|
Name |
Accession |
Description |
Interval |
E-value |
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
3-490 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 1102.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 3 TNPFIFGVSALVEKKAGRIAQIIGPVLDVSFPPGSMPRIYNSLIVKDNDTTGQPISVTCEVQQLLGNNKVRAVAMSATDG 82
Cdd:CHL00060 1 INPTGPGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 83 LMRGMKVIDTGGPLSVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAPAFTQLDIKFSILETGIKVVDLLAPYRR 162
Cdd:CHL00060 81 LMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 163 GGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYKEMKESGVINEQNISESKVALVYGQMNEPPG 242
Cdd:CHL00060 161 GGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 243 ARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSI 322
Cdd:CHL00060 241 ARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 323 QAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPSIVGKEHYETAQGVKQTLQRYKELQDI 402
Cdd:CHL00060 321 QAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 403 IAILGLDELSEDDRLIVARARKIERFLSQPFFVAEVFTGSPGKYVSLIETIRGFQMILSGELDGLPEQSFYLVGNIDEAT 482
Cdd:CHL00060 401 IAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEAT 480
|
....*...
gi 2216741363 483 AKAMNLKE 490
Cdd:CHL00060 481 AKAANLEV 488
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
19-490 |
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: 944.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 19 GRIAQIIGPVLDVSFPPGSMPRIYNSLIVKDNDttgqPISVTCEVQQLLGNNKVRAVAMSATDGLMRGMKVIDTGGPLSV 98
Cdd:COG0055 6 GKIVQVIGPVVDVEFPEGELPAIYNALEVENEG----GGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 99 PVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAPAFTQLDIKFSILETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 178
Cdd:COG0055 82 PVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 179 LIMELINNIAKAHGGVSVFGGVGERTREGNDLYKEMKESGVINeqnisesKVALVYGQMNEPPGARMRVGLTALTMAEYF 258
Cdd:COG0055 162 LIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTMAEYF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 259 RDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPA 338
Cdd:COG0055 235 RDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 339 TTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPSIVGKEHYETAQGVKQTLQRYKELQDIIAILGLDELSEDDRLI 418
Cdd:COG0055 315 TTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLT 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2216741363 419 VARARKIERFLSQPFFVAEVFTGSPGKYVSLIETIRGFQMILSGELDGLPEQSFYLVGNIDEATAKAMNLKE 490
Cdd:COG0055 395 VARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKA 466
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
17-488 |
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: 835.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 17 KAGRIAQIIGPVLDVSFPPGSMPRIYNSLIVKdndtTGQPISVTCEVQQLLGNNKVRAVAMSATDGLMRGMKVIDTGGPL 96
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQ----NRAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 97 SVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAPAFTQLDIKFSILETGIKVVDLLAPYRRGGKIGLFGGAGVGK 176
Cdd:TIGR01039 77 SVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 177 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYKEMKESGVINeqnisesKVALVYGQMNEPPGARMRVGLTALTMAE 256
Cdd:TIGR01039 157 TVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 257 YFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 336
Cdd:TIGR01039 230 YFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 337 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPSIVGKEHYETAQGVKQTLQRYKELQDIIAILGLDELSEDDR 416
Cdd:TIGR01039 310 PATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDK 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2216741363 417 LIVARARKIERFLSQPFFVAEVFTGSPGKYVSLIETIRGFQMILSGELDGLPEQSFYLVGNIDEATAKAMNL 488
Cdd:TIGR01039 390 LTVERARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
19-481 |
0e+00 |
|
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 beta subunit of this apparent second ATP synthase.
Pssm-ID: 132348 [Multi-domain] Cd Length: 449 Bit Score: 582.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 19 GRIAQIIGPVLDVSFPpGSMPRIYNSLIVKDNDttgqpiSVTCEVQQLLGNNKVRAVAMSATDGLMRGMKVIDTGGPLSV 98
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFD-GELPAIHSVLRAGREG------EVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 99 PVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAPAFTQLDIKFSILETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 178
Cdd:TIGR03305 74 PVGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 179 LIMELINNIAKAHGGVSVFGGVGERTREGNDLYKEMKESGVINEqniseskVALVYGQMNEPPGARMRVGLTALTMAEYF 258
Cdd:TIGR03305 154 LLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDN-------TVMVFGQMNEPPGARFRVGHTALTMAEYF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 259 RDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPA 338
Cdd:TIGR03305 227 RDDEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 339 TTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPSIVGKEHYETAQGVKQTLQRYKELQDIIAILGLDELSEDDRLI 418
Cdd:TIGR03305 307 HTFSHLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRV 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2216741363 419 VARARKIERFLSQPFFVAEVFTGSPGKYVSLIETIRGFQMILSGELDGLPEQSFYLVGNIDEA 481
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 ... |
97-375 |
0e+00 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 578.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 97 SVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAPAFTQLDIKFSILETGIKVVDLLAPYRRGGKIGLFGGAGVGK 176
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 177 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYKEMKESGVINEqnISESKVALVYGQMNEPPGARMRVGLTALTMAE 256
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINL--DGLSKVALVYGQMNEPPGARARVALTGLTMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 257 YFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 336
