|
Name |
Accession |
Description |
Interval |
E-value |
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
1-485 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 1148.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 1 GPGVSALEKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDTIGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRG 80
Cdd:CHL00060 5 GPGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 81 MEVIDTGAPLSVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKI 160
Cdd:CHL00060 85 MEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 161 GLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEENIAESKVALVYGQMNEPPGARMR 240
Cdd:CHL00060 165 GLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 241 VGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVY 320
Cdd:CHL00060 245 VGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 321 VPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPQIVGEEHYETAQRVKQTLQRYKELQDIIAIL 400
Cdd:CHL00060 325 VPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAIL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 401 GLDELSEEDRLTVSRARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFKLILSGELDSLPEQAFYLVGNIDEATAKAM 480
Cdd:CHL00060 405 GLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAA 484
|
....*
gi 62085151 481 NLETE 485
Cdd:CHL00060 485 NLEVE 489
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
8-485 |
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: 950.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 8 EKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDtigqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTG 87
Cdd:COG0055 1 MAMNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEG----GGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 88 APLSVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAG 167
Cdd:COG0055 77 APISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 168 VGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeeniaesKVALVYGQMNEPPGARMRVGLTALT 247
Cdd:COG0055 157 VGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 248 MAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLT 327
Cdd:COG0055 230 MAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 328 DPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPQIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSE 407
Cdd:COG0055 310 DPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSE 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62085151 408 EDRLTVSRARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFKLILSGELDSLPEQAFYLVGNIDEATAKAMNLETE 485
Cdd:COG0055 390 EDKLTVARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAE 467
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
11-482 |
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: 841.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 11 NLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRdtigQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 90
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNR----AESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 91 SVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 170
Cdd:TIGR01039 77 SVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 171 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeeniaesKVALVYGQMNEPPGARMRVGLTALTMAE 250
Cdd:TIGR01039 157 TVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 251 YFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 330
Cdd:TIGR01039 230 YFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 331 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPQIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDR 410
Cdd:TIGR01039 310 PATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDK 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62085151 411 LTVSRARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFKLILSGELDSLPEQAFYLVGNIDEATAKAMNL 482
Cdd:TIGR01039 390 LTVERARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
13-475 |
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: 582.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 13 GRIAQIIGPVLDVAFPpGKMPNIYNALvvkgrdTIGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSV 92
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFD-GELPAIHSVL------RAGREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 93 PVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 172
Cdd:TIGR03305 74 PVGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 173 LIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEeniaeskVALVYGQMNEPPGARMRVGLTALTMAEYF 252
Cdd:TIGR03305 154 LLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDN-------TVMVFGQMNEPPGARFRVGHTALTMAEYF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 253 RDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPA 332
Cdd:TIGR03305 227 RDDEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 333 TTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPQIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLT 412
Cdd:TIGR03305 307 HTFSHLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRV 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62085151 413 VSRARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFKLILSGELDSLPEQAFYLVGNIDEA 475
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 ... |
91-369 |
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: 578.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 91 SVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 170
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 171 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEENIaeSKVALVYGQMNEPPGARMRVGLTALTMAE 250
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGL--SKVALVYGQMNEPPGARARVALTGLTMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 251 YFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 330
Cdd:cd01133 159 YFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPA 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 62085151 331 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP 369
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 ... |
91-366 |
9.21e-133 |
|
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: 384.89 E-value: 9.21e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 91 SVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 170
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 171 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGvineeniAESKVALVYGQMNEPPGARMRVGLTALTMAE 250
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSG-------AMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 251 YFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK--EGSITSIQAVYVPADDLTD 328
Cdd:cd19476 154 YFRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTD 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 62085151 329 PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTM 366
Cdd:cd19476 233 PIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
144-364 |
4.31e-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: 263.45 E-value: 4.31e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 144 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKahgGVSVFGGVGERTREGNDLYMEMKESGVIneeniaeSK 223
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-------KR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 224 VALVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQE 303
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62085151 304 RITSTKE--GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 364
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 ... |
371-478 |
2.86e-77 |
|
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic.
