|
Name |
Accession |
Description |
Interval |
E-value |
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
23-507 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 1079.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 23 EIKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESSNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSE 102
Cdd:CHL00059 1 EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 103 SYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 182
Cdd:CHL00059 81 AYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 183 TILNQKGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTGAALAEYFMYRERHTLIIYD 262
Cdd:CHL00059 161 TILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 263 DLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQ 342
Cdd:CHL00059 241 DLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 343 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLK 422
Cdd:CHL00059 321 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 423 QSQAAPLRVEEQVATIYTGANGYLDSLEIGQVKKFLVQLRTHLKTNKPQFQEIISSTKTLTGDAEALLKEAIQEQLELFL 502
Cdd:CHL00059 401 QSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQLELFL 480
|
....*
gi 190358244 503 LQEQT 507
Cdd:CHL00059 481 LQEQT 485
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
3-496 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 960.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 3 TIRADEISNIIRERIEQYNREIKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESSNVGVVLMGDGLM 82
Cdd:PRK09281 2 QINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 83 IQEGSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR 162
Cdd:PRK09281 82 IKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 163 GQRELIIGDRQTGKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYT 242
Cdd:PRK09281 162 GQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 243 GAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVET 322
Cdd:PRK09281 242 GCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIET 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 323 QSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELEAFAQFASD 402
Cdd:PRK09281 322 QAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 403 LDKATQNQLARGQRLRELLKQSQAAPLRVEEQVATIYTGANGYLDSLEIGQVKKFLVQLRTHLKTNKPQFQEIISSTKTL 482
Cdd:PRK09281 402 LDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKDL 481
|
490
....*....|....
gi 190358244 483 TGDAEALLKEAIQE 496
Cdd:PRK09281 482 SDEIEAKLKAAIEE 495
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
3-496 |
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: 957.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 3 TIRADEISNIIRERIEQYNREIKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESSNVGVVLMGDGLM 82
Cdd:COG0056 2 QIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 83 IQEGSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR 162
Cdd:COG0056 82 IKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 163 GQRELIIGDRQTGKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYT 242
Cdd:COG0056 162 GQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 243 GAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVET 322
Cdd:COG0056 242 GCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIET 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 323 QSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELEAFAQFASD 402
Cdd:COG0056 322 QAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 403 LDKATQNQLARGQRLRELLKQSQAAPLRVEEQVATIYTGANGYLDSLEIGQVKKFLVQLRTHLKTNKPQFQEIISSTKTL 482
Cdd:COG0056 402 LDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGKL 481
|
490
....*....|....
gi 190358244 483 TGDAEALLKEAIQE 496
Cdd:COG0056 482 DDEIEEKLKAAIEE 495
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
3-496 |
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: 823.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 3 TIRADEISNIIRERIEQYNREIKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESSNVGVVLMGDGLM 82
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 83 IQEGSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR 162
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 163 GQRELIIGDRQTGKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYT 242
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 243 GAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVET 322
Cdd:TIGR00962 241 GCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 323 QSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELEAFAQFASD 402
Cdd:TIGR00962 321 QAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 403 LDKATQNQLARGQRLRELLKQSQAAPLRVEEQVATIYTGANGYLDSLEIGQVKKFLVQLRTHLKTNKPQFQEIISSTKTL 482
Cdd:TIGR00962 401 LDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKL 480
|
490
....*....|....
gi 190358244 483 TGDAEALLKEAIQE 496
Cdd:TIGR00962 481 TEELEAKLKEALKN 494
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
4-501 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 746.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 4 IRADEISNIIRERIEQYNREIKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESSNVGVVLMGDGLMI 83
Cdd:PRK13343 3 SNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 84 QEGSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRG 163
Cdd:PRK13343 83 LAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 164 QRELIIGDRQTGKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTG 243
Cdd:PRK13343 163 QRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 244 AALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVETQ 323
Cdd:PRK13343 243 CAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 324 SGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELEAFAQFASDL 403
Cdd:PRK13343 323 AGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 404 DKATQNQLARGQRLRELLKQSQAAPLRVEEQVATIYTGANGYLDSLEIGQVKKFLVQLRTHLKTNKPQFQEIISSTKTLT 483
Cdd:PRK13343 403 DAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRELD 482
|
490
....*....|....*...
gi 190358244 484 GDAEALLKEAIQEQLELF 501
Cdd:PRK13343 483 EAWLAALEEILREAGERF 500
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
95-368 |
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: 582.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 95 IAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQT 174
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 175 GKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTGAALAEYFMYRE 254
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 255 RHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVETQSGDVSAYIPTN 334
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 190358244 335 VISITDGQIFLSADLFNAGIRPAINVGISVSRVG 368
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
7-454 |
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: 545.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 7 DEISNIIRERIEQYNREIKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESSNVGVVLMGDGLMIQEG 86
Cdd:TIGR03324 6 DKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 87 SSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRE 166
Cdd:TIGR03324 86 DEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 167 LIIGDRQTGKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTGAAL 246
Cdd:TIGR03324 166 LILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 247 AEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVETQSGD 326
Cdd:TIGR03324 246 GEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 327 VSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELEAFAQFASDLDKA 406
Cdd:TIGR03324 326 ISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDEN 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 190358244 407 TQNQLARGQRLRELLKQSQAAPLRVEEQVATIYTGANGYLDSLEIGQV 454
Cdd:TIGR03324 406 TRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAM 453
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
62-457 |
1.36e-116 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 355.12 E-value: 1.36e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 62 GIALNLESSN-VGVVLMGDGLMIQEGSSVKATGRIAQIPVSESYLGRVINALAKPIDgRGEISASESRL--------IES 132
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVP-VGLLTRSRALLeseqtlgkVDA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 133 PAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQN--------VICVYVAIGQKAS 204
Cdd:PTZ00185 159 GAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINqqilsknaVISIYVSIGQRCS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 205 SVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGR 284
Cdd:PTZ00185 239 NVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 285 EAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISV