|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
18-484 |
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: 909.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 18 TAGEGRIVRIIGPVVDVK-FDDVVPTIYNALTIDADtpiGHISTVLEVEMQLPGSVVRTVAMTSTDGLRRGLRVQDTGEP 96
Cdd:COG0055 2 AMNTGKIVQVIGPVVDVEfPEGELPAIYNALEVENE---GGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 97 MKMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAAPTFDELTTNMEIFETGIKAVDLLEPYIRGGKTGLFGGAGVG 176
Cdd:COG0055 79 ISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 177 KTVLIQELIYNLAQQHGGTSVFTGVGERTREGTDLYLEMKESGVLDKTCLVYGQMNEPPGARLRVGLAGLTTAEYFRD-R 255
Cdd:COG0055 159 KTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 256 GQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITSTKTGSITSVQAVYVPADDLTDPAPATTFT 335
Cdd:COG0055 239 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 336 HLDSTTVLSRNIASLGLYPAIDPLASTSDALDPDIVGERHYSVASKVQELLQQYADLQDIIAILGMDELSDEQRTTVNRA 415
Cdd:COG0055 319 HLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503473399 416 RKIQQFLSQSFHVAEKFTGNPGVYVRVEDTVDSFAAIVNGDVDDLPEQAFRFAGTLDDVRERAAKMGAK 484
Cdd:COG0055 399 RKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAE 467
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
21-481 |
0e+00 |
|
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 211621 [Multi-domain] Cd Length: 461 Bit Score: 770.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 21 EGRIVRIIGPVVDVK-FDDVVPTIYNALTIDADtpiGHISTVLEVEMQLPGSVVRTVAMTSTDGLRRGLRVQDTGEPMKM 99
Cdd:TIGR01039 2 KGKVVQVIGPVVDVEfEQGELPRIYNALKVQNR---AESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 100 PVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAAPTFDELTTNMEIFETGIKAVDLLEPYIRGGKTGLFGGAGVGKTV 179
Cdd:TIGR01039 79 PVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 180 LIQELIYNLAQQHGGTSVFTGVGERTREGTDLYLEMKESGVLDKTCLVYGQMNEPPGARLRVGLAGLTTAEYFRD-RGQD 258
Cdd:TIGR01039 159 LIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 259 VLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITSTKTGSITSVQAVYVPADDLTDPAPATTFTHLD 338
Cdd:TIGR01039 239 VLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 339 STTVLSRNIASLGLYPAIDPLASTSDALDPDIVGERHYSVASKVQELLQQYADLQDIIAILGMDELSDEQRTTVNRARKI 418
Cdd:TIGR01039 319 ATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRI 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503473399 419 QQFLSQSFHVAEKFTGNPGVYVRVEDTVDSFAAIVNGDVDDLPEQAFRFAGTLDDVRERAAKM 481
Cdd:TIGR01039 399 QRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
22-484 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 759.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 22 GRIVRIIGPVVDVK-FDDVVPTIYNALTI-DADTPIGHISTVLEVEMQLPGSVVRTVAMTSTDGLRRGLRVQDTGEPMKM 99
Cdd:CHL00060 17 GRITQIIGPVLDVAfPPGKMPNIYNALVVkGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 100 PVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAAPTFDELTTNMEIFETGIKAVDLLEPYIRGGKTGLFGGAGVGKTV 179
Cdd:CHL00060 97 PVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 180 LIQELIYNLAQQHGGTSVFTGVGERTREGTDLYLEMKESGVLD-------KTCLVYGQMNEPPGARLRVGLAGLTTAEYF 252
Cdd:CHL00060 177 LIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 253 RD-RGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITSTKTGSITSVQAVYVPADDLTDPAPA 331
Cdd:CHL00060 257 RDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 332 TTFTHLDSTTVLSRNIASLGLYPAIDPLASTSDALDPDIVGERHYSVASKVQELLQQYADLQDIIAILGMDELSDEQRTT 411
Cdd:CHL00060 337 TTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLT 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503473399 412 VNRARKIQQFLSQSFHVAEKFTGNPGVYVRVEDTVDSFAAIVNGDVDDLPEQAFRFAGTLDDVRERAAKMGAK 484
Cdd:CHL00060 417 VARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLEVE 489
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
22-473 |
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: 563.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 22 GRIVRIIGPVVDVKFDDVVPTIYNALTIDADTPIghistVLEVEMQLPGSVVRTVAMTSTDGLRRGLRVQDTGEPMKMPV 101
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGELPAIHSVLRAGREGEV-----VVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 102 GQATLGRIWNVLGEPVD-GKPAGQIEERyPIHHAAPTFDELTTNMEIFETGIKAVDLLEPYIRGGKTGLFGGAGVGKTVL 180
Cdd:TIGR03305 76 GKPTLSRMFDVFGNTIDrREPPKDVEWR-SVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 181 IQELIYNLAQQHGGTSVFTGVGERTREGTDLYLEMKESGVLDKTCLVYGQMNEPPGARLRVGLAGLTTAEYFRD-RGQDV 259
Cdd:TIGR03305 155 LTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDdEKQDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 260 LLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITSTKTGSITSVQAVYVPADDLTDPAPATTFTHLDS 339
Cdd:TIGR03305 235 LLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 340 TTVLSRNIASLGLYPAIDPLASTSDALDPDIVGERHYSVASKVQELLQQYADLQDIIAILGMDELSDEQRTTVNRARKIQ 419
Cdd:TIGR03305 315 SLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLE 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 503473399 420 QFLSQSFHVAEKFTGNPGVYVRVEDTVDSFAAIVNGDVDDLPEQAFRFAGTLDD 473
Cdd:TIGR03305 395 RFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDE 448
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
98-368 |
0e+00 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 549.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 98 KMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAAPTFDELTTNMEIFETGIKAVDLLEPYIRGGKTGLFGGAGVGK 177
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 178 TVLIQELIYNLAQQHGGTSVFTGVGERTREGTDLYLEMKESGV-----LDKTCLVYGQMNEPPGARLRVGLAGLTTAEYF 252
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVinldgLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 253 RD-RGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITSTKTGSITSVQAVYVPADDLTDPAPA 331
Cdd:cd01133 161 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPA 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 503473399 332 TTFTHLDSTTVLSRNIASLGLYPAIDPLASTSDALDP 368
Cdd:cd01133 241 TTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
98-363 |
3.05e-122 |
|
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: 357.92 E-value: 3.05e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 98 KMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAAPTFDELTTNMEIFETGIKAVDLLEPYIRGGKTGLFGGAGVGK 177
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 178 TVLIQELIYNLAQQHGGTSVFTGVGERTREGTDLYLEMKESGVLDKTCLVYGQMNEPPGARLRVGLAGLTTAEYFRDRGQ 257
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 258 DVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITSTKT--GSITSVQAVYVPADDLTDPAPATTFT 335
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDggGSITAIPAVSTPGDDLTDPIPDNTFA 240
|
250 260
....*....|....*....|....*...
