|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-465 |
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: 989.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 1 MQGFISQVLGPVVDVDF-NDYLPQINEAIVVNFESEGKkhkLVLEVAAHLGDNRVRTIAMDMTDGLVRGLKAEALGAPIS 79
Cdd:COG0055 4 NTGKIVQVIGPVVDVEFpEGELPAIYNALEVENEGGGE---LVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 80 VPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGKT 159
Cdd:COG0055 81 VPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 160 VIIMELIHNVAFKHSGYSVFAGVGERTREGNDLYNEMKESNVLDKVALCYGQMNEPPGARNRIALTGLTMAEYFRDEMGL 239
Cdd:COG0055 161 VLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 240 DVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITSTKKGSITSVQAVYVPADDLTDPAPATVFAHL 319
Cdd:COG0055 241 DVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 320 DATTVLNRAIAEKGIYPAVDPLDSTSRMLDPNIIGEEHYKVARGVQSVLQKYKDLQDIIAILGMDELSEEDKLVVERARK 399
Cdd:COG0055 321 DATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARK 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488979391 400 IEKFLSQPFFVAEVFTGSPGKYISLEDTIAGFKGILEGKYDHLPENAFYMVGNIDEAIAKADKLKG 465
Cdd:COG0055 401 IQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKA 466
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
1-463 |
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: 894.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 1 MQGFISQVLGPVVDVDF-NDYLPQINEAIVVNFESEGKkhkLVLEVAAHLGDNRVRTIAMDMTDGLVRGLKAEALGAPIS 79
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFeQGELPRIYNALKVQNRAESE---LTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 80 VPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGKT 159
Cdd:TIGR01039 78 VPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 160 VIIMELIHNVAFKHSGYSVFAGVGERTREGNDLYNEMKESNVLDKVALCYGQMNEPPGARNRIALTGLTMAEYFRDEMGL 239
Cdd:TIGR01039 158 VLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 240 DVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITSTKKGSITSVQAVYVPADDLTDPAPATVFAHL 319
Cdd:TIGR01039 238 DVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 320 DATTVLNRAIAEKGIYPAVDPLDSTSRMLDPNIIGEEHYKVARGVQSVLQKYKDLQDIIAILGMDELSEEDKLVVERARK 399
Cdd:TIGR01039 318 DATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488979391 400 IEKFLSQPFFVAEVFTGSPGKYISLEDTIAGFKGILEGKYDHLPENAFYMVGNIDEAIAKADKL 463
Cdd:TIGR01039 398 IQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
2-464 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 835.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 2 QGFISQVLGPVVDVDF-NDYLPQINEAIVV-NFESEGKKHKLVLEVAAHLGDNRVRTIAMDMTDGLVRGLKAEALGAPIS 79
Cdd:CHL00060 16 LGRITQIIGPVLDVAFpPGKMPNIYNALVVkGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 80 VPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGKT 159
Cdd:CHL00060 96 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 160 VIIMELIHNVAFKHSGYSVFAGVGERTREGNDLYNEMKESNVLD-------KVALCYGQMNEPPGARNRIALTGLTMAEY 232
Cdd:CHL00060 176 VLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 233 FRDEMGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITSTKKGSITSVQAVYVPADDLTDPAP 312
Cdd:CHL00060 256 FRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 313 ATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLDPNIIGEEHYKVARGVQSVLQKYKDLQDIIAILGMDELSEEDKL 392
Cdd:CHL00060 336 ATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRL 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488979391 393 VVERARKIEKFLSQPFFVAEVFTGSPGKYISLEDTIAGFKGILEGKYDHLPENAFYMVGNIDEAIAKADKLK 464
Cdd:CHL00060 416 TVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLE 487
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
3-456 |
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: 587.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 3 GFISQVLGPVVDVDFNDYLPQINEAIVVNFESEgkkhkLVLEVAAHLGDNRVRTIAMDMTDGLVRGLKAEALGAPISVPV 82
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGELPAIHSVLRAGREGE-----VVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 83 GEKVLGRIFNVTGDLIDEREEISfDKKW-AIHRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGKTVI 161
Cdd:TIGR03305 76 GKPTLSRMFDVFGNTIDRREPPK-DVEWrSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 162 IMELIHNVAFKHSGYSVFAGVGERTREGNDLYNEMKESNVLDKVALCYGQMNEPPGARNRIALTGLTMAEYFRDEMGLDV 241
Cdd:TIGR03305 155 LTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 242 LMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITSTKKGSITSVQAVYVPADDLTDPAPATVFAHLDA 321
Cdd:TIGR03305 235 LLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 322 TTVLNRAIAEKGIYPAVDPLDSTSRMLDPNIIGEEHYKVARGVQSVLQKYKDLQDIIAILGMDELSEEDKLVVERARKIE 401
Cdd:TIGR03305 315 SLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLE 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 488979391 402 KFLSQPFFVAEVFTGSPGKYISLEDTIAGFKGILEGKYDHLPENAFYMVGNIDEA 456
Cdd:TIGR03305 395 RFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
79-350 |
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: 582.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 79 SVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGK 158
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 159 TVIIMELIHNVAFKHSGYSVFAGVGERTREGNDLYNEMKESNV-----LDKVALCYGQMNEPPGARNRIALTGLTMAEYF 233
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVinldgLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 234 RDEMGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITSTKKGSITSVQAVYVPADDLTDPAPA 313
Cdd:cd01133 161 RDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPA 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 488979391 314 TVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLDP 350
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 ... |
79-347 |
2.56e-130 |
|
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: 377.95 E-value: 2.56e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 79 SVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGK 158
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 159 TVIIMELIHNVAFKHSGYSVFAGVGERTREGNDLYNEMKESNVLDKVALCYGQMNEPPGARNRIALTGLTMAEYFRDeMG 238
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRD-NG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 239 LDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITSTK--KGSITSVQAVYVPADDLTDPAPATVF 316
Cdd:cd19476 160 QHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDPIPDNTF 239
|
250 260 270
....*....|....*....|....*....|.
gi 488979391 317 AHLDATTVLNRAIAEKGIYPAVDPLDSTSRM 347
Cdd:cd19476 240 AILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
132-345 |
2.01e-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: 286.56 E-value: 2.01e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 132 GIKVVDLLAPYAKGGKVGLFGGAGVGKTVIIMELIHNVAFkhsGYSVFAGVGERTREGNDLYNEMKESNVLDKVALCYGQ 211
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 212 MNEPPGARNRIALTGLTMAEYFRDeMGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITST-- 289
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVkg 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488979391 290 KKGSITSVQAVYVPADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTS 345
Cdd:pfam00006 157 KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 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 ... |
352-459 |
1.53e-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: 234.29 E-value: 1.53e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 352 IIGEEHYKVARGVQSVLQKYKDLQDIIAILGMDELSEEDKLVVERARKIEKFLSQPFFVAEVFTGSPGKYISLEDTIAGF 431
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 488979391 432 KGILEGKYDHLPENAFYMVGNIDEAIAK 459
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
51-435 |
4.55e-60 |
|
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: 202.57 E-value: 4.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 51 DNRVRTIAMDMTDGLVRGLKAEALGAPISVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQSTKSEIFE 130
Cdd:COG1157 63 GDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 131 TGIKVVDLLAPYAKGGKVGLFGGAGVGKTVIIMELIHNVAFKhsgYSVFAGVGERTRE-----GNDLYNE-MKESnVL-- 202
Cdd:COG1157 143 TGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARNTEAD---VNVIALIGERGREvrefiEDDLGEEgLARS-VVvv 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 203 ---DkvalcygqmnEPPGARNRIALTGLTMAEYFRDEmGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEM 279
Cdd:COG1157 219 atsD----------EPPLMRLRAAYTATAIAEYFRDQ-GKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 280 GKFQERITSTKKGSITSVQAVYVPADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLdPNIIGEEHYK 359
Cdd:COG1157 288 PRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 360 VARGVQSVLQKYKDLQDIIAI----LGMDELSEEdklVVERARKIEKFLSQpffvaevftgSPGKYISLEDTIAGFKGIL 435
Cdd:COG1157 367 LARRLRRLLARYEENEDLIRIgayqPGSDPELDE---AIALIPAIEAFLRQ----------GMDERVSFEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
79-346 |
4.15e-57 |
|
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: 189.69 E-value: 4.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 79 SVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGK 158
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 159 TVIIMELIHNVAFKhsgYSVFAGVGERTREGNDLYNEMKESNVLDKVALCYGQMNEPPGARNRIALTGLTMAEYFRDEmG 238
Cdd:cd01136 81 STLLGMIARNTDAD---VNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQ-G 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 239 LDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITSTKKGSITSVQAVYVPADDLTDPAPATVFAH 318
Cdd:cd01136 157 KKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSI 236
|
250 260
....*....|....*....|....*...
gi 488979391 319 LDATTVLNRAIAEKGIYPAVDPLDSTSR 346
Cdd:cd01136 237 LDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
33-380 |
5.95e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 173.37 E-value: 5.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 33 ESEGKKHKLVLEVAAhLGDNRVRTIAMDMTDGLVRGLKAEALGAPISVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAI 112
Cdd:PRK07721 47 TKGGGDKAIKAEVVG-FKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVST 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 113 HRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGKTVIIMELIHNVAfkhSGYSVFAGVGERTRE---- 188
Cdd:PRK07721 126 DQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTS---ADLNVIALIGERGREvref 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 189 -GNDLYNE-MKESNVLdkVALCygqmNEPPGARNRIALTGLTMAEYFRDEmGLDVLMFIDNIFRFSQSGSEMSALLGRIP 266
Cdd:PRK07721 203 iERDLGPEgLKRSIVV--VATS----DQPALMRIKGAYTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 267 SAVGYQPTLASEMGKFQERITSTKKGSITSVQAVYVPADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSR 346
Cdd:PRK07721 276 TTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSR 355
|
330 340 350
....*....|....*....|....*....|....
