|
Name |
Accession |
Description |
Interval |
E-value |
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
6-498 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 1124.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 6 TTSSSGVATLDKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDTVGQPINVTCEVQQLLGNNRVRAVAMSATDGL 85
Cdd:CHL00060 2 NPTGPGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 86 TRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRG 165
Cdd:CHL00060 82 MRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 166 GKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGA 245
Cdd:CHL00060 162 GKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 246 RMRVGLTALTMAEYFRDVNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQ 325
Cdd:CHL00060 242 RMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 326 AVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQQVKQTLQRYKELQDII 405
Cdd:CHL00060 322 AVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDII 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 406 AILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATA 485
Cdd:CHL00060 402 AILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATA 481
|
490
....*....|...
gi 675273976 486 KAINLEMESNLKK 498
Cdd:CHL00060 482 KAANLEVESKLKK 494
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
18-494 |
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: 953.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 18 KNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDtvgqPINVTCEVQQLLGNNRVRAVAMSATDGLTRGMDVIDTGAP 97
Cdd:COG0055 3 MNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEG----GGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 98 LSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 177
Cdd:COG0055 79 ISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 178 KTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMA 257
Cdd:COG0055 159 KTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTMA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 258 EYFRDVNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDP 337
Cdd:COG0055 232 EYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 338 APATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQQVKQTLQRYKELQDIIAILGLDELSEED 417
Cdd:COG0055 312 APATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEED 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 675273976 418 RLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAINLEMES 494
Cdd:COG0055 392 KLTVARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAEA 468
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
19-490 |
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: 842.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 19 NLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRdtvgQPINVTCEVQQLLGNNRVRAVAMSATDGLTRGMDVIDTGAPL 98
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNR----AESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 99 SVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 178
Cdd:TIGR01039 77 SVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 179 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAE 258
Cdd:TIGR01039 157 TVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 259 YFRDVNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 338
Cdd:TIGR01039 230 YFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 339 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDR 418
Cdd:TIGR01039 310 PATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDK 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 675273976 419 LTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAINL 490
Cdd:TIGR01039 390 LTVERARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
21-483 |
0e+00 |
|
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 beta subunit of this apparent second ATP synthase.
Pssm-ID: 132348 [Multi-domain] Cd Length: 449 Bit Score: 585.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 21 GRIAQIIGPVLDVAFPpGKMPNIYNALvvkgrdTVGQPINVTCEVQQLLGNNRVRAVAMSATDGLTRGMDVIDTGAPLSV 100
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFD-GELPAIHSVL------RAGREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 101 PVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 180
Cdd:TIGR03305 74 PVGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 181 LIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEqniaeskVALVYGQMNEPPGARMRVGLTALTMAEYF 260
Cdd:TIGR03305 154 LLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDN-------TVMVFGQMNEPPGARFRVGHTALTMAEYF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 261 RDVNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPA 340
Cdd:TIGR03305 227 RDDEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 341 TTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLT 420
Cdd:TIGR03305 307 HTFSHLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRV 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 675273976 421 VARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEA 483
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 ... |
99-377 |
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: 579.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 99 SVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 178
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 179 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIaeSKVALVYGQMNEPPGARMRVGLTALTMAE 258
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGL--SKVALVYGQMNEPPGARARVALTGLTMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 259 YFRDVNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 338
Cdd:cd01133 159 YFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPA 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 675273976 339 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP 377
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 ... |
99-374 |
4.24e-132 |
|
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: 383.73 E-value: 4.24e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 99 SVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 178
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 179 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGvineqniAESKVALVYGQMNEPPGARMRVGLTALTMAE 258
