|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-459 |
0e+00 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 939.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 1 MVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGL 80
Cdd:COG0056 52 LLEFPGGVYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVER 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 81 KAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKrfndgtdeKKKLYCIYVAIGQKRS 160
Cdd:COG0056 132 PAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKAS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 161 TVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGR 240
Cdd:COG0056 204 TVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 241 EAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSV 320
Cdd:COG0056 284 EAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 321 SRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRG 400
Cdd:COG0056 364 SRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNG 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 149029485 401 YLDKLEPSKITKFESAFLSHVVSQHQSLLGNIRSDGKISEQSDAKLKEIVTNFLAGFEP 459
Cdd:COG0056 444 YLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGKLDDEIEEKLKAAIEEFKKTFAA 502
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-459 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 938.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 1 MVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGL 80
Cdd:PRK09281 52 LLEFPGGVYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVER 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 81 KAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKrfndgtdeKKKLYCIYVAIGQKRS 160
Cdd:PRK09281 132 KAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKAS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 161 TVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGR 240
Cdd:PRK09281 204 TVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 241 EAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSV 320
Cdd:PRK09281 284 EAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 321 SRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRG 400
Cdd:PRK09281 364 SRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNG 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 149029485 401 YLDKLEPSKITKFESAFLSHVVSQHQSLLGNIRSDGKISEQSDAKLKEIVTNFLAGFEP 459
Cdd:PRK09281 444 YLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKDLSDEIEAKLKAAIEEFKKTFAA 502
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
1-459 |
0e+00 |
|
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273365 [Multi-domain] Cd Length: 501 Bit Score: 779.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 1 MVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGL 80
Cdd:TIGR00962 51 LIEFEGGVQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 81 KAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKrfndgtdeKKKLYCIYVAIGQKRS 160
Cdd:TIGR00962 131 IAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIINQK--------DSDVYCIYVAIGQKAS 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 161 TVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGR 240
Cdd:TIGR00962 203 TVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 241 EAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSV 320
Cdd:TIGR00962 283 EAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 321 SRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRG 400
Cdd:TIGR00962 363 SRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKG 442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 149029485 401 YLDKLEPSKITKFESAFLSHVVSQHQSLLGNIRSDGKISEQSDAKLKEIVTNFLAGFEP 459
Cdd:TIGR00962 443 YLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKLTEELEAKLKEALKNFKKTFAW 501
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
1-457 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 724.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 1 MVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGL 80
Cdd:CHL00059 31 LVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIES 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 81 KAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKrfndgtdeKKKLYCIYVAIGQKRS 160
Cdd:CHL00059 111 PAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQK--------GQNVICVYVAIGQKAS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 161 TVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGR 240
Cdd:CHL00059 183 SVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGR 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 241 EAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSV 320
Cdd:CHL00059 263 EAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 321 SRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRG 400
Cdd:CHL00059 343 SRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQSAPLTVEEQVATIYTGTNG 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 149029485 401 YLDKLEPSKITKFESAFLSHVVSQHQSLLGNIRSDGKISEQSDAKLKEIVTNFLAGF 457
Cdd:CHL00059 423 YLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQLELF 479
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-459 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 702.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 1 MVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGL 80
Cdd:PRK13343 52 LLRFEGGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLER 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 81 KAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKrfndgtdeKKKLYCIYVAIGQKRS 160
Cdd:PRK13343 132 PAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIINQK--------DSDVICVYVAIGQKAS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 161 TVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGR 240
Cdd:PRK13343 204 AVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 241 EAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSV 320
Cdd:PRK13343 284 EAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 321 SRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRG 400
Cdd:PRK13343 364 SRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEG 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 149029485 401 YLDKLEPSKITKFESAFLSHVVSQHQSLLGNIRSDGKISEQSDAKLKEIVTNFLAGFEP 459
Cdd:PRK13343 444 LLDAVPLANIQAFEERLLEKLDARFAALSLALESPRELDEAWLAALEEILREAGERFAA 502
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
43-324 |
0e+00 |
|
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: 611.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 43 IVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQT 122
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 123 GKTSIAIDTIINQKRfndgtdekKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSM 202
Cdd:cd01132 81 GKTAIAIDTIINQKG--------KKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 203 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGD 282
Cdd:cd01132 153 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 149029485 283 VSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVG 324
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
1-441 |
0e+00 |
|
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic species, including Methanosarcina barkeri, 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 alpha subunit of this apparent second ATP synthase.
