|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
69-478 |
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: 852.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI 148
Cdd:COG0056 101 EALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 149 DTIINQKrfndgtdeKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDN 228
Cdd:COG0056 181 DTIINQK--------GKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 229 GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPT 308
Cdd:COG0056 253 GKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPT 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 309 NVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR 388
Cdd:COG0056 333 NVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLER 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 389 GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQSLLGNIRSDGKISEQSDAKLKEI 468
Cdd:COG0056 413 GERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGKLDDEIEEKLKAA 492
|
410
....*....|
gi 148677500 469 VTNFLAGFEP 478
Cdd:COG0056 493 IEEFKKTFAA 502
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
69-478 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 850.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI 148
Cdd:PRK09281 101 EALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 149 DTIINQKrfndgtdeKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDN 228
Cdd:PRK09281 181 DTIINQK--------GKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDN 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 229 GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPT 308
Cdd:PRK09281 253 GKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPT 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 309 NVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR 388
Cdd:PRK09281 333 NVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLER 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 389 GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQSLLGNIRSDGKISEQSDAKLKEI 468
Cdd:PRK09281 413 GQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKDLSDEIEAKLKAA 492
|
410
....*....|
gi 148677500 469 VTNFLAGFEP 478
Cdd:PRK09281 493 IEEFKKTFAA 502
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
69-478 |
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: 713.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI 148
Cdd:TIGR00962 100 DGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAI 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 149 DTIINQKrfndgtdeKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDN 228
Cdd:TIGR00962 180 DTIINQK--------DSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDN 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 229 GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPT 308
Cdd:TIGR00962 252 GKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIETQAGDVSAYIPT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 309 NVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR 388
Cdd:TIGR00962 332 NVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASDLDEATKKQLER 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 389 GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQSLLGNIRSDGKISEQSDAKLKEI 468
Cdd:TIGR00962 412 GQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKLTEELEAKLKEA 491
|
410
....*....|
gi 148677500 469 VTNFLAGFEP 478
Cdd:TIGR00962 492 LKNFKKTFAW 501
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
69-476 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 668.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI 148
Cdd:CHL00059 80 EAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVAT 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 149 DTIINQKrfndgtdeKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDN 228
Cdd:CHL00059 160 DTILNQK--------GQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 229 GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPT 308
Cdd:CHL00059 232 GRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPT 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 309 NVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR 388
Cdd:CHL00059 312 NVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLAR 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 389 GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQSLLGNIRSDGKISEQSDAKLKEI 468
Cdd:CHL00059 392 GQRLRELLKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEA 471
|
....*...
gi 148677500 469 VTNFLAGF 476
Cdd:CHL00059 472 IQEQLELF 479
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
69-478 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 643.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI 148
Cdd:PRK13343 101 DGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 149 DTIINQKrfndgtdeKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDN 228
Cdd:PRK13343 181 DAIINQK--------DSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 229 GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPT 308
Cdd:PRK13343 253 GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETLAGELSAYIPT 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 309 NVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR 388
Cdd:PRK13343 333 NLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLLDAGTQKQITR 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 389 GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQSLLGNIRSDGKISEQSDAKLKEI 468
Cdd:PRK13343 413 GRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRELDEAWLAALEEI 492
|
410
....*....|
gi 148677500 469 VTNFLAGFEP 478
Cdd:PRK13343 493 LREAGERFAA 502
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
69-343 |
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: 601.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI 148
Cdd:cd01132 8 EALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTAIAI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 149 DTIINQKRfndgtdekKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDN 228
Cdd:cd01132 88 DTIINQKG--------KKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 229 GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPT 308
Cdd:cd01132 160 GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPT 239
|
250 260 270
....*....|....*....|....*....|....*
gi 148677500 309 NVISITDGQIFLETELFYKGIRPAINVGLSVSRVG 343
Cdd:cd01132 240 NVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
69-460 |
1.03e-162 |
|
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: 469.25 E-value: 1.03e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI 148
Cdd:TIGR03324 101 DGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDRQTGKTAIAI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 149 DTIINQKRFNdgtdekkkLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDN 228
Cdd:TIGR03324 181 DTILNQKGRN--------VLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSIGEHFMEQ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 229 GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPT 308
Cdd:TIGR03324 253 GRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQNISAYIPT 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 309 NVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR 388
Cdd:TIGR03324 333 NLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDENTRKTIEH 412
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148677500 389 GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQSLLGNIRSDGKISEQ 460
Cdd:TIGR03324 413 GRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSDE 484
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
69-342 |
1.98e-133 |
|
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: 386.04 E-value: 1.98e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI 148
Cdd:cd19476 6 PELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 149 DTIINQKrfndgtdEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDN 228
Cdd:cd19476 86 QLARNQA-------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 229 GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDsfGGGSLTALPVIETQAGDVSAYIPT 308
Cdd:cd19476 159 GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPD 236
|
250 260 270
....*....|....*....|....*....|....