gi 503473399 336 HLDSTTVLSRNIASLGLYPAIDPLASTS 363
Cdd:cd19476 241 ILDGQIVLSRELARKGIYPAINVLDSTS 268
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
151-363 |
4.17e-95 |
|
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: 286.17 E-value: 4.17e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 151 GIKAVDLLEPYIRGGKTGLFGGAGVGKTVLIQELIynlAQQHGGTSVFTGVGERTREGTDLYLEMKESGVLDKTCLVYGQ 230
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIA---RQASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 231 MNEPPGARLRVGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITST--K 308
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVkgK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503473399 309 TGSITSVQAVYVPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTS 363
Cdd:pfam00006 158 GGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
21-453 |
2.54e-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: 214.51 E-value: 2.54e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 21 EGRIVRIIGpvvdvkfddvvptiynaLTIDADTPIGHISTVLEVEMQ----LPGSVV-----RTVAM--TSTDGLRRGLR 89
Cdd:COG1157 20 SGRVTRVVG-----------------LLIEAVGPDASIGELCEIETAdgrpVLAEVVgfrgdRVLLMplGDLEGISPGAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 90 VQDTGEPMKMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAAPtfDELTTNM--EIFETGIKAVDLLEPYIRGGKT 167
Cdd:COG1157 83 VVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPP--NPLERARitEPLDTGVRAIDGLLTVGRGQRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 168 GLFGGAGVGKTVLIQELIynlaqqhGGTS----VFTGVGERTREGTDlYLE--MKESGvLDKTCLVYGQMNEPPGARLRV 241
Cdd:COG1157 161 GIFAGSGVGKSTLLGMIA-------RNTEadvnVIALIGERGREVRE-FIEddLGEEG-LARSVVVVATSDEPPLMRLRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 242 GLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITSTKTGSITSVQAVYVP 321
Cdd:COG1157 232 AYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 322 ADDLTDP----APATtfthLDSTTVLSRNIASLGLYPAIDPLASTSDALdPDIVGERHYSVASKVQELLQQYADLQDIIA 397
Cdd:COG1157 312 GDDMNDPiadaVRGI----LDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLLARYEENEDLIR 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 398 I----LGMDELSDEqrtTVNRARKIQQFLSQSFHvaEKFTgnpgvyvrVEDTVDSFAAIV 453
Cdd:COG1157 387 IgayqPGSDPELDE---AIALIPAIEAFLRQGMD--ERVS--------FEESLAQLAELL 433
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
370-477 |
5.80e-61 |
|
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: 194.62 E-value: 5.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 370 IVGERHYSVASKVQELLQQYADLQDIIAILGMDELSDEQRTTVNRARKIQQFLSQSFHVAEKFTGNPGVYVRVEDTVDSF 449
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 503473399 450 AAIVNGDVDDLPEQAFRFAGTLDDVRER 477
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
100-363 |
8.83e-56 |
|
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: 186.61 E-value: 8.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 100 PVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAAPtfDELTTNM--EIFETGIKAVDLLEPYIRGGKTGLFGGAGVGK 177
Cdd:cd01136 3 PVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPP--NPLKRAPieQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 178 TVLIQELIYNLAQQhggTSVFTGVGERTREGTDLYLEMKESGVLDKTCLVYGQMNEPPGARLRVGLAGLTTAEYFRDRGQ 257
Cdd:cd01136 81 STLLGMIARNTDAD---VNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 258 DVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITSTKTGSITSVQAVYVPADDLTDPAPATTFTHL 337
Cdd:cd01136 158 KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSIL 237
|
250 260
....*....|....*....|....*.
gi 503473399 338 DSTTVLSRNIASLGLYPAIDPLASTS 363
Cdd:cd01136 238 DGHIVLSRRLAERGHYPAIDVLASIS 263
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
80-425 |
5.48e-53 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 184.63 E-value: 5.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 80 STDGLRRGLRVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKPAGQIEERyPIHHAAPtfDELTTNM--EIFETGIKAVDL 157
Cdd:PRK06820 80 SSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWR-ELDCPPP--SPLTRQPieQMLTTGIRAIDG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 158 LEPYIRGGKTGLFGGAGVGKTVLIQELIynlAQQHGGTSVFTGVGERTREGTDLYLEMKESGVLDKTCLVYGQMNEPPGA 237
Cdd:PRK06820 157 ILSCGEGQRIGIFAAAGVGKSTLLGMLC---ADSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 238 RLRVGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITSTKTGSITSVQA 317
Cdd:PRK06820 234 RLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 318 VYVPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTSDALdPDIVGERHYSVASKVQELLQQYADLQDIIA 397
Cdd:PRK06820 314 VLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIELLVR 392
|
330 340 350
....*....|....*....|....*....|..