Pssm-ID: 132367 [Multi-domain] Cd Length: 497 Bit Score: 523.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 1 MVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGL 80
Cdd:TIGR03324 52 LLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIER 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 81 KAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNdgtdekkkLYCIYVAIGQKRS 160
Cdd:TIGR03324 132 PAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDRQTGKTAIAIDTILNQKGRN--------VLCIYCAIGQRAS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 161 TVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGR 240
Cdd:TIGR03324 204 AVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSIGEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 241 EAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSV 320
Cdd:TIGR03324 284 EAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQNISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 321 SRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRG 400
Cdd:TIGR03324 364 SRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDENTRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNG 443
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 149029485 401 YLDKLEPSKITKFESAFLSHVVSQHQSLLGNIRSDGKISEQ 441
Cdd:TIGR03324 444 LFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSDE 484
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
45-323 |
3.60e-135 |
|
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: 389.89 E-value: 3.60e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 45 DVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGK 124
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 125 TSIAIDTIINQKrfndgtdEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGE 204
Cdd:cd19476 81 TVLAMQLARNQA-------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 205 YFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDsfGGGSLTALPVIETQAGDVS 284
Cdd:cd19476 154 YFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLT 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 149029485 285 AYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 323
Cdd:cd19476 232 DPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
10-414 |
1.92e-127 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 381.31 E-value: 1.92e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 10 GMSLNLEPDN-VGVVVFGNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIdgkgPVGSKIRRR----------- 77
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEV----PVGLLTRSRalleseqtlgk 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 78 VGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQ 157
Cdd:PTZ00185 156 VDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVISIYVSIGQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 158 KRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRP 237
Cdd:PTZ00185 236 RCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 238 PGREAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVG 317
Cdd:PTZ00185 316 PGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 318 LSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATqqlLSRGVRLTELLKQGQysPMAIEEQVAVIYAG 397
Cdd:PTZ00185 396 LSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNALVSLYAC 470
|
410
....*....|....*..
gi 149029485 398 VRGYLDKLEPSKITKFE 414
Cdd:PTZ00185 471 LNGYLDDVKVNYAKLYE 487
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
98-321 |
1.87e-117 |
|
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: 342.41 E-value: 1.87e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 98 GIKAVDSLVPIGRGQRELIIGDRQTGKTSIAiDTIINQKRFNdgtdekkklYCIYVAIGQKRSTVAQLVKRLTDADAMKY 177
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD---------VVVYALIGERGREVREFIEELLGSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 178 TIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLER 257
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149029485 258 AAKMNDsfGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVS 321
Cdd:pfam00006 151 AGRVKG--KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
41-384 |
5.97e-101 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 311.14 E-value: 5.97e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 41 GAIVDVPVGDEL---------------LGRVVDALGNAI---------DGKGPVGSKIRRrvglKAPGIIPRISVREPMQ 96
Cdd:PRK07165 53 NEKGKIKINDELielnntnkvktskeyFGKIIDIDGNIIypeaqnplsKKFLPNTSSIFN----LAHGLMTVKTLNEQLY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 97 TGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRfndgTDEKkklyCIYVAIGQKRSTVAQLVKRLTDADAMK 176
Cdd:PRK07165 129 TGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKN----TNVK----CIYVAIGQKRENLSRIYETLKEHDALK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 177 YTIVVSAtASDAAPLQYLAPYSGCSMGE---YFRDngkhALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSR 253
Cdd:PRK07165 201 NTIIIDA-PSTSPYEQYLAPYVAMAHAEnisYNDD----VLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 254 LLERAAKMNdsfGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMK 333
Cdd:PRK07165 276 LLERAGKFK---NRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTIT 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 149029485 334 QVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSP 384