gi 148677500 309 NVISITDGQIFLETELFYKGIRPAINVGLSVSRV 342
Cdd:cd19476 237 NTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
71-433 |
1.59e-118 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 359.35 E-value: 1.59e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 71 LLGRVVDALGNAIdgkgPIGSKTRRR-----------VGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDR 139
Cdd:PTZ00185 123 VLGKVVNPLGHEV----PVGLLTRSRalleseqtlgkVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 140 QTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGC 219
Cdd:PTZ00185 199 QTGKTSIAVSTIINQVRINQQILSKNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 220 SMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQA 299
Cdd:PTZ00185 279 TMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLS 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 300 GDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLD 379
Cdd:PTZ00185 359 NDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQ 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 148677500 380 AATqqlLSRGVRLTELLKQGQysPMAIEEQVAVIYAGVRGYLDKLEPSKITKFE 433
Cdd:PTZ00185 439 TVP---MIRGARFVALFNQKN--PSFFMNALVSLYACLNGYLDDVKVNYAKLYE 487
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
117-340 |
2.91e-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: 342.80 E-value: 2.91e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 117 GIKAVDSLVPIGRGQRELIIGDRQTGKTSIAiDTIINQKRFNdgtdekkklYCIYVAIGQKRSTVAQLVKRLTDADAMKY 196
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD---------VVVYALIGERGREVREFIEELLGSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 197 TIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLER 276
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148677500 277 AAKMNDsfGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVS 340
Cdd:pfam00006 151 AGRVKG--KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
100-403 |
1.70e-100 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 310.37 E-value: 1.70e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 100 KAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRfndgTDEKkklyCIYVAIGQKRS 179
Cdd:PRK07165 113 LAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKN----TNVK----CIYVAIGQKRE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 180 TVAQLVKRLTDADAMKYTIVVSAtASDAAPLQYLAPYSGCSMGE---YFRDngkhALIIYDDLSKQAVAYRQMSLLLRRP 256
Cdd:PRK07165 185 NLSRIYETLKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAEnisYNDD----VLIVFDDLTKHANIYREIALLTNKP 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 257 PGREAYPGDVFYLHSRLLERAAKMNdsfGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVG 336
Cdd:PRK07165 260 VGKEAFPGDMFFAHSKLLERAGKFK---NRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDID 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148677500 337 LSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSP 403
Cdd:PRK07165 337 LSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKGKMIEKMFNQKGFSL 403
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
351-476 |
2.43e-67 |
|
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: 211.46 E-value: 2.43e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 351 MKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKIT 430
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 148677500 431 KFENAFLSHVISQHQSLLGNIRSDGKISEQSDAKLKEIVTNFLAGF 476
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
347-472 |
1.03e-65 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 207.29 E-value: 1.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 347 QTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEP 426
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 148677500 427 SKITKFENAFLSHVISQHQSLLGNIRSDGKISEQSDAKLKEIVTNF 472
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
69-342 |
9.82e-47 |
|
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: 162.73 E-value: 9.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTsiai 148
Cdd:cd01136 6 DGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 149 dTIINQKRFNDGTDekkklycIYVA--IGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR 226
Cdd:cd01136 82 -TLLGMIARNTDAD-------VNVIalIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 227 DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmndsFGGGSLTALPVIETQAGDVSAYI 306
Cdd:cd01136 154 DQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN----GEKGSITAFYTVLVEGDDFNDPI 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 148677500 307 PTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 342
Cdd:cd01136 230 ADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
69-418 |
6.64e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 154.53 E-value: 6.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIaI 148
Cdd:PRK06936 101 EHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTL-L 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 149 DTIINqkrfndGTDEKkklYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDN 228
Cdd:PRK06936 180 ASLIR------SAEVD---VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 229 GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNDSfggGSLTALPVIETQAGDVSAYIPT 308
Cdd:PRK06936 251 GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG-QSDK---GSITALYTVLVEGDDMTEPVAD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 309 NVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGS---DLDAATQQL 385
Cdd:PRK06936 327 ETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEyqkGQDKEADQA 406
|
330 340 350
....*....|....*....|....*....|...