Cdd:cd01133 159 YFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPA 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 2216741363 337 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP 375
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 ... |
97-372 |
1.91e-131 |
|
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: 381.80 E-value: 1.91e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 97 SVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAPAFTQLDIKFSILETGIKVVDLLAPYRRGGKIGLFGGAGVGK 176
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 177 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYKEMKESGVineqnisESKVALVYGQMNEPPGARMRVGLTALTMAE 256
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGA-------MERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 257 YFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK--EGSITSIQAVYVPADDLTD 334
Cdd:cd19476 154 YFRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTD 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 2216741363 335 PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTM 372
Cdd:cd19476 233 PIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
150-370 |
2.66e-87 |
|
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: 266.53 E-value: 2.66e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 150 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKahgGVSVFGGVGERTREGNDLYKEMKESGVIneqniseSK 229
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-------KR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 230 VALVYGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQE 309
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2216741363 310 RITSTKE--GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 370
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 ... |
377-484 |
5.03e-76 |
|
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: 233.91 E-value: 5.03e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 377 IVGKEHYETAQGVKQTLQRYKELQDIIAILGLDELSEDDRLIVARARKIERFLSQPFFVAEVFTGSPGKYVSLIETIRGF 456
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 2216741363 457 QMILSGELDGLPEQSFYLVGNIDEATAK 484
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
19-432 |
2.29e-65 |
|
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: 217.21 E-value: 2.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 19 GRIAQIIGPVLDVSFPP---GSMPRIYNSlivkdndtTGQPIsvTCEVqqlLG--NNKVRAVAMSATDGLMRGMKVIDTG 93
Cdd:COG1157 21 GRVTRVVGLLIEAVGPDasiGELCEIETA--------DGRPV--LAEV---VGfrGDRVLLMPLGDLEGISPGARVVPTG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 94 GPLSVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAP-AFTQLDIKfSILETGIKVVDLLAPYRRGGKIGLFGGA 172
Cdd:COG1157 88 RPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPnPLERARIT-EPLDTGVRAIDGLLTVGRGQRIGIFAGS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 173 GVGKTVLIMELINN----------IAkahggvsvfggvgERTREGND-LYKEMKESGVineqniseSKVALVYGQMNEPP 241
Cdd:COG1157 167 GVGKSTLLGMIARNteadvnvialIG-------------ERGREVREfIEDDLGEEGL--------ARSVVVVATSDEPP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 242 GARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITS 321
Cdd:COG1157 226 LMRLRAAYTATAIAEYFRDQGK-NVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 322 IQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMlqPSIVGKEHYETAQGVKQTLQRYKELQ 400
Cdd:COG1157 305 FYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISrVM--PDIVSPEHRALARRLRRLLARYEENE 382
|
410 420 430
....*....|....*....|....*....|....*.
gi 2216741363 401 DIIAI----LGLDElsEDDRlIVARARKIERFLSQP 432
Cdd:COG1157 383 DLIRIgayqPGSDP--ELDE-AIALIPAIEAFLRQG 415
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
97-370 |
8.80e-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: 181.60 E-value: 8.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 97 SVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAP-AFTQLDIKfSILETGIKVVDLLAPYRRGGKIGLFGGAGVG 175
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPnPLKRAPIE-QPLPTGVRAIDGLLTCGEGQRIGIFAGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 176 KTVLIMELINNiAKAhgGVSVFGGVGERTREGND-LYKEMKESGVineqniseSKVALVYGQMNEPPGARMRVGLTALTM 254
Cdd:cd01136 80 KSTLLGMIARN-TDA--DVNVIALIGERGREVREfIEKDLGEEGL--------KRSVLVVATSDESPLLRVRAAYTATAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 255 AEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTD 334
Cdd:cd01136 149 AEYFRDQGK-KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFND 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 2216741363 335 PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 370
Cdd:cd01136 228 PIADEVRSILDGHIVLSRRLAERGHYPAIDVLASIS 263
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
19-431 |
7.45e-50 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 176.48 E-value: 7.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 19 GRIAQIIGPVLDVSFPpgsMPRIYNSLIVKDNDttgQPISVTCEVQQLlgnnkVRAVAMSATDGLMRGM----KVIDTGG 94
Cdd:PRK06936 25 GRVTQVTGTILKAVVP---GVRIGELCYLRNPD---NSLSLQAEVIGF-----AQHQALLTPLGEMYGIssntEVSPTGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 95 PLSVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAPAFTQLDIKFSILETGIKVVDLLAPYRRGGKIGLFGGAGV 174
Cdd:PRK06936 94 MHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 175 GKTVLIMELINNiakAHGGVSVFGGVGERTREgndlYKEMKESGVINEqniSESKVALVYGQMNEPPGARMRVGLTALTM 254
Cdd:PRK06936 174 GKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIESDLGEE---GLRKAVLVVATSDRPSMERAKAGFVATSI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 255 AEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTD 334
Cdd:PRK06936 244 AEYFRDQGKR-VLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 335 PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpSIVGKEHYETAQGVKQTLQRYKELQDIIAI----LGLDE 410
Cdd:PRK06936 323 PVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDK 401
|
410 420
....*....|....*....|.