gi 503473399 398 I----LGMDELSDEqrtTVNRARKIQQFLSQS 425
Cdd:PRK06820 393 VgeyqAGEDLQADE---ALQRYPAICAFLQQD 421
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
83-432 |
1.63e-49 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 175.33 E-value: 1.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 83 GLRRGLRVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAAPtfDELTTNM--EIFETGIKAVDLLEP 160
Cdd:PRK06936 81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAP--APMSRRLieTPLSLGVRVIDGLLT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 161 YIRGGKTGLFGGAGVGKTVLIQELIYNLAQQhggTSVFTGVGERTREGTD-LYLEMKESGvLDKTCLVYGQMNEPPGARL 239
Cdd:PRK06936 159 CGEGQRMGIFAAAGGGKSTLLASLIRSAEVD---VTVLALIGERGREVREfIESDLGEEG-LRKAVLVVATSDRPSMERA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 240 RVGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITSTKTGSITSVQAVY 319
Cdd:PRK06936 235 KAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 320 VPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTSDALDpDIVGERHYSVASKVQELLQQYADLQDIIAI- 398
Cdd:PRK06936 315 VEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIg 393
|
330 340 350
....*....|....*....|....*....|....*..
gi 503473399 399 ---LGMDELSDEqrtTVNRARKIQQFLSQSFHVAEKF 432
Cdd:PRK06936 394 eyqKGQDKEADQ---AIERIGAIRGFLRQGTHELSHF 427
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
78-433 |
2.54e-49 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 174.41 E-value: 2.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 78 MTSTDGLRRGLRVQDTGEPMKMPVGQATLGRIWNVLGEPVD----GKPAGQIEERYPIHHAAPTFDELTTNMEIFETGIK 153
Cdd:PRK08149 61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVErfdaPPTVGPISEERVIDVAPPSYAERRPIREPLITGVR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 154 AVDLLEPYIRGGKTGLFGGAGVGKTVLIQELIynlaqQHGGTSVFT-G-VGERTREGTDLYLEMKESGVLDKTCLVYGQM 231
Cdd:PRK08149 141 AIDGLLTCGVGQRMGIFASAGCGKTSLMNMLI-----EHSEADVFViGlIGERGREVTEFVESLRASSRREKCVLVYATS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 232 NEPPGARLRVGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITSTKTGS 311
Cdd:PRK08149 216 DFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 312 ITSVQAVYVPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTSDALDpDIVGERHYSVASKVQELLQQYAD 391
Cdd:PRK08149 296 ITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVTDPKHRQLAAAFRKLLTRLEE 374
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 503473399 392 LQDIIAI----LGMDELSDEqrtTVNRARKIQQFLSQSfhVAEKFT 433
Cdd:PRK08149 375 LQLFIDLgeyrRGENADNDR---AMDKRPALEAFLKQD--VAEKSS 415
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
82-454 |
6.58e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 173.72 E-value: 6.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 82 DGLRRGLRVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAAptFDELTTNM--EIFETGIKAVDLLE 159
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAP--IAAMKRGLidEVFSVGVKSIDGLL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 160 PYIRGGKTGLFGGAGVGKTVLIQELIYN-LAQqhggTSVFTGVGERTREGTDlYLEMKESGVLDKTCLVYGQMNEPPGAR 238
Cdd:PRK08472 153 TCGKGQKLGIFAGSGVGKSTLMGMIVKGcLAP----IKVVALIGERGREIPE-FIEKNLGGDLENTVIVVATSDDSPLMR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 239 LRVGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITSTKT-GSITSVQA 317
Cdd:PRK08472 228 KYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGkGSITAFFT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 318 VYVPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTSDALDpDIVGERHYSVASKVQELLQQYADLQDIIA 397
Cdd:PRK08472 308 VLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIR 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503473399 398 I----LGMDELSDEqrtTVNRARKIQQFLSQSFHVAEKFtgnpgvyvrvEDTVDSFAAIVN 454
Cdd:PRK08472 387 IgayqKGNDKELDE---AISKKEFMEQFLKQNPNELFPF----------EQTFEQLEEILR 434
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
87-398 |
5.19e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 165.67 E-value: 5.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 87 GLRVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAAPTFDELTTNMEIFETGIKAVDLLEPYIRGGK 166
Cdd:PRK07721 81 GCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 167 TGLFGGAGVGKTVLIQELIYNLAQQhggTSVFTGVGERTREGTDlYLE--MKESGvLDKTCLVYGQMNEPPGARLRVGLA 244
Cdd:PRK07721 161 VGIFAGSGVGKSTLMGMIARNTSAD---LNVIALIGERGREVRE-FIErdLGPEG-LKRSIVVVATSDQPALMRIKGAYT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 245 GLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITSTKTGSITSVQAVYVPADD 324
Cdd:PRK07721 236 ATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDD 315
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503473399 325 LTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTSDALdPDIVGERHYSVASKVQELLQQYADLQDIIAI 398
Cdd:PRK07721 316 MNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
56-425 |
4.28e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 163.75 E-value: 4.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 56 GHISTVLEVE-MQLPGSVVRTVAMTSTDGLRRGLRVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIhhA 134
Cdd:PRK05688 59 SYHPVQVEAEvMGFSGDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPM--D 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 135 APTFDELTTN--MEIFETGIKAVDLLEPYIRGGKTGLFGGAGVGKTVLIqeliynlaqqhGGTSVFTG--------VGER 204
Cdd:PRK05688 137 GPTINPLNRHpiSEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLL-----------GMMTRFTEadiivvglIGER 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 205 TREGTDLYLEMKESGVLDKTCLVYGQMNEPPGARLRVGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMP 284
Cdd:PRK05688 206 GREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 285 SAVGYQPTLATEMGDLQERITSTKT--GSITSVQAVYVPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLAST 362
Cdd:PRK05688 286 ATKGYPPSVFAKLPKLVERAGNAEPggGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASI 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503473399 363 SDALdPDIVGERHYSVASKVQELLQQYADLQDIIAILGMDELSD-EQRTTVNRARKIQQFLSQS 425
Cdd:PRK05688 366 SRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLISVGAYVAGGDpETDLAIARFPHLVQFLRQG 428
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