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSG-------AMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 259 YFRDvNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK--EGSITSIQAVYVPADDLTD 336
Cdd:cd19476 154 YFRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTD 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 675273976 337 PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTM 374
Cdd:cd19476 233 PIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
152-372 |
4.53e-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: 263.83 E-value: 4.53e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 152 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKahgGVSVFGGVGERTREGNDLYMEMKESGVIneqniaeSK 231
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-------KR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 232 VALVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQE 311
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 675273976 312 RITSTKE--GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 372
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 ... |
379-486 |
3.65e-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: 236.99 E-value: 3.65e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 379 IVGEEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGF 458
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 675273976 459 QLILSGELDGLPEQAFYLVGNIDEATAK 486
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
21-462 |
5.11e-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: 5.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 21 GRIAQIIGPVLDVAFPPGKMpniyNALV-VKGRDtvGQPInvTCEVqqlLG--NNRVRAVAMSATDGLTRGMDVIDTGAP 97
Cdd:COG1157 21 GRVTRVVGLLIEAVGPDASI----GELCeIETAD--GRPV--LAEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 98 LSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQ---LDTKLsifETGIKVVDLLAPYRRGGKIGLFGGA 174
Cdd:COG1157 90 LSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLErarITEPL---DTGVRAIDGLLTVGRGQRIGIFAGS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 175 GVGKTVLIMELINN----------IAkahggvsvfggvgERTREGNDlYME-------MKESGVIneqnIAESkvalvyg 237
Cdd:COG1157 167 GVGKSTLLGMIARNteadvnvialIG-------------ERGREVRE-FIEddlgeegLARSVVV----VATS------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 238 qmNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK 317
Cdd:COG1157 222 --DEPPLMRLRAAYTATAIAEYFRDQG-KNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 318 EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMlqPRIVGEEHYETAQQVKQTLQ 396
Cdd:COG1157 299 KGSITAFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISrVM--PDIVSPEHRALARRLRRLLA 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675273976 397 RYKELQDIIAIlG---------LDElseedrlTVARARKIERFLSQpffvaevftgSPGKYVGLAETIRGFQLIL 462
Cdd:COG1157 377 RYEENEDLIRI-GayqpgsdpeLDE-------AIALIPAIEAFLRQ----------GMDERVSFEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
99-372 |
7.14e-54 |
|
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: 181.99 E-value: 7.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 99 SVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 178
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 179 TVLIMELINNiAKAhgGVSVFGGVGERTREGNDlYMEmkesGVINEQNIaeSKVALVYGQMNEPPGARMRVGLTALTMAE 258
Cdd:cd01136 81 STLLGMIARN-TDA--DVNVIALIGERGREVRE-FIE----KDLGEEGL--KRSVLVVATSDESPLLRVRAAYTATAIAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 259 YFRDvNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 338
Cdd:cd01136 151 YFRD-QGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPI 229
|
250 260 270
....*....|....*....|....*....|....
gi 675273976 339 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 372
Cdd:cd01136 230 ADEVRSILDGHIVLSRRLAERGHYPAIDVLASIS 263
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
68-433 |
3.06e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 172.31 E-value: 3.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 68 LLGNNRVRA--VAM----------SATDGLTRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNlGPVDNSTTFPIHRS 135
Cdd:PRK06820 55 RIEPQGMLAevVSIeqemallspfASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 136 APAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELInniAKAHGGVSVFGGVGERTREGNDLYme 215
Cdd:PRK06820 134 PPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLC---ADSAADVMVLALIGERGREVREFL-- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 216 mkesgvinEQNI---AESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFVDNIFRFVQAGSEVSALLGRM 292
Cdd:PRK06820 209 --------EQVLtpeARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRG-KKVLLMADSLTRYARAAREIGLAAGEP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 293 PSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 372
Cdd:PRK06820 280 PAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVS 359
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 675273976 373 TMLqPRIVGEEHYETAQQVKQTLQRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQ 433
Cdd:PRK06820 360 RIM-PQIVSAGQLAMAQKLRRMLACYQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
84-433 |
3.57e-47 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 169.16 E-value: 3.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 84 GLTRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQ---LDTKLSifeTGIKVVDLLA 160
Cdd:PRK06936 81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSrrlIETPLS---LGVRVIDGLL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 161 PYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFGGVGERTREgndlYMEMKESGvINEQNIAESkvALVYGQMN 240
Cdd:PRK06936 158 TCGEGQRMGIFAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIESD-LGEEGLRKA--VLVVATSD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 241 EPPGARMRVGLTALTMAEYFRDvNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGS 320
Cdd:PRK06936 228 RPSMERAKAGFVATSIAEYFRD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGS 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 321 ITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQQVKQTLQRYKE 400
Cdd:PRK06936 307 ITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEE 385
|
330 340 350
....*....|....*....|....*....|....*..