gi 2216741363 411 LSEDdrlIVARARKIERFLSQ 431
Cdd:PRK06936 402 EADQ---AIERIGAIRGFLRQ 419
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
65-433 |
1.90e-48 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 172.49 E-value: 1.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 65 QLLGNNKVRAV--AMSATDGLMRGMKVIDTGGPLSVPVGETTLGRIFNVLGEPVDNLG-PVDALTTS---PIHRSAPAFT 138
Cdd:PRK08149 47 QVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDaPPTVGPISeerVIDVAPPSYA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 139 QLDIKFSILETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFGGVGERTREGNDLYKEMKESG 218
Cdd:PRK08149 127 ERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFVESLRASS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 219 vineqniSESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQP 298
Cdd:PRK08149 204 -------RREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGK-RVVLFIDSMTRYARALRDVALAAGELPARRGYPA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 299 TLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpSIV 378
Cdd:PRK08149 276 SVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVT 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2216741363 379 GKEHYETAQGVKQTLQRYKELQDIIAiLG---LDELSEDDRLIVARArKIERFLSQPF 433
Cdd:PRK08149 355 DPKHRQLAAAFRKLLTRLEELQLFID-LGeyrRGENADNDRAMDKRP-ALEAFLKQDV 410
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
78-431 |
6.31e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 171.15 E-value: 6.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 78 SATDGLMRGMKVIDTGGPLSVPVGETTLGRIFNVLGEPVDNlGPVDALTTSPIHRSAPAFTQLDIKFSILETGIKVVDLL 157
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 158 APYRRGGKIGLFGGAGVGKTVLIMELInniAKAHGGVSVFGGVGERTREGNDLYkemkesgvinEQNISE---SKVALVY 234
Cdd:PRK06820 158 LSCGEGQRIGIFAAAGVGKSTLLGMLC---ADSAADVMVLALIGERGREVREFL----------EQVLTPearARTVVVV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 235 GQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITST 314
Cdd:PRK06820 225 ATSDRPALERLKGLSTATTIAEYFRDRGK-KVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNS 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 315 KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPSIVGKEHYETAQGVKQTLQ 394
Cdd:PRK06820 304 DRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLA 382
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2216741363 395 RYKELQDIIAI----LGLDELSEDdrlIVARARKIERFLSQ 431
Cdd:PRK06820 383 CYQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
19-405 |
6.05e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 168.76 E-value: 6.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 19 GRIAQIIGPVLDVSFPPGSMPRiyNSLIVkdNDTTGQPISVTCEVQQLLGNnKVRAVAMSATDGLMRGMKVIDTGGPLSV 98
Cdd:PRK05688 29 GRLLRMVGLTLEAEGLRAAVGS--RCLVI--NDDSYHPVQVEAEVMGFSGD-KVFLMPVGSVAGIAPGARVVPLADTGRL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 99 PVGETTLGRIFNVLGEPVDNLGPV--------DALTTSPIHRsAPAFTQLDIkfsiletGIKVVDLLAPYRRGGKIGLFG 170
Cdd:PRK05688 104 PMGMSMLGRVLDGAGRALDGKGPMkaedwvpmDGPTINPLNR-HPISEPLDV-------GIRSINGLLTVGRGQRLGLFA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 171 GAGVGKTVLiMELINNIAKAHGGVSVFGGvgERTREgndlYKEMKESgVINEQNISESKValVYGQMNEPPGARMRVGLT 250
Cdd:PRK05688 176 GTGVGKSVL-LGMMTRFTEADIIVVGLIG--ERGRE----VKEFIEH-ILGEEGLKRSVV--VASPADDAPLMRLRAAMY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 251 ALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEG--SITSIQAVYVP 328
Cdd:PRK05688 246 CTRIAEYFRDKGK-NVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITAFYTVLSE 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2216741363 329 ADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPSIVGKEHYETAQGVKQTLQRYKELQDIIAI 405
Cdd:PRK05688 325 GDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLISV 400
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
59-431 |
2.70e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 158.60 E-value: 2.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 59 VTCEVQQLLGNNKVrAVAMSATDGLMRGMKVIDTGGPLSVPVGETTLGRIFN----VLGEPVDNLG----PVDAlttSPI 130
Cdd:PRK06793 53 VLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSangeVLNEEAENIPlqkiKLDA---PPI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 131 HrsapAFTQLDIKfSILETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGvgERTREGND- 209
Cdd:PRK06793 129 H----AFEREEIT-DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKADINVISLVG--ERGREVKDf 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 210 LYKEMKESGVineqniseSKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGR 289
Cdd:PRK06793 201 IRKELGEEGM--------RKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGN-NVLLMMDSVTRFADARRSVDIAVKE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 290 MPSAvGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDST 369
Cdd:PRK06793 272 LPIG-GKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSV 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2216741363 370 STMLQpSIVGKEHYETAQGVKQTLQRYKElQDIIAILGLDELSEDDRLIVARARKIE---RFLSQ 431
Cdd:PRK06793 351 SRIME-EIVSPNHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAYIFECKNKVEginTFLKQ 413
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
81-432 |
3.09e-43 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 158.39 E-value: 3.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 81 DGLMRGMKVIDTGGPLSVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAPAFTQLDIKFSILETGIKVVDLLAPY 160