74-425 |
4.35e-45 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 163.40 E-value: 4.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 74 RTVAMTS----TDGLRRGLRVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAAPtfDELTTNM--EI 147
Cdd:PRK09099 69 RDVALLSpfgeLGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPP--DPMSRRMveAP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 148 FETGIKAVDLLEPYIRGGKTGLFGGAGVGKTVLIQELIYNLAQQhggTSVFTGVGERTREGTD-LYLEMKESGvLDKTCL 226
Cdd:PRK09099 147 LPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCD---VNVIALIGERGREVREfIELILGEDG-MARSVV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 227 VYGQMNEPPGARLRVGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITS 306
Cdd:PRK09099 223 VCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 307 TKTGSITSVQAVYVPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTSDALdPDIVGERHYSVASKVQELL 386
Cdd:PRK09099 303 GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLL 381
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 503473399 387 QQYADLQDIIAI----LGMDELSDEqrtTVNRARKIQQFLSQS 425
Cdd:PRK09099 382 AKHREVETLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
45-425 |
5.11e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 163.23 E-value: 5.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 45 NALTIDADTPI------GHISTVLEVEMQLPGSVV-----RTVAMT--STDGLRRGLRVQDTGEPMKMPVGQATLGRIWN 111
Cdd:PRK08927 25 RGLLVEVAGPIhalsvgARIVVETRGGRPVPCEVVgfrgdRALLMPfgPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 112 VLGEPVDGK-PAGQIEERYPIHHAAPTFDELTTNMEIFETGIKAVDLLEPYIRGGKTGLFGGAGVGKTVLIQELIYNLAQ 190
Cdd:PRK08927 105 ALGEPIDGKgPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 191 QhggTSVFTGVGERTREGTDlYLE--MKESGvLDKTCLVYGQMNEPPGARLRVGLAGLTTAEYFRDRGQDVLLFIDNIFR 268
Cdd:PRK08927 185 D---VSVIGLIGERGREVQE-FLQddLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 269 FSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERI--TSTKTGSITSVQAVYVPADDLTDPAPATTFTHLDSTTVLSRN 346
Cdd:PRK08927 260 FAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 347 IASLGLYPAIDPLASTSDALdPDIVGERHYSVASKVQELLQQYADLQDIIAI----LGMDELSDEqrtTVNRARKIQQFL 422
Cdd:PRK08927 340 IAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRLgayrAGSDPEVDE---AIRLNPALEAFL 415
|
...
gi 503473399 423 SQS 425
Cdd:PRK08927 416 RQG 418
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
107-425 |
8.95e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 162.86 E-value: 8.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 107 GRIWNVLGEPVDGK-PAGQIEERYPIHHAAPTFDELTTNMEIFETGIKAVDLLEPYIRGGKTGLFGGAGVGKTVLIQELi 185
Cdd:PRK06002 107 GRVINALGEPIDGLgPLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 186 ynlAQQHGGTSVFTG-VGERTREGTDlYLEMKESGVLDKTCLVYGQMNEPPGARLRVGLAGLTTAEYFRDRGQDVLLFID 264
Cdd:PRK06002 186 ---ARADAFDTVVIAlVGERGREVRE-FLEDTLADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVD 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 265 NIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERI--TSTKTGSITSVQAVYVPADDLTDPAPATTFTHLDSTTV 342
Cdd:PRK06002 262 SVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIV 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 343 LSRNIASLGLYPAIDPLASTS----DALDPDivgERhySVASKVQELLQQYADLQDIIAILGMDELSD-EQRTTVNRARK 417
Cdd:PRK06002 342 LDRAIAEQGRYPAVDPLASISrlarHAWTPE---QR--KLVSRLKSMIARFEETRDLRLIGGYRAGSDpDLDQAVDLVPR 416
|
....*...
gi 503473399 418 IQQFLSQS 425
Cdd:PRK06002 417 IYEALRQS 424
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
58-424 |
2.20e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 161.30 E-value: 2.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 58 ISTVLEVEMQLPgsvvrtvaMTSTDGLRRGLRVQDTGEPMKMPVGQATLGRIWN----VLGEPVDGKPAGQIE-ERYPIH 132
Cdd:PRK06793 58 IAIEKENNMLLP--------FEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSangeVLNEEAENIPLQKIKlDAPPIH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 133 haAPTFDELTtnmEIFETGIKAVDLLEPYIRGGKTGLFGGAGVGKTVLIQELIYNlaqQHGGTSVFTGVGERTREGTD-L 211
Cdd:PRK06793 130 --AFEREEIT---DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN---AKADINVISLVGERGREVKDfI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 212 YLEMKESGvLDKTCLVYGQMNEPPGARLRVGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAvGYQP 291
Cdd:PRK06793 202 RKELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 292 TLATEMGDLQERITSTKTGSITSVQAVYVPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTSDALDpDIV 371
Cdd:PRK06793 280 LMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIV 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 503473399 372 GERHYSVASKVQELLQQYADlQDIIAILGMDELSDEQR---TTVNRARKIQQFLSQ 424
Cdd:PRK06793 359 SPNHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAyifECKNKVEGINTFLKQ 413
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
17-398 |
2.98e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 161.41 E-value: 2.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 17 RTAGEGRIVRIIGpvvdvkfddvvptiynaLTIDA---DTPIGHISTVLEVEMQLPGSVV-----RTVAMTSTD--GLRR 86
Cdd:PRK08972 22 RAVASGKLVRVVG-----------------LTLEAtgcRAPVGSLCSIETMAGELEAEVVgfdgdLLYLMPIEElrGVLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 87 GLRVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHhaAPTFDELTTN--MEIFETGIKAVDLLEPYIRG 164
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRRpiTEPLDVGVRAINAMLTVGKG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 165 GKTGLFGGAGVGKTVLiqeliynLAQQHGGTS---VFTG-VGERTREGTDLYLEMKESGVLDKTCLVYGQMNEPPGARLR 240
Cdd:PRK08972 163 QRMGLFAGSGVGKSVL-------LGMMTRGTTadvIVVGlVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 241 VGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERI--TSTKTGSITSVQAV 318
Cdd:PRK08972 236 GCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAgnGGPGQGSITAFYTV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 319 YVPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTSDALdPDIVGERHYSVASKVQELLQQYADLQDIIAI 398
Cdd:PRK08972 316 LTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
54-425 |
6.21e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 160.12 E-value: 6.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 54 PIGHISTVLEVEmqlpGSVVRTVAMTSTDGLRRGLRVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKPAGQIEERypiHH 133