gi 675273976 401 LQDIIAI----LGLDELSEEdrlTVARARKIERFLSQ 433
Cdd:PRK06936 386 VELLLQIgeyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
67-435 |
1.38e-45 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 164.78 E-value: 1.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 67 QLLGNNRVRAV--AMSATDGLTRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLG----PVDNSTTFPIHRSAPAFI 140
Cdd:PRK08149 47 QVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDapptVGPISEERVIDVAPPSYA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 141 QLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFGGVGERTREGNDLYMEMKESG 220
Cdd:PRK08149 127 ERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFVESLRASS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 221 vineqniAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQP 300
Cdd:PRK08149 204 -------RREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQG-KRVVLFIDSMTRYARALRDVALAAGELPARRGYPA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 301 TLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIV 380
Cdd:PRK08149 276 SVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVT 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 675273976 381 GEEHYETAQQVKQTLQRYKELQDIIAiLG---LDELSEEDRlTVARARKIERFLSQPF 435
Cdd:PRK08149 355 DPKHRQLAAAFRKLLTRLEELQLFID-LGeyrRGENADNDR-AMDKRPALEAFLKQDV 410
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
83-434 |
2.39e-45 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 164.56 E-value: 2.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 83 DGLTRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQ---LDTKLSifeTGIKVVDLL 159
Cdd:PRK09099 81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSrrmVEAPLP---TGVRIVDGL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 160 APYRRGGKIGLFGGAGVGKTVLIMEL-------INNIAkahggvsvfgGVGERTREGNDlYMEMkesgVINEQNIAESKV 232
Cdd:PRK09099 158 MTLGEGQRMGIFAPAGVGKSTLMGMFargtqcdVNVIA----------LIGERGREVRE-FIEL----ILGEDGMARSVV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 233 alVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQdVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER 312
Cdd:PRK09099 223 --VCATSDRSSIERAKAAYVATAIAEYFRDRGLR-VLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLER 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 313 ITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQQVK 392
Cdd:PRK09099 300 AGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLR 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 675273976 393 QTLQRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQP 434
Cdd:PRK09099 379 QLLAKHREVETLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
12-468 |
1.55e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 159.37 E-value: 1.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 12 VATLDKKNL-GRIAQIIGPVLDVAFPPGKMpNIYNALVVKGRDTVGqpinVTCEVqqlLGNNRVRAVAM--SATDGLTRG 88
Cdd:PRK08927 9 IGDIDTLVIyGRVVAVRGLLVEVAGPIHAL-SVGARIVVETRGGRP----VPCEV---VGFRGDRALLMpfGPLEGVRRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 89 MDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDNSTT-FPIHRSAP---AFIQLDTKLsifETGIKVVDLLAPYRR 164
Cdd:PRK08927 81 CRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVpYPLRAPPPpahSRARVGEPL---DLGVRALNTFLTCCR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 165 GGKIGLFGGAGVGKTVLIMELINNIAKAhggVSVFGGVGERTREGNDLYMEmkesgVINEQNIAESKValVYGQMNEPPG 244
Cdd:PRK08927 158 GQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREVQEFLQD-----DLGPEGLARSVV--VVATSDEPAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 245 ARMRVGLTALTMAEYFRDvNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI--TSTKEGSIT 322
Cdd:PRK08927 228 MRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTIT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 323 SIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMlqPRIVGEEHYETAQQVKQTLQRYKEL 401
Cdd:PRK08927 307 GLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSrTM--PGCNDPEENPLVRRARQLMATYADM 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 675273976 402 QDIIAI----LGLDelSEEDRlTVARARKIERFLSQpffvaevftgSPGKYVGLAETIRGFQLILSGELDG 468
Cdd:PRK08927 385 EELIRLgayrAGSD--PEVDE-AIRLNPALEAFLRQ----------GKDEATSLAEGYARLAQILGGPETE 442
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
98-433 |
1.98e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 156.38 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 98 LSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 177
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 178 KTVLiMELINNIAKAhgGVSVFGGVGERTRE---------GNDLymemkESGVINEQNIAESKVALVYGqmneppgarmr 248
Cdd:PRK08472 170 KSTL-MGMIVKGCLA--PIKVVALIGERGREipefieknlGGDL-----ENTVIVVATSDDSPLMRKYG----------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 249 vGLTALTMAEYFRDVNEqDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK-EGSITSIQAV 327
Cdd:PRK08472 231 -AFCAMSVAEYFKNQGL-DVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 328 YVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQQVKQTLQRYKELQDIIAI 407
Cdd:PRK08472 309 LVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIRI 387
|
330 340 350
....*....|....*....|....*....|.
gi 675273976 408 ----LGLD-ELSEedrlTVARARKIERFLSQ 433
Cdd:PRK08472 388 gayqKGNDkELDE----AISKKEFMEQFLKQ 414
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
58-433 |
3.16e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 156.04 E-value: 3.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 58 PINVTCEVQQLLGNnRVRAVAMSATDGLTRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPV--------DNSTT 129
Cdd:PRK05688 62 PVQVEAEVMGFSGD-KVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMkaedwvpmDGPTI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 130 FPIHRsAPAFIQLDTklsifetGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLiMELINNIAKAHGGVSVFGGvgERTREg 209
Cdd:PRK05688 141 NPLNR-HPISEPLDV-------GIRSINGLLTVGRGQRLGLFAGTGVGKSVL-LGMMTRFTEADIIVVGLIG--ERGRE- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 210 ndlymeMKE--SGVINEQNIAESKValVYGQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFVDNIFRFVQAGSEVSA 287
Cdd:PRK05688 209 ------VKEfiEHILGEEGLKRSVV--VASPADDAPLMRLRAAMYCTRIAEYFRDKG-KNVLLLMDSLTRFAQAQREIAL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 288 LLGRMPSAVGYQPTLSTEMGSLQERITSTKEG--SITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAV 365
Cdd:PRK05688 280 AIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAI 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 675273976 366 DPLDSTSTMLqPRIVGEEHYETAQQVKQTLQRYKELQDIIAI----LGLDelsEEDRLTVARARKIERFLSQ 433
Cdd:PRK05688 360 DIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLISVgayvAGGD---PETDLAIARFPHLVQFLRQ 427
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
84-407 |
1.28e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 154.47 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 84 GLTRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHrsAPAFIQLDTKlSIFE---TGIKVVDLLA 160
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRR-PITEpldVGVRAINAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 161 PYRRGGKIGLFGGAGVGKTVLI-MELINNIAKAhggvSVFGGVGERTREGNDLYMEmkesgVINEQNIAESKValVYGQM 239
Cdd:PRK08972 158 TVGKGQRMGLFAGSGVGKSVLLgMMTRGTTADV----IVVGLVGERGREVKEFIEE-----ILGEEGRARSVV--VAAPA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 240 NEPPGARMRVGLTALTMAEYFRDVNeQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERIT--STK 317
Cdd:PRK08972 227 DTSPLMRLKGCETATTIAEYFRDQG-LNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 318 EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQQVKQTLQR 397
Cdd:PRK08972 306 QGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSL 384
|
330
....*....|
gi 675273976 398 YKELQDIIAI 407
Cdd:PRK08972 385 YQQNRDLISI 394
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
108-409 |
1.39e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 154.39 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 108 GRIFNVLGEPIDNLGPVDNST-TFPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELi 186
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTrPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 187 nniAKA-HGGVSVFGGVGERTREgndlYMEMKEsGVINEqniAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNE 265
Cdd:PRK06002 186 ---ARAdAFDTVVIALVGERGRE----VREFLE-DTLAD---NLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 266 qDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE--GSITSIQAVYVPADDLTDPAPATTF 343
Cdd:PRK06002 255 -NVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEggGSITGIFSVLVDGDDHNDPVADSIR 333
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 675273976 344 AHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHyETAQQVKQTLQRYKELQDIIAILG 409
Cdd:PRK06002 334 GTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQR-KLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
94-407 |
2.12e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 153.72 E-value: 2.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 94 TGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGG 173
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 174 AGVGKTVLIMEL-------INNIAkahggvsvfgGVGERTREGNDlYMEmKESGvinEQNIAESKValVYGQMNEPPGAR 246
Cdd:PRK07721 167 SGVGKSTLMGMIarntsadLNVIA----------LIGERGREVRE-FIE-RDLG---PEGLKRSIV--VVATSDQPALMR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 247 MRVGLTALTMAEYFRDVNeQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQA 326
Cdd:PRK07721 230 IKGAYTATAIAEYFRDQG-LNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 327 VYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQQVKQTLQRYKELQDIIA 406
Cdd:PRK07721 309 VLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLIN 387
|
.
gi 675273976 407 I 407
Cdd:PRK07721 388 I 388
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
60-433 |
2.09e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 150.90 E-value: 2.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 60 NVTCEVQQLLGNNRVrAVAMSATDGLTRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNlgPVDNSTTFPIHRSAP-- 137
Cdd:PRK06793 52 NVLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPpi 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 138 -AFIQLDTKlSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGvgERTREGND-LYME 215
Cdd:PRK06793 129 hAFEREEIT-DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKADINVISLVG--ERGREVKDfIRKE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 216 MKESGVineqniaeSKVALVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSA 295
Cdd:PRK06793 205 LGEEGM--------RKSVVVVATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELPIG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 296 vGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTML 375
Cdd:PRK06793 276 -GKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIM 354
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 675273976 376 QpRIVGEEHYETAQQVKQTLQRYKElQDIIAILGLDELSEEDRLTVARARKIE---RFLSQ 433
Cdd:PRK06793 355 E-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 ... |
19-98 |
1.61e-38 |
|
