|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
55-563 |
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: 1001.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 55 KASPTEVSSILEQRIRGVQEEAGLAETGRVLSVGDGIARVHGMTNVQAEELVEFASGVKGMCMNLEAGQVGVVLFGSDRL 134
Cdd:COG0056 2 QIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 135 VKEGETVKRTGEIVDVPVGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGR 214
Cdd:COG0056 82 IKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 215 GQRELIIGDRQTGKTAVALDAMLNQKrwnnssdeSKKLYCIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAP 294
Cdd:COG0056 162 GQRELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 295 LQYLAPFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDKHGGGSL 374
Cdd:COG0056 234 LQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 375 TALPVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVA 454
Cdd:COG0056 314 TALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 455 AFAQFGSDLDASTKQTLNRGERLTELLKQKQYSPMAVSDMVPLIFAGVNGYLDQIPVAKILQWEADFLAFLKSNHPEVQE 534
Cdd:COG0056 394 AFAQFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLK 473
|
490 500
....*....|....*....|....*....
gi 1832863686 535 TIDKEGQVSKDLEAQLKELIVGFNKSFNA 563
Cdd:COG0056 474 EIRETGKLDDEIEEKLKAAIEEFKKTFAA 502
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
57-563 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 999.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 57 SPTEVSSILEQRIRGVQEEAGLAETGRVLSVGDGIARVHGMTNVQAEELVEFASGVKGMCMNLEAGQVGVVLFGSDRLVK 136
Cdd:PRK09281 4 NPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 137 EGETVKRTGEIVDVPVGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQ 216
Cdd:PRK09281 84 EGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 217 RELIIGDRQTGKTAVALDAMLNQKrwnnssdeSKKLYCIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAPLQ 296
Cdd:PRK09281 164 RELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 297 YLAPFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDKHGGGSLTA 376
Cdd:PRK09281 236 YLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 377 LPVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVAAF 456
Cdd:PRK09281 316 LPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 457 AQFGSDLDASTKQTLNRGERLTELLKQKQYSPMAVSDMVPLIFAGVNGYLDQIPVAKILQWEADFLAFLKSNHPEVQETI 536
Cdd:PRK09281 396 AQFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEI 475
|
490 500
....*....|....*....|....*..
gi 1832863686 537 DKEGQVSKDLEAQLKELIVGFNKSFNA 563
Cdd:PRK09281 476 RETKDLSDEIEAKLKAAIEEFKKTFAA 502
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
58-561 |
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: 826.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 58 PTEVSSILEQRIRGVQEEAGLAETGRVLSVGDGIARVHGMTNVQAEELVEFASGVKGMCMNLEAGQVGVVLFGSDRLVKE 137
Cdd:TIGR00962 4 LEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 138 GETVKRTGEIVDVPVGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQR 217
Cdd:TIGR00962 84 GSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 218 ELIIGDRQTGKTAVALDAMLNQKrwnnssdeSKKLYCIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAPLQY 297
Cdd:TIGR00962 164 ELIIGDRQTGKTAVAIDTIINQK--------DSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 298 LAPFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDKHGGGSLTAL 377
Cdd:TIGR00962 236 LAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 378 PVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVAAFA 457
Cdd:TIGR00962 316 PIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 458 QFGSDLDASTKQTLNRGERLTELLKQKQYSPMAVSDMVPLIFAGVNGYLDQIPVAKILQWEADFLAFLKSNHPEVQETID 537
Cdd:TIGR00962 396 QFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEIN 475
|
490 500
....*....|....*....|....
gi 1832863686 538 KEGQVSKDLEAQLKELIVGFNKSF 561
Cdd:TIGR00962 476 TTKKLTEELEAKLKEALKNFKKTF 499
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
75-561 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 754.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 75 EAGLAETGRVLSVGDGIARVHGMTNVQAEELVEFASGVKGMCMNLEAGQVGVVLFGSDRLVKEGETVKRTGEIVDVPVGP 154
Cdd:CHL00059 1 EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 155 EMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQRELIIGDRQTGKTAVALD 234
Cdd:CHL00059 81 AYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 235 AMLNQKrwnnssdeSKKLYCIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAPLQYLAPFTGCAMGEWFRDNG 314
Cdd:CHL00059 161 TILNQK--------GQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 315 RHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDKHGGGSLTALPVIETQGGDVSAYIPTN 394
Cdd:CHL00059 233 RHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 395 VISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLNRG 474
Cdd:CHL00059 313 VISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 475 ERLTELLKQKQYSPMAVSDMVPLIFAGVNGYLDQIPVAKILQWEADFLAFLKSNHPEVQETIDKEGQVSKDLEAQLKELI 554
Cdd:CHL00059 393 QRLRELLKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAI 472
|
....*..
gi 1832863686 555 VGFNKSF 561
Cdd:CHL00059 473 QEQLELF 479
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
55-563 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 727.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 55 KASPTEVSSILEQRIRGVQEEAGLAETGRVLSVGDGIARVHGMTNVQAEELVEFASGVKGMCMNLEAGQVGVVLFGSDRL 134
Cdd:PRK13343 2 KSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 135 VKEGETVKRTGEIVDVPVGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGR 214
Cdd:PRK13343 82 ILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 215 GQRELIIGDRQTGKTAVALDAMLNQKrwnnssdeSKKLYCIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAP 294
Cdd:PRK13343 162 GQRELIIGDRQTGKTAIAIDAIINQK--------DSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 295 LQYLAPFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDKHGGGSL 374
Cdd:PRK13343 234 LQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 375 TALPVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVA 454
Cdd:PRK13343 314 TALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 455 AFAQFGSDLDASTKQTLNRGERLTELLKQKQYSPMAVSDMVPLIFAGVNGYLDQIPVAKILQWEADFLAFLKSNHPEVQE 534
Cdd:PRK13343 394 AFTRFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSL 473
|
490 500
....*....|....*....|....*....