Pssm-ID: 349745 [Multi-domain] Cd Length: 108 Bit Score: 236.61 E-value: 2.86e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 371 IVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVSRARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGF 450
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 62085151 451 KLILSGELDSLPEQAFYLVGNIDEATAK 478
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
13-454 |
2.96e-64 |
|
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: 214.12 E-value: 2.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 13 GRIAQIIGPVLDVAFPPGKMpniyNALV-VKGRDtigqQINVTCEVqqlLG--NNRVRAVAMSATDGLMRGMEVIDTGAP 89
Cdd:COG1157 21 GRVTRVVGLLIEAVGPDASI----GELCeIETAD----GRPVLAEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 90 LSVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSAPAFIQ---LDTKLsifETGIKVVDLLAPYRRGGKIGLFGGA 166
Cdd:COG1157 90 LSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLErarITEPL---DTGVRAIDGLLTVGRGQRIGIFAGS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 167 GVGKTVLIMELINN----------IAkahggvsvfggvgERTREGNDlYMEMkesgVINEENIAESKValVYGQMNEPPG 236
Cdd:COG1157 167 GVGKSTLLGMIARNteadvnvialIG-------------ERGREVRE-FIED----DLGEEGLARSVV--VVATSDEPPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 237 ARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSI 316
Cdd:COG1157 227 MRLRAAYTATAIAEYFRDQG-KNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 317 QAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMlqPQIVGEEHYETAQRVKQTLQRYKELQD 395
Cdd:COG1157 306 YTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISrVM--PDIVSPEHRALARRLRRLLARYEENED 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62085151 396 IIAIlG---------LDElseedrlTVSRARKIERFLSQpffvaevftgSPGKYVGLAETIRGFKLIL 454
Cdd:COG1157 384 LIRI-GayqpgsdpeLDE-------AIALIPAIEAFLRQ----------GMDERVSFEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
91-364 |
3.88e-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: 179.68 E-value: 3.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 91 SVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 170
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 171 TVLIMELINNiAKAhgGVSVFGGVGERTREGNDlYMEmkesGVINEENIaeSKVALVYGQMNEPPGARMRVGLTALTMAE 250
Cdd:cd01136 81 STLLGMIARN-TDA--DVNVIALIGERGREVRE-FIE----KDLGEEGL--KRSVLVVATSDESPLLRVRAAYTATAIAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 251 YFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 330
Cdd:cd01136 151 YFRD-QGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPI 229
|
250 260 270
....*....|....*....|....*....|....
gi 62085151 331 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 364
Cdd:cd01136 230 ADEVRSILDGHIVLSRRLAERGHYPAIDVLASIS 263
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
60-425 |
8.13e-49 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 173.46 E-value: 8.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 60 LLGNNRVRA--VAM----------SATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDDLGPVDTHTtSPIHRS 127
Cdd:PRK06820 55 RIEPQGMLAevVSIeqemallspfASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQW-RELDCP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 128 APAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELInniAKAHGGVSVFGGVGERTREGNDlYME 207
Cdd:PRK06820 134 PPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLC---ADSAADVMVLALIGERGREVRE-FLE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 208 MkesgVINEEniAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSA 287
Cdd:PRK06820 210 Q----VLTPE--ARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRG-KKVLLMADSLTRYARAAREIGLAAGEPPAA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 288 VGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTML 367
Cdd:PRK06820 283 GSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62085151 368 qPQIVGEEHYETAQRVKQTLQRYKELQDIIAI----LGLDELSEEdrlTVSRARKIERFLSQ 425
Cdd:PRK06820 363 -PQIVSAGQLAMAQKLRRMLACYQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
76-425 |
1.59e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 172.63 E-value: 1.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 76 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSAPAFIQ---LDTKLSifeTGIKVVDLLA 152
Cdd:PRK06936 81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSrrlIETPLS---LGVRVIDGLL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 153 PYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFGGVGERTREgndlYMEMKESGvINEENIAESkvALVYGQMN 232
Cdd:PRK06936 158 TCGEGQRMGIFAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIESD-LGEEGLRKA--VLVVATSD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 233 EPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGS 312
Cdd:PRK06936 228 RPSMERAKAGFVATSIAEYFRD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGS 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 313 ITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpQIVGEEHYETAQRVKQTLQRYKE 392
Cdd:PRK06936 307 ITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEE 385
|
330 340 350
....*....|....*....|....*....|....*..