Cdd:PRK07594 50 PGEELAEVVGIN----GSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRELPDVCWK---DY 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 134 AAPTFDELTTN--MEIFETGIKAVDLLEPYIRGGKTGLFGGAGVGKTVLIQELIynlAQQHGGTSVFTGVGERTREGTDl 211
Cdd:PRK07594 123 DAMPPPAMVRQpiTQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLC---NAPDADSNVLVLIGERGREVRE- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 212 YLEMKESGVLDKTCL-VYGQMNEPPGARLRVGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQ 290
Cdd:PRK07594 199 FIDFTLSEETRKRCViVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 291 PTLATEMGDLQERITSTKTGSITSVQAVYVPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTSDALdPDI 370
Cdd:PRK07594 279 PGVFSALPRLLERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVV 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 503473399 371 VGERHYSVASKVQELLQQYADLQDIIAI----LGMDELSDEqrtTVNRARKIQQFLSQS 425
Cdd:PRK07594 358 TSHEHRQLAAILRRCLALYQEVELLIRIgeyqRGVDTDTDK---AIDTYPDICTFLRQS 413
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
83-424 |
4.66e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 146.96 E-value: 4.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 83 GLRRGLRVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKpaGQIEERYPIHHAAPTFDELTTNM--EIFETGIKAVDLLEP 160
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGK--GQLGGSTPLQQQLPQIHPLQRRAvdTPLDVGVNAINGLLT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 161 YIRGGKTGLFGGAGVGKTVLIQeLIYNLAQqhGGTSVFTGVGERTREGTDLYLEMKESGVLDKTCLVYGQMNEPPGARLR 240
Cdd:PRK07196 152 IGKGQRVGLMAGSGVGKSVLLG-MITRYTQ--ADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 241 VGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERI-TSTKTGSITSVQAVY 319
Cdd:PRK07196 229 ATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMTAIYTVL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 320 VPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTSDALDpDIVGERHYSVASKVQELLQQYADLQDIIA-- 397
Cdd:PRK07196 309 AEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAIKPLIPlg 387
|
330 340
....*....|....*....|....*....
gi 503473399 398 --ILGMDELSDEqrtTVNRARKIQQFLSQ 424
Cdd:PRK07196 388 gyVAGADPMADQ---AVHYYPAITQFLRQ 413
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
63-424 |
3.72e-37 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 141.84 E-value: 3.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 63 EVEMQLPGSVVRTvamtstdglrRGLRVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIhhAAPTFDEL- 141
Cdd:PRK07960 84 EVEGILPGARVYA----------RNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGAL--ITPPFNPLq 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 142 -TTNMEIFETGIKAVDLLEPYIRGGKTGLFGGAGVGKTVLIQELiynlAQQHGGTSVFTG-VGERTREGTDLYLEMKESG 219
Cdd:PRK07960 152 rTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMM----ARYTQADVIVVGlIGERGREVKDFIENILGAE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 220 VLDKTCLVYGQMNEPPGARLRVGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGD 299
Cdd:PRK07960 228 GRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 300 LQERITS--TKTGSITSVQAVYVPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTSDALdPDIVGERHYS 377
Cdd:PRK07960 308 LVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAM-TALIDEQHYA 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 503473399 378 VASKVQELLQQYADLQDIIAI----LGMDELSDEqrtTVNRARKIQQFLSQ 424
Cdd:PRK07960 387 RVRQFKQLLSSFQRNRDLVSVgayaKGSDPMLDK---AIALWPQLEAFLQQ 434
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
80-427 |
6.64e-35 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 135.72 E-value: 6.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 80 STDGL-RRGLRVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAA--PTFDELTTnmEIFETGIKAVD 156
Cdd:PRK04196 58 GTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVAREYPE--EFIQTGISAID 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 157 LLEPYIRGGKTGLFGGAGVGKtvliQELIYNLAQQ---HGGTS----VFTGVGERTREGTDLYLEMKESGVLDKTCLVYG 229
Cdd:PRK04196 136 GLNTLVRGQKLPIFSGSGLPH----NELAAQIARQakvLGEEEnfavVFAAMGITFEEANFFMEDFEETGALERSVVFLN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 230 QMNEPPGARLRVGLAGLTTAEYFR-DRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQER--ITS 306
Cdd:PRK04196 212 LADDPAIERILTPRMALTAAEYLAfEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 307 TKTGSITSVQAVYVPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTS----DALDPDIVGERHYSVASkv 382
Cdd:PRK04196 292 GKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSrlmkDGIGEGKTREDHKDVAN-- 369
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 503473399 383 qELLQQYA---DLQDIIAILGMDELSDEQRTTVNRARKI-QQFLSQSFH 427
Cdd:PRK04196 370 -QLYAAYArgkDLRELAAIVGEEALSERDRKYLKFADAFeREFVNQGFD 417
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
56-461 |
8.86e-33 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 130.42 E-value: 8.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 56 GHISTVLEVEMQLPGSVVrtvaMTSTDGLRRGLRVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAA 135
Cdd:PRK13343 58 GSRGFAFNLEEELVGAVL----LDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 136 PTFDELTTNMEIFETGIKAVDLLEPYIRGGKTGLFGGAGVGKTVLIQELIYNlaQQHGGT-SVFTGVGERTREGTDLYLE 214
Cdd:PRK13343 134 PAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN--QKDSDViCVYVAIGQKASAVARVIET 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 215 MKESGVLDKTCLVYGQMNEPPGARLRVGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYqPtla 294
Cdd:PRK13343 212 LREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAY-P--- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 295 temGD-------LQERIT----STKTGSITSVQAVYVPADDLTDPAPattfTHLDSTT----VLSRNIASLGLYPAIDPL 359
Cdd:PRK13343 288 ---GDifylhsrLLERAAklspELGGGSLTALPIIETLAGELSAYIP----TNLISITdgqiYLDSDLFAAGQRPAVDVG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 360 ASTS----DALDPDIvgeRHYSVASKVQelLQQYADLQdIIAILGMDeLSDEQRTTVNRARKIQQFLSQSFHVAekftgn 435
Cdd:PRK13343 361 LSVSrvggKAQHPAI---RKESGRLRLD--YAQFLELE-AFTRFGGL-LDAGTQKQITRGRRLRELLKQPRFSP------ 427
|
410 420
....*....|....*....|....*.