gi 488979391 347 MLdPNIIGEEHYKVARGVQSVLQKYKDLQDIIAI 380
Cdd:PRK07721 356 VM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
68-436 |
1.68e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 169.48 E-value: 1.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 68 GLKAEALGAPISVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGK 147
Cdd:PRK08472 80 GDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQK 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 148 VGLFGGAGVGKTViIMELIhnVAFKHSGYSVFAGVGERTREgndlYNEMKESNV---LDKVALCYGQMNEPPGARNRIAL 224
Cdd:PRK08472 160 LGIFAGSGVGKST-LMGMI--VKGCLAPIKVVALIGERGRE----IPEFIEKNLggdLENTVIVVATSDDSPLMRKYGAF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 225 TGLTMAEYFRDEmGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITSTK-KGSITSVQAVYVP 303
Cdd:PRK08472 233 CAMSVAEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTVLVE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 304 ADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLDpNIIGEEHYKVARGVQSVLQKYKDLQDIIAI--- 380
Cdd:PRK08472 312 GDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIRIgay 390
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 488979391 381 -LGMD-ELSEedklVVERARKIEKFLSQpffvaevftgSPGKYISLEDTIAGFKGILE 436
Cdd:PRK08472 391 qKGNDkELDE----AISKKEFMEQFLKQ----------NPNELFPFEQTFEQLEEILR 434
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
38-406 |
7.18e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 164.77 E-value: 7.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 38 KHKLVLEVAAHLGDNRVrTIAMDMTDGLVRGLKAEALGAPISVPVGEKVLGRIFNVTGDLIDEREE-ISFDKkwaIHRDP 116
Cdd:PRK06793 50 EHNVLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAEnIPLQK---IKLDA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 117 P---AFEDQSTkSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGKTVIIMELIHNVafkHSGYSVFAGVGERTREGNDLY 193
Cdd:PRK06793 126 PpihAFEREEI-TDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNA---KADINVISLVGERGREVKDFI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 194 NEMKESNVLDKVALCYGQMNEPPGARNRIALTGLTMAEYFRDEmGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAvGYQP 273
Cdd:PRK06793 202 RKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 274 TLASEMGKFQERITSTKKGSITSVQAVYVPADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLDpNII 353
Cdd:PRK06793 280 LMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIV 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 488979391 354 GEEHYKVARGVQSVLQKYKDlQDIIAILGMDELSEEDKLVVERARKIE---KFLSQ 406
Cdd:PRK06793 359 SPNHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAYIFECKNKVEginTFLKQ 413
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
44-408 |
1.28e-45 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 164.01 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 44 EVAAH---LGDNRVRTIAMDMTDGlvRGLKAEAL----GAPISVPVGEKVLGRIFNVTGDlIDER-----EEISFDKKWA 111
Cdd:PRK08149 41 EVIARaqvVGFQRERTILSLIGNA--QGLSRQVVlkptGKPLSVWVGEALLGAVLDPTGK-IVERfdappTVGPISEERV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 112 IHRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGKTVIIMELIhnvafKHSGYSVF--AGVGERTREG 189
Cdd:PRK08149 118 IDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLI-----EHSEADVFviGLIGERGREV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 190 NDLYNEMKESNVLDKVALCYGQMNEPPGARNRIALTGLTMAEYFRDeMGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAV 269
Cdd:PRK08149 193 TEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPARR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 270 GYQPTLASEMGKFQERITSTKKGSITSVQAVYVPADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLD 349
Cdd:PRK08149 272 GYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488979391 350 pNIIGEEHYKVARGVQSVLQKYKDLQDIIAiLG---MDELSEEDKLVVERArKIEKFLSQPF 408
Cdd:PRK08149 352 -QVTDPKHRQLAAAFRKLLTRLEELQLFID-LGeyrRGENADNDRAMDKRP-ALEAFLKQDV 410
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
60-406 |
7.65e-45 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 162.29 E-value: 7.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 60 DMTDGLVRGLKAEALGAPISVPVGEKVLGRIFNVTGDLIDEREEISFDKKwAIHRDPPAFEDQSTKSEIFETGIKVVDLL 139
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWR-ELDCPPPSPLTRQPIEQMLTTGIRAIDGI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 140 APYAKGGKVGLFGGAGVGK-TVIIMELIHNVAfkhsGYSVFAGVGERTREGNDLYNEMKESNVLDKVALCYGQMNEPPGA 218
Cdd:PRK06820 158 LSCGEGQRIGIFAAAGVGKsTLLGMLCADSAA----DVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 219 RNRIALTGLTMAEYFRDEmGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITSTKKGSITSVQ 298
Cdd:PRK06820 234 RLKGLSTATTIAEYFRDR-GKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFY 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 299 AVYVPADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLdPNIIGEEHYKVARGVQSVLQKYKDLQDII 378
Cdd:PRK06820 313 TVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIELLV 391
|
330 340 350
....*....|....*....|....*....|..
gi 488979391 379 AI----LGMDELSEEdklVVERARKIEKFLSQ 406
Cdd:PRK06820 392 RVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
75-436 |
3.78e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 157.61 E-value: 3.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 75 GAPISVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGKVGLFGGA 154
Cdd:PRK06936 92 GTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 155 GVGKTVIIMELIHNVAfkhSGYSVFAGVGERTREgndlYNEMKESNV----LDKVALCYGQMNEPPGARNRIALTGLTMA 230
Cdd:PRK06936 172 GGGKSTLLASLIRSAE---VDVTVLALIGERGRE----VREFIESDLgeegLRKAVLVVATSDRPSMERAKAGFVATSIA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 231 EYFRDEmGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITSTKKGSITSVQAVYVPADDLTDP 310
Cdd:PRK06936 245 EYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEP 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 311 APATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLDpNIIGEEHYKVARGVQSVLQKYKDLQDIIAI----LGMDEL 386
Cdd:PRK06936 324 VADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKE 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 488979391 387 SEEdklVVERARKIEKFLSQPffvaevfTGSPGkyiSLEDTIAGFKGILE 436
Cdd:PRK06936 403 ADQ---AIERIGAIRGFLRQG-------THELS---HFNETLNLLETLTQ 439
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
88-382 |
1.46e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 156.31 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 88 GRIFNVTGDLIDEREEI-SFDKKWAIHRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGKTVIIMELI 166