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: 134.95 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 19 NLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDtvgqPINVTCEVQQLLGNNRVRAVAMSATDGLTRGMDVIDTGAPL 98
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDD----GKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
84-452 |
6.71e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 138.49 E-value: 6.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 84 GLTRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYR 163
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 164 RGGKIGLFGGAGVGKTVLiMELINNIAKAHGGVSVFGGvgERTREGNDLY-MEMKESGVineqniaeSKVALVYGQMNEP 242
Cdd:PRK07196 154 KGQRVGLMAGSGVGKSVL-LGMITRYTQADVVVVGLIG--ERGREVKEFIeHSLQAAGM--------AKSVVVAAPADES 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 243 PGARMRVGLTALTMAEYFRDVNeQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI-TSTKEGSI 321
Cdd:PRK07196 223 PLMRIKATELCHAIATYYRDKG-HDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 322 TSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQQVKQTLQRYKEL 401
Cdd:PRK07196 302 TAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAI 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 675273976 402 QDIIA----ILGLDELSEEdrlTVARARKIERFLSQPFFVAEVFTGSPGKYVGLA 452
Cdd:PRK07196 381 KPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQEVGHPALFSASVEQLTGMF 432
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
80-407 |
5.66e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 135.85 E-value: 5.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 80 SATDGLTRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNL----GPVDNSTTFPihrsAPAFIQLDTKLSIFeTGIKV 155
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRelpdVCWKDYDAMP----PPAMVRQPITQPLM-TGIRA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 156 VDLLAPYRRGGKIGLFGGAGVGKTVLIMELINniaKAHGGVSVFGGVGERTREgndlYMEMKESGVINEqniAESKVALV 235
Cdd:PRK07594 146 IDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFIDFTLSEE---TRKRCVIV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 236 YGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS 315
Cdd:PRK07594 216 VATSDRPALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGM 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 316 TKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQQVKQTL 395
Cdd:PRK07594 295 GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCL 373
|
330
....*....|..
gi 675273976 396 QRYKELQDIIAI 407
Cdd:PRK07594 374 ALYQEVELLIRI 385
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
100-436 |
1.91e-32 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 129.13 E-value: 1.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 100 VPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIhrSAPAF--IQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 177
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGAL--ITPPFnpLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 178 KTVLiMELINNIAKAHGGVSVFGGvgERTREGNDlYMEmkesGVINEQNIAESKValVYGQMNEPPGARMRVGLTALTMA 257
Cdd:PRK07960 188 KSVL-LGMMARYTQADVIVVGLIG--ERGREVKD-FIE----NILGAEGRARSVV--IAAPADVSPLLRMQGAAYATRIA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 258 EYFRDvNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS--TKEGSITSIQAVYVPADDLT 335
Cdd:PRK07960 258 EDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQ 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 336 DPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQQVKQTLQRYKELQDIIAI----LGLD 411
Cdd:PRK07960 337 DPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALIDEQHYARVRQFKQLLSSFQRNRDLVSVgayaKGSD 415
|
330 340
....*....|....*....|....*
gi 675273976 412 ELSEEdrlTVARARKIERFLSQPFF 436
Cdd:PRK07960 416 PMLDK---AIALWPQLEAFLQQGIF 437
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
23-435 |
6.26e-30 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 121.86 E-value: 6.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 23 IAQIIGPVLDVAfppgKMPNI-YNALVV----KGRDTVGQPINVTCE--VQQLLGNnrvravamsaTDGL-TRGMDVIDT 94
Cdd:PRK04196 7 VSEIKGPLLFVE----GVEGVaYGEIVEielpNGEKRRGQVLEVSEDkaVVQVFEG----------TTGLdLKDTKVRFT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 95 GAPLSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSA--PA-------FIQldtklsifeTGIKVVDLLAPYRRG 165
Cdd:PRK04196 73 GEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVareypeeFIQ---------TGISAIDGLNTLVRG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 166 GKIGLFGGAGvgktvlimeLINNIAKAHGGVSVFGGVGE------------RTREGNDLYMEMKESGVINeqniaesKVA 233
Cdd:PRK04196 144 QKLPIFSGSG---------LPHNELAAQIARQAKVLGEEenfavvfaamgiTFEEANFFMEDFEETGALE-------RSV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 234 LVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER- 312
Cdd:PRK04196 208 VFLNLADDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERa 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 313 -ITSTKEGSITSIQAVYVPADDLTDPAPattfahlDAT-------TVLSRGLAAKGIYPAVDPLDSTSTMLQPRIvG--- 381
Cdd:PRK04196 288 gRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegqIVLSRELHRKGIYPPIDVLPSLSRLMKDGI-Gegk 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 675273976 382 --EEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQPF 435
Cdd:PRK04196 360 trEDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFErEFVNQGF 416
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
77-465 |
3.87e-29 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 119.24 E-value: 3.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 77 VAMSATDGLTRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQLDTKLSIFETGIKVV 156
Cdd:PRK05922 69 MSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 157 DLLAPYRRGGKIGLFGGAGVGKTvlimELINNIAK-AHGGVSVFGGVGERTREGNDlYMEMKESGvineqnIAESKVALV 235
Cdd:PRK05922 149 DAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVRE-YIEQHKEG------LAAQRTIII 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 236 YGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS 315
Cdd:PRK05922 218 ASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 316 TKEGSITSIQAV-YVP--ADDLTDPAPATTFAHLDATTVlSRGLAAkgiyPAVDPLDSTSTMLQpRIVGEEHYETAQQVK 392
Cdd:PRK05922 297 NDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSRSAR-QLALPHHYAAAEELR 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 675273976 393 QTLQRYKELQDIIAI----LGLDElsEEDRlTVARARKIERFLSQPFfvaevftgspGKYVGLAETIRGFQLILSGE 465
Cdd:PRK05922 371 SLLKAYHEALDIIQLgayvPGQDA--HLDR-AVKLLPSIKQFLSQPL----------SSYCALHNTLKQLEALLKHE 434
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
69-498 |
8.49e-28 |
|
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273365 [Multi-domain] Cd Length: 501 Bit Score: 116.33 E-value: 8.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 69 LGNNRVRAVAMSATDGLTRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQLDTKLSI 148
Cdd:TIGR00962 65 LEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 149 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESGVIN 223
Cdd:TIGR00962 145 LQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIIN------------------QKDSDVYciyvaIGQKASTVAQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 224 EQNIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGY 298
Cdd:TIGR00962 207 VVRKLEEHGAMAYtivvaATASDSASLQYLAPYTGCTMGEYFRD-NGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 299 QPTLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTStm 374
Cdd:TIGR00962 286 PGDVFYLHSRLLERAAKLNDekggGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVS-- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 375 lqpRIVGEEHYETAQQVKQTLQ----RYKELqDIIAILGLDeLSEEDRLTVARARKIERFLSQPFF--------VAEVFT 442
Cdd:TIGR00962 364 ---RVGGAAQIKAMKQVAGSLRlelaQYREL-EAFSQFASD-LDEATKKQLERGQRVVELLKQPQYkplsveeqVVILFA 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 675273976 443 GSPG--KYVGLAEtIRGFQLILSGELDGlpEQAFYLvgniDE-ATAKAINLEMESNLKK 498
Cdd:TIGR00962 439 GTKGylDDIPVDK-IRKFEQALLAYLDA--NHPDIL----EEiNTTKKLTEELEAKLKE 490
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
69-436 |
6.18e-27 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 113.47 E-value: 6.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 69 LGNNRVRAVAMSATDGLTRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQLDTKLSI 148
Cdd:PRK13343 66 LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 149 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESGVIN 223
Cdd:PRK13343 146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN------------------QKDSDVIcvyvaIGQKASAVAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 224 -----EQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGY 298
Cdd:PRK13343 208 vietlREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAY 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 299 QPTLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTStm 374
Cdd:PRK13343 287 PGDIFYLHSRLLERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVS-- 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 675273976 375 lqpRIVGEEHY----ETAQQVKQTLQRYKELQdIIAILGLDeLSEEDRLTVARARKIERFLSQPFF 436
Cdd:PRK13343 365 ---RVGGKAQHpairKESGRLRLDYAQFLELE-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 ... |
97-376 |
2.08e-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: 105.38 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 97 PLSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSA--PA-------FIQldtklsifeTGIKVVDLLAPYRRGGK 167
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPinPVariypeeMIQ---------TGISAIDVMNTLVRGQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 168 IGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGERTREGNDLYMEMKESgviNEQNIAESKVALVYGQMNEPPGARM 247
Cdd:cd01135 72 LPIFSGSGLPHNELAAQIARQ-AGVVGSEENFAIVFAAMGVTMEEARFFKDD---FEETGALERVVLFLNLANDPTIERI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 248 RVGLTALTMAEYFRDVNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER--ITSTKEGSITSIQ 325
Cdd:cd01135 148 ITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIP 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 675273976 326 AVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ 376
Cdd:cd01135 228 ILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMK 278
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
86-433 |
1.51e-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: 97.10 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 86 TRGMDVID-----TGAPLSVPVGGATLGRIFNVLGEPIDNLGPV--------DNSTTFPIHRSAPAfiqldtklSIFETG 152
Cdd:TIGR01040 57 TSGIDAKKttcefTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVlaedyldiNGQPINPYARIYPE--------EMIQTG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 153 IKVVDLLAPYRRGGKIGLFGGAGVGKTvlimELINNIAKAHGGVSVFGGVGERTREGNdLYMEMKESGViN--------- 223
Cdd:TIGR01040 129 ISAIDVMNSIARGQKIPIFSAAGLPHN----EIAAQICRQAGLVKLPTKDVHDGHEDN-FAIVFAAMGV-Nmetarffkq 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 224 --EQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPT 301
Cdd:TIGR01040 203 dfEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGY 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 302 LSTEMGSLQERI--TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRI 379
Cdd:TIGR01040 283 MYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAI 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 380 vGE-----EHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIER-FLSQ 433
Cdd:TIGR01040 363 -GEgmtrkDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
97-372 |
7.86e-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: 92.64 E-value: 7.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 97 PLSVPVGGATLGRIFNVLGEPIDNLGPVD--------NSTTFPIHRSAPAFIQLDTKLsIFETGIKVVDLLAPYRRGGKI 168
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAETGsifiprgvNVQRWPVRQPRPVKEKLPPNV-PLLTGQRVLDTLFPVAKGGTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 169 GLFGGAGVGKTVlimeLINNIAK-AHGGVSVFGGVGERTREGNDLYMEMKE-SGVINEQNIAEsKVALVYGQMNEPPGAR 246