Cdd:PRK09099 81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 161 RRGGKIGLFGGAGVGKTVLIMEL-------INNIAkahggvsvfgGVGERTREgndlYKEMKESgVINEQNISESKValV 233
Cdd:PRK09099 161 GEGQRMGIFAPAGVGKSTLMGMFargtqcdVNVIA----------LIGERGRE----VREFIEL-ILGEDGMARSVV--V 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 234 YGQMNEPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS 313
Cdd:PRK09099 224 CATSDRSSIERAKAAYVATAIAEYFRDRGLR-VLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 314 TKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPSIVGKEHYETAQGVKQTL 393
Cdd:PRK09099 303 GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLL 381
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2216741363 394 QRYKELQDIIAI----LGLDELSEDdrlIVARARKIERFLSQP 432
Cdd:PRK09099 382 AKHREVETLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
82-405 |
5.93e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 157.94 E-value: 5.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 82 GLMRGMKVIDTGGPLSVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHrsAPAFTQLDIKfSI---LETGIKVVDLLA 158
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRR-PItepLDVGVRAINAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 159 PYRRGGKIGLFGGAGVGKTVLI-MELINNIAKAhggvSVFGGVGERTREgndlYKEMKESgVINEQNISESKValVYGQM 237
Cdd:PRK08972 158 TVGKGQRMGLFAGSGVGKSVLLgMMTRGTTADV----IVVGLVGERGRE----VKEFIEE-ILGEEGRARSVV--VAAPA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 238 NEPPGARMRVGLTALTMAEYFRDVNkQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERIT--STK 315
Cdd:PRK08972 227 DTSPLMRLKGCETATTIAEYFRDQG-LNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 316 EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPSIVGKEHYETAQGVKQTLQR 395
Cdd:PRK08972 306 QGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSL 384
|
330
....*....|
gi 2216741363 396 YKELQDIIAI 405
Cdd:PRK08972 385 YQQNRDLISI 394
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
96-431 |
4.78e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 155.23 E-value: 4.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 96 LSVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAPAFTQLDIKFSILETGIKVVDLLAPYRRGGKIGLFGGAGVG 175
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 176 KTVLiMELINNIAKAhgGVSVFGGVGERTRE---------GNDLykemkESGVINEQNISESKVALVYGqmneppgarmr 246
Cdd:PRK08472 170 KSTL-MGMIVKGCLA--PIKVVALIGERGREipefieknlGGDL-----ENTVIVVATSDDSPLMRKYG----------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 247 vGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK-EGSITSIQAV 325
Cdd:PRK08472 231 -AFCAMSVAEYFKNQGL-DVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 326 YVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpSIVGKEHYETAQGVKQTLQRYKELQDIIAI 405
Cdd:PRK08472 309 LVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIRI 387
|
330 340 350
....*....|....*....|....*....|.
gi 2216741363 406 ----LGLD-ELSEddrlIVARARKIERFLSQ 431
Cdd:PRK08472 388 gayqKGNDkELDE----AISKKEFMEQFLKQ 414
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
92-405 |
1.66e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 153.72 E-value: 1.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 92 TGGPLSVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAP-AFTQLDIKfSILETGIKVVDLLAPYRRGGKIGLFG 170
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPnPLKRPPIR-EPMEVGVRAIDSLLTVGKGQRVGIFA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 171 GAGVGKTVLIMEL-------INNIAkahggvsvfgGVGERTREGND-LYKEMKESGVineqniseSKVALVYGQMNEPPG 242
Cdd:PRK07721 166 GSGVGKSTLMGMIarntsadLNVIA----------LIGERGREVREfIERDLGPEGL--------KRSIVVVATSDQPAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 243 ARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSI 322
Cdd:PRK07721 228 MRIKGAYTATAIAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAF 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 323 QAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPSIVGKEHYETAQGVKQTLQRYKELQDI 402
Cdd:PRK07721 307 YTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDL 385
|
...
gi 2216741363 403 IAI 405
Cdd:PRK07721 386 INI 388
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
94-407 |
3.07e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 153.23 E-value: 3.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 94 GPLSVPVGETTLGRIFNVLGEPVDNLGPVDALTTS-PIHRSAP-AFTQLDIKfSILETGIKVVDLLAPYRRGGKIGLFGG 171
Cdd:PRK06002 95 GPLRIRPDPSWKGRVINALGEPIDGLGPLAPGTRPmSIDATAPpAMTRARVE-TGLRTGVRVIDIFTPLCAGQRIGIFAG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 172 AGVGKTVLIMELinniAKA-HGGVSVFGGVGERTREgndlYKEMKEsGVINEqniSESKVALVYGQMNEPPGARMRVGLT 250
Cdd:PRK06002 174 SGVGKSTLLAML----ARAdAFDTVVIALVGERGRE----VREFLE-DTLAD---NLKKAVAVVATSDESPMMRRLAPLT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 251 ALTMAEYFRDVNkQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE--GSITSIQAVYVP 328
Cdd:PRK06002 242 ATAIAEYFRDRG-ENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEggGSITGIFSVLVD 320
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2216741363 329 ADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPSIVGkEHYETAQGVKQTLQRYKELQDIIAILG 407
Cdd:PRK06002 321 GDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTP-EQRKLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