Cdd:PRK06002 107 GRVINALGEPIDGLGPLaPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 167 HNVAFKHSgysVFAGVGERTREGNDLYNEMKESNvLDKVALCYGQMNEPPGARNRIALTGLTMAEYFRDEmGLDVLMFID 246
Cdd:PRK06002 187 RADAFDTV---VIALVGERGREVREFLEDTLADN-LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDR-GENVLLIVD 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 247 NIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERI--TSTKKGSITSVQAVYVPADDLTDPAPATVFAHLDATTV 324
Cdd:PRK06002 262 SVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIV 341
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 488979391 325 LNRAIAEKGIYPAVDPLDSTSRMLDPNIIGEEHyKVARGVQSVLQKYKDLQDIIAILG 382
Cdd:PRK06002 342 LDRAIAEQGRYPAVDPLASISRLARHAWTPEQR-KLVSRLKSMIARFEETRDLRLIGG 398
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
63-407 |
3.97e-42 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 154.93 E-value: 3.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 63 DGLVRGLKAEALGAPISVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQSTKSEIFETGIKVVDLLAPY 142
Cdd:PRK09099 81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 143 AKGGKVGLFGGAGVGKTVIIMELIHNVAfkhSGYSVFAGVGERTREGNDLYNE-MKESNVLDKVALCyGQMNEPPGARNR 221
Cdd:PRK09099 161 GEGQRMGIFAPAGVGKSTLMGMFARGTQ---CDVNVIALIGERGREVREFIELiLGEDGMARSVVVC-ATSDRSSIERAK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 222 IALTGLTMAEYFRDEmGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITSTKKGSITSVQAVY 301
Cdd:PRK09099 237 AAYVATAIAEYFRDR-GLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 302 VPADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLdPNIIGEEHYKVARGVQSVLQKYKDLQDIIAI- 380
Cdd:PRK09099 316 AEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVg 394
|
330 340 350
....*....|....*....|....*....|
gi 488979391 381 ---LGMDELSEEdklVVERARKIEKFLSQP 407
Cdd:PRK09099 395 eyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
51-406 |
5.48e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 154.75 E-value: 5.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 51 DNRVRTIAMDMTDGLVRGLKAEALGAPISVPVGEKVLGRIFNVTGDLIDEREEIS-FDKKWAIHRDPPAFEDQSTKSEIF 129
Cdd:PRK08927 63 GDRALLMPFGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPqGPVPYPLRAPPPPAHSRARVGEPL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 130 ETGIKVVDLLAPYAKGGKVGLFGGAGVGKTVIIMELIHNVAfkhSGYSVFAGVGERTRE-----GNDLYNE-MKESNVLd 203
Cdd:PRK08927 143 DLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNAD---ADVSVIGLIGERGREvqeflQDDLGPEgLARSVVV- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 204 kVALCygqmNEPPGARNRIALTGLTMAEYFRDEmGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQ 283
Cdd:PRK08927 219 -VATS----DEPALMRRQAAYLTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 284 ERIT--STKKGSITSVQAVYVPADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLdPNIIGEEHYKVA 361
Cdd:PRK08927 293 ERAGpgPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLV 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488979391 362 RGVQSVLQKYKDLQDIIAI----LGMDELSEEdklVVERARKIEKFLSQ 406
Cdd:PRK08927 372 RRARQLMATYADMEELIRLgayrAGSDPEVDE---AIRLNPALEAFLRQ 417
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
62-380 |
1.27e-41 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 153.57 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 62 TDGLVRGLKAEALGAPISVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQSTKSEIFeTGIKVVDLLAP 141
Cdd:PRK07594 73 TIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRELPDVCWKDYDAMPPPAMVRQPITQPLM-TGIRAIDSVAT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 142 YAKGGKVGLFGGAGVGKTVIIMELihnVAFKHSGYSVFAGVGERTREGNDLYNEMKESNVLDKVALCYGQMNEPPGARNR 221
Cdd:PRK07594 152 CGEGQRVGIFSAPGVGKSTLLAML---CNAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 222 IALTGLTMAEYFRDEmGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITSTKKGSITSVQAVY 301
Cdd:PRK07594 229 ALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYTVL 307
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488979391 302 VPADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLdPNIIGEEHYKVARGVQSVLQKYKDLQDIIAI 380
Cdd:PRK07594 308 VEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVELLIRI 385
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
64-380 |
3.75e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 152.16 E-value: 3.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 64 GLVRGLKAEALGAPISVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQSTKSEIFETGIKVVDLLAPYA 143
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 144 KGGKVGLFGGAGVGKTVII-MELIHNVAfkhsGYSVFAGVGERTREGNDLYNEM------KESNVLDKVAlcygqmNEPP 216
Cdd:PRK08972 161 KGQRMGLFAGSGVGKSVLLgMMTRGTTA----DVIVVGLVGERGREVKEFIEEIlgeegrARSVVVAAPA------DTSP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 217 GARNRIALTGLTMAEYFRDeMGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERIT--STKKGSI 294
Cdd:PRK08972 231 LMRLKGCETATTIAEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPGQGSI 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 295 TSVQAVYVPADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLdPNIIGEEHYKVARGVQSVLQKYKDL 374
Cdd:PRK08972 310 TAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQN 388
|
....*.
gi 488979391 375 QDIIAI 380
Cdd:PRK08972 389 RDLISI 394
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
63-406 |
1.44e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 145.26 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 63 DGLVRGLKAEALGAPISVPVGEKVLGRIFNVTGDLIDEREEISFDKKwaIHRDPPAFE--DQSTKSEIFETGIKVVDLLA 140
Cdd:PRK05688 86 AGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDW--VPMDGPTINplNRHPISEPLDVGIRSINGLL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 141 PYAKGGKVGLFGGAGVGKTVIIMELIHnvaFKHSGYSVFAGVGERTREGNDLYNEMKESNVLDKVALCYGQMNEPPGARN 220
Cdd:PRK05688 164 TVGRGQRLGLFAGTGVGKSVLLGMMTR---FTEADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 221 RIALTGLTMAEYFRDEmGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITSTKKG--SITSVQ 298
Cdd:PRK05688 241 RAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITAFY 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 299 AVYVPADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLdPNIIGEEHYKVARGVQSVLQKYKDLQDII 378
Cdd:PRK05688 320 TVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLI 398
|
330 340 350
....*....|....*....|....*....|..