gi 62085151 393 LQDIIAI----LGLDELSEEdrlTVSRARKIERFLSQ 425
Cdd:PRK06936 386 VELLLQIgeyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
18-427 |
6.92e-47 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 167.86 E-value: 6.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 18 IIGPVLDVAFPP---GKMPNIYNALVvkGRDTIGQQinvtcevqQLLGNNRVRAV--AMSATDGLMRGMEVIDTGAPLSV 92
Cdd:PRK08149 13 IQGPIIEAELPDvaiGEICEIRAGWH--SNEVIARA--------QVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 93 PVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHR----SAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGV 168
Cdd:PRK08149 83 WVGEALLGAVLDPTGKIVERFDAPPTVGPISEERvidvAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 169 GKTVLIMELINNiakAHGGVSVFGGVGERTREGNDLYMEMKESGvineeniAESKVALVYGQMNEPPGARMRVGLTALTM 248
Cdd:PRK08149 163 GKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFVESLRASS-------RREKCVLVYATSDFSSVDRCNAALVATTV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 249 AEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTD 328
Cdd:PRK08149 233 AEYFRDQG-KRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 329 PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpQIVGEEHYETAQRVKQTLQRYKELQDIIAiLG---LDEL 405
Cdd:PRK08149 312 PIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVTDPKHRQLAAAFRKLLTRLEELQLFID-LGeyrRGEN 389
|
410 420
....*....|....*....|..
gi 62085151 406 SEEDRlTVSRARKIERFLSQPF 427
Cdd:PRK08149 390 ADNDR-AMDKRPALEAFLKQDV 410
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
75-426 |
4.53e-46 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 166.10 E-value: 4.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 75 DGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSAPAFIQ---LDTKLSifeTGIKVVDLL 151
Cdd:PRK09099 81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSrrmVEAPLP---TGVRIVDGL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 152 APYRRGGKIGLFGGAGVGKTVLIMEL-------INNIAkahggvsvfgGVGERTREGNDlYMEMkesgVINEENIAESKV 224
Cdd:PRK09099 158 MTLGEGQRMGIFAPAGVGKSTLMGMFargtqcdVNVIA----------LIGERGREVRE-FIEL----ILGEDGMARSVV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 225 alVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER 304
Cdd:PRK09099 223 --VCATSDRSSIERAKAAYVATAIAEYFRDRGLR-VLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLER 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 305 ITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPQIVGEEHYETAQRVK 384
Cdd:PRK09099 300 AGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLR 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 62085151 385 QTLQRYKELQDIIAI----LGLDELSEEdrlTVSRARKIERFLSQP 426
Cdd:PRK09099 379 QLLAKHREVETLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
76-399 |
3.48e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 163.72 E-value: 3.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 76 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHrsAPAFIQLDTKlSIFE---TGIKVVDLLA 152
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRR-PITEpldVGVRAINAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 153 PYRRGGKIGLFGGAGVGKTVLI-MELINNIAKAhggvSVFGGVGERTREGNDLYMEmkesgVINEENIAESKValVYGQM 231
Cdd:PRK08972 158 TVGKGQRMGLFAGSGVGKSVLLgMMTRGTTADV----IVVGLVGERGREVKEFIEE-----ILGEEGRARSVV--VAAPA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 232 NEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERIT--STK 309
Cdd:PRK08972 227 DTSPLMRLKGCETATTIAEYFRDQG-LNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 310 EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPQIVGEEHYETAQRVKQTLQR 389
Cdd:PRK08972 306 QGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSL 384
|
330
....*....|
gi 62085151 390 YKELQDIIAI 399
Cdd:PRK08972 385 YQQNRDLISI 394
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
4-425 |
1.08e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 159.76 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 4 VSALEKKNL-GRIAQIIGPVLDVAFPPGkmpniynALVVKGRDTIGQQIN--VTCEVqqlLGNNRVRAVAM--SATDGLM 78
Cdd:PRK08927 9 IGDIDTLVIyGRVVAVRGLLVEVAGPIH-------ALSVGARIVVETRGGrpVPCEV---VGFRGDRALLMpfGPLEGVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 79 RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDDLGPVDTHTTS-PIHRSAP---AFIQLDTKLsifETGIKVVDLLAPY 154
Cdd:PRK08927 79 RGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPyPLRAPPPpahSRARVGEPL---DLGVRALNTFLTC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 155 RRGGKIGLFGGAGVGKTVLIMELINNIAKAhggVSVFGGVGERTREGNDLYMEmkesgVINEENIAESKValVYGQMNEP 234
Cdd:PRK08927 156 CRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREVQEFLQD-----DLGPEGLARSVV--VVATSDEP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 235 PGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI--TSTKEGS 312
Cdd:PRK08927 226 ALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 313 ITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMlqPQIVGEEHYETAQRVKQTLQRYK 391
Cdd:PRK08927 305 ITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSrTM--PGCNDPEENPLVRRARQLMATYA 382
|
410 420 430
....*....|....*....|....*....|....*....