19-466 |
3.37e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 150.13 E-value: 3.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 19 GRIAQIIGPVLDVSFPPGSMpRIYNSLIVKDNDTTgqpiSVTCEVqqlLGNNKVRAVAM--SATDGLMRGMKVIDTGGPL 96
Cdd:PRK08927 19 GRVVAVRGLLVEVAGPIHAL-SVGARIVVETRGGR----PVPCEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 97 SVPVGETTLGRIFNVLGEPVDNLGPVDALTTS-PIHRSAPAFTQLDIKFSILETGIKVVDLLAPYRRGGKIGLFGGAGVG 175
Cdd:PRK08927 91 AVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPyPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 176 KTVLIMELINNIAKAhggVSVFGGVGERTREGNDLYKEmkesgVINEQNISESKValVYGQMNEPPGARMRVGLTALTMA 255
Cdd:PRK08927 171 KSVLLSMLARNADAD---VSVIGLIGERGREVQEFLQD-----DLGPEGLARSVV--VVATSDEPALMRRQAAYLTLAIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 256 EYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI--TSTKEGSITSIQAVYVPADDLT 333
Cdd:PRK08927 241 EYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 334 DPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMlqPSIVGKEHYETAQGVKQTLQRYKELQDIIAI----LGL 408
Cdd:PRK08927 320 EPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSrTM--PGCNDPEENPLVRRARQLMATYADMEELIRLgayrAGS 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2216741363 409 DelSEDDRLIvARARKIERFLSQpffvaevftgSPGKYVSLIETIRGFQMILSGELDG 466
Cdd:PRK08927 398 D--PEVDEAI-RLNPALEAFLRQ----------GKDEATSLAEGYARLAQILGGPETE 442
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
78-405 |
2.98e-37 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 142.01 E-value: 2.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 78 SATDGLMRGMKVIDTGGPLSVPVGETTLGRIFNVLGEPVDNL----GPVDALTTSPihrsAPAFTQLDIKFSILeTGIKV 153
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRelpdVCWKDYDAMP----PPAMVRQPITQPLM-TGIRA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 154 VDLLAPYRRGGKIGLFGGAGVGKTVLIMELINniaKAHGGVSVFGGVGERTREgndlYKEMKESGVINEqniSESKVALV 233
Cdd:PRK07594 146 IDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFIDFTLSEE---TRKRCVIV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 234 YGQMNEPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS 313
Cdd:PRK07594 216 VATSDRPALERVRALFVATTIAEFFRDNGKR-VVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGM 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 314 TKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPSIVGKEHYETAQGVKQTL 393
Cdd:PRK07594 295 GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCL 373
|
330
....*....|..
gi 2216741363 394 QRYKELQDIIAI 405
Cdd:PRK07594 374 ALYQEVELLIRI 385
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
19-96 |
3.39e-36 |
|
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: 128.40 E-value: 3.39e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2216741363 19 GRIAQIIGPVLDVSFPPGSMPRIYNSLIVKDNDttgqPISVTCEVQQLLGNNKVRAVAMSATDGLMRGMKVIDTGGPL 96
Cdd:cd18115 3 GKIVQVIGPVVDVEFPEGELPPIYNALEVKGDD----GKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
82-431 |
2.03e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 136.94 E-value: 2.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 82 GLMRGMKVIDTGGPLSVPVGETTLGRIFNVLGEPVDNLGPVDAltTSPIHRSAPAFTQLDIKF--SILETGIKVVDLLAP 159
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGG--STPLQQQLPQIHPLQRRAvdTPLDVGVNAINGLLT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 160 YRRGGKIGLFGGAGVGKTVLiMELINNIAKAHGGVSVFGGvgERTREgndlYKEMKESGVineQNISESKVALVYGQMNE 239
Cdd:PRK07196 152 IGKGQRVGLMAGSGVGKSVL-LGMITRYTQADVVVVGLIG--ERGRE----VKEFIEHSL---QAAGMAKSVVVAAPADE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 240 PPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI-TSTKEGS 318
Cdd:PRK07196 222 SPLMRIKATELCHAIATYYRDKGH-DVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGT 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 319 ITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpSIVGKEHYETAQGVKQTLQRYKE 398
Cdd:PRK07196 301 MTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMA 379
|
330 340 350
....*....|....*....|....*....|....*..
gi 2216741363 399 LQDIIA----ILGLDELSEDdrlIVARARKIERFLSQ 431
Cdd:PRK07196 380 IKPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQ 413
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
98-434 |
2.35e-31 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 125.67 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 98 VPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIhrSAPAFTQLD---IKfSILETGIKVVDLLAPYRRGGKIGLFGGAGV 174
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGAL--ITPPFNPLQrtpIE-HVLDTGVRAINALLTVGRGQRMGLFAGSGV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 175 GKTVLiMELINNIAKAHGGVSVFGGvgERTREGNDLYKEmkesgVINEQNISESKValVYGQMNEPPGARMRVGLTALTM 254
Cdd:PRK07960 187 GKSVL-LGMMARYTQADVIVVGLIG--ERGREVKDFIEN-----ILGAEGRARSVV--IAAPADVSPLLRMQGAAYATRI 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 255 AEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS--TKEGSITSIQAVYVPADDL 332
Cdd:PRK07960 257 AEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQ 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 333 TDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpSIVGKEHYETAQGVKQTLQRYKELQDIIAI----LGL 408
Cdd:PRK07960 336 QDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALIDEQHYARVRQFKQLLSSFQRNRDLVSVgayaKGS 414
|
330 340
....*....|....*....|....*.