Cdd:cd01134 80 AIPGPFGCGKTV----ISQSLSKwSNSDVVIYVGCGERGNEMAEVLEEFPElKDPITGESLME-RTVLIANTSNMPVAAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 247 MRVGLTALTMAEYFRDVNeQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI-------TSTKEG 319
Cdd:cd01134 155 EASIYTGITIAEYFRDMG-YNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSPGREG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 675273976 320 SITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 372
Cdd:cd01134 234 SVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYS 286
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
252-433 |
1.90e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 94.46 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 252 TALTMAEYFRDvneQ--DVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER----IT-STKEGSITSI 324
Cdd:PRK04192 311 TGITIAEYYRD---MgyDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTII 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 325 QAVYVPADDLTDPapaTTFAHLDATTV---LSRGLAAKGIYPAVDPLDSTS---TMLQP---RIVGEEHYETAQQVKQTL 395
Cdd:PRK04192 388 GAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAINWLTSYSlylDQVAPwweENVDPDWRELRDEAMDLL 464
|
170 180 190
....*....|....*....|....*....|....*....
gi 675273976 396 QRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 433
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, ... |
384-447 |
3.43e-19 |
|
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: 81.34 E-value: 3.43e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 675273976 384 HYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGK 447
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEK 64
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
23-95 |
1.22e-18 |
|
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: 79.90 E-value: 1.22e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 675273976 23 IAQIIGPVLDVAFPPGKMPNIYNALVVKGRDtvgqPINVTCEVQQLLGNNRVRAVAMSATDGLTRGMDVIDTG 95
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVE----FGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
204-445 |
1.71e-18 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 88.93 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 204 ERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFVDNIFRFVQAGS 283
Cdd:PRK14698 692 ERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMG-YDVALMADSTSRWAEALR 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 284 EVSALLGRMPSAVGYQPTLSTEMGSLQERI-------TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGL 356
Cdd:PRK14698 771 EISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 357 AAKGIYPAVDPLDSTSTMLQP------RIVGEEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ER 429
Cdd:PRK14698 851 ARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAILLVARMLrED 930
|
250
....*....|....*.
gi 675273976 430 FLSQPFFvAEVFTGSP 445
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 ... |
98-372 |
3.02e-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: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 98 LSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 177
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 178 KTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESGVINEQNIAESKVALVY-----GQMNEPPGARM 247
Cdd:cd01132 82 KTAIAIDTIIN------------------QKGKKVYciyvaIGQKRSTVAQIVKTLEEHGAMEYtivvaATASDPAPLQY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 248 RVGLTALTMAEYFRDvNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE----GSITS 323
Cdd:cd01132 144 LAPYAGCAMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSLTA 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 675273976 324 IQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 372
Cdd:cd01132 223 LPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVS 271
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
74-293 |
1.26e-16 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 82.42 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 74 VRAVAMSATDGLTRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQldtKLSIFE--- 150
Cdd:PRK09281 71 VGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID---RKSVHEplq 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 151 TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESGVINEQ 225
Cdd:PRK09281 148 TGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN------------------QKGKDVIciyvaIGQKASTVAQVV 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 675273976 226 NIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFVDNIFRFVQAGSEVSALLGRMP 293
Cdd:PRK09281 210 RKLEEHGAMEYtivvaATASDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
69-165 |
4.62e-16 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 80.47 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 69 LGNNRVRAVAMSATDGLTRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIQLDtklSI 148
Cdd:COG0056 66 LEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQ---PV 142
|
90 100
....*....|....*....|
gi 675273976 149 FE---TGIKVVDLLAPYRRG 165
Cdd:COG0056 143 HEplqTGIKAIDAMIPIGRG 162
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
82-342 |
1.75e-13 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 72.37 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 82 TDGLTRGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNlGPVDNSTTFPIhrSAPAFIQLDTKL--SIFETGIKVVDLL 159
Cdd:PRK02118 58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GPELEGEPIEI--GGPSVNPVKRIVprEMIRTGIPMIDVF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 160 APYRRGGKIGLFGGAGVGKTVLIMElINNIAKAHGGVSVFGGVGertregNDLYMEMKESgviNEQNIAESKVALVYGQM 239
Cdd:PRK02118 135 NTLVESQKIPIFSVSGEPYNALLAR-IALQAEADIIILGGMGLT------FDDYLFFKDT---FENAGALDRTVMFIHTA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 240 NEPPGARMRVGLTALTMAEYFRDVNEQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE- 318
Cdd:PRK02118 205 SDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEDg 284
|
250 260
....*....|....*....|....