Cdd:PRK07165 353 KVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKGKMIEKMFNQKGFSL 403
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
332-457 |
8.71e-68 |
|
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) 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 alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349748 [Multi-domain] Cd Length: 126 Bit Score: 212.23 E-value: 8.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 332 MKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKIT 411
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 149029485 412 KFESAFLSHVVSQHQSLLGNIRSDGKISEQSDAKLKEIVTNFLAGF 457
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
328-453 |
2.69e-66 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 208.45 E-value: 2.69e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 328 QTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEP 407
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 149029485 408 SKITKFESAFLSHVVSQHQSLLGNIRSDGKISEQSDAKLKEIVTNF 453
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
46-323 |
8.32e-50 |
|
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: 170.43 E-value: 8.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 46 VPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 125
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 126 siaidTIINQKRFNDGTDekkklycIYVA--IGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMG 203
Cdd:cd01136 82 -----TLLGMIARNTDAD-------VNVIalIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 204 EYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmndsFGGGSLTALPVIETQAGDV 283
Cdd:cd01136 150 EYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN----GEKGSITAFYTVLVEGDDF 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 149029485 284 SAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 323
Cdd:cd01136 226 NDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
37-399 |
6.19e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 164.93 E-value: 6.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 37 VKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELI 116
Cdd:PRK06936 88 VSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 117 IGDRQTGKTSIaIDTIINqkrfndGTDEKkklYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAP 196
Cdd:PRK06936 168 FAAAGGGKSTL-LASLIR------SAEVD---VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 197 YSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNDSfggGSLTALPVI 276
Cdd:PRK06936 238 FVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG-QSDK---GSITALYTV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 277 ETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFG 356
Cdd:PRK06936 314 LVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIG 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 149029485 357 S---DLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVR 399
Cdd:PRK06936 394 EyqkGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETLTQ 439
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
22-389 |
1.05e-45 |
|
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: 164.05 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 22 VVVFGNDKL----------IKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIPRISV 91
Cdd:COG1157 58 VVGFRGDRVllmplgdlegISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 92 REPMQTGIKAVDSLVPIGRGQReliIGdr---qtGKTS----IA----IDTIInqkrfndgtdekkklyciyVA-IGQKR 159
Cdd:COG1157 138 TEPLDTGVRAIDGLLTVGRGQR---IGifagsgvGKSTllgmIArnteADVNV-------------------IAlIGERG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 160 STVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPG 239
Cdd:COG1157 196 REVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 240 REAYPGDVFYLHSRLLERAAKmndsFGGGSLTAL------------PVIETqagdvsayiptnVISITDGQIFLETELFY 307
Cdd:COG1157 276 TRGYPPSVFALLPRLLERAGN----GGKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 308 KGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVA------AFAQfGSD--LDAAtqqlLSRGVRLTELLKQ 379
Cdd:COG1157 340 RGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEdlirigAYQP-GSDpeLDEA----IALIPAIEAFLRQ 414
|
410
....*....|
gi 149029485 380 GQYSPMAIEE 389
Cdd:COG1157 415 GMDERVSFEE 424
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
46-356 |
5.82e-44 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 159.93 E-value: 5.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 46 VPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 125
Cdd:PRK09099 98 VPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 126 SIaidtiinQKRFNDGTDekkklyC---IYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSM 202
Cdd:PRK09099 178 TL-------MGMFARGTQ------CdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAI 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 203 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNDSfggGSLTALPVIETQAGD 282
Cdd:PRK09099 245 AEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-MGET---GSITALYTVLAEDES 320
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149029485 283 VSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFG 356