gi 2216741363 409 DELSedDRLIvARARKIERFLSQPFF 434
Cdd:PRK07960 415 DPML--DKAI-ALWPQLEAFLQQGIF 437
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
80-433 |
3.59e-29 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 119.55 E-value: 3.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 80 TDGLM-RGMKVIDTGGPLSVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSA--PAFTQLDIKFsiLETGIKVVDL 156
Cdd:PRK04196 59 TTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVAREYPEEF--IQTGISAIDG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 157 LAPYRRGGKIGLFGGAGvgktvlimeLINNIAKAHGGVSVFGGVGE------------RTREGNDLYKEMKESGVINeqn 224
Cdd:PRK04196 137 LNTLVRGQKLPIFSGSG---------LPHNELAAQIARQAKVLGEEenfavvfaamgiTFEEANFFMEDFEETGALE--- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 225 isesKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEM 304
Cdd:PRK04196 205 ----RSVVFLNLADDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 305 GSLQER--ITSTKEGSITSIQAVYVPADDLTDPAPattfahlDAT-------TVLSRGLAAKGIYPAVDPLDSTSTMLQP 375
Cdd:PRK04196 281 ATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegqIVLSRELHRKGIYPPIDVLPSLSRLMKD 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2216741363 376 SIvGKEHY-ETAQGVKQTL----QRYKELQDIIAILGLDELSEDDRLIVARARKIE-RFLSQPF 433
Cdd:PRK04196 354 GI-GEGKTrEDHKDVANQLyaayARGKDLRELAAIVGEEALSERDRKYLKFADAFErEFVNQGF 416
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
95-377 |
1.04e-26 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 109.23 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 95 PLSVPVGETTLGRIFNVLGEPVDNLGPVDA-----LTTSPIHRSAPAFTQldikfSILETGIKVVDLLAPYRRGGKIGLF 169
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPedyldINGPPINPVARIYPE-----EMIQTGISAIDVMNTLVRGQKLPIF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 170 GGAGVGKTvlimELINNIAKAHGGVSVFGGVG-------ERTREGNDLYKEMKESGVINeqnisesKVALVYGQMNEPPG 242
Cdd:cd01135 76 SGSGLPHN----ELAAQIARQAGVVGSEENFAivfaamgVTMEEARFFKDDFEETGALE-------RVVLFLNLANDPTI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 243 ARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER--ITSTKEGSIT 320
Cdd:cd01135 145 ERIITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSIT 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2216741363 321 SIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPSI 377
Cdd:cd01135 225 QIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGI 281
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
69-463 |
5.03e-26 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 109.99 E-value: 5.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 69 NNKVRAVAMSATDGLMRGMKVIDTGGPLSVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAPAFTQLDIKFSILE 148
Cdd:PRK05922 63 NRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 149 TGIKVVDLLAPYRRGGKIGLFGGAGVGKTvlimELINNIAK-AHGGVSVFGGVGERTREGNDlYKEMKESGvineqnISE 227
Cdd:PRK05922 143 TGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVRE-YIEQHKEG------LAA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 228 SKVALVYGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSL 307
Cdd:PRK05922 212 QRTIIIASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 308 QERITSTKEGSITSIQAV-YVP--ADDLTDPAPATTFAHLDATTVlSRGLAAkgiyPAVDPLDSTSTMLQpSIVGKEHYE 384
Cdd:PRK05922 291 TERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSRSAR-QLALPHHYA 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 385 TAQGVKQTLQRYKELQDIIAiLGLDELSEDDRLivARARK----IERFLSQPFfvaevftgspGKYVSLIETIRGFQMIL 460
Cdd:PRK05922 365 AAEELRSLLKAYHEALDIIQ-LGAYVPGQDAHL--DRAVKllpsIKQFLSQPL----------SSYCALHNTLKQLEALL 431
|
...
gi 2216741363 461 SGE 463
Cdd:PRK05922 432 KHE 434
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
67-434 |
1.31e-25 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 109.62 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 67 LGNNKVRAVAMSATDGLMRGMKVIDTGGPLSVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAPAFTQLDIKFSI 146
Cdd:PRK13343 66 LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 147 LETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGNDLY-----KEMKESGVIN 221
Cdd:PRK13343 146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN------------------QKDSDVIcvyvaIGQKASAVAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 222 ------EQNISESKVaLVYGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVG 295
Cdd:PRK13343 208 vietlrEHGALEYTT-VVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 296 YQPTLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTST 371
Cdd:PRK13343 286 YPGDIFYLHSRLLERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2216741363 372 M---LQPSIVGKEhyetAQGVKQTLQRYKELQdIIAILGLDeLSEDDRLIVARARKIERFLSQPFF 434
Cdd:PRK13343 366 VggkAQHPAIRKE----SGRLRLDYAQFLELE-AFTRFGGL-LDAGTQKQITRGRRLRELLKQPRF 425
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
92-431 |
3.11e-22 |
|
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: 99.03 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 92 TGGPLSVPVGETTLGRIFNVLGEPVDNLGPVDA-----LTTSPIHRSAPAFTQldikfSILETGIKVVDLLAPYRRGGKI 166
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAedyldINGQPINPYARIYPE-----EMIQTGISAIDVMNSIARGQKI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 167 GLFGGAGVGKTvlimELINNIAKAHGGVSVFGGVGERTREGN--DLYKEMkesGViN-----------EQNISESKVALV 233
Cdd:TIGR01040 145 PIFSAAGLPHN----EIAAQICRQAGLVKLPTKDVHDGHEDNfaIVFAAM---GV-NmetarffkqdfEENGSMERVCLF 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 234 YGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI-- 311
Cdd:TIGR01040 217 LNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgr 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 312 TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPSI----VGKEHYETAQ 387
Cdd:TIGR01040 297 VEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIgegmTRKDHSDVSN 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2216741363 388 GVKQTLQRYKELQDIIAILGLDELSEDDRLIVARARKIER-FLSQ 431
Cdd:TIGR01040 377 QLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
95-370 |
5.79e-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: 93.02 E-value: 5.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 95 PLSVPVGETTLGRIFNVLGEPVDNLgpvdALTTS------------PIHRSAPAFTQLDiKFSILETGIKVVDLLAPYRR 162