gi 1832863686 535 TIDKEGQVSKDLEAQLKELIVGFNKSFNA 563
Cdd:PRK13343 474 ALESPRELDEAWLAALEEILREAGERFAA 502
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
147-428 |
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: 609.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 147 IVDVPVGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQRELIIGDRQT 226
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 227 GKTAVALDAMLNQKRwnnssdesKKLYCIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAPLQYLAPFTGCAM 306
Cdd:cd01132 81 GKTAIAIDTIINQKG--------KKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 307 GEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDKHGGGSLTALPVIETQGGD 386
Cdd:cd01132 153 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1832863686 387 VSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVG 428
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
65-545 |
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: 533.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 65 LEQRIRGVQEEAGLAETGRVLSVGDGIARVHGMTNVQAEELVEFASGVKGMCMNLEAGQVGVVLFGSDRLVKEGETVKRT 144
Cdd:TIGR03324 12 LDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 145 GEIVDVPVGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQRELIIGDR 224
Cdd:TIGR03324 92 GRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 225 QTGKTAVALDAMLNQKRWNnssdeskkLYCIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAPLQYLAPFTGC 304
Cdd:TIGR03324 172 QTGKTAIAIDTILNQKGRN--------VLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 305 AMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDKHGGGSLTALPVIETQG 384
Cdd:TIGR03324 244 SIGEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 385 GDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVAAFAQFGSDLD 464
Cdd:TIGR03324 324 QNISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 465 ASTKQTLNRGERLTELLKQKQYSPMAVSDMVPLIFAGVNGYLDQIPVAKILQWEADFLAFLKSNHPEVQETIDKEGQVSK 544
Cdd:TIGR03324 404 ENTRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSD 483
|
.
gi 1832863686 545 D 545
Cdd:TIGR03324 484 E 484
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
114-518 |
7.94e-125 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 378.61 E-value: 7.94e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 114 GMCMNLEA-GQVGVVLFGSDRLVKEGETVKRTGEIVDVPVGPEMLGRVVDALGNPIdgkgPINTKAKSRAQLK------- 185
Cdd:PTZ00185 80 GLVFNLEKdGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEV----PVGLLTRSRALLEseqtlgk 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 186 ----APGILPRRSVNQPVQTGMKCVDSMVPIGRGQRELIIGDRQTGKTAVALDAMLNQKRWNNSSDESKKLYCIYVAIGQ 261
Cdd:PTZ00185 156 vdagAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVISIYVSIGQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 262 KRSTVAQLVKTLEENDAMKYSIVVAATASEAAPLQYLAPFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRP 341
Cdd:PTZ00185 236 RCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 342 PGREAYPGDVFYLHSRLLERAAKMNDKHGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVG 421
Cdd:PTZ00185 316 PGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 422 LSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVAAFAQFGSDLDAStkqTLNRGERLTELLKQKQysPMAVSDMVPLIFAG 501
Cdd:PTZ00185 396 LSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTV---PMIRGARFVALFNQKN--PSFFMNALVSLYAC 470
|
410
....*....|....*..
gi 1832863686 502 VNGYLDQIPVAKILQWE 518
Cdd:PTZ00185 471 LNGYLDDVKVNYAKLYE 487
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
149-427 |
3.24e-122 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 360.62 E-value: 3.24e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 149 DVPVGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQRELIIGDRQTGK 228
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 229 TAVALDAMLNQKrwnnssdESKKLYCIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAPLQYLAPFTGCAMGE 308
Cdd:cd19476 81 TVLAMQLARNQA-------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 309 WFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMndKHGGGSLTALPVIETQGGDVS 388
Cdd:cd19476 154 YFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKV--KDGGGSITAIPAVSTPGDDLT 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 1832863686 389 AYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRV 427
Cdd:cd19476 232 DPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
202-425 |
1.13e-114 |
|
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: 338.95 E-value: 1.13e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 202 GMKCVDSMVPIGRGQRELIIGDRQTGKTAVAlDAMLNQkrwnnssdeSKKLYCIYVAIGQKRSTVAQLVKTLEENDAMKY 281
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQ---------ASADVVVYALIGERGREVREFIEELLGSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 282 SIVVAATASEAAPLQYLAPFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLER 361
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832863686 362 AAKMNDKhgGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVS 425
Cdd:pfam00006 151 AGRVKGK--GGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
155-488 |
2.45e-102 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 318.07 E-value: 2.45e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 155 EMLGRVVDALGNPIDGKGPINTKAKSRAQL-----KAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQRELIIGDRQTGKT 229
Cdd:PRK07165 78 EYFGKIIDIDGNIIYPEAQNPLSKKFLPNTssifnLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 230 AVALDAMLNQKRWNnssdeskkLYCIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAAtASEAAPLQYLAPFTGCAMGE- 308
Cdd:PRK07165 158 HIALNTIINQKNTN--------VKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAEn 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 309 --WFRDngrhAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDKHgggSLTALPVIETQGGD 386
Cdd:PRK07165 229 isYNDD----VLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNRK---TITALPILQTVDND 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 387 VSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSL-KLFLAqYREVAAFAQFGSDLDA 465
Cdd:PRK07165 302 ITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEIsKIYRA-YKRQLKLSMLDYDLNK 380
|
330 340
....*....|....*....|...