gi 503473399 436 pgvyVRVEDTVDSFAAIVNGDVDDLP 461
Cdd:PRK13343 428 ----LSVEEQIALLYALNEGLLDAVP 449
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
76-454 |
1.32e-31 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 126.17 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 76 VAMTSTDGLRRGLRVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAAPTFDELTTNMEIFETGIKAV 155
Cdd:PRK05922 69 MSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 156 DLLEPYIRGGKTGLFGGAGVGKTVLIQELIYNLAQQhggTSVFTGVGERTREGTDlYLEMKESGVLD-KTCLVYGQMNEP 234
Cdd:PRK05922 149 DAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKST---INVIALIGERGREVRE-YIEQHKEGLAAqRTIIIASPAHET 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 235 PGARLRVGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITSTKTGSITS 314
Cdd:PRK05922 225 APTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 315 VQAV-YVP--ADDLTDPAPATtfthLDSTTVLSRNIASLGlYPAIDPLASTSDALDpDIVGERHYSVASKVQELLQQYAD 391
Cdd:PRK05922 305 LYAIlHYPnhPDIFTDYLKSL----LDGHFFLTPQGKALA-SPPIDILTSLSRSAR-QLALPHHYAAAEELRSLLKAYHE 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503473399 392 LQDIIAILGMDELSDEQrttVNRARK----IQQFLSQSFhvaekftgnpGVYVRVEDTVDSFAAIVN 454
Cdd:PRK05922 379 ALDIIQLGAYVPGQDAH---LDRAVKllpsIKQFLSQPL----------SSYCALHNTLKQLEALLK 432
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
96-363 |
1.80e-31 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 122.33 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 96 PMKMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAA--PTFDELTTNMeiFETGIKAVDLLEPYIRGGKTGLFGGA 173
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPinPVARIYPEEM--IQTGISAIDVMNTLVRGQKLPIFSGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 174 GvgktvliqeLIYN--LAQ----------QHGGTSVFTGVGERTREGTDLYLEMKESGVLDKTCLVYGQMNEPPGARLRV 241
Cdd:cd01135 79 G---------LPHNelAAQiarqagvvgsEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIIT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 242 GLAGLTTAEYFR-DRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQER--ITSTKTGSITSVQAV 318
Cdd:cd01135 150 PRMALTTAEYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPIL 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 503473399 319 YVPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTS 363
Cdd:cd01135 230 TMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLS 274
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
121-363 |
1.65e-28 |
|
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: 114.21 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 121 PAGQIEERYPIHHAAPTFDELTTNmEIFETGIKAVDLLEPYIRGGKTGLFGGAGVGKTVLIQELIYNLAQQhggTSVFTG 200
Cdd:cd01134 34 PRGVNVQRWPVRQPRPVKEKLPPN-VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSLSKWSNSD---VVIYVG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 201 VGERTREGTD-------LYLEMKESGVLDKTCLVYGQMNEPPGARLRVGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAG 273
Cdd:cd01134 110 CGERGNEMAEvleefpeLKDPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 274 SEVSALLGRMPSAVGYQPTLATEMGDLQERITSTKT-------GSITSVQAVYVPADDLTDPAPATTfthLDSTTV---L 343
Cdd:cd01134 190 REISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRClgspgreGSVTIVGAVSPPGGDFSEPVTQAT---LRIVQVfwgL 266
|
250 260
....*....|....*....|
gi 503473399 344 SRNIASLGLYPAIDPLASTS 363
Cdd:cd01134 267 DKKLAQRRHFPSINWLISYS 286
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
146-427 |
5.74e-25 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 107.95 E-value: 5.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 146 EIFETGIKAVDLLEPYIRGGKTGLFGGAGVGKTVLIQEL---------IYnlaqqhggtsvfTGVGERTREGTDLYLEMK 216
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQLakwadadivIY------------VGCGERGNEMTEVLEEFP 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 217 E-----SG--VLDKTCLVYGQMNEPPGARLRVGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGY 289
Cdd:PRK04192 277 ElidpkTGrpLMERTVLIANTSNMPVAAREASIYTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGY 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 290 QPTLATEMGDLQER----IT-STKTGSITSVQAVYVPADDLTDPAPATTfthLDSTTV---LSRNIASLGLYPAIDPLAS 361
Cdd:PRK04192 357 PAYLASRLAEFYERagrvKTlGGEEGSVTIIGAVSPPGGDFSEPVTQNT---LRIVKVfwaLDAELADRRHFPAINWLTS 433
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503473399 362 TS---DALDP---DIVGERHYSVASKVQELLQQYADLQDIIAILGMDELSDEQRTTVNRARKIQQ-FLSQS-FH 427
Cdd:PRK04192 434 YSlylDQVAPwweENVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIREdFLQQNaFD 507
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
184-424 |
5.84e-25 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 108.96 E-value: 5.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 184 LIYNLAQQH-------GGTSVFTGVGERTREGTDLYLEMKE-------SGVLDKTCLVYGQMNEPPGARLRVGLAGLTTA 249
Cdd:PRK14698 666 LLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIA 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 250 EYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERI-------TSTKTGSITSVQAVYVPA 322
Cdd:PRK14698 746 EYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPG 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 323 DDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTS---DA--------LDPDIVGERhysvaSKVQELLQQYAD 391
Cdd:PRK14698 826 GDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSlyvDAvkdwwhknVDPEWKAMR-----DKAMELLQKEAE 900
|
250 260 270
....*....|....*....|....*....|....