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVI----AETGSifiprgvnvqrwPVRQPRPVKEKLP-PNVPLLTGQRVLDTLFPVAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 163 GGKIGLFGGAGVGKTVlimeLINNIAK-AHGGVSVFGGVGERTREGNDLYKEMKE-SGVINEQNISEsKVALVYGQMNEP 240
Cdd:cd01134 76 GGTAAIPGPFGCGKTV----ISQSLSKwSNSDVVIYVGCGERGNEMAEVLEEFPElKDPITGESLME-RTVLIANTSNMP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 241 PGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI-------TS 313
Cdd:cd01134 151 VAAREASIYTGITIAEYFRDMGY-NVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSP 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2216741363 314 TKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 370
Cdd:cd01134 230 GREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYS 286
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
250-460 |
4.99e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 92.92 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 250 TALTMAEYFRDvnkQ--DVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER----IT-STKEGSITSI 322
Cdd:PRK04192 311 TGITIAEYYRD---MgyDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTII 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 323 QAVYVPADDLTDPapaTTFAHLDATTV---LSRGLAAKGIYPAVDPLDSTS---TMLQPSI---VGKEHYETAQGVKQTL 393
Cdd:PRK04192 388 GAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAINWLTSYSlylDQVAPWWeenVDPDWRELRDEAMDLL 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2216741363 394 QRYKELQDIIAILGLDELSEDDRLIVARARKI-ERFLSQPFFvAEVFTgspgkYVSLIETIRGFQMIL 460
Cdd:PRK04192 465 QREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQNAF-DPVDT-----YCPPEKQYEMLKLIL 526
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
202-456 |
7.19e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 90.08 E-value: 7.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 202 ERTREGNDLYKEMKESGVINEQNISESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNkQDVLLFIDNIFRFVQAGS 281
Cdd:PRK14698 692 ERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMG-YDVALMADSTSRWAEALR 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 282 EVSALLGRMPSAVGYQPTLSTEMGSLQERI-------TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGL 354
Cdd:PRK14698 771 EISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 355 AAKGIYPAVDPLDSTSTMLQP------SIVGKEHYETAQGVKQTLQRYKELQDIIAILGLDELSEDDRLIVARARKI-ER 427
Cdd:PRK14698 851 ARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAILLVARMLrED 930
|
250 260
....*....|....*....|....*....
gi 2216741363 428 FLSQPFFVAEVFTGSPGKYVSLIETIRGF 456
Cdd:PRK14698 931 YLQQDAFDEVDTYCPPEKQVTMMRVLLNF 959
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
382-451 |
4.74e-18 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 78.25 E-value: 4.74e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 382 HYETAQGVKQTLQRYKELQDIIAILGLDELSEDDRLIVARARKIERFLSQPFFVAEVFTGSPGKYVSLIE 451
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
21-93 |
1.06e-17 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 77.20 E-value: 1.06e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2216741363 21 IAQIIGPVLDVSFPPGSMPRIYNSLIVKDNDttgqPISVTCEVQQLLGNNKVRAVAMSATDGLMRGMKVIDTG 93
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVE----FGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-370 |
2.43e-16 |
|
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: 79.14 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 96 LSVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAPAFTQLDIKFSILETGIKVVDLLAPYRRGGKIGLFGGAGVG 175
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 176 KTVLIMELINNiakahggvsvfggvgertREGNDLY-----KEMKESGVINEQNISESKVALVY-----GQMNEPPGARM 245
Cdd:cd01132 82 KTAIAIDTIIN------------------QKGKKVYciyvaIGQKRSTVAQIVKTLEEHGAMEYtivvaATASDPAPLQY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 246 RVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE----GSITS 321
Cdd:cd01132 144 LAPYAGCAMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSLTA 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2216741363 322 IQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 370
Cdd:cd01132 223 LPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVS 271
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
72-291 |
6.92e-15 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 77.03 E-value: 6.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 72 VRAVAMSATDGLMRGMKVIDTGGPLSVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAPAFTQldiKFSI---LE 148
Cdd:PRK09281 71 VGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID---RKSVhepLQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 149 TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertregndlykeMKESGV------INE 222
Cdd:PRK09281 148 TGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN---------------------------QKGKDViciyvaIGQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 223 QNiseSKVALV------YGQM----------NEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSAL 286
Cdd:PRK09281 201 KA---STVAQVvrkleeHGAMeytivvaataSDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLL 276
|
....*
gi 2216741363 287 LGRMP 291
Cdd:PRK09281 277 LRRPP 281
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
80-340 |
3.31e-14 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 74.30 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 80 TDGLMRGMKVIDTGGPLSVPVGETTLGRIFNVLGEPVDNlGPvdALTTSPIHRSAPAF--TQLDIKFSILETGIKVVDLL 157
Cdd:PRK02118 58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GP--ELEGEPIEIGGPSVnpVKRIVPREMIRTGIPMIDVF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 158 APYRRGGKIGLFGGAGVGKTVLIMElINNIAKAHGGVSVFGGVGertregNDLY----KEMKESGVIneqniseSKVALV 233
Cdd:PRK02118 135 NTLVESQKIPIFSVSGEPYNALLAR-IALQAEADIIILGGMGLT------FDDYlffkDTFENAGAL-------DRTVMF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 234 YGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS 313
Cdd:PRK02118 201 IHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVD 280
|
250 260
....*....|....*....|....*...