gi 488979391 379 AI----LGMDelsEEDKLVVERARKIEKFLSQ 406
Cdd:PRK05688 399 SVgayvAGGD---PETDLAIARFPHLVQFLRQ 427
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
62-408 |
5.27e-38 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 143.81 E-value: 5.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 62 TDGL-VRGLKAEALGAPISVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIH--------RDPPafedqstkSEIFETG 132
Cdd:PRK04196 59 TTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINgapinpvaREYP--------EEFIQTG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 133 IKVVDLLAPYAKGGKVGLFGGAGvgktviimeLIHN-----------VAFKHSGYS-VFAGVGERTREGNDLYNEMKESN 200
Cdd:PRK04196 131 ISAIDGLNTLVRGQKLPIFSGSG---------LPHNelaaqiarqakVLGEEENFAvVFAAMGITFEEANFFMEDFEETG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 201 VLDKVALCYGQMNEPpgARNRIAL--TGLTMAEYFRDEMGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASE 278
Cdd:PRK04196 202 ALERSVVFLNLADDP--AIERILTprMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 279 MGKFQER--ITSTKKGSITSVQAVYVPADDLTDPAPatvfahlDAT-------TVLNRAIAEKGIYPAVDPLDSTSRMLD 349
Cdd:PRK04196 280 LATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegqIVLSRELHRKGIYPPIDVLPSLSRLMK 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488979391 350 pNIIG-----EEHYKVARGVQSVLQKYKDLQDIIAILGMDELSEEDKLVVERARKIE-KFLSQPF 408
Cdd:PRK04196 353 -DGIGegktrEDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFErEFVNQGF 416
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
82-406 |
6.47e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 132.32 E-value: 6.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 82 VGEKVLGRIFNVTGDLIDEREEISFDKKWAIHrdPPAFEDQSTKS--EIFETGIKVVDLLAPYAKGGKVGLFGGAGVGKT 159
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQ--LPQIHPLQRRAvdTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 160 VIIMELIHnvaFKHSGYSVFAGVGERTREGNDLYNEMKESNVLDKVALCYGQMNEPPGARNRIALTGLTMAEYFRDEmGL 239
Cdd:PRK07196 170 VLLGMITR---YTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDK-GH 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 240 DVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERI-TSTKKGSITSVQAVYVPADDLTDPAPATVFAH 318
Cdd:PRK07196 246 DVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMTAIYTVLAEGDDQQDPIVDCARAV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 319 LDATTVLNRAIAEKGIYPAVDPLDSTSRMLDpNIIGEEHYKVARGVQSVLQKYKDLQDIIA----ILGMDELSEEdklVV 394
Cdd:PRK07196 326 LDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAIKPLIPlggyVAGADPMADQ---AV 401
|
330
....*....|..
gi 488979391 395 ERARKIEKFLSQ 406
Cdd:PRK07196 402 HYYPAITQFLRQ 413
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
100-406 |
1.33e-31 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 127.59 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 100 EREEISFDKKWAIhRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGKTViimeLIHNVAfKHSG--YS 177
Cdd:PRK04192 183 EGVELTMMQKWPV-RRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTV----TQHQLA-KWADadIV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 178 VFAGVGERTregndlyNEMKEsnVLDKV----------ALcygqM----------NEPPGARNRIALTGLTMAEYFRDeM 237
Cdd:PRK04192 257 IYVGCGERG-------NEMTE--VLEEFpelidpktgrPL----MertvliantsNMPVAAREASIYTGITIAEYYRD-M 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 238 GLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQER----IT-STKKGSITSVQAVYVPADDLTDP-A 311
Cdd:PRK04192 323 GYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTIIGAVSPPGGDFSEPvT 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 312 PAT-----VFAHLDAttvlNRAIAEKgiYPAVDPLDSTSRMLD-------PNIIGEEHYKVARGVqSVLQKYKDLQDIIA 379
Cdd:PRK04192 403 QNTlrivkVFWALDA----ELADRRH--FPAINWLTSYSLYLDqvapwweENVDPDWRELRDEAM-DLLQREAELQEIVR 475
|
330 340
....*....|....*....|....*...
gi 488979391 380 ILGMDELSEEDKLVVERARKI-EKFLSQ 406
Cdd:PRK04192 476 LVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
77-346 |
2.33e-31 |
|
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: 121.91 E-value: 2.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 77 PISVPVGEKVLGRIFnvtgDLIDEREEISFDK------------KWAIhRDPPAFEDQSTKSEIFETGIKVVDLLAPYAK 144
Cdd:cd01134 1 PLSVELGPGLLGSIF----DGIQRPLEVIAETgsifiprgvnvqRWPV-RQPRPVKEKLPPNVPLLTGQRVLDTLFPVAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 145 GGKVGLFGGAGVGKTVIIMELihnvafkhSGYS-----VFAGVGERtreGND----------LYNEMKESNVLDKVALCY 209
Cdd:cd01134 76 GGTAAIPGPFGCGKTVISQSL--------SKWSnsdvvIYVGCGER---GNEmaevleefpeLKDPITGESLMERTVLIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 210 GQMNEPPGARNRIALTGLTMAEYFRDeMGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERI--- 286
Cdd:cd01134 145 NTSNMPVAAREASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrv 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 287 ----TSTKKGSITSVQAVYVPADDLTDP-APAT-----VFAHLDAttvlnrAIAEKGIYPAVDPLDSTSR 346
Cdd:cd01134 224 rclgSPGREGSVTIVGAVSPPGGDFSEPvTQATlrivqVFWGLDK------KLAQRRHFPSINWLISYSK 287
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
77-354 |
1.46e-30 |
|
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: 119.63 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 77 PISVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIH--------RDPPafedqstkSEIFETGIKVVDLLAPYAKGGKV 148
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINgppinpvaRIYP--------EEMIQTGISAIDVMNTLVRGQKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 149 GLFGGAGVGKTVIIMELIHNVAFKHSGYS---VFAGVGERTREGNDLYNEMKESNVLDKVALCYGQMNEPPGAR---NRI 222
Cdd:cd01135 73 PIFSGSGLPHNELAAQIARQAGVVGSEENfaiVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERiitPRM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 223 AltgLTMAEYFRDEMGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQER--ITSTKKGSITSVQAV 300