Cdd:PRK09099 321 GSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVG 394
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
31-394 |
6.48e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 159.50 E-value: 6.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 31 IKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDG----KGPVGSKIRRrvglKAPGIIPRISVREPMQTGIKAVDSLV 106
Cdd:PRK07721 78 IAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGsalpKGLAPVSTDQ----DPPNPLKRPPIREPMEVGVRAIDSLL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 107 PIGRGQRELIIGDRQTGKTS----IAIDTiinQKRFNdgtdekkklycIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVS 182
Cdd:PRK07721 154 TVGKGQRVGIFAGSGVGKSTlmgmIARNT---SADLN-----------VIALIGERGREVREFIERDLGPEGLKRSIVVV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 183 ATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmN 262
Cdd:PRK07721 220 ATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGT-N 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 263 DSfggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLE 342
Cdd:PRK07721 299 AS---GSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFREL 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 149029485 343 LAQYREVAAFAQFGS-------DLDAATQqllsRGVRLTELLKQGQYSPMAIEEQVAVI 394
Cdd:PRK07721 376 LSTYQNSEDLINIGAykrgssrEIDEAIQ----FYPQIISFLKQGTDEKATFEESIQAL 430
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
6-385 |
9.91e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 159.21 E-value: 9.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 6 SGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGlKAPGI 85
Cdd:PRK06820 59 QGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWRELDC-PPPSP 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 86 IPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAidtiinqKRFNDGTDEKkklyCIYVA-IGQKRSTVAQ 164
Cdd:PRK06820 138 LTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLL-------GMLCADSAAD----VMVLAlIGERGREVRE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 165 LVKRLTDADAMKYTIVVSATaSDAAPLQYL-APYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY 243
Cdd:PRK06820 207 FLEQVLTPEARARTVVVVAT-SDRPALERLkGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 244 PGDVFYLHSRLLERAAKMNDsfggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 323
Cdd:PRK06820 286 PPSVFANLPRLLERTGNSDR----GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRI 361
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149029485 324 GSAAQTRAMKQVAGTMKLELAQYREVAAFAQFG---SDLDAATQQLLSRGVRLTELLKQ--GQYSPM 385
Cdd:PRK06820 362 MPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGeyqAGEDLQADEALQRYPAICAFLQQdhSETAHL 428
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
46-400 |
2.21e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 147.57 E-value: 2.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 46 VPVGDELLGRVVDALGNAIDGKGPVgsKIRRRVGLKAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTG 123
Cdd:PRK05688 103 LPMGMSMLGRVLDGAGRALDGKGPM--KAEDWVPMDGPTINPlnRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 124 KtSIAIDTIinqKRFNDGTdekkklycIYVA--IGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAaPLQYLAPYSGCS 201
Cdd:PRK05688 181 K-SVLLGMM---TRFTEAD--------IIVVglIGERGREVKEFIEHILGEEGLKRSVVVASPADDA-PLMRLRAAMYCT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 202 -MGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNDSFGGGSLTALPVIETQA 280
Cdd:PRK05688 248 rIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 281 GDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYRE------VAAFAQ 354
Cdd:PRK05688 326 DDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQsrdlisVGAYVA 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 149029485 355 FGsdlDAATQQLLSRGVRLTELLKQG--QYSPMA-IEEQVAVIYAGVRG 400
Cdd:PRK05688 406 GG---DPETDLAIARFPHLVQFLRQGlrENVSLAqSREQLAAIFAPAAG 451
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
10-380 |
1.76e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 144.83 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 10 GMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVgLKAP------ 83
Cdd:PRK08472 56 GMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPI-MKAPiaamkr 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 84 GIIprisvREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKtSIAIDTIINqkrfndGTDEKKKLyciyVA-IGQKRSTV 162
Cdd:PRK08472 135 GLI-----DEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGK-STLMGMIVK------GCLAPIKV----VAlIGERGREI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 163 AQLVKRLTDADaMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREA 242
Cdd:PRK08472 199 PEFIEKNLGGD-LENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 243 YPGDVFYLHSRLLERAAKMNdsfGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSR 322
Cdd:PRK08472 278 YPPSVLSLLPQLMERAGKEE---GKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASR 354
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149029485 323 VGSAAQTRAMKQVAGTMKLELAQYRE------VAAFaQFGSD--LDAAtqqlLSRGVRLTELLKQG 380
Cdd:PRK08472 355 VMNDIISPEHKLAARKFKRLYSLLKEnevlirIGAY-QKGNDkeLDEA----ISKKEFMEQFLKQN 415
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