gi 62085151 392 ELQDIIAI----LGLD-ELSEEDRLtvsrARKIERFLSQ 425
Cdd:PRK08927 383 DMEELIRLgayrAGSDpEVDEAIRL----NPALEAFLRQ 417
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
51-399 |
4.83e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 157.97 E-value: 4.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 51 INVTCEVQQLLGNnRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDDLGPV--------DTHTTS 122
Cdd:PRK05688 63 VQVEAEVMGFSGD-KVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMkaedwvpmDGPTIN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 123 PIHRsAPAFIQLDTklsifetGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLiMELINNIAKAHGGVSVFGGvgERTREgn 202
Cdd:PRK05688 142 PLNR-HPISEPLDV-------GIRSINGLLTVGRGQRLGLFAGTGVGKSVL-LGMMTRFTEADIIVVGLIG--ERGRE-- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 203 dlymeMKE--SGVINEENIAESKValVYGQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSAL 280
Cdd:PRK05688 209 -----VKEfiEHILGEEGLKRSVV--VASPADDAPLMRLRAAMYCTRIAEYFRDKG-KNVLLLMDSLTRFAQAQREIALA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 281 LGRMPSAVGYQPTLSTEMGSLQERITSTKEG--SITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 358
Cdd:PRK05688 281 IGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAID 360
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 62085151 359 PLDSTSTMLqPQIVGEEHYETAQRVKQTLQRYKELQDIIAI 399
Cdd:PRK05688 361 IEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLISV 400
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
90-425 |
7.70e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 157.15 E-value: 7.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 90 LSVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 169
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 170 KTVLiMELINNIAKAhgGVSVFGGVGERTRE---------GNDLymemkESGVINEENIAESKVALVYGqmneppgarmr 240
Cdd:PRK08472 170 KSTL-MGMIVKGCLA--PIKVVALIGERGREipefieknlGGDL-----ENTVIVVATSDDSPLMRKYG----------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 241 vGLTALTMAEYFRDVNEqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK-EGSITSIQAV 319
Cdd:PRK08472 231 -AFCAMSVAEYFKNQGL-DVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 320 YVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpQIVGEEHYETAQRVKQTLQRYKELQDIIAI 399
Cdd:PRK08472 309 LVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIRI 387
|
330 340 350
....*....|....*....|....*....|.
gi 62085151 400 ----LGLD-ELSEedrlTVSRARKIERFLSQ 425
Cdd:PRK08472 388 gayqKGNDkELDE----AISKKEFMEQFLKQ 414
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
86-399 |
2.15e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 156.04 E-value: 2.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 86 TGAPLSVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGG 165
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 166 AGVGKTVLIMEL-------INNIAkahggvsvfgGVGERTREGNDlYMEmKESGvinEENIAESKValVYGQMNEPPGAR 238
Cdd:PRK07721 167 SGVGKSTLMGMIarntsadLNVIA----------LIGERGREVRE-FIE-RDLG---PEGLKRSIV--VVATSDQPALMR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 239 MRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQA 318
Cdd:PRK07721 230 IKGAYTATAIAEYFRDQG-LNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 319 VYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPQIVGEEHYETAQRVKQTLQRYKELQDIIA 398
Cdd:PRK07721 309 VLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLIN 387
|
.
gi 62085151 399 I 399
Cdd:PRK07721 388 I 388
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
100-401 |
2.29e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 156.31 E-value: 2.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 100 GRIFNVLGEPVDDLGPVDTHTTS-PIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELi 178
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPmSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 179 nniAKA-HGGVSVFGGVGERTREGNDLYmemkesgvinEENIAE--SKVALVYGQMNEPPGARMRVGLTALTMAEYFRDV 255
Cdd:PRK06002 186 ---ARAdAFDTVVIALVGERGREVREFL----------EDTLADnlKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDR 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 256 NEqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE--GSITSIQAVYVPADDLTDPAPAT 333
Cdd:PRK06002 253 GE-NVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEggGSITGIFSVLVDGDDHNDPVADS 331
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62085151 334 TFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPQIVGEEHyETAQRVKQTLQRYKELQDIIAILG 401
Cdd:PRK06002 332 IRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQR-KLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
52-425 |
3.19e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 150.13 E-value: 3.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 52 NVTCEVQQLLGNNRVrAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFN----VLGEPVDDLG----PVDThttSP 123
Cdd:PRK06793 52 NVLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSangeVLNEEAENIPlqkiKLDA---PP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 124 IHrsapAFIQLDTKlSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGvgERTREGND 203
Cdd:PRK06793 128 IH----AFEREEIT-DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKADINVISLVG--ERGREVKD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 204 -LYMEMKESGVineeniaeSKVALVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLG 282
Cdd:PRK06793 200 fIRKELGEEGM--------RKSVVVVATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 283 RMPSAvGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDS 362