Cdd:cd01135 153 A---LTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPIL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488979391 301 YVPADDLTDPAPatvfahlDAT-------TVLNRAIAEKGIYPAVDPLDSTSRMLDpNIIG 354
Cdd:cd01135 230 TMPNDDITHPIP-------DLTgyitegqIYLDRDLHNKGIYPPIDVLPSLSRLMK-SGIG 282
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
74-436 |
4.33e-30 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 121.55 E-value: 4.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 74 LGAPISVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGKVGLFGG 153
Cdd:PRK05922 86 LRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 154 AGVGKTviimELIHNVAF-KHSGYSVFAGVGERTREGNDLYNEMKESNVLDKVALCYGQMNEPPGARNRIALTGLTMAEY 232
Cdd:PRK05922 166 PGSGKS----SLLSTIAKgSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 233 FRDEmGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITSTKKGSITSVQAV-YVP--ADDLTD 309
Cdd:PRK05922 242 FRDQ-GHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTD 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 310 PAPATVFAHLDATTVlNRAIAEkgiyPAVDPLDSTSRMLDpNIIGEEHYKVARGVQSVLQKYKDLQDIIAiLGMDELSEE 389
Cdd:PRK05922 321 YLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSRSAR-QLALPHHYAAAEELRSLLKAYHEALDIIQ-LGAYVPGQD 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 488979391 390 DKLvvERARK----IEKFLSQPFfvaevftgspGKYISLEDTIAGFKGILE 436
Cdd:PRK05922 394 AHL--DRAVKllpsIKQFLSQPL----------SSYCALHNTLKQLEALLK 432
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
1-78 |
6.80e-30 |
|
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: 111.07 E-value: 6.80e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488979391 1 MQGFISQVLGPVVDVDF-NDYLPQINEAIVVNFESEGKkhkLVLEVAAHLGDNRVRTIAMDMTDGLVRGLKAEALGAPI 78
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFpEGELPPIYNALEVKGDDGKK---LVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
45-443 |
1.63e-28 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 117.71 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 45 VAAHLGDNRVRTIAMDMTDGLVRGLKAEALGAPISVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQST 124
Cdd:PRK13343 62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 125 KSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGKTVIIMELIHNVafKHSG-YSVFAGVGERTREGNDLYNEMKESNVLD 203
Cdd:PRK13343 142 VTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIINQ--KDSDvICVYVAIGQKASAVARVIETLREHGALE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 204 KVALCYGQMNEPPGARNRIALTGLTMAEYFRDEmGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQ 283
Cdd:PRK13343 220 YTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 284 ERIT--STKK--GSITSVQAVYVPADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRmldpniIG--EEH 357
Cdd:PRK13343 299 ERAAklSPELggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR------VGgkAQH 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 358 ---YKVARGVQSVLQKYKDLQdIIAILGMDeLSEEDKLVVERARKIEKFLSQPFFvaevftgSPgkyISLEDTIAGFKGI 434
Cdd:PRK13343 373 paiRKESGRLRLDYAQFLELE-AFTRFGGL-LDAGTQKQITRGRRLRELLKQPRF-------SP---LSVEEQIALLYAL 440
|
....*....
gi 488979391 435 LEGKYDHLP 443
Cdd:PRK13343 441 NEGLLDAVP 449
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
67-409 |
7.25e-28 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 115.27 E-value: 7.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 67 RGLKAEALGAPISVPVGEKVLGRIFNVTGDLID--EREEISFDkkwAIHRDPPAFEDQSTK-SEIFETGIKVVDLLAPYA 143
Cdd:PRK07960 97 RNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDglPAPDTGET---GALITPPFNPLQRTPiEHVLDTGVRAINALLTVG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 144 KGGKVGLFGGAGVGKTVIIMELIHnvaFKHSGYSVFAGVGERTREGNDLYNEMKESNVLDKVALCYGQMNEPPGARNRIA 223
Cdd:PRK07960 174 RGQRMGLFAGSGVGKSVLLGMMAR---YTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 224 LTGLTMAEYFRDEmGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITS--TKKGSITSVQAVY 301
Cdd:PRK07960 251 AYATRIAEDFRDR-GQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 302 VPADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLdPNIIGEEHYKVARGVQSVLQKYKDLQDIIAI- 380
Cdd:PRK07960 330 TEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAM-TALIDEQHYARVRQFKQLLSSFQRNRDLVSVg 408
|
330 340 350
....*....|....*....|....*....|..
gi 488979391 381 ---LGMDELSEEdklVVERARKIEKFLSQPFF 409
Cdd:PRK07960 409 ayaKGSDPMLDK---AIALWPQLEAFLQQGIF 437
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
5-406 |
1.21e-27 |
|
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: 114.82 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 5 ISQVLGPVVDVDfNDYLPQINEAIVVNFESEGKKHKLVLEVAahlGDNRVRTIaMDMTDGL-VRGLKAEALGAPISVPVG 83
Cdd:TIGR01040 5 VSGVNGPLVILD-NVKFPRFAEIVNLTLPDGTVRSGQVLEVS---GNKAVVQV-FEGTSGIdAKKTTCEFTGDILRTPVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 84 EKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGKTVIIM 163
Cdd:TIGR01040 80 EDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 164 ELIHNVAF-------KHSGYS-----VFAGVGERTREGNDLYNEMKESNVLDKVALCYGQMNEPPGAR---NRIAltgLT 228
Cdd:TIGR01040 160 QICRQAGLvklptkdVHDGHEdnfaiVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERiitPRLA---LT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 229 MAEYFRDEMGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERI--TSTKKGSITSVQAVYVPADD 306
Cdd:TIGR01040 237 TAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 307 LTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLDpNIIGE-----EHYKVARGVQSVLQKYKDLQDIIAIL 381
Cdd:TIGR01040 317 ITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMK-SAIGEgmtrkDHSDVSNQLYACYAIGKDVQAMKAVV 395
|
410 420
....*....|....*....|....*.