36-396 |
1.28e-36 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 139.36 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 36 IVKRTGAIVDVPVGDELLGRVVDALGNAI---DGKGPVGSKIRRR-VGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRG 111
Cdd:PRK08149 72 VLKPTGKPLSVWVGEALLGAVLDPTGKIVerfDAPPTVGPISEERvIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 112 QRELIIGDRQTGKTSIaIDTIINQKRFNdgtdekkklycIYVA--IGQKRSTVAQLVKRLTDADAMKYTIVVSATaSDAA 189
Cdd:PRK08149 152 QRMGIFASAGCGKTSL-MNMLIEHSEAD-----------VFVIglIGERGREVTEFVESLRASSRREKCVLVYAT-SDFS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 190 PLQYL-APYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmndsFGGG 268
Cdd:PRK08149 219 SVDRCnAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGA----TLAG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 269 SLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYRE 348
Cdd:PRK08149 295 SITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEE 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 149029485 349 VAAFAQFG-------SDLDAATQQllsRGVrLTELLKQGQYSPMAIEEQVAVIYA 396
Cdd:PRK08149 375 LQLFIDLGeyrrgenADNDRAMDK---RPA-LEAFLKQDVAEKSSFSDTLERLNE 425
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
46-380 |
1.36e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 139.84 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 46 VPVGDELLGRVVDALGNAIDGKGPVGSKirRRVGLKAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTG 123
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIYTD--QRASRHSPPINPlsRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 124 KtSIAIDTIINqkrfndGTDEKkklyCIYVA-IGQKRSTVAQLVKRLTDADAMKYTIVVSATAsDAAPLQYLapySGC-- 200
Cdd:PRK08972 175 K-SVLLGMMTR------GTTAD----VIVVGlVGERGREVKEFIEEILGEEGRARSVVVAAPA-DTSPLMRL---KGCet 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 201 --SMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNDSFGGGSLTALPVIET 278
Cdd:PRK08972 240 atTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAG--NGGPGQGSITAFYTVLT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 279 QAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYRE------VAAF 352
Cdd:PRK08972 318 EGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQnrdlisIGAY 397
|
330 340
....*....|....*....|....*...
gi 149029485 353 AQfGSdlDAATQQLLSRGVRLTELLKQG 380
Cdd:PRK08972 398 KQ-GS--DPRIDNAIRLQPAMNAFLQQT 422
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
46-388 |
2.70e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 138.55 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 46 VPVGDELLGRVVDALGNAIDGKgPVGSKIRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 125
Cdd:PRK07594 91 VPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 126 siaidTIINQKRFNDGTDEKkklycIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEY 205
Cdd:PRK07594 170 -----TLLAMLCNAPDADSN-----VLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEF 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 206 FRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNDSfggGSLTALPVIETQAGDVSA 285
Cdd:PRK07594 240 FRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-MGEK---GSITAFYTVLVEGDDMNE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 286 YIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGS---DLDAA 362
Cdd:PRK07594 316 PLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEyqrGVDTD 395
|
330 340
....*....|....*....|....*.
gi 149029485 363 TQQLLSRGVRLTELLKQGQYSPMAIE 388
Cdd:PRK07594 396 TDKAIDTYPDICTFLRQSKDEVCGPE 421
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
48-392 |
1.46e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 136.56 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 48 VGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKtSI 127
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGK-SV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 128 AIDTIinqkrfndgTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATAsDAAPLQYLAPYSGC-SMGEYF 206
Cdd:PRK07196 171 LLGMI---------TRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPA-DESPLMRIKATELChAIATYY 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 207 RDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmnDSFGGGSLTALPVIETQAGDVSAY 286
Cdd:PRK07196 241 RDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQDP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 287 IPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDL---DAAT 363
Cdd:PRK07196 318 IVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVagaDPMA 397
|
330 340
....*....|....*....|....*....
gi 149029485 364 QQLLSRGVRLTELLKQGQYSPMAIEEQVA 392
Cdd:PRK07196 398 DQAVHYYPAITQFLRQEVGHPALFSASVE 426
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
16-379 |
2.67e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 133.58 E-value: 2.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 16 EPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPvGDELLGRVVDALGNAIDGKGPVGSKIRRR-VGLKAPGIIPRISVREP 94
Cdd:PRK06002 70 DPDGVTVKPFEPRIEIGLGDAVFRKGPLRIRP-DPSWKGRVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 95 MQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSI--------AIDTIInqkrfndgtdekkklyciyVA-IGQKRSTVAQL 165
