62902810 371 VGEEHYETAQRVKQTLQRYKELQDIIAIlG---------LDElseedrlTVARARKIERFLSQP 425
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRI-GayqagsdpeIDE-------AIAKRPAINAFLRQG 56
|
|
| ATP-synt_V_A-type_alpha_C |
cd18111 |
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of ... |
380-424 |
2.59e-04 |
|
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of the V1/A1 complex of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349746 [Multi-domain] Cd Length: 105 Bit Score: 40.45 E-value: 2.59e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 62902810 380 QRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 424
Cdd:cd18111 6 TEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIrEDFLQQ 51
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| 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 ... |
390-424 |
3.46e-04 |
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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: 39.72 E-value: 3.46e-04
10 20 30
....*....|....*....|....*....|....*.
gi 62902810 390 KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ 424
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFErEFINQ 57
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| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
155-283 |
3.99e-03 |
|
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: 37.74 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62902810 155 RGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYmemkesgvineqniaeskvaLVYGQMNEPP 234
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLL--------------------LIIVGGKKAS 60
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90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 62902810 235 GARMRVGLTALTMAEYFRdvneqDVLLFIDNIFRFVQAGSEVSALLGRM 283
Cdd:smart00382 61 GSGELRLRLALALARKLK-----PDVLILDEITSLLDAEQEALLLLLEE 104
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| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
11-87 |
6.98e-03 |
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ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 35.37 E-value: 6.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62902810 11 LGRIAQIIGPVLDVAFSTGKMpniYNALVVKGRDTSGHTMNVICEVQQLLGNNqVRAVAMSATDGLMRGMDVIDTGA 87
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVA---IGEVCEIERGDGNNETVLKAEVIGFRGDR-AILQLFESTRGLSRGALVEPTGR 73
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