gi 488979391 382 GMDELSEEDKLVVERARKIEK-FLSQ 406
Cdd:TIGR01040 396 GEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
165-418 |
2.55e-23 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 103.56 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 165 LIHNVAFKH-------SGYSVFAGVGERTREGNDLYNE---MKESN----VLDKVALCYGQMNEPPGARNRIALTGLTMA 230
Cdd:PRK14698 666 LLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEfpkLKDPKtgkpLMERTVLIANTSNMPVAAREASIYTGITIA 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 231 EYFRDeMGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERI-------TSTKKGSITSVQAVYVP 303
Cdd:PRK14698 746 EYFRD-MGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPP 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 304 ADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRMLDP------NIIGEEHYKVARGVQSVLQKYKDLQDI 377
Cdd:PRK14698 825 GGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEI 904
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 488979391 378 IAILGMDELSEEDKLVVERARKI-EKFLSQPFFvAEVFTGSP 418
Cdd:PRK14698 905 VRIVGPDALPERERAILLVARMLrEDYLQQDAF-DEVDTYCP 945
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
78-346 |
6.53e-20 |
|
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: 89.15 E-value: 6.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 78 ISVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQSTKSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVG 157
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 158 KTVIIMELIHNVafKHSG-YSVFAGVGERTREGNDLYNEMKESNVLDKVALCYGQMNEPPGARNRIALTGLTMAEYFRDE 236
Cdd:cd01132 82 KTAIAIDTIINQ--KGKKvYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 237 mGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGY-------QPTLASEMGKFQERItstKKGSITSVQAVYVPADDLTD 309
Cdd:cd01132 160 -GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYpgdvfylHSRLLERAAKLSDEL---GGGSLTALPIIETQAGDVSA 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 488979391 310 PAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSR 346
Cdd:cd01132 236 YIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
357-420 |
7.87e-20 |
|
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: 83.26 E-value: 7.87e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488979391 357 HYKVARGVQSVLQKYKDLQDIIAILGMDELSEEDKLVVERARKIEKFLSQPFFVAEVFTGSPGK 420
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEK 64
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
5-75 |
3.80e-15 |
|
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: 69.88 E-value: 3.80e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488979391 5 ISQVLGPVVDVDF-NDYLPQINEAIVVNFESEGKkhkLVLEVAAHLGDNRVRTIAMDMTDGLVRGLKAEALG 75
Cdd:pfam02874 1 IVQVIGPVVDVEFgIGRLPGLLNALEVELVEFGS---LVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
62-402 |
9.00e-15 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 75.84 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 62 TDGLVRGLKAEALGAPISVPVGEKVLGRIFNVTGDLIDEREEIsFDKKWAIhrDPPAFEDQSTK--SEIFETGIKVVDLL 139
Cdd:PRK02118 58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPEL-EGEPIEI--GGPSVNPVKRIvpREMIRTGIPMIDVF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 140 APYAKGGKVGLFGGAGVGKTviimELIHNVAFK-HSGYSVFAGVGERTREGNDLYNEMKESNVLDKVALCYGQMNEPPGA 218
Cdd:PRK02118 135 NTLVESQKIPIFSVSGEPYN----ALLARIALQaEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 219 RNRIALTGLTMAEYFRDEMGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLASEMGKFQERITSTKK-GSITSV 297
Cdd:PRK02118 211 CLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEDgGSITII 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 298 QAVYVPADDLTDPAPatvfahlDATTVlnraIAEKGIY---PAVDPLDSTSRmLDPNIIG----EEHYKVArgvQSVLQK 370
Cdd:PRK02118 291 AVTTMPGDDVTHPVP-------DNTGY----ITEGQFYlrrGRIDPFGSLSR-LKQLVIGkktrEDHGDLM---NAMIRL 355
|
330 340 350
....*....|....*....|....*....|...