gi 503473399 392 LQDIIAILGMDELSDEQRTTVNRARKIQQ-FLSQ 424
Cdd:PRK14698 901 LQEIVRIVGPDALPERERAILLVARMLREdYLQQ 934
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
89-427 |
5.13e-23 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 101.34 E-value: 5.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 89 RVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKPAgQIEERY------PIHHAAPTFDElttnmEIFETGIKAVDLLEPYI 162
Cdd:TIGR01040 66 TCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPP-VLAEDYldingqPINPYARIYPE-----EMIQTGISAIDVMNSIA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 163 RGGKTGLFGGAGVGKtvliQELIYNLAQQHGGTS----------------VFTGVGERTREGTDLYLEMKESGVLDKTCL 226
Cdd:TIGR01040 140 RGQKIPIFSAAGLPH----NEIAAQICRQAGLVKlptkdvhdghednfaiVFAAMGVNMETARFFKQDFEENGSMERVCL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 227 VYGQMNEPPGARLRVGLAGLTTAEYFR-DRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERI- 304
Cdd:TIGR01040 216 FLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAg 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 305 -TSTKTGSITSVQAVYVPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTS----DALDPDIVGERHYSVA 379
Cdd:TIGR01040 296 rVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSrlmkSAIGEGMTRKDHSDVS 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 503473399 380 SkvqELLQQYA---DLQDIIAILGMDELSDEQRTTVNRARKIQQ-FLSQSFH 427
Cdd:TIGR01040 376 N---QLYACYAigkDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQGPY 424
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
97-363 |
4.62e-22 |
|
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: 95.70 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 97 MKMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAAPTFDELTTNMEIFETGIKAVDLLEPYIRGGKTGLFGGAGVG 176
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 177 KTVLIQELIYNlaqQHGG--TSVFTGVGERTREGTDLYLEMKESGVLDKTCLVYGQMNEPPGARLRVGLAGLTTAEYFRD 254
Cdd:cd01132 82 KTAIAIDTIIN---QKGKkvYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 255 RGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYqPtlatemGD-------LQERITSTK----TGSITSVQAVYVPAD 323
Cdd:cd01132 159 NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY-P------GDvfylhsrLLERAAKLSdelgGGSLTALPIIETQAG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 503473399 324 DLTDPAPattfTHLDSTT----VLSRNIASLGLYPAIDPLASTS 363
Cdd:cd01132 232 DVSAYIP----TNVISITdgqiFLESELFNKGIRPAINVGLSVS 271
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
21-96 |
3.62e-17 |
|
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: 76.02 E-value: 3.62e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503473399 21 EGRIVRIIGPVVDVK-FDDVVPTIYNALTIDADTPIghiSTVLEVEMQLPGSVVRTVAMTSTDGLRRGLRVQDTGEP 96
Cdd:cd18115 2 TGKIVQVIGPVVDVEfPEGELPPIYNALEVKGDDGK---KLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAP 75
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
82-476 |
6.36e-17 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 83.09 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 82 DGLR--RGLRVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKPAGQIEERYPIHHAAPTFDELTTNMEIFETGIKAVDLLE 159
Cdd:CHL00059 57 DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 160 PYIRGGKTGLFGGAGVGKTVLIQELIYNLAQQhGGTSVFTGVGERTREGTDLYLEMKESGVLDKTCLVYGQMNEPpgARL 239
Cdd:CHL00059 137 PIGRGQRELIIGDRQTGKTAVATDTILNQKGQ-NVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSP--ATL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 240 RVgLA---GLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYqPtlatemGD-------LQERITSTKT 309
Cdd:CHL00059 214 QY-LApytGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAY-P------GDvfylhsrLLERAAKLSS 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 310 ----GSITSVQAVYVPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTS---DALDPDIVGErhysVASKV 382
Cdd:CHL00059 286 qlgeGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSrvgSAAQIKAMKQ----VAGKL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 383 QELLQQYADLQDIIAIlgmdeLSDEQRTTVN---RARKIQQFLSQSfhvaekfTGNPgvyVRVEDTVDSFAAIVNGDVDD 459
Cdd:CHL00059 362 KLELAQFAELEAFAQF-----ASDLDKATQNqlaRGQRLRELLKQS-------QSAP---LTVEEQVATIYTGTNGYLDS 426
|
410
....*....|....*...
gi 503473399 460 LP-EQAFRFagtLDDVRE 476
Cdd:CHL00059 427 LEiGQVRKF---LVELRT 441
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
81-333 |
6.87e-17 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 82.77 E-value: 6.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 81 TDGLRRGLRVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKPagQIEERyPIHHAAPTFDEL--TTNMEIFETGIKAVDLL 158
Cdd:PRK02118 58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGP--ELEGE-PIEIGGPSVNPVkrIVPREMIRTGIPMIDVF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 159 EPYIRGGKTGLFGGAGVGktvlIQELIYNLA-QQHGGTSVFTGVGERtregTDLYL----EMKESGVLDKTCLVYGQMNE 233
Cdd:PRK02118 135 NTLVESQKIPIFSVSGEP----YNALLARIAlQAEADIIILGGMGLT----FDDYLffkdTFENAGALDRTVMFIHTASD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 234 PPGARLRVGLAGLTTAEYFR-DRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEMGDLQERITSTK-TGS 311
Cdd:PRK02118 207 PPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEdGGS 286
|
250 260
....*....|....*....|..