gi 2216741363 314 TKE-GSITSIQAVYVPADDLTDPAPATT 340
Cdd:PRK02118 281 FEDgGSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
67-364 |
1.87e-10 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 63.06 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 67 LGNNKVRAVAMSatDGLM--RGMKVIDTGGPLSVPVGETTLGRIFNVLGEPVDNLGPVDALTTSPIHRSAPAFTQLDIKF 144
Cdd:CHL00059 45 LESNNVGVVLMG--DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVY 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 145 SILETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGND---LYKEM--KESGV 219
Cdd:CHL00059 123 EPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN------------------QKGQNvicVYVAIgqKASSV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 220 INEQNISESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRdVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAV 294
Cdd:CHL00059 185 AQVVTTLQERGAMEYtivvaETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGRE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 295 GY--------------QPTLSTEMGslqeritstkEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIY 360
Cdd:CHL00059 264 AYpgdvfylhsrllerAAKLSSQLG----------EGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIR 333
|
....
gi 2216741363 361 PAVD 364
Cdd:CHL00059 334 PAIN 337
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
19-364 |
2.49e-09 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 59.67 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 19 GRIAQIIGPVLDVSFPPGSMPRIYNSLIVKDNDTTGQPISVTCEVQQllgNNKVRAVAMSATDGLMRGMKVIDTGGPLSV 98
Cdd:PTZ00185 41 GYVHSIDGTIATLIPAPGNPGVAYNTIIMIQVSPTTFAAGLVFNLEK---DGRIGIILMDNITEVQSGQKVMATGKLLYI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 99 PVGETTLGRIFNVLGEPV---------------DNLGPVDALTTSPIHRSAPAFTQLdikfsileTGIKVVDLLAPYRRG 163
Cdd:PTZ00185 118 PVGAGVLGKVVNPLGHEVpvglltrsralleseQTLGKVDAGAPNIVSRSPVNYNLL--------TGFKAVDTMIPIGRG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 164 GKIGLFGGAGVGKTVLIMELINN-------IAKAHGGVSVFGGVGERTREGNDLYKEMKESGVINEQNISESKVAlvygq 236
Cdd:PTZ00185 190 QRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAA----- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 237 mnEPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE 316
Cdd:PTZ00185 265 --EPAGLQYLAPYSGVTMGEYFMNRGRH-CLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSP 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2216741363 317 ----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 364
Cdd:PTZ00185 342 gkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVN 393
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
378-432 |
2.78e-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: 39.34 E-value: 2.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2216741363 378 VGKEHYETAQGVKQTLQRYKELQDIIAI----LGLDelSEDDRLIVARArKIERFLSQP 432
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIgayqAGSD--PEIDEAIAKRP-AINAFLRQG 56
|
|
| 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 ... |
397-431 |
2.98e-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: 2.98e-04
10 20 30
....*....|....*....|....*....|....*.
gi 2216741363 397 KELQDIIAILGLDELSEDDRLIVARARKIE-RFLSQ 431
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFErEFINQ 57
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| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
19-94 |
7.19e-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: 38.06 E-value: 7.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2216741363 19 GRIAQIIGPVLDVSFPPGsmPRIYNSLIVKDNDTTGQPIsVTCEVQQLLGNNkVRAVAMSATDGLMRGMKVIDTGG 94
Cdd:cd01426 2 GRVIRVNGPLVEAELEGE--VAIGEVCEIERGDGNNETV-LKAEVIGFRGDR-AILQLFESTRGLSRGALVEPTGR 73
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| ATP-synt_V_A-type_alpha_C |
cd18111 |
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of ... |
393-431 |
1.02e-03 |
|
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: 38.52 E-value: 1.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2216741363 393 LQRYKELQDIIAILGLDELSEDDRLIVARARKI-ERFLSQ 431
Cdd:cd18111 12 LQEEAELQEIVQLVGPDALPEEDRLTLEVARMIrEDFLQQ 51
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| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
162-290 |
2.38e-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: 38.51 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216741363 162 RGGKIGLFGGAGVGKTVLIMELINNIAKAHggVSVFGGVGERTREGNDLYKEMKESGVINEQNISESKVALvygqmnepp 241
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPG--GGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRL--------- 69
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90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2216741363 242 garmrvgltALTMAEYFRdvnkqDVLLFIDNIFRFVQAGSEVSALLGRM 290
Cdd:smart00382 70 ---------ALALARKLK-----PDVLILDEITSLLDAEQEALLLLLEE 104
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