gi 1832863686 466 STKQTLNRGERLTELLKQKQYSP 488
Cdd:PRK07165 381 ETSDLLFKGKMIEKMFNQKGFSL 403
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
436-561 |
1.91e-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: 216.85 E-value: 1.91e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 436 MKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLNRGERLTELLKQKQYSPMAVSDMVPLIFAGVNGYLDQIPVAKIL 515
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1832863686 516 QWEADFLAFLKSNHPEVQETIDKEGQVSKDLEAQLKELIVGFNKSF 561
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
432-557 |
5.50e-68 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 215.77 E-value: 5.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 432 QVKAMKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLNRGERLTELLKQKQYSPMAVSDMVPLIFAGVNGYLDQIPV 511
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1832863686 512 AKILQWEADFLAFLKSNHPEVQETIDKEGQVSKDLEAQLKELIVGF 557
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
150-427 |
3.76e-48 |
|
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: 168.51 E-value: 3.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 150 VPVGPEMLGRVVDALGNPIDGKGPIntKAKSRAQLKAPGILP--RRSVNQPVQTGMKCVDSMVPIGRGQRELIIGDRQTG 227
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLP--DEPERRPLIAAPPNPlkRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 228 KTavALDAMLNQkrwNNSSDeskklycIYVA--IGQK-RSTVAQLVKTLEEnDAMKYSIVVAATASEAAPLQYLAPFTGC 304
Cdd:cd01136 80 KS--TLLGMIAR---NTDAD-------VNVIalIGERgREVREFIEKDLGE-EGLKRSVLVVATSDESPLLRVRAAYTAT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 305 AMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNDKhggGSLTALPVIETQG 384
Cdd:cd01136 147 AIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAG-NGEK---GSITAFYTVLVEG 222
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1832863686 385 GDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRV 427
Cdd:cd01136 223 DDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
65-488 |
7.95e-46 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 167.25 E-value: 7.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 65 LEQRIRGVqeeAGLAETGRVLSVGDGIARVHGMtNVQAEELVEFASGvKGMCMNlEAGQVG-------VVLFGSDRLVKE 137
Cdd:PRK09099 12 LERELAAL---PAVRRTGKVVEVIGTLLRVSGL-DVTLGELCELRQR-DGTLLQ-RAEVVGfsrdvalLSPFGELGGLSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 138 GETVKRTGEIVDVPVGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQR 217
Cdd:PRK09099 86 GTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 218 ELIIGDRQTGKTavALDAMLNQkrwNNSSDESkklycIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAPLQY 297
Cdd:PRK09099 166 MGIFAPAGVGKS--TLMGMFAR---GTQCDVN-----VIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 298 LAPFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNDKhggGSLTAL 377
Cdd:PRK09099 236 KAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-MGET---GSITAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 378 PVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVAAFA 457
Cdd:PRK09099 312 YTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLL 391
|
410 420 430
....*....|....*....|....*....|....*.
gi 1832863686 458 QFG---SDLDASTKQTLNRGERLTELLKQK--QYSP 488
Cdd:PRK09099 392 QVGeyrAGSDPVADEAIAKIDAIRDFLSQRtdEYSD 427
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
141-495 |
2.49e-45 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 165.70 E-value: 2.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 141 VKRTGEIVDVPVGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQRELI 220
Cdd:PRK06936 88 VSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 221 IGDRQTGKTavALDAMLNQkrwNNSSDeskklYCIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAPLQYLAP 300
Cdd:PRK06936 168 FAAAGGGKS--TLLASLIR---SAEVD-----VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 301 FTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNDKhggGSLTALPVI 380
Cdd:PRK06936 238 FVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG-QSDK---GSITALYTV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 381 ETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVAAFAQFG 460
Cdd:PRK06936 314 LVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIG 393
|
330 340 350
....*....|....*....|....*....|....*...