Cdd:PRK06002 149 LRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLlamlaradAFDTVV-------------------IAlVGERGREVREF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 166 VKRlTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPG 245
Cdd:PRK06002 210 LED-TLADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 246 DVFYLHSRLLERAAKMNDsfGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGS 325
Cdd:PRK06002 289 SVFSELPRLLERAGPGAE--GGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLAR 366
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149029485 326 AAQTRAMKQVAGTMKLELAQYRE------VAAFaQFGSD--LDAATQQLlsrgVRLTELLKQ 379
Cdd:PRK06002 367 HAWTPEQRKLVSRLKSMIARFEEtrdlrlIGGY-RAGSDpdLDQAVDLV----PRIYEALRQ 423
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
46-322 |
6.00e-33 |
|
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: 125.80 E-value: 6.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 46 VPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGlkAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTG 123
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDIN--GPPINPvaRIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 124 KTSIAIdTIINQKRFNDGTDEKKklyCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMG 203
Cdd:cd01135 82 HNELAA-QIARQAGVVGSEENFA---IVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 204 EYFR-DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMNDSfgGGSLTALPVIETQ 279
Cdd:cd01135 158 EYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTMP 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 149029485 280 AGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSR 322
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
46-366 |
9.75e-31 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 123.35 E-value: 9.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 46 VPVGDELLGRVVDALGNAIDGKGPvgSKIRRRVGLKAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTG 123
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPA--PDTGETGALITPPFNPlqRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 124 KtSIAIDTIinqKRFNDGTdekkklyCIYVA-IGQKRSTVAQLVKRLTDADAMKYTIVVSATAsDAAPLQYL--APYSgC 200
Cdd:PRK07960 188 K-SVLLGMM---ARYTQAD-------VIVVGlIGERGREVKDFIENILGAEGRARSVVIAAPA-DVSPLLRMqgAAYA-T 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 201 SMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNDSFGGGSLTALPVIETQA 280
Cdd:PRK07960 255 RIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG--NGISGGGSITAFYTVLTEG 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 281 GDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSA-------AQTRAMKQ-----------------VA 336
Cdd:PRK07960 333 DDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAlideqhyARVRQFKQllssfqrnrdlvsvgayAK 412
|
330 340 350
....*....|....*....|....*....|....*..
gi 149029485 337 GTMKL---ELAQYREVAAFAQFG----SDLDAATQQL 366
Cdd:PRK07960 413 GSDPMldkAIALWPQLEAFLQQGiferADWEDSLQAL 449
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
13-395 |
1.87e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 122.39 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 13 LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGkgPVGSKIRRRVGLKAPGI--IPRIS 90
Cdd:PRK06793 58 IAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIhaFEREE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 91 VREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTsiaidTIINQKRFNDGTDEKkklycIYVAIGQKRSTVAQLVKRLT 170
Cdd:PRK06793 136 ITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKS-----TLLGMIAKNAKADIN-----VISLVGERGREVKDFIRKEL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 171 DADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPgreaYPGDVFYL 250
Cdd:PRK06793 206 GEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 251 HS---RLLERAAKMNDsfggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAA 327
Cdd:PRK06793 282 ESymkKLLERSGKTQK----GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEI 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149029485 328 QTRAMKQVAGTMKLELAQYREVAAFAQFGS----DLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIY 395
Cdd:PRK06793 358 VSPNHWQLANEMRKILSIYKENELYFKLGTiqenAENAYIFECKNKVEGINTFLKQGRSDSFQFDDIVEAMH 429
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
46-386 |
8.48e-30 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 120.39 E-value: 8.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 46 VPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 125
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 126 SIaIDTIinqkrfndGTDEKKKLYCIYVaIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEY 205
Cdd:PRK05922 172 SL-LSTI--------AKGSKSTINVIAL-IGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 206 FRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmNDSfggGSLTALPVIETQAGDVSA 285
Cdd:PRK05922 242 FRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-NDK---GSITALYAILHYPNHPDI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 286 YIPTnVISITDGQIFL---ETELFykgiRPAINVGLSVSRvgSAAQTRAMKQVAGTMKLE--LAQYREVAAFAQFGSDLD 360
Cdd:PRK05922 318 FTDY-LKSLLDGHFFLtpqGKALA----SPPIDILTSLSR--SARQLALPHHYAAAEELRslLKAYHEALDIIQLGAYVP 390
|
330 340
....*....|....*....|....*.