Cdd:PRK06793 271 ELPIG-GKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDS 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62085151 363 TSTMLQpQIVGEEHYETAQRVKQTLQRYKElQDIIAILGLDELSEEDRLTVSRARKIE---RFLSQ 425
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 ... |
11-90 |
6.62e-39 |
|
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: 135.72 E-value: 6.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 11 NLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDtigqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 90
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDD----GKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
72-399 |
4.88e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 135.85 E-value: 4.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 72 SATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDDL----GPVDTHTTSPihrsAPAFIQLDTKLSIFeTGIKV 147
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRelpdVCWKDYDAMP----PPAMVRQPITQPLM-TGIRA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 148 VDLLAPYRRGGKIGLFGGAGVGKTVLIMELINniaKAHGGVSVFGGVGERTREGNDlYMEMkesgVINEEniAESKVALV 227
Cdd:PRK07594 146 IDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGREVRE-FIDF----TLSEE--TRKRCVIV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 228 YGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS 307
Cdd:PRK07594 216 VATSDRPALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGM 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 308 TKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPQIVGEEHYETAQRVKQTL 387
Cdd:PRK07594 295 GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCL 373
|
330
....*....|..
gi 62085151 388 QRYKELQDIIAI 399
Cdd:PRK07594 374 ALYQEVELLIRI 385
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
76-444 |
7.11e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 135.40 E-value: 7.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 76 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDDLGPVDTHTtsPIHRSAPAFIQLDTKL--SIFETGIKVVDLLAP 153
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGST--PLQQQLPQIHPLQRRAvdTPLDVGVNAINGLLT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 154 YRRGGKIGLFGGAGVGKTVLiMELINNIAKAHGGVSVFGGvgERTREGNDLYmemkeSGVINEENIAESkvALVYGQMNE 233
Cdd:PRK07196 152 IGKGQRVGLMAGSGVGKSVL-LGMITRYTQADVVVVGLIG--ERGREVKEFI-----EHSLQAAGMAKS--VVVAAPADE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 234 PPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI-TSTKEGS 312
Cdd:PRK07196 222 SPLMRIKATELCHAIATYYRDKG-HDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGT 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 313 ITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpQIVGEEHYETAQRVKQTLQRYKE 392
Cdd:PRK07196 301 MTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMA 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 62085151 393 LQDIIA----ILGLDELSEEdrlTVSRARKIERFLSQPFFVAEVFTGSPGKYVGLA 444
Cdd:PRK07196 380 IKPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQEVGHPALFSASVEQLTGMF 432
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
92-399 |
1.82e-32 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 128.75 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 92 VPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIhrSAPAF--IQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 169
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGAL--ITPPFnpLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 170 KTVLiMELINNIAKAHGGVSVFGGvgERTREGNDlYMEmkesGVINEENIAESKValVYGQMNEPPGARMRVGLTALTMA 249
Cdd:PRK07960 188 KSVL-LGMMARYTQADVIVVGLIG--ERGREVKD-FIE----NILGAEGRARSVV--IAAPADVSPLLRMQGAAYATRIA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 250 EYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS--TKEGSITSIQAVYVPADDLT 327
Cdd:PRK07960 258 EDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQ 336
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62085151 328 DPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpQIVGEEHYETAQRVKQTLQRYKELQDIIAI 399
Cdd:PRK07960 337 DPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALIDEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
69-457 |
2.63e-29 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 119.62 E-value: 2.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 69 VAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSAPAFIQLDTKLSIFETGIKVV 148
Cdd:PRK05922 69 MSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 149 DLLAPYRRGGKIGLFGGAGVGKTvlimELINNIAK-AHGGVSVFGGVGERTREGNDlYMEMKESGvineenIAESKVALV 227
Cdd:PRK05922 149 DAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVRE-YIEQHKEG------LAAQRTIII 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 228 YGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS 307
Cdd:PRK05922 218 ASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 308 TKEGSITSIQAV-YVP--ADDLTDPAPATTFAHLDATTVlSRGLAAkgiyPAVDPLDSTSTMLQpQIVGEEHYETAQRVK 384
Cdd:PRK05922 297 NDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSRSAR-QLALPHHYAAAEELR 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62085151 385 QTLQRYKELQDIIAI----LGLD-ELSEEDRLTVSrarkIERFLSQPFfvaevftgspGKYVGLAETIRGFKLILSGE 457
Cdd:PRK05922 371 SLLKAYHEALDIIQLgayvPGQDaHLDRAVKLLPS----IKQFLSQPL----------SSYCALHNTLKQLEALLKHE 434
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
15-427 |