gi 148677500 386 LSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVR 418
Cdd:PRK06936 407 IERIGAIRGFLRQGTHELSHFNETLNLLETLTQ 439
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
71-375 |
1.63e-41 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 153.39 E-value: 1.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 71 LLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIaidt 150
Cdd:PRK09099 104 LLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTL---- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 151 iinQKRFNDGTDekkklyC---IYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRD 227
Cdd:PRK09099 180 ---MGMFARGTQ------CdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 228 NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNDSfggGSLTALPVIETQAGDVSAYIP 307
Cdd:PRK09099 251 RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-MGET---GSITALYTVLAEDESGSDPIA 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148677500 308 TNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFG 375
Cdd:PRK09099 327 EEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVG 394
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
69-408 |
1.21e-40 |
|
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: 150.95 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQReliIGdr---qtGKTS 145
Cdd:COG1157 96 DGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR---IGifagsgvGKST 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 146 ----IA----IDTIInqkrfndgtdekkklyciyVA-IGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPY 216
Cdd:COG1157 173 llgmIArnteADVNV-------------------IAlIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAY 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 217 SGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmndsFGGGSLTAL---- 292
Cdd:COG1157 234 TATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN----GGKGSITAFytvl 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 293 --------PVIETqagdvsayiptnVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQ 364
Cdd:COG1157 310 vegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLAR 377
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 148677500 365 YREVA------AFAQfGSD--LDAAtqqlLSRGVRLTELLKQGQYSPMAIEE 408
Cdd:COG1157 378 YEENEdlirigAYQP-GSDpeLDEA----IALIPAIEAFLRQGMDERVSFEE 424
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
70-404 |
1.95e-39 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 148.04 E-value: 1.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 70 ELLGRVVDALGNAIDGKGPIGSKTRRRVGlKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAid 149
Cdd:PRK06820 104 DLAGRILDGLGAPIDGGPPLTGQWRELDC-PPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLL-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 150 tiinqKRFNDGTDEKkklyCIYVA-IGQKRSTVAQLVKRLTDADAMKYTIVVSATaSDAAPLQYL-APYSGCSMGEYFRD 227
Cdd:PRK06820 181 -----GMLCADSAAD----VMVLAlIGERGREVREFLEQVLTPEARARTVVVVAT-SDRPALERLkGLSTATTIAEYFRD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 228 NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDsfggGSLTALPVIETQAGDVSAYIP 307
Cdd:PRK06820 251 RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDR----GSITAFYTVLVEGDDMNEPVA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 308 TNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFG---SDLDAATQQ 384
Cdd:PRK06820 327 DEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGeyqAGEDLQADE 406
|
330 340
....*....|....*....|..
gi 148677500 385 LLSRGVRLTELLKQ--GQYSPM 404
Cdd:PRK06820 407 ALQRYPAICAFLQQdhSETAHL 428
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
70-413 |
6.72e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 146.41 E-value: 6.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 70 ELLGRVVDALGNAIDG----KGPIGSKTRRrvglKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTS 145
Cdd:PRK07721 98 GLIGQVLDALGEPLDGsalpKGLAPVSTDQ----DPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKST 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 146 ----IAIDTiinQKRFNdgtdekkklycIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSM 221
Cdd:PRK07721 174 lmgmIARNT---SADLN-----------VIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 222 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmNDSfggGSLTALPVIETQAGD 301
Cdd:PRK07721 240 AEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGT-NAS---GSITAFYTVLVDGDD 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 302 VSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGS----- 376
Cdd:PRK07721 316 MNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAykrgs 395
|
330 340 350
....*....|....*....|....*....|....*....