gi 1832863686 461 S---DLDASTKQTLNRGERLTELLKQKQYSPMAVSDMV 495
Cdd:PRK06936 394 EyqkGQDKEADQAIERIGAIRGFLRQGTHELSHFNETL 431
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
64-483 |
5.76e-44 |
|
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: 161.74 E-value: 5.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 64 ILEQRIRGVQEEAGLAETGRVLSVGDGIARVHGMtNVQAEELVEFASG----VKGMCMNLEAGQVGVVLFGSDRLVKEGE 139
Cdd:COG1157 3 RLARLLARLEELPPVRVSGRVTRVVGLLIEAVGP-DASIGELCEIETAdgrpVLAEVVGFRGDRVLLMPLGDLEGISPGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 140 TVKRTGEIVDVPVGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQRel 219
Cdd:COG1157 82 RVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 220 iIGdr---qtGKTAvaLDAMLNQkrwNNSSDeskklycIYVaIGqkrstvaqLV------------KTLEEnDAMKYSIV 284
Cdd:COG1157 160 -IGifagsgvGKST--LLGMIAR---NTEAD-------VNV-IA--------LIgergrevrefieDDLGE-EGLARSVV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 285 VAATASEAAPLQYLAPFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAK 364
Cdd:COG1157 217 VVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 365 MndkhGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLK 444
Cdd:COG1157 297 G----GKGSITAFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLR 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1832863686 445 LFLAQYREVA------AFAQfGSD--LDAStkqtLNRGERLTELLKQ 483
Cdd:COG1157 373 RLLARYEENEdlirigAYQP-GSDpeLDEA----IALIPAIEAFLRQ 414
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
61-484 |
3.61e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 159.59 E-value: 3.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 61 VSSILEQRI-RGVQEEAGLAETGRVLSVGDGIARVhGMTNVQAEELVEFA-SGVKGMCMNLEAGQVGVVLFGSDRLVKEG 138
Cdd:PRK06820 9 LTPRLQQQLtRPSAPPEGLRYRGPIVEIGPTLLRA-SLPGVAQGELCRIEpQGMLAEVVSIEQEMALLSPFASSDGLRCG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 139 ETVKRTGEIVDVPVGPEMLGRVVDALGNPIDGKGPINTKAKSRaQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQRE 218
Cdd:PRK06820 88 QWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWREL-DCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 219 LIIGDRQTGKTAvaLDAMLnqkrwnnsSDESKKLYCIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATaSEAAPLQYL 298
Cdd:PRK06820 167 GIFAAAGVGKST--LLGML--------CADSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVAT-SDRPALERL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 299 -APFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDkhggGSLTAL 377
Cdd:PRK06820 236 kGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDR----GSITAF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 378 PVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVAAFA 457
Cdd:PRK06820 312 YTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLV 391
|
410 420 430
....*....|....*....|....*....|
gi 1832863686 458 QFG---SDLDASTKQTLNRGERLTELLKQK 484
Cdd:PRK06820 392 RVGeyqAGEDLQADEALQRYPAICAFLQQD 421
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
81-483 |
8.09e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 158.70 E-value: 8.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 81 TGRVLSVGDgIARVHGMTNvQAEELvefasgvkGMCMNLEAGQVGVVLFGSDRLVKEGETVKRTGEIVDVPVGPEMLGRV 160
Cdd:PRK08472 33 DGLNPSVGD-IVKIESSDN-GKECL--------GMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLLGRV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 161 VDALGNPIDGKGPINTKAKSrAQLKAP-GILPRRSVNQPVQTGMKCVDSMVPIGRGQRELIIGDRQTGKTAvaLDAMLNQ 239
Cdd:PRK08472 103 VDPLGRPIDGKGAIDYERYA-PIMKAPiAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKST--LMGMIVK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 240 krwnNSSDESKklyciYVA-IGQKRSTVAQLV-KTLeeNDAMKYSIVVAATASEAAPLQYLAPFTGCAMGEWFRDNGRHA 317
Cdd:PRK08472 180 ----GCLAPIK-----VVAlIGERGREIPEFIeKNL--GGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 318 VIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDKhggGSLTALPVIETQGGDVSAYIPTNVIS 397
Cdd:PRK08472 249 LFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGK---GSITAFFTVLVEGDDMSDPIADQSRS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 398 ITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYRE------VAAFaQFGSD--LDastkQ 469
Cdd:PRK08472 326 ILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKEnevlirIGAY-QKGNDkeLD----E 400
|
410
....*....|....
gi 1832863686 470 TLNRGERLTELLKQ 483
Cdd:PRK08472 401 AISKKEFMEQFLKQ 414
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
138-499 |
1.45e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 155.27 E-value: 1.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 138 GETVKRTGEIVDVPVGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQR 217
Cdd:PRK07721 81 GCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 218 ELIIGDRQTGKTAvaLDAMLNQkrwNNSSDESkklycIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAPLQY 297
Cdd:PRK07721 161 VGIFAGSGVGKST--LMGMIAR---NTSADLN-----VIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 298 LAPFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmNDKhggGSLTAL 377
Cdd:PRK07721 231 KGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGT-NAS---GSITAF 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 378 PVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVAAFA 457
Cdd:PRK07721 307 YTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLI 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1832863686 458 QFGSDLDASTK---QTLNRGERLTELLKQKQYSPMAVSDMVPLIF 499
Cdd:PRK07721 387 NIGAYKRGSSReidEAIQFYPQIISFLKQGTDEKATFEESIQALL 431
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
112-484 |
1.47e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 155.24 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 112 VKGMCMNLEAGQVGvvlFGSDRL----------VKEGETVKRTGEIVDVPVGPEMLGRVVDALGNPIDGKGPINTKAksR 181
Cdd:PRK08972 52 IETMAGELEAEVVG---FDGDLLylmpieelrgVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQ--R 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 182 AQLKAPGILP--RRSVNQPVQTGMKCVDSMVPIGRGQRELIIGDRQTGKTaVALDAMLNqkrwNNSSDeskklyCIYVA- 258
Cdd:PRK08972 127 ASRHSPPINPlsRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKS-VLLGMMTR----GTTAD------VIVVGl 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 259 IGQKRSTVAQLVKTLEENDAMKYSIVVAATAsEAAPLQYL-APFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLL 337
Cdd:PRK08972 196 VGERGREVKEFIEEILGEEGRARSVVVAAPA-DTSPLMRLkGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 338 LRRPPGREAYPGDVFYLHSRLLERAAkmNDKHGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPA 417
Cdd:PRK08972 275 VGEPPATKGYPPSVFAKLPALVERAG--NGGPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPA 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832863686 418 INVGLSVSRVG----SAAQVKAMKQVagslKLFLAQYRE------VAAFAQfGSD--LDastkQTLNRGERLTELLKQK 484
Cdd:PRK08972 353 IDIEASISRVMpmviSEEHLEAMRRV----KQVYSLYQQnrdlisIGAYKQ-GSDprID----NAIRLQPAMNAFLQQT 422
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
150-492 |
2.58e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 146.41 E-value: 2.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 150 VPVGPEMLGRVVDALGNPIDGKGPIntKAKSRAQLKAPGILP--RRSVNQPVQTGMKCVDSMVPIGRGQRELIIGDRQTG 227
Cdd:PRK05688 103 LPMGMSMLGRVLDGAGRALDGKGPM--KAEDWVPMDGPTINPlnRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 228 KTaVALDAMlnqKRWNNSSdeskklycIYVA--IGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAaPLQYLAPFTGCA 305
Cdd:PRK05688 181 KS-VLLGMM---TRFTEAD--------IIVVglIGERGREVKEFIEHILGEEGLKRSVVVASPADDA-PLMRLRAAMYCT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 306 -MGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNDKHGGGSLTALPVIETQG 384
Cdd:PRK05688 248 rIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 385 GDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYRE------VAAFAQ 458
Cdd:PRK05688 326 DDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQsrdlisVGAYVA 405
|
330 340 350
....*....|....*....|....*....|....*.