6.18e-28 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 115.69 E-value: 6.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 15 IAQIIGPVLDVAfppgKMPNI-YNALVV----KGRDTIGQQINVTCE--VQQLLGNnrvravamsaTDGLM-RGMEVIDT 86
Cdd:PRK04196 7 VSEIKGPLLFVE----GVEGVaYGEIVEielpNGEKRRGQVLEVSEDkaVVQVFEG----------TTGLDlKDTKVRFT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 87 GAPLSVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSA--PA-------FIQldtklsifeTGIKVVDLLAPYRRG 157
Cdd:PRK04196 73 GEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVareypeeFIQ---------TGISAIDGLNTLVRG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 158 GKIGLFGGAGvgktvlimeLINNIAKAHGGVSVFGGVGE------------RTREGNDLYMEMKESGVINeeniaesKVA 225
Cdd:PRK04196 144 QKLPIFSGSG---------LPHNELAAQIARQAKVLGEEenfavvfaamgiTFEEANFFMEDFEETGALE-------RSV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 226 LVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER- 304
Cdd:PRK04196 208 VFLNLADDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERa 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 305 -ITSTKEGSITSIQAVYVPADDLTDPAPattfahlDAT-------TVLSRGLAAKGIYPAVDPLDSTSTMLQPQIvG--- 373
Cdd:PRK04196 288 gRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegqIVLSRELHRKGIYPPIDVLPSLSRLMKDGI-Gegk 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 62085151 374 --EEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVSRARKIE-RFLSQPF 427
Cdd:PRK04196 360 trEDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFErEFVNQGF 416
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
61-428 |
1.26e-27 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 115.40 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 61 LGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSAPAFIQLDTKLSI 140
Cdd:PRK13343 66 LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 141 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESGVIN 215
Cdd:PRK13343 146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN------------------QKDSDVIcvyvaIGQKASAVAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 216 -----EENIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGY 290
Cdd:PRK13343 208 vietlREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAY 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 291 QPTLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTM 366
Cdd:PRK13343 287 PGDIFYLHSRLLERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRV 366
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62085151 367 ---LQPQIVGEEhyetAQRVKQTLQRYKELQdIIAILGLDeLSEEDRLTVSRARKIERFLSQPFF 428
Cdd:PRK13343 367 ggkAQHPAIRKE----SGRLRLDYAQFLELE-AFTRFGGL-LDAGTQKQITRGRRLRELLKQPRF 425
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
89-368 |
3.73e-25 |
|
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: 104.61 E-value: 3.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 89 PLSVPVGGATLGRIFNVLGEPVDDLGPV------DTHTTS--PIHRSAPA-FIQldtklsifeTGIKVVDLLAPYRRGGK 159
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPIlpedylDINGPPinPVARIYPEeMIQ---------TGISAIDVMNTLVRGQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 160 IGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGERTREGNDLYMEMKESgviNEENIAESKVALVYGQMNEPPGARM 239
Cdd:cd01135 72 LPIFSGSGLPHNELAAQIARQ-AGVVGSEENFAIVFAAMGVTMEEARFFKDD---FEETGALERVVLFLNLANDPTIERI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 240 RVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER--ITSTKEGSITSIQ 317
Cdd:cd01135 148 ITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIP 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 62085151 318 AVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ 368
Cdd:cd01135 228 ILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMK 278
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
89-364 |
1.49e-21 |
|
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: 94.56 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 89 PLSVPVGGATLGRIFNVLGEPVDDL----GP-----VDTHTTsPIHRSAPAFIQLDTKLsIFETGIKVVDLLAPYRRGGK 159
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIaetgSIfiprgVNVQRW-PVRQPRPVKEKLPPNV-PLLTGQRVLDTLFPVAKGGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 160 IGLFGGAGVGKTVlimeLINNIAK-AHGGVSVFGGVGERTREGNDLYMEMKE-SGVINEENIAEsKVALVYGQMNEPPGA 237
Cdd:cd01134 79 AAIPGPFGCGKTV----ISQSLSKwSNSDVVIYVGCGERGNEMAEVLEEFPElKDPITGESLME-RTVLIANTSNMPVAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 238 RMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI-------TSTKE 310
Cdd:cd01134 154 REASIYTGITIAEYFRDMG-YNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSPGRE 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 62085151 311 GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 364
Cdd:cd01134 233 GSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYS 286
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
86-425 |
8.69e-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: 8.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 86 TGAPLSVPVGGATLGRIFNVLGEPVDDLGPV------DTHTtSPIHRSAPAFIQldtklSIFETGIKVVDLLAPYRRGGK 159
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVlaedylDING-QPINPYARIYPE-----EMIQTGISAIDVMNSIARGQK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 160 IGLFGGAGVGKTvlimELINNIAKAHGGVSVFGGVGERTREGNdLYMEMKESGViN-----------EENIAESKVALVY 228
Cdd:TIGR01040 144 IPIFSAAGLPHN----EIAAQICRQAGLVKLPTKDVHDGHEDN-FAIVFAAMGV-NmetarffkqdfEENGSMERVCLFL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 229 GQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI--T 306