gi 149029485 361 AATQQlLSRGVRLTELLKQGQYSPMA 386
Cdd:PRK05922 391 GQDAH-LDRAVKLLPSIKQFLSQPLS 415
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
28-323 |
1.05e-27 |
|
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: 114.82 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 28 DKLIKeGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVP 107
Cdd:TIGR01039 61 DGLVR-GLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 108 IGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGtdekkklYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASD 187
Cdd:TIGR01039 140 YAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGG-------YSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 188 AAPLQYLAPYSGCSMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmndSFG 266
Cdd:TIGR01039 213 PPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERIT----STK 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 149029485 267 GGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 323
Cdd:TIGR01039 289 TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRL 345
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
9-389 |
1.69e-27 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 114.15 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 9 KGMSLNLEPDNVGVVVF-GNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIP 87
Cdd:PRK04196 40 RGQVLEVSEDKAVVQVFeGTTGLDLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 88 RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDtIINQKRFNdGTDEKkkLYCIYVAIGQKRSTVAQLVK 167
Cdd:PRK04196 120 REYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQ-IARQAKVL-GEEEN--FAVVFAAMGITFEEANFFME 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 168 RLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR-DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGd 246
Cdd:PRK04196 196 DFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 247 vfYLHSRL---LERAAKMNDSfgGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSR- 322
Cdd:PRK04196 275 --YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRl 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149029485 323 ----VGsAAQTRA-MKQVAGTMKLELAQYREVAAFAQF-GSD-LDAATQQLLSRGVRL-TELLKQGQYSPMAIEE 389
Cdd:PRK04196 351 mkdgIG-EGKTREdHKDVANQLYAAYARGKDLRELAAIvGEEaLSERDRKYLKFADAFeREFVNQGFDENRSIEE 424
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
53-389 |
1.93e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 110.84 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 53 LGRVVDALGNAIDGKGPVGSKIRRRVgLKA--PGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSI--- 127
Cdd:PRK08927 99 LGRVVNALGEPIDGKGPLPQGPVPYP-LRAppPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLlsm 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 128 -----AIDTIInqkrfndgtdekkklycIYVaIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSM 202
Cdd:PRK08927 178 larnaDADVSV-----------------IGL-IGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 203 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmnDSFGGGSLTALPVIETQAGD 282
Cdd:PRK08927 240 AEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGP--GPIGEGTITGLFTVLVDGDD 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 283 VSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSdLDAA 362
Cdd:PRK08927 318 HNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGA-YRAG 396
|
330 340 350
....*....|....*....|....*....|.
gi 149029485 363 TQQLLSRGVR----LTELLKQGQYSPMAIEE 389
Cdd:PRK08927 397 SDPEVDEAIRlnpaLEAFLRQGKDEATSLAE 427
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
40-332 |
2.04e-23 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 102.49 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 40 TGAIVDVPVGDELLGRVVDALGNAIDGKGPV---------GSKIRRRVglkapgiipRISVREPMQTGIKAVDSLVPIGR 110
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVlaedyldinGQPINPYA---------RIYPEEMIQTGISAIDVMNSIAR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 111 GQRELIIGDRQTGKTSIAIDTI----INQKRFNDGTDEKKKLYCI-YVAIGQKRSTvAQLVKR-LTDADAMKYTIVVSAT 184
Cdd:TIGR01040 141 GQKIPIFSAAGLPHNEIAAQICrqagLVKLPTKDVHDGHEDNFAIvFAAMGVNMET-ARFFKQdFEENGSMERVCLFLNL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 185 ASDAAPLQYLAPYSGCSMGEYFR-DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMND 263
Cdd:TIGR01040 220 ANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEG 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149029485 264 SfgGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAM 332
Cdd:TIGR01040 300 R--NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
332-399 |
6.13e-23 |
|
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: 91.74 E-value: 6.13e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 332 MKQVAGTMKLELAQYREVAAFAQFGSD--LDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVR 399
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
46-323 |
6.66e-21 |
|
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: 92.28 E-value: 6.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 46 VPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 125
Cdd:cd01133 2 VPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 126 SIAIDTIINQKRFNDGtdekkklYCIYVAIGQKRSTVAQLVkrltdaDAMKYTIVVSATASDAAPLQY-----------L 194
Cdd:cd01133 82 VLIMELINNIAKAHGG-------YSVFAGVGERTREGNDLY------HEMKESGVINLDGLSKVALVYgqmneppgaraR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 195 APYSGCSMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmndSFGGGSLTAL 273
Cdd:cd01133 149 VALTGLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERIT----STKKGSITSV 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 149029485 274 PVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 323
Cdd:cd01133 225 QAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
13-301 |