gi 1832863686 459 FGsdlDASTKQTLNRGERLTELLKQ--KQYSPMAVS 492
Cdd:PRK05688 406 GG---DPETDLAIARFPHLVQFLRQglRENVSLAQS 438
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
61-495 |
5.83e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 145.10 E-value: 5.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 61 VSSILEQRIRGVQEEA-GLAETGRVLSVGDGIARVHgMTNVQAEELV------EFASGVKgmcmnLEAGQVGVVLFGSDR 133
Cdd:PRK07594 1 MKNELMQRLRLKYPPPdGYCRWGRIQDVSATLLNAW-LPGVFMGELCcikpgeELAEVVG-----INGSKALLSPFTSTI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 134 LVKEGETVKRTGEIVDVPVGPEMLGRVVDALGNPIDGKgPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIG 213
Cdd:PRK07594 75 GLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 214 RGQRELIIGDRQTGKTAvaLDAMLNqkrwnNSSDESKKlycIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAA 293
Cdd:PRK07594 154 EGQRVGIFSAPGVGKST--LLAMLC-----NAPDADSN---VLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 294 PLQYLAPFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNDKhggGS 373
Cdd:PRK07594 224 LERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-MGEK---GS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 374 LTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREV 453
Cdd:PRK07594 300 ITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEV 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1832863686 454 AAFAQFGS---DLDASTKQTLNRGERLTELLKQKQYSPMAVSDMV 495
Cdd:PRK07594 380 ELLIRIGEyqrGVDTDTDKAIDTYPDICTFLRQSKDEVCGPELLI 424
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
152-483 |
6.29e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 136.56 E-value: 6.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 152 VGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQRELIIGDRQTGKTav 231
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKS-- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 232 ALDAMLNQkrwnnssdESKKLYCIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEaAPLQYLAPFTGC-AMGEWF 310
Cdd:PRK07196 170 VLLGMITR--------YTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADE-SPLMRIKATELChAIATYY 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 311 RDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmnDKHGGGSLTALPVIETQGGDVSAY 390
Cdd:PRK07196 241 RDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQDP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 391 IPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVAAFAQFGSDL---DAST 467
Cdd:PRK07196 318 IVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVagaDPMA 397
|
330
....*....|....*.
gi 1832863686 468 KQTLNRGERLTELLKQ 483
Cdd:PRK07196 398 DQAVHYYPAITQFLRQ 413
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
82-452 |
7.15e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 136.67 E-value: 7.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 82 GRVLSVGDGIARVHGMTN-VQAEELVEFASG---VKGMCMNLEAGQVGVVLFGSDRLVKEGETVKRTGEIVDVPvGPEML 157
Cdd:PRK06002 28 GTVSEVTASHYRVRGLSRfVRLGDFVAIRADggtHLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGPLRIRP-DPSWK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 158 GRVVDALGNPIDGKGPINTKAKSRA-QLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQRELIIGDRQTGKTAvaLDAM 236
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPMSiDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKST--LLAM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 237 LNQkrwnnsSDESKKlycIYVA-IGQKRSTVAQLvktLEEN--DAMKYSIVVAATASEAAPLQYLAPFTGCAMGEWFRDN 313
Cdd:PRK06002 185 LAR------ADAFDT---VVIAlVGERGREVREF---LEDTlaDNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 314 GRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDkhGGGSLTALPVIETQGGDVSAYIPT 393
Cdd:PRK06002 253 GENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLVDGDDHNDPVAD 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1832863686 394 NVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYRE 452
Cdd:PRK06002 331 SIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEE 389
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
150-462 |
4.41e-33 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 131.83 E-value: 4.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 150 VPVGPEMLGRVVDALGNPIDGKGPINTKakSRAQLKAPGILP--RRSVNQPVQTGMKCVDSMVPIGRGQRELIIGDRQTG 227
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTG--ETGALITPPFNPlqRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 228 KTaVALDAMlnqKRWNNSSdeskklyCIYVA-IGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAPLQYLAPFTGCAM 306
Cdd:PRK07960 188 KS-VLLGMM---ARYTQAD-------VIVVGlIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRI 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 307 GEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNDKHGGGSLTALPVIETQGGD 386
Cdd:PRK07960 257 AEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG--NGISGGGSITAFYTVLTEGDD 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 387 VSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSA-------AQVKAMKQVagslklfLAQYRE------V 453
Cdd:PRK07960 335 QQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAlideqhyARVRQFKQL-------LSSFQRnrdlvsV 407
|
....*....