gi 488979391 371 YKDLQDIIAILGMD-ELSEEDKLVVERARKIEK 402
Cdd:PRK02118 356 YADSREAKEKMAMGfKLSNWDEKLLKFSELFES 388
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
51-347 |
1.36e-12 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 69.68 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 51 DNRVRTIAMDMTDGLVRGLKAEALGAPISVPVGEKVLGRIFNVTGDLID----EREEISFDKKWAIHR---DPPAFEDQS 123
Cdd:PTZ00185 88 DGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvgllTRSRALLESEQTLGKvdaGAPNIVSRS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 124 TKSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGKTVIIMELIHN-------VAFKHSGYSVFAGVGERTREGNDLYNEM 196
Cdd:PTZ00185 168 PVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSNVARIHRLL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 197 KESNVLDKVALCYGQMNEPPGARNRIALTGLTMAEYFRDEmGLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYQPTLA 276
Cdd:PTZ00185 248 RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNR-GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVF 326
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488979391 277 SEMGKFQER--ITSTKK--GSITSVQAVYVPADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSRM 347
Cdd:PTZ00185 327 YLHSRLLERaaMLSPGKggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRV 401
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
63-266 |
3.00e-09 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 58.92 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 63 DGLVRGLKAEALGAPISVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIHRDPPAFEDQSTKSEIFETGIKVVDLLAPY 142
Cdd:PRK09281 80 EDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 143 AKGGKVGLFGGAGVGKTVIIMELIHNVafKHSG-YSVFAGVGErtregndlynemKESNV------LDKvalcYGQM--- 212
Cdd:PRK09281 160 GRGQRELIIGDRQTGKTAIAIDTIINQ--KGKDvICIYVAIGQ------------KASTVaqvvrkLEE----HGAMeyt 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488979391 213 -------NEPPGARNRIALTGLTMAEYFRDEmGLDVLMFIDNIFRFSQSGSEMSALLGRIP 266
Cdd:PRK09281 222 ivvaataSDPAPLQYLAPYAGCAMGEYFMDN-GKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
58-346 |
4.01e-08 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 55.35 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 58 AMDMTDGL--VRGLKAEALGAPISVPVGEKVLGRIFNVTGDLIDEREEISFDKKWAIhrDPPAFEDQSTKS--EIFETGI 133
Cdd:CHL00059 52 VVLMGDGLmiQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLI--ESPAPGIISRRSvyEPLQTGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 134 KVVDLLAPYAKGGKVGLFGGAGVGKTVIIMELIHNVAFKhSGYSVFAGVGERTREGNDLYNEMKESNVLDKVALCYGQMN 213
Cdd:CHL00059 130 IAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQ-NVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETAD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 214 EpPGARNRIA-LTGLTMAEYFrdeM--GLDVLMFIDNIFRFSQSGSEMSALLGRIPSAVGYqP---------------TL 275
Cdd:CHL00059 209 S-PATLQYLApYTGAALAEYF---MyrGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAY-PgdvfylhsrlleraaKL 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488979391 276 ASEMGkfqeritstkKGSITSVQAVYVPADDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSR 346
Cdd:CHL00059 284 SSQLG----------EGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR 344
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
88-409 |
8.18e-07 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 51.13 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 88 GRIFNVTGDLIDEREEISFDKKWAIHRDPpAFEDQS------TKSEIFETGIKVVDLLAPYAKGGKVGLFGGAGVGKTVI 161
Cdd:PRK07165 81 GKIIDIDGNIIYPEAQNPLSKKFLPNTSS-IFNLAHglmtvkTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 162 IMELIHNVafKHSGYS-VFAGVGERTREGNDLYNEMKESNVLDKVALcygqMNEP---PGARNRIALTGLTMAEYFRDEM 237
Cdd:PRK07165 160 ALNTIINQ--KNTNVKcIYVAIGQKRENLSRIYETLKEHDALKNTII----IDAPstsPYEQYLAPYVAMAHAENISYND 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 238 glDVLMFID------NIFRfsqsgsEMSALLGR------IPSAVGY-QPTLASEMGKFQERitstkkGSITSVQAVYVPA 304
Cdd:PRK07165 234 --DVLIVFDdltkhaNIYR------EIALLTNKpvgkeaFPGDMFFaHSKLLERAGKFKNR------KTITALPILQTVD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 305 DDLTDPAPATVFAHLDATTVLNRAIAEKGIYPAVDPLDSTSR----MLDPNIIgeehyKVARGVQSVLQKYKDlQDIIAI 380
Cdd:PRK07165 300 NDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRtgssVQSKTIT-----KVAGEISKIYRAYKR-QLKLSM 373
|
330 340
....*....|....*....|....*....
gi 488979391 381 LGMDeLSEEDKLVVERARKIEKFLSQPFF 409
Cdd:PRK07165 374 LDYD-LNKETSDLLFKGKMIEKMFNQKGF 401
|
|
| 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 ... |
366-406 |
3.13e-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: 42.76 E-value: 3.13e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 488979391 366 SVLQKYKDLQDIIAILGMDELSEEDKLVVERARKI-EKFLSQ 406
Cdd:cd18111 10 EILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIrEDFLQQ 51
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|
| ATP-synt_V_A-type_beta_C |
cd18112 |
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 ... |
372-406 |
5.72e-05 |
|
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: 41.65 E-value: 5.72e-05
10 20 30
....*....|....*....|....*....|....*.
gi 488979391 372 KDLQDIIAILGMDELSEEDKLVVERARKIE-KFLSQ 406
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFErEFINQ 57
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|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
144-264 |
1.39e-04 |
|
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: 41.98 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 144 KGGKVGLFGGAGVGKTVIIMELIHNVAFKHSGYSVFAGVGERTREGNDLYNEMKESNVLDKValcygqmnepPGARNRIA 223
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS----------GELRLRLA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 488979391 224 ltgLTMAEYFRdemgLDVLmFIDNIFRFSQSGSEMSALLGR 264
Cdd:smart00382 71 ---LALARKLK----PDVL-ILDEITSLLDAEQEALLLLLE 103
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
2-76 |
5.97e-04 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 38.45 E-value: 5.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488979391 2 QGFISQVLGPVVDVDFNDYLPqINEaiVVNFESEGKKHKLVL--EVAAHLGDnRVRTIAMDMTDGLVRGLKAEALGA 76
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVA-IGE--VCEIERGDGNNETVLkaEVIGFRGD-RAILQLFESTRGLSRGALVEPTGR 73
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
84-198 |
1.35e-03 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 41.16 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488979391 84 EKVLGRIFNVTGDLiderEEISFDKKWAIHRDPPAFEDQSTKSEIFeTGIKVVDLLAPYAKGGKVGLFGGAGVGKTVIIM 163
Cdd:PRK14698 171 EEVIAKVKTPSGEI----KELKMYQRWPVRVKRPYKEKLPPEVPLI-TGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDGD 245
|
90 100 110
....*....|....*....|....*....|....*....
gi 488979391 164 ELIHNVAFK----HSGYSVFAGVGERTREGNDLYNEMKE 198
Cdd:PRK14698 246 TLILTKEFGlikiKDLYEILDGKGKKTVEGNEEWTELEE 284
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