gi 148677500 377 --DLDAATQqllsRGVRLTELLKQGQYSPMAIEEQVAVI 413
Cdd:PRK07721 396 srEIDEAIQ----FYPQIISFLKQGTDEKATFEESIQAL 430
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
69-419 |
5.82e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 144.10 E-value: 5.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIgsKTRRRVGLKAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKtSI 146
Cdd:PRK05688 107 MSMLGRVLDGAGRALDGKGPM--KAEDWVPMDGPTINPlnRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK-SV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 147 AIDTIinqKRFNDGTdekkklycIYVA--IGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAaPLQYLAPYSGCS-MGE 223
Cdd:PRK05688 184 LLGMM---TRFTEAD--------IIVVglIGERGREVKEFIEHILGEEGLKRSVVVASPADDA-PLMRLRAAMYCTrIAE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 224 YFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNDSFGGGSLTALPVIETQAGDVS 303
Cdd:PRK05688 252 YFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEGDDQQ 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 304 AYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYRE------VAAFAQFGsd 377
Cdd:PRK05688 330 DPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQsrdlisVGAYVAGG-- 407
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 148677500 378 lDAATQQLLSRGVRLTELLKQG--QYSPMA-IEEQVAVIYAGVRG 419
Cdd:PRK05688 408 -DPETDLAIARFPHLVQFLRQGlrENVSLAqSREQLAAIFAPAAG 451
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
70-399 |
1.04e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 137.52 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 70 ELLGRVVDALGNAIDGKGPIgsKTRRRVGLKAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKtSIA 147
Cdd:PRK08972 102 SLLGRVIDGVGNPLDGLGPI--YTDQRASRHSPPINPlsRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGK-SVL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 148 IDTIINqkrfndGTDEKkklyCIYVA-IGQKRSTVAQLVKRLTDADAMKYTIVVSATAsDAAPLQYLapySGC----SMG 222
Cdd:PRK08972 179 LGMMTR------GTTAD----VIVVGlVGERGREVKEFIEEILGEEGRARSVVVAAPA-DTSPLMRL---KGCetatTIA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 223 EYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNDSFGGGSLTALPVIETQAGDV 302
Cdd:PRK08972 245 EYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAG--NGGPGQGSITAFYTVLTEGDDL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 303 SAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYRE------VAAFAQfGS 376
Cdd:PRK08972 323 QDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQnrdlisIGAYKQ-GS 401
|
330 340
....*....|....*....|...
gi 148677500 377 dlDAATQQLLSRGVRLTELLKQG 399
Cdd:PRK08972 402 --DPRIDNAIRLQPAMNAFLQQT 422
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
69-399 |
3.08e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 135.97 E-value: 3.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIGSKTRRRVgLKAP------GIIprisvREPMQTGIKAVDSLVPIGRGQRELIIGDRQTG 142
Cdd:PRK08472 96 RNLLGRVVDPLGRPIDGKGAIDYERYAPI-MKAPiaamkrGLI-----DEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 143 KtSIAIDTIINqkrfndGTDEKKKLyciyVA-IGQKRSTVAQLVKRLTDADaMKYTIVVSATASDAAPLQYLAPYSGCSM 221
Cdd:PRK08472 170 K-STLMGMIVK------GCLAPIKV----VAlIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSPLMRKYGAFCAMSV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 222 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNdsfGGGSLTALPVIETQAGD 301
Cdd:PRK08472 238 AEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEE---GKGSITAFFTVLVEGDD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 302 VSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYRE------VAAFaQFG 375
Cdd:PRK08472 315 MSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKEnevlirIGAY-QKG 393
|
330 340
....*....|....*....|....*.
gi 148677500 376 SD--LDAAtqqlLSRGVRLTELLKQG 399
Cdd:PRK08472 394 NDkeLDEA----ISKKEFMEQFLKQN 415
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
72-411 |
1.03e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 134.63 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 72 LGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKtSIAIDTI 151
Cdd:PRK07196 97 LGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGK-SVLLGMI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 152 inqkrfndgTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATAsDAAPLQYLAPYSGC-SMGEYFRDNGK 230
Cdd:PRK07196 176 ---------TRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPA-DESPLMRIKATELChAIATYYRDKGH 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 231 HALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmnDSFGGGSLTALPVIETQAGDVSAYIPTNV 310
Cdd:PRK07196 246 DVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQDPIVDCA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 311 ISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDL---DAATQQLLS 387
Cdd:PRK07196 323 RAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVagaDPMADQAVH 402
|
330 340
....*....|....*....|....
gi 148677500 388 RGVRLTELLKQGQYSPMAIEEQVA 411
Cdd:PRK07196 403 YYPAITQFLRQEVGHPALFSASVE 426
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
69-407 |
1.09e-33 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 131.61 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKgPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTsiai 148
Cdd:PRK07594 95 EALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKS---- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 149 dTIINQKRFNDGTDEKkklycIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDN 228
Cdd:PRK07594 170 -TLLAMLCNAPDADSN-----VLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 229 GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNDSfggGSLTALPVIETQAGDVSAYIPT 308
Cdd:PRK07594 244 GKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-MGEK---GSITAFYTVLVEGDDMNEPLAD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 309 NVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGS---DLDAATQQL 385
Cdd:PRK07594 320 EVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEyqrGVDTDTDKA 399
|
330 340
....*....|....*....|..
gi 148677500 386 LSRGVRLTELLKQGQYSPMAIE 407
Cdd:PRK07594 400 IDTYPDICTFLRQSKDEVCGPE 421
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
73-398 |
4.20e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 130.50 E-value: 4.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 73 GRVVDALGNAIDGKGPIGSKTRRR-VGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSI----- 146
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLlamla 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 147 ---AIDTIInqkrfndgtdekkklyciyVA-IGQKRSTVAQLVKRlTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMG 222
Cdd:PRK06002 187 radAFDTVV-------------------IAlVGERGREVREFLED-TLADNLKKAVAVVATSDESPMMRRLAPLTATAIA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 223 EYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDsfGGGSLTALPVIETQAGDV 302
Cdd:PRK06002 247 EYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLVDGDDH 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 303 SAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYRE------VAAFaQFGS 376
Cdd:PRK06002 325 NDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdlrlIGGY-RAGS 403
|
330 340
....*....|....*....|....
gi 148677500 377 D--LDAATQQLlsrgVRLTELLKQ 398
Cdd:PRK06002 404 DpdLDQAVDLV----PRIYEALRQ 423
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
69-415 |
5.55e-33 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 129.73 E-value: 5.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNaIDGK--GPIGSKTR---RRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGK 143
Cdd:PRK08149 86 EALLGAVLDPTGK-IVERfdAPPTVGPIseeRVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 144 TSIaIDTIINQKRFNdgtdekkklycIYVA--IGQKRSTVAQLVKRLTDADAMKYTIVVSATaSDAAPLQYL-APYSGCS 220
Cdd:PRK08149 165 TSL-MNMLIEHSEAD-----------VFVIglIGERGREVTEFVESLRASSRREKCVLVYAT-SDFSSVDRCnAALVATT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 221 MGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmndsFGGGSLTALPVIETQAG 300
Cdd:PRK08149 232 VAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGA----TLAGSITAFYTVLLESE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 301 DVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFG----- 375
Cdd:PRK08149 308 EEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGeyrrg 387
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 148677500 376 --SDLDAATQQllsRGVrLTELLKQGQYSPMAIEEQVAVIYA 415
Cdd:PRK08149 388 enADNDRAMDK---RPA-LEAFLKQDVAEKSSFSDTLERLNE 425
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
69-341 |
1.59e-31 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 122.33 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIGSKTRRRVGlkAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSI 146
Cdd:cd01135 8 EDMLGRIFNGSGKPIDGGPPILPEDYLDIN--GPPINPvaRIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLPHNEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 147 AIdTIINQKRFNDGTDEKKklyCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR 226
Cdd:cd01135 86 AA-QIARQAGVVGSEENFA---IVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 227 -DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMNDSfgGGSLTALPVIETQAGDV 302
Cdd:cd01135 162 yEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTMPNDDI 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 148677500 303 SAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSR 341
Cdd:cd01135 237 THPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
70-385 |
1.91e-29 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 120.27 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 70 ELLGRVVDALGNAIDGKGPigSKTRRRVGLKAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKtSIA 147
Cdd:PRK07960 115 ALLGRVLDGSGKPLDGLPA--PDTGETGALITPPFNPlqRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK-SVL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 148 IDTIinqKRFNDGTdekkklyCIYVA-IGQKRSTVAQLVKRLTDADAMKYTIVVSATAsDAAPLQYL--APYSgCSMGEY 224
Cdd:PRK07960 192 LGMM---ARYTQAD-------VIVVGlIGERGREVKDFIENILGAEGRARSVVIAAPA-DVSPLLRMqgAAYA-TRIAED 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 225 FRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNDSFGGGSLTALPVIETQAGDVSA 304
Cdd:PRK07960 260 FRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG--NGISGGGSITAFYTVLTEGDDQQD 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 305 YIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSA-------AQTRAMKQ-----------------VAGTMKL 360
Cdd:PRK07960 338 PIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAlideqhyARVRQFKQllssfqrnrdlvsvgayAKGSDPM 417
|
330 340 350
....*....|....*....|....*....|..
gi 148677500 361 ---ELAQYREVAAFAQFG----SDLDAATQQL 385
Cdd:PRK07960 418 ldkAIALWPQLEAFLQQGiferADWEDSLQAL 449
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
69-405 |
3.22e-28 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 116.16 E-value: 3.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIgSKTRRRVGLKAPgiiPRISVREPMQ----TGIKAVDSLVPIGRGQRELIIGDRQTGKT 144
Cdd:PRK05922 96 DHLLGRVLDGFGNPLDGKEQL-PKTHLKPLFSSP---PSPMSRQPIQeifpTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 145 SIaIDTIinqkrfndGTDEKKKLYCIYVaIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEY 224
Cdd:PRK05922 172 SL-LSTI--------AKGSKSTINVIAL-IGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 225 FRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmNDSfggGSLTALPVIETQAGDVSA 304
Cdd:PRK05922 242 FRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-NDK---GSITALYAILHYPNHPDI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 305 YIPTnVISITDGQIFL---ETELFykgiRPAINVGLSVSRvgSAAQTRAMKQVAGTMKLE--LAQYREVAAFAQFGSDLD 379
Cdd:PRK05922 318 FTDY-LKSLLDGHFFLtpqGKALA----SPPIDILTSLSR--SARQLALPHHYAAAEELRslLKAYHEALDIIQLGAYVP 390
|
330 340
....*....|....*....|....*.
gi 148677500 380 AATQQlLSRGVRLTELLKQGQYSPMA 405
Cdd:PRK05922 391 GQDAH-LDRAVKLLPSIKQFLSQPLS 415
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
72-408 |
4.87e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 112.77 E-value: 4.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 72 LGRVVDALGNAIDGKGPIGSKTRRRVgLKA--PGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSI--- 146
Cdd:PRK08927 99 LGRVVNALGEPIDGKGPLPQGPVPYP-LRAppPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLlsm 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 147 -----AIDTIInqkrfndgtdekkklycIYVaIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSM 221
Cdd:PRK08927 178 larnaDADVSV-----------------IGL-IGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 222 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmnDSFGGGSLTALPVIETQAGD 301
Cdd:PRK08927 240 AEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGP--GPIGEGTITGLFTVLVDGDD 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 302 VSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSdLDAA 381
Cdd:PRK08927 318 HNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGA-YRAG 396
|
330 340 350
....*....|....*....|....*....|.
gi 148677500 382 TQQLLSRGVR----LTELLKQGQYSPMAIEE 408
Cdd:PRK08927 397 SDPEVDEAIRlnpaLEAFLRQGKDEATSLAE 427
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
69-414 |
6.79e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 112.38 E-value: 6.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGkgPIGSKTRRRVGLKAPGI--IPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTsi 146
Cdd:PRK06793 95 NHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKS-- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 147 aidTIINQKRFNDGTDEKkklycIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR 226
Cdd:PRK06793 171 ---TLLGMIAKNAKADIN-----VISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFR 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 227 DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPgreaYPGDVFYLHS---RLLERAAKMNDsfggGSLTALPVIETQAGDVS 303
Cdd:PRK06793 243 DQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK----GSITGIYTVLVDGDDLN 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 304 AYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGS----DLD 379
Cdd:PRK06793 315 GPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTiqenAEN 394
|
330 340 350
....*....|....*....|....*....|....*
gi 148677500 380 AATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIY 414
Cdd:PRK06793 395 AYIFECKNKVEGINTFLKQGRSDSFQFDDIVEAMH 429
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
69-408 |
5.57e-25 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 107.22 E-value: 5.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI 148
Cdd:PRK04196 82 EDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 149 DtIINQKRFNdGTDEKkkLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR-D 227
Cdd:PRK04196 162 Q-IARQAKVL-GEEEN--FAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 228 NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMNDSfgGGSLTALPVIETQAGDVSA 304
Cdd:PRK04196 238 KGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITH 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 305 YIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSR-----VGsAAQTRA-MKQVAGTMKLELAQYREVAAFAQF-GSD 377
Cdd:PRK04196 313 PIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRlmkdgIG-EGKTREdHKDVANQLYAAYARGKDLRELAAIvGEE 391
|
330 340 350
....*....|....*....|....*....|...
gi 148677500 378 -LDAATQQLLSRGVRL-TELLKQGQYSPMAIEE 408
Cdd:PRK04196 392 aLSERDRKYLKFADAFeREFVNQGFDENRSIEE 424
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
69-342 |
5.47e-23 |
|
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: 101.33 E-value: 5.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI 148
Cdd:TIGR01039 82 KETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 149 DTIINQKRFNDGtdekkklYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRD- 227
Cdd:TIGR01039 162 ELINNIAKEHGG-------YSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDe 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 228 NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmndSFGGGSLTALPVIETQAGDVSAYIP 307
Cdd:TIGR01039 235 QGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERIT----STKTGSITSVQAVYVPADDLTDPAP 310
|
250 260 270
....*....|....*....|....*....|....*
gi 148677500 308 TNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 342
Cdd:TIGR01039 311 ATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRL 345
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
351-418 |
1.09e-22 |
|
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: 91.35 E-value: 1.09e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 351 MKQVAGTMKLELAQYREVAAFAQFGSD--LDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVR 418
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
30-351 |
8.57e-21 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 94.79 E-value: 8.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 30 FVGARNLHASNTRLQKTGtaemssileeRILGADTSvdlEELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRIS 109
Cdd:TIGR01040 54 FEGTSGIDAKKTTCEFTG----------DILRTPVS---EDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 110 VREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTI----INQKRFNDGTDEKKKLYCI-YVAIGQKRSTvAQL 184
Cdd:TIGR01040 121 PEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICrqagLVKLPTKDVHDGHEDNFAIvFAAMGVNMET-ARF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 185 VKR-LTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR-DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY 262
Cdd:TIGR01040 200 FKQdFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 263 PGDVFYLHSRLLERAAKMNDSfgGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 342
Cdd:TIGR01040 280 PGYMYTDLATIYERAGRVEGR--NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 357
|
....*....
gi 148677500 343 GSAAQTRAM 351
Cdd:TIGR01040 358 MKSAIGEGM 366
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
69-342 |
6.19e-18 |
|
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: 83.81 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 69 EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI 148
Cdd:cd01133 6 EETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 149 DTIINQKRFNDGtdekkklYCIYVAIGQKRSTVAQLVkrltdaDAMKYTIVVSATASDAAPLQY-----------LAPYS 217
Cdd:cd01133 86 ELINNIAKAHGG-------YSVFAGVGERTREGNDLY------HEMKESGVINLDGLSKVALVYgqmneppgaraRVALT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 218 GCSMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmndSFGGGSLTALPVIE 296
Cdd:cd01133 153 GLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERIT----STKKGSITSVQAVY 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 148677500 297 TQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 342
Cdd:cd01133 229 VPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
112-341 |
2.41e-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: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 112 EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTsiaidtIINQK--RFNDgTDekkklYCIYVAIGQKRSTVA------- 182
Cdd:cd01134 58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKT------VISQSlsKWSN-SD-----VVIYVGCGERGNEMAevleefp 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 183 QLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY 262
Cdd:cd01134 126 ELKDPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGY 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 263 PGdvfYLHSRL---LERA--AKMNDSFG-GGSLTALPVIETQAGDVSAYIPTNVISITdgQIF--LETELFYKGIRPAIN 334
Cdd:cd01134 206 PA---YLGARLaefYERAgrVRCLGSPGrEGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSIN 280
|
....*..
gi 148677500 335 VGLSVSR 341
Cdd:cd01134 281 WLISYSK 287
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
23-320 |
5.77e-14 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 73.53 E-value: 5.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 23 KNALGSSFVGARNLHASNTRLQK-TGTAEMSSILEERILGADTSVDL-EELLGRVVDALGNAIDGkGPigSKTRRRVGLK 100
Cdd:PRK02118 32 ERKDGSSLAQVIRLDGDKVTLQVfGGTRGISTGDEVVFLGRPMQVTYsESLLGRRFNGSGKPIDG-GP--ELEGEPIEIG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 101 APGIIP--RISVREPMQTGIKAVD---SLV-----PI----GRGQRELIIgdrqtgktSIAIDTiinqkrfndgtdEKKK 166
Cdd:PRK02118 109 GPSVNPvkRIVPREMIRTGIPMIDvfnTLVesqkiPIfsvsGEPYNALLA--------RIALQA------------EADI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 167 LycIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR-DNGKHALIIYDDLSKQAVA 245
Cdd:PRK02118 169 I--ILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADA 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148677500 246 YRQMSLLLRRPPGREAYPGDvfyLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFL 320
Cdd:PRK02118 247 LKEISITMDQIPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
170-354 |
4.29e-11 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 65.43 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 170 IYVAIGQKRSTVAQLVK---RLTDADA----MKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQ 242
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEefpKLKDPKTgkplMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 243 AVAYRQMSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDG 316
Cdd:PRK14698 766 AEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKV 842
|
170 180 190
....*....|....*....|....*....|....*...
gi 148677500 317 QIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQV 354
Cdd:PRK14698 843 FWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNV 880
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
107-291 |
3.52e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 59.03 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 107 RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT----SIAidtiinqkRFNDgTDekkklYCIYVAIGQKRSTVA 182
Cdd:PRK04192 204 KLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTvtqhQLA--------KWAD-AD-----IVIYVGCGERGNEMT 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 183 QLVK---RLTDADA----MKYTIVVSAT-----ASDAAPLqylapYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMS 250
Cdd:PRK04192 270 EVLEefpELIDPKTgrplMERTVLIANTsnmpvAAREASI-----YTGITIAEYYRDMGYDVLLMADSTSRWAEALREIS 344
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 148677500 251 LLLRRPPGREAYPGdvfYLHSRL---LERA--AKMNDSfGGGSLTA 291
Cdd:PRK04192 345 GRLEEMPGEEGYPA---YLASRLaefYERAgrVKTLGG-EEGSVTI 386
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
61-334 |
8.86e-07 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 51.19 E-value: 8.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 61 GADTSVDL-EELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGII---PRISVREpmqTGIKAVDSLVPIGRGQRELII 136
Cdd:CHL00060 91 GAPLSVPVgGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTKLSIFE---TGIKVVDLLAPYRRGGKIGLF 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 137 GDRQTGKTSIAIDTIINQKRFNDG----------TDEKKKLYciyvaIGQKRSTVAQLVKRLTDADAMKY---------T 197
Cdd:CHL00060 168 GGAGVGKTVLIMELINNIAKAHGGvsvfggvgerTREGNDLY-----MEMKESGVINEQNIAESKVALVYgqmneppgaR 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148677500 198 IVVSATASdaaplqylapysgcSMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLER 276
Cdd:CHL00060 243 MRVGLTAL--------------TMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 148677500 277 AAKMNDsfggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAIN 334
Cdd:CHL00060 309 ITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 362
|
|
| |