gi 1832863686 454 AAFAQfGSD 462
Cdd:PRK07960 408 GAYAK-GSD 415
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
150-441 |
8.31e-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: 126.95 E-value: 8.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 150 VPVGPEMLGRVVDALGNPIDGKGPIntKAKSRAQLKAPGILP--RRSVNQPVQTGMKCVDSMVPIGRGQRELIIGDrqTG 227
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDGGPPI--LPEDYLDINGPPINPvaRIYPEEMIQTGISAIDVMNTLVRGQKLPIFSG--SG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 228 KTAVALDAMLNQKRWNNSSDESKKLycIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAPLQYLAPFTGCAMG 307
Cdd:cd01135 80 LPHNELAAQIARQAGVVGSEENFAI--VFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 308 EWFR-DNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMNDKhgGGSLTALPVIETQ 383
Cdd:cd01135 158 EYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTMP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1832863686 384 GGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVgsaaqvkaMKQVAG 441
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRL--------MKSGIG 282
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
80-145 |
5.46e-32 |
|
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: 117.55 E-value: 5.46e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832863686 80 ETGRVLSVGDGIARVHGMTNVQAEELVEFASGVKGMCMNLEAGQVGVVLFGSDRLVKEGETVKRTG 145
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTG 66
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
141-493 |
3.20e-30 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 122.80 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 141 VKRTGEIVDVPVGPEMLGRVVDALGN---PIDGKGPINTKAKSRA-QLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQ 216
Cdd:PRK08149 73 LKPTGKPLSVWVGEALLGAVLDPTGKiveRFDAPPTVGPISEERViDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 217 RELIIGDRQTGKTAvaLDAMLnqkrWNNSSDEskklycIYVA--IGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAP 294
Cdd:PRK08149 153 RMGIFASAGCGKTS--LMNML----IEHSEAD------VFVIglIGERGREVTEFVESLRASSRREKCVLVYATSDFSSV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 295 LQYLAPFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMndkhGGGSL 374
Cdd:PRK08149 221 DRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT----LAGSI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 375 TALPVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVA 454
Cdd:PRK08149 297 TAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQ 376
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1832863686 455 AFAQFGS---DLDASTKQTLNRGERLTELLKQKQYSPMAVSD 493
Cdd:PRK08149 377 LFIDLGEyrrGENADNDRAMDKRPALEAFLKQDVAEKSSFSD 418
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
68-426 |
3.72e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 123.17 E-value: 3.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 68 RIRGVQ----EEAGLAetgRVLSVGDGIARVHGMTNVQAEELVEFaSGVKGMCMNleagqvgvvlFGSDRLVKEGETVKR 143
Cdd:PRK08927 20 RVVAVRgllvEVAGPI---HALSVGARIVVETRGGRPVPCEVVGF-RGDRALLMP----------FGPLEGVRRGCRAVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 144 TGEIVDVPVGPEMLGRVVDALGNPIDGKGPInTKAKSRAQLKA--PGILPRRSVNQPVQTGMKCVDSMVPIGRGQRELII 221
Cdd:PRK08927 86 ANAAAAVRPSRAWLGRVVNALGEPIDGKGPL-PQGPVPYPLRAppPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 222 GDRQTGKTAvaLDAMLNQkrwNNSSDESkklycIYVAIGQKRSTVAQLVK-TLEEnDAMKYSIVVAATASEAAPLQYLAP 300
Cdd:PRK08927 165 AGSGVGKSV--LLSMLAR---NADADVS-----VIGLIGERGREVQEFLQdDLGP-EGLARSVVVVATSDEPALMRRQAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 301 FTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmnDKHGGGSLTALPVI 380
Cdd:PRK08927 234 YLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGP--GPIGEGTITGLFTV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1832863686 381 ETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSR 426
Cdd:PRK08927 312 LVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSR 357
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
94-426 |
7.55e-29 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 119.55 E-value: 7.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 94 VHGMTNVQAEELVEF--ASGVKGMCMNLEA--GQVGVVLF-GSDRLVKEGETVKRTGEIVDVPVGPEMLGRVVDALGNPI 168
Cdd:PRK04196 17 VEGVEGVAYGEIVEIelPNGEKRRGQVLEVseDKAVVQVFeGTTGLDLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 169 DGKGPINTKAKSRAQLKApgILP--RRSVNQPVQTGMKCVDSMVPIGRGQReLII--GdrqTGKTAVALDAMLnqKRWNN 244
Cdd:PRK04196 97 DGGPEIIPEKRLDINGAP--INPvaREYPEEFIQTGISAIDGLNTLVRGQK-LPIfsG---SGLPHNELAAQI--ARQAK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 245 SSDESKKLYCIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAPLQYLAPFTGCAMGEWFR-DNGRHAVIIYDD 323
Cdd:PRK04196 169 VLGEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMHVLVILTD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 324 LSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMNDKHGggSLTALPVIETQGGDVSAYIPTNVISITD 400
Cdd:PRK04196 249 MTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGKKG--SITQIPILTMPDDDITHPIPDLTGYITE 323
|
330 340
....*....|....*....|....*.
gi 1832863686 401 GQIFLESELFYKGIRPAINVGLSVSR 426
Cdd:PRK04196 324 GQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
138-498 |
7.60e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 116.23 E-value: 7.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 138 GETVKRTGEIVDVPVGPEMLGRVVDALGNPIDGkgPINTKAKSRAQLKAPGI--LPRRSVNQPVQTGMKCVDSMVPIGRG 215
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 216 QRELIIGDRQTGKTAvaLDAMLNQkrwNNSSDESkklycIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAPL 295
Cdd:PRK06793 157 QKIGIFAGSGVGKST--LLGMIAK---NAKADIN-----VISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 296 QYLAPFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPgreaYPGDVFYLHS---RLLERAAKMNDkhggG 372
Cdd:PRK06793 227 QLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK----G 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 373 SLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYRE 452
Cdd:PRK06793 299 SITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKE 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1832863686 453 VAAFAQFGS----DLDASTKQTLNRGERLTELLKQKQYSPMAVSDMVPLI 498
Cdd:PRK06793 379 NELYFKLGTiqenAENAYIFECKNKVEGINTFLKQGRSDSFQFDDIVEAM 428
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
126-504 |
5.45e-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: 114.05 E-value: 5.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 126 VVLFGSDRLVKeGETVKRTGEIVDVPVGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKC 205
Cdd:TIGR01039 55 IAMGSTDGLVR-GLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 206 VDSMVPIGRGQRELIIGDRQTGKTavaldaMLNQKRWNNSSDESKKlYCIYVAIGQkrstvaqlvKTLEEND---AMKYS 282
Cdd:TIGR01039 134 IDLLAPYAKGGKIGLFGGAGVGKT------VLIQELINNIAKEHGG-YSVFAGVGE---------RTREGNDlyhEMKES 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 283 IVVAATA------SEAAPLQYLAPFTGCAMGEWFRDNGRHAVIIY-DDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLH 355
Cdd:TIGR01039 198 GVIDKTAlvygqmNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFiDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 356 SRLLERAAKMNdkhgGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQV-K 434
Cdd:TIGR01039 278 GELQERITSTK----TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVgE 353
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832863686 435 AMKQVAGSLKLFLAQYREVA-AFAQFGSD-LDASTKQTLNRGERLTELLKQkqysPMAVSDmvplIFAGVNG 504
Cdd:TIGR01039 354 EHYDVARGVQQILQRYKELQdIIAILGMDeLSEEDKLTVERARRIQRFLSQ----PFFVAE----VFTGQPG 417
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
150-490 |
9.30e-27 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 113.08 E-value: 9.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 150 VPVGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQRELIIGDRQTGKT 229
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 230 AVaLDAMlnqkrwnnsSDESKKLYCIYVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEAAPLQYLAPFTGCAMGEW 309
Cdd:PRK05922 172 SL-LSTI---------AKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 310 FRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmNDKhggGSLTALPVIetqggdvsA 389
Cdd:PRK05922 242 FRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-NDK---GSITALYAI--------L 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 390 YIPTN-------VISITDGQIFLESElfYKGI-RPAINVGLSVSRVGSAAQVKAMKQVAGSLKLFLAQYREVAAFAQFGS 461
Cdd:PRK05922 310 HYPNHpdiftdyLKSLLDGHFFLTPQ--GKALaSPPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGA 387
|
330 340
....*....|....*....|....*....
gi 1832863686 462 DLDASTKQtLNRGERLTELLKQKQYSPMA 490
Cdd:PRK05922 388 YVPGQDAH-LDRAVKLLPSIKQFLSQPLS 415
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
140-436 |
9.86e-25 |
|
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: 107.50 E-value: 9.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 140 TVKRTGEIVDVPVGPEMLGRVVDALGNPIDgKGPiNTKAKSRAQLKAPGILPRRSV--NQPVQTGMKCVDSMVPIGRGQR 217
Cdd:TIGR01040 66 TCEFTGDILRTPVSEDMLGRVFNGSGKPID-KGP-PVLAEDYLDINGQPINPYARIypEEMIQTGISAIDVMNSIARGQK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 218 ELIIGDRQTGKTAVALD----AMLNQKRWNNSSDESKKLYCI-YVAIGQKRSTVAQLVKTLEENDAMKYSIVVAATASEA 292
Cdd:TIGR01040 144 IPIFSAAGLPHNEIAAQicrqAGLVKLPTKDVHDGHEDNFAIvFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 293 APLQYLAPFTGCAMGEWFR-DNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDKhgG 371
Cdd:TIGR01040 224 TIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR--N 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832863686 372 GSLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQVKAM 436
Cdd:TIGR01040 302 GSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
150-426 |
8.15e-17 |
|
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: 81.08 E-value: 8.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 150 VPVGPEMLGRVVDALGNPIDgkgpINTKAKS-------RAQlKAPGILPRRSV-----NQPVQTGMKCVDSMVPIGRGQR 217
Cdd:cd01134 4 VELGPGLLGSIFDGIQRPLE----VIAETGSifiprgvNVQ-RWPVRQPRPVKeklppNVPLLTGQRVLDTLFPVAKGGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 218 ELIIGDRQTGKTavaldaMLNQK--RWNNSSdeskklYCIYVAIGQKRSTVA-------QLVKTLEENDAMKYSIVVAAT 288
Cdd:cd01134 79 AAIPGPFGCGKT------VISQSlsKWSNSD------VVIYVGCGERGNEMAevleefpELKDPITGESLMERTVLIANT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 289 ------ASEAAPlqylapFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---L 359
Cdd:cd01134 147 snmpvaAREASI------YTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefY 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832863686 360 ERAAK---MNDKHGGGSLTALPVIETQGGDVSAYIPTNVISITdgQIF--LESELFYKGIRPAINVGLSVSR 426
Cdd:cd01134 218 ERAGRvrcLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
436-503 |
7.90e-16 |
|