4.18e-19 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 89.32 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 13 LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGkGPvgSKIRRRVGLKAPGIIP--RIS 90
Cdd:PRK02118 43 IRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GP--ELEGEPIEIGGPSVNPvkRIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 91 VREPMQTGIKAVD---SLV-----PI----GRGQRELIIgdrqtgktSIAIDTiinqkrfndgtdEKKKLycIYVAIGQK 158
Cdd:PRK02118 120 PREMIRTGIPMIDvfnTLVesqkiPIfsvsGEPYNALLA--------RIALQA------------EADII--ILGGMGLT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 159 RSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR-DNGKHALIIYDDLSKQAVAYRQMSLLLRRP 237
Cdd:PRK02118 178 FDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQI 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149029485 238 PGREAYPGDvfyLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFL 301
Cdd:PRK02118 258 PSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
1-42 |
5.08e-18 |
|
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) 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, in 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 alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349740 [Multi-domain] Cd Length: 67 Bit Score: 77.88 E-value: 5.08e-18
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 149029485 1 MVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGA 42
Cdd:cd18116 26 LVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
34-111 |
5.25e-17 |
|
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: 82.83 E-value: 5.25e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149029485 34 GDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRG 111
Cdd:COG0055 69 GMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKG 146
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
93-322 |
2.62e-16 |
|
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: 79.16 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 93 EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTsiaidtIINQK--RFNDgTDekkklYCIYVAIGQKRSTVA------- 163
Cdd:cd01134 58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKT------VISQSlsKWSN-SD-----VVIYVGCGERGNEMAevleefp 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 164 QLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY 243
Cdd:cd01134 126 ELKDPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGY 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 244 PGdvfYLHSRL---LERA--AKMNDSFG-GGSLTALPVIETQAGDVSAYIPTNVISITdgQIF--LETELFYKGIRPAIN 315
Cdd:cd01134 206 PA---YLGARLaefYERAgrVRCLGSPGrEGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSIN 280
|
....*..
gi 149029485 316 VGLSVSR 322
Cdd:cd01134 281 WLISYSK 287
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
151-335 |
5.48e-11 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 65.04 E-value: 5.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 151 IYVAIGQKRSTVAQLVK---RLTDADA----MKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQ 223
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEefpKLKDPKTgkplMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 224 AVAYRQMSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDG 297
Cdd:PRK14698 766 AEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKV 842
|
170 180 190
....*....|....*....|....*....|....*...
gi 149029485 298 QIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQV 335
Cdd:PRK14698 843 FWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNV 880
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
31-315 |
7.11e-11 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 63.91 E-value: 7.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 31 IKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGII---PRISVREpmqTGIKAVDSLVP 107
Cdd:CHL00060 81 LMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTKLSIFE---TGIKVVDLLAP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 108 IGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDG----------TDEKKKLYciyvaIGQKRSTVAQLVKRLTDADAMKY 177
Cdd:CHL00060 158 YRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGvsvfggvgerTREGNDLY-----MEMKESGVINEQNIAESKVALVY 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 178 ---------TIVVSATASdaaplqylapysgcSMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDV 247
Cdd:CHL00060 233 gqmneppgaRMRVGLTAL--------------TMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTL 298
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149029485 248 FYLHSRLLERAAKMNDsfggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAIN 315
Cdd:CHL00060 299 STEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 362
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
88-272 |
6.60e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 57.87 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 88 RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT----SIAidtiinqkRFNDgTDekkklYCIYVAIGQKRSTVA 163
Cdd:PRK04192 204 KLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTvtqhQLA--------KWAD-AD-----IVIYVGCGERGNEMT 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149029485 164 QLVK---RLTDADA----MKYTIVVSAT-----ASDAAPLqylapYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMS 231
Cdd:PRK04192 270 EVLEefpELIDPKTgrplMERTVLIANTsnmpvAAREASI-----YTGITIAEYYRDMGYDVLLMADSTSRWAEALREIS 344
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 149029485 232 LLLRRPPGREAYPGdvfYLHSRL---LERA--AKMNDSfGGGSLTA 272
Cdd:PRK04192 345 GRLEEMPGEEGYPA---YLASRLaefYERAgrVKTLGG-EEGSVTI 386
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
1-41 |
1.70e-08 |
|
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: 51.01 E-value: 1.70e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 149029485 1 MVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTG 41
Cdd:pfam02874 29 LVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| |