Cdd:TIGR01040 218 NLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrV 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 307 STKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPQIvGE-----EHYETAQ 381
Cdd:TIGR01040 298 EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHSDVSN 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 62085151 382 RVKQTLQRYKELQDIIAILGLDELSEEDRLTVSRARKIER-FLSQ 425
Cdd:TIGR01040 377 QLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
244-425 |
1.51e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 94.46 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 244 TALTMAEYFRDvneQ--DVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER----IT-STKEGSITSI 316
Cdd:PRK04192 311 TGITIAEYYRD---MgyDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTII 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 317 QAVYVPADDLTDPapaTTFAHLDATTV---LSRGLAAKGIYPAVDPLDSTS---TMLQPQI---VGEEHYETAQRVKQTL 387
Cdd:PRK04192 388 GAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAINWLTSYSlylDQVAPWWeenVDPDWRELRDEAMDLL 464
|
170 180 190
....*....|....*....|....*....|....*....
gi 62085151 388 QRYKELQDIIAILGLDELSEEDRLTVSRARKI-ERFLSQ 425
Cdd:PRK04192 465 QREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
15-87 |
1.10e-19 |
|
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: 82.98 E-value: 1.10e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62085151 15 IAQIIGPVLDVAFPPGKMPNIYNALVVKGRDtigqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTG 87
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVE----FGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
376-439 |
1.24e-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: 79.80 E-value: 1.24e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62085151 376 HYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVSRARKIERFLSQPFFVAEVFTGSPGK 439
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEK 64
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
196-437 |
4.99e-18 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 87.38 E-value: 4.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 196 ERTREGNDLYMEMKESGVINEENIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGS 275
Cdd:PRK14698 692 ERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMG-YDVALMADSTSRWAEALR 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 276 EVSALLGRMPSAVGYQPTLSTEMGSLQERI-------TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGL 348
Cdd:PRK14698 771 EISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 349 AAKGIYPAVDPLDSTSTMLQP------QIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVSRARKI-ER 421
Cdd:PRK14698 851 ARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAILLVARMLrED 930
|
250
....*....|....*.
gi 62085151 422 FLSQPFFvAEVFTGSP 437
Cdd:PRK14698 931 YLQQDAF-DEVDTYCP 945
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
90-364 |
4.64e-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: 81.07 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 90 LSVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 169
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 170 KTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESGVINEENIAESKVALVY-----GQMNEPPGARM 239
Cdd:cd01132 82 KTAIAIDTIIN------------------QKGKKVYciyvaIGQKRSTVAQIVKTLEEHGAMEYtivvaATASDPAPLQY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 240 RVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE----GSITS 315
Cdd:cd01132 144 LAPYAGCAMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSLTA 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 62085151 316 IQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 364
Cdd:cd01132 223 LPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVS 271
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
66-285 |
6.74e-16 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 80.11 E-value: 6.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 66 VRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSPIHRSAPAFIQldtKLSIFE--- 142
Cdd:PRK09281 71 VGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID---RKSVHEplq 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 143 TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESGVINEE 217
Cdd:PRK09281 148 TGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN------------------QKGKDVIciyvaIGQKASTVAQVV 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62085151 218 NIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMP 285
Cdd:PRK09281 210 RKLEEHGAMEYtivvaATASDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
74-334 |
8.15e-14 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 73.14 E-value: 8.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 74 TDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVD-------DLGPVDTHTTSPIHRSAPAfiqldtklSIFETGIK 146
Cdd:PRK02118 58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDggpelegEPIEIGGPSVNPVKRIVPR--------EMIRTGIP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 147 VVDLLAPYRRGGKIGLFGGAGVGKTVLIMElINNIAKAHGGVSVFGGVGertregNDLYMEMKESgviNEENIAESKVAL 226
Cdd:PRK02118 130 MIDVFNTLVESQKIPIFSVSGEPYNALLAR-IALQAEADIIILGGMGLT------FDDYLFFKDT---FENAGALDRTVM 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 227 VYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERIT 306
Cdd:PRK02118 200 FIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAV 279
|
250 260
....*....|....*....|....*....
gi 62085151 307 STKE-GSITSIQAVYVPADDLTDPAPATT 334
Cdd:PRK02118 280 DFEDgGSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
46-358 |
1.44e-11 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 66.53 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 46 TIGQQINvtcevqqlLGNNRVRAVAMSatDGLM--RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDDLGPVDTHTTSP 123
Cdd:CHL00059 38 TIGIALN--------LESNNVGVVLMG--DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 124 IHRSAPAFIqldTKLSIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertRE 200
Cdd:CHL00059 108 IESPAPGII---SRRSVYEplqTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN------------------QK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 201 GND---LYMEM--KESGVINEENIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRdVNEQDVLLFIDNIFRF 270
Cdd:CHL00059 167 GQNvicVYVAIgqKASSVAQVVTTLQERGAMEYtivvaETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 271 VQAGSEVSALLGRMPSAVGY--------------QPTLSTEMGslqeritstkEGSITSIQAVYVPADDLTDPAPATTFA 336
Cdd:CHL00059 246 AQAYRQMSLLLRRPPGREAYpgdvfylhsrllerAAKLSSQLG----------EGSMTALPIVETQAGDVSAYIPTNVIS 315
|
330 340
....*....|....*....|..
gi 62085151 337 HLDATTVLSRGLAAKGIYPAVD 358
Cdd:CHL00059 316 ITDGQIFLSADLFNAGIRPAIN 337
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
57-358 |
2.48e-08 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 56.20 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 57 VQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPV---------------DDLGPVDTHTT 121
Cdd:PTZ00185 82 VFNLEKDGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVpvglltrsralleseQTLGKVDAGAP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 122 SPIHRSAPAFIQLdtklsifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGErtreg 201
Cdd:PTZ00185 162 NIVSRSPVNYNLL--------TGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVIS----- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 202 ndLYMEMKE--SGVINEENIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFiDNIFRFVQAG 274
Cdd:PTZ00185 229 --IYVSIGQrcSNVARIHRLLRSYGALRYttvmaATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVY-DDLSKQAVAY 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 275 SEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAA 350
Cdd:PTZ00185 306 RQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFT 385
|
....*...
gi 62085151 351 KGIYPAVD 358
Cdd:PTZ00185 386 GGQRPAVN 393
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
12-88 |
2.85e-04 |
|
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: 39.22 E-value: 2.85e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62085151 12 LGRIAQIIGPVLDVAFPPGKMpniYNALVVKGRDTIGQQINVTCEVQQLLGNnRVRAVAMSATDGLMRGMEVIDTGA 88
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVA---IGEVCEIERGDGNNETVLKAEVIGFRGD-RAILQLFESTRGLSRGALVEPTGR 73
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
372-426 |
3.57e-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: 38.95 E-value: 3.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62085151 372 VGEEHYETAQRVKQTLQRYKELQDIIAIlG---------LDElseedrlTVSRARKIERFLSQP 426
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRI-GayqagsdpeIDE-------AIAKRPAINAFLRQG 56
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| 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 ... |
381-425 |
3.88e-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: 39.68 E-value: 3.88e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 62085151 381 QRVKQTLQRYKELQDIIAILGLDELSEEDRLTVSRARKI-ERFLSQ 425
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 ... |
391-425 |
5.93e-04 |
|
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: 38.95 E-value: 5.93e-04
10 20 30
....*....|....*....|....*....|....*.
gi 62085151 391 KELQDIIAILGLDELSEEDRLTVSRARKIE-RFLSQ 425
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFErEFINQ 57
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| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
156-284 |
2.89e-03 |
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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: 38.12 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62085151 156 RGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSvfggvgertregndlymemkesgVINEENIAE---SKVALVYGQMN 232
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI-----------------------YIDGEDILEevlDQLLLIIVGGK 57
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 62085151 233 EPPGARMRVGLTALTMAEYFRdvneqDVLLFIDNIFRFVQAGSEVSALLGRM 284
Cdd:smart00382 58 KASGSGELRLRLALALARKLK-----PDVLILDEITSLLDAEQEALLLLLEE 104
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