gi 503473399 312 ITSVQAVYVPADDLTDPAPATT 333
Cdd:PRK02118 287 ITIIAVTTMPGDDVTHPVPDNT 308
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
76-467 |
4.79e-15 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 77.39 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 76 VAMTSTDGLRRGLRVQDTGEPMKMPVGQATLGRIWNVLGEPVdgkPAGQIEERYPIHHAAPTFDELTT-----------N 144
Cdd:PTZ00185 94 ILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEV---PVGLLTRSRALLESEQTLGKVDAgapnivsrspvN 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 145 MEIFeTGIKAVDLLEPYIRGGKTGLFGGAGVGKTVLIQELIYN-------LAQQHGGTSVFTGVGERTREGTDLYLEMKE 217
Cdd:PTZ00185 171 YNLL-TGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSNVARIHRLLRS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 218 SGVLDKTCLVYGQMNEPPGARLRVGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMPSAVGYQPTLATEM 297
Cdd:PTZ00185 250 YGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLH 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 298 GDLQERITSTKT----GSITSVQAVYVPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAIDPLASTSdALDPDIVGE 373
Cdd:PTZ00185 330 SRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVS-RVGSSAQNV 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 374 RHYSVASKVQELLQQYADlqdiiaiLGMDELSDEQRTTVNRARKIQqflsqsfHVAEKFTGNPGVYVrveDTVDSFAAIV 453
Cdd:PTZ00185 409 AMKAVAGKLKGILAEYRK-------LAADSVGGSQVQTVPMIRGAR-------FVALFNQKNPSFFM---NALVSLYACL 471
|
410
....*....|....
gi 503473399 454 NGDVDDLPEQAFRF 467
Cdd:PTZ00185 472 NGYLDDVKVNYAKL 485
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
375-434 |
9.64e-15 |
|
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: 69.01 E-value: 9.64e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 375 HYSVASKVQELLQQYADLQDIIAILGMDELSDEQRTTVNRARKIQQFLSQSFHVAEKFTG 434
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIED 60
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
76-284 |
2.32e-14 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 75.10 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 76 VAMTSTDGLRRGLRVQDTGEPMKMPVGQATLGRIWNVLGEPVDGKpaGQIE--ERYPIHHAAPTFdelttnM------EI 147
Cdd:PRK09281 74 VILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGK--GPIEatETRPVERKAPGV------IdrksvhEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 148 FETGIKAVDLLEPYIRGGKTGLFGGAGVGKTVLIQELIYNlaqQHG-------------GTSVFTGVGErtregtdlyLE 214
Cdd:PRK09281 146 LQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN---QKGkdviciyvaigqkASTVAQVVRK---------LE 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 215 mkESGVLDKTCLVYGQMNEPPGARLRVGLAGLTTAEYFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRMP 284
Cdd:PRK09281 214 --EHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
24-94 |
5.59e-07 |
|
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: 46.77 E-value: 5.59e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503473399 24 IVRIIGP-VVDVKFDDVVPTIYNALTIDADTPIghiSTVLEVEMQLPGSVVRTVAMTSTDGLRRGLRVQDTG 94
Cdd:pfam02874 1 IVQVIGPvVDVEFGIGRLPGLLNALEVELVEFG---SLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| 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 ... |
381-433 |
5.53e-05 |
|
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: 41.99 E-value: 5.53e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 503473399 381 KVQELLQQYADLQDIIAILGMDELSDEQRTTVNRARKIQQ-FLSQS-FHVAEKFT 433
Cdd:cd18111 7 EAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREdFLQQNaFDEVDTYC 61
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
163-283 |
6.13e-05 |
|
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: 43.13 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 163 RGGKTGLFGGAGVGKTVLIQELIYNLAQQHGGtsVFTGVGERTREGTDLYLEMKESGVldktclvyGQMNEPPGARLRVG 242
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG--VIYIDGEDILEEVLDQLLLIIVGG--------KKASGSGELRLRLA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 503473399 243 LAglttaeyFRDRGQDVLLFIDNIFRFSQAGSEVSALLGRM 283
Cdd:smart00382 71 LA-------LARKLKPDVLILDEITSLLDAEQEALLLLLEE 104
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
107-357 |
3.45e-04 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 43.04 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 107 GRIWNVLGEPVDGKPAGQ-IEERYPIHHAAptFdELTTNM-------EIFETGIKAVDLLEPYIRGGKTGLFGGAGVGKT 178
Cdd:PRK07165 81 GKIIDIDGNIIYPEAQNPlSKKFLPNTSSI--F-NLAHGLmtvktlnEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 179 VLIQELIYNlaQQHGGTS-VFTGVGERTREGTDLYLEMKESGVLDKTCLV-------YGQMNEPpgarlRVGLAGLTTAE 250
Cdd:PRK07165 158 HIALNTIIN--QKNTNVKcIYVAIGQKRENLSRIYETLKEHDALKNTIIIdapstspYEQYLAP-----YVAMAHAENIS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503473399 251 YFrdrgQDVLLFID------NIFRfsqagsEVSALLGR------MPSAVGYQPTlatemgDLQERITSTKTG-SITSVQA 317
Cdd:PRK07165 231 YN----DDVLIVFDdltkhaNIYR------EIALLTNKpvgkeaFPGDMFFAHS------KLLERAGKFKNRkTITALPI 294
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 503473399 318 VYVPADDLTDPAPATTFTHLDSTTVLSRNIASLGLYPAID 357
Cdd:PRK07165 295 LQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAID 334
|
|
| |