gi 675273976 319 GSITSIQAVYVPADDLTDPAPATT 342
Cdd:PRK02118 285 GSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
69-366 |
5.82e-12 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 67.68 E-value: 5.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 69 LGNNRVRAVAMSatDGLT--RGMDVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDNSTTFPIHRSAPAFIqldTKL 146
Cdd:CHL00059 45 LESNNVGVVLMG--DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGII---SRR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 147 SIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGND---LYMEM--KE 218
Cdd:CHL00059 120 SVYEplqTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN------------------QKGQNvicVYVAIgqKA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 219 SGVINEQNIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRdVNEQDVLLFVDNIFRFVQAGSEVSALLGRMP 293
Cdd:CHL00059 182 SSVAQVVTTLQERGAMEYtivvaETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 294 SAVGY--------------QPTLSTEMGslqeritstkEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAK 359
Cdd:CHL00059 261 GREAYpgdvfylhsrllerAAKLSSQLG----------EGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNA 330
|
....*..
gi 675273976 360 GIYPAVD 366
Cdd:CHL00059 331 GIRPAIN 337
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
65-366 |
2.38e-07 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 53.12 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 65 VQQLLGNNRVRAVAMSATDGLTRGMDVIDTGAPLSVPVGGATLGRIFNVLG---------------EPIDNLGPVDNSTT 129
Cdd:PTZ00185 82 VFNLEKDGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGhevpvglltrsrallESEQTLGKVDAGAP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 130 FPIHRSAPAFIQLdtklsifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGErtreg 209
Cdd:PTZ00185 162 NIVSRSPVNYNLL--------TGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVIS----- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 210 ndLYMEMKE--SGVINEQNIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRDVNEQdVLLFVDNIFRFVQAG 282
Cdd:PTZ00185 229 --IYVSIGQrcSNVARIHRLLRSYGALRYttvmaATAAEPAGLQYLAPYSGVTMGEYFMNRGRH-CLCVYDDLSKQAVAY 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 283 SEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAA 358
Cdd:PTZ00185 306 RQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFT 385
|
....*...
gi 675273976 359 KGIYPAVD 366
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 ... |
380-434 |
2.08e-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: 39.72 E-value: 2.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 675273976 380 VGEEHYETAQQVKQTLQRYKELQDIIAIlG---------LDElseedrlTVARARKIERFLSQP 434
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 ... |
389-433 |
2.95e-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: 40.07 E-value: 2.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 675273976 389 QQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 433
Cdd:cd18111 6 TEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIrEDFLQQ 51
|
|
| 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 ... |
399-433 |
2.97e-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: 39.72 E-value: 2.97e-04
10 20 30
....*....|....*....|....*....|....*.
gi 675273976 399 KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ 433
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFErEFINQ 57
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
20-96 |
5.94e-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: 38.45 E-value: 5.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 675273976 20 LGRIAQIIGPVLDVAFPPGKMpniYNALVVKGRDTVGQPINVTCEVQQLLGNnRVRAVAMSATDGLTRGMDVIDTGA 96
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVA---IGEVCEIERGDGNNETVLKAEVIGFRGD-RAILQLFESTRGLSRGALVEPTGR 73
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
164-292 |
7.49e-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: 36.97 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 675273976 164 RGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYmemkesgvineqniaeskvaLVYGQMNEPP 243
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLL--------------------LIIVGGKKAS 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 675273976 244 GARMRVGLTALTMAEYFRdvneqDVLLFVDNIFRFVQAGSEVSALLGRM 292
Cdd:smart00382 61 GSGELRLRLALALARKLK-----PDVLILDEITSLLDAEQEALLLLLEE 104
|
|
| |