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: 72.09 E-value: 7.90e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 436 MKQVAGSLKLFLAQYREVAAFAQFGSD--LDASTKQTLNRGERLTELLKQKQYSPMAVSDMVPLIFAGVN 503
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 ... |
150-427 |
1.37e-15 |
|
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: 77.26 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 150 VPVGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRGQRELIIGDRQTGKT 229
Cdd:cd01133 2 VPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 230 avaldaMLNQKRWNNSSdESKKLYCIYVAIGQkrstvaqlvKTLEEND---AMKYSIVVAATASEAAPLQY--------- 297
Cdd:cd01133 82 ------VLIMELINNIA-KAHGGYSVFAGVGE---------RTREGNDlyhEMKESGVINLDGLSKVALVYgqmneppga 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 298 --LAPFTGCAMGEWFRD-NGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNDKHggGSL 374
Cdd:cd01133 146 raRVALTGLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERIT--STKK--GSI 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1832863686 375 TALPVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRV 427
Cdd:cd01133 222 TSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
118-405 |
1.51e-15 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 78.92 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 118 NLEAGQVGVVLFGSDRLVKEGETVKRTGEIVDVPVGPEMLGRVVDALGNPIDGKGPINTKaksRAQLKAPGILP-RRSV- 195
Cdd:PRK02118 44 RLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGE---PIEIGGPSVNPvKRIVp 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 196 NQPVQTGMKCVDSMVPIGRGQRELIIGDrqTGKTAVALDAML-NQKrwnnssdESKKLycIYVAIGQKRSTVAQLVKTLE 274
Cdd:PRK02118 121 REMIRTGIPMIDVFNTLVESQKIPIFSV--SGEPYNALLARIaLQA-------EADII--ILGGMGLTFDDYLFFKDTFE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 275 ENDAMKYSIVVAATASEAAPLQYLAPFTGCAMGEWFR-DNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDvfy 353
Cdd:PRK02118 190 NAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGS--- 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1832863686 354 LHSRLLERAAKMNDKHGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFL 405
Cdd:PRK02118 267 LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
79-145 |
1.06e-14 |
|
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: 68.73 E-value: 1.06e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832863686 79 AETGRVLSVGDGIARVHGMTNVQAEELVEFASGVKGMCMNLEAGQVGVVLFGSDRLVKEGETVKRTG 145
Cdd:pfam02874 3 QVIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
138-215 |
2.99e-13 |
|
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: 72.04 E-value: 2.99e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832863686 138 GETVKRTGEIVDVPVGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKCVDSMVPIGRG 215
Cdd:COG0055 69 GMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKG 146
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
279-419 |
2.08e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 63.89 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 279 MKYSIVVAATASEAAPLQYLAPFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL 358
Cdd:PRK14698 717 MERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASKL 793
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832863686 359 LE------RAAKMNDKHGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAIN 419
Cdd:PRK14698 794 AEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAIN 860
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
196-419 |
1.56e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 60.57 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 196 NQPVQTGMKCVDSMVPIGRGQRELIIGDRQTGKTavaldaMLNQK--RWNNSSdeskklYCIYVAIGQKRSTVaqlVKTL 273
Cdd:PRK04192 208 VEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT------VTQHQlaKWADAD------IVIYVGCGERGNEM---TEVL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 274 EE----------NDAMKYSIVVAAT------ASEAAPlqylapFTGCAMGEWFRDNGRHAVIIYDDLSKQAVAYRQMSLL 337
Cdd:PRK04192 273 EEfpelidpktgRPLMERTVLIANTsnmpvaAREASI------YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGR 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 338 LRRPPGREAYPGdvfYLHSRL---LERAAKMNDKHGG-GSLTALPVIETQGGDVSAYIPTNVISITdgQIF--LESELFY 411
Cdd:PRK04192 347 LEEMPGEEGYPA---YLASRLaefYERAGRVKTLGGEeGSVTIIGAVSPPGGDFSEPVTQNTLRIV--KVFwaLDAELAD 421
|
....*...
gi 1832863686 412 KGIRPAIN 419
Cdd:PRK04192 422 RRHFPAIN 429
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
126-419 |
2.11e-07 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 53.51 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 126 VVLFGSDRLvKEGETVKRTGEIVDVPVGPEMLGRVVDALGNPIDGKGPINTKAKSRAQLKAPGILPRRSVNQPVQTGMKC 205
Cdd:CHL00060 73 VAMSATDGL-MRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 206 VDSMVPIGRGQRELIIGDRQTGKTAVALDAMlnqkrwNNSSdeskKLY---CIYVAIGQkrstvaqlvKTLEEND---AM 279
Cdd:CHL00060 152 VDLLAPYRRGGKIGLFGGAGVGKTVLIMELI------NNIA----KAHggvSVFGGVGE---------RTREGNDlymEM 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832863686 280 KYSIVVAA---TASEAAPL--QYLAP--------FTGCAMGEWFRDNGRHAVIIY-DDLSKQAVAYRQMSLLLRRPPGRE 345
Cdd:CHL00060 213 KESGVINEqniAESKVALVygQMNEPpgarmrvgLTALTMAEYFRDVNKQDVLLFiDNIFRFVQAGSEVSALLGRMPSAV 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832863686 346 AYPGDVFYLHSRLLERAAKMNDkhggGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFYKGIRPAIN 419
Cdd:CHL00060 293 GYQPTLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 362
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
81-146 |
1.86e-03 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 37.29 E-value: 1.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832863686 81 TGRVLSVGDGIARVHGMTNVQAEELVEF-------ASGVKGMCMNLEAGQVGVVLFGSDRLVKEGETVKRTGE 146
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIergdgnnETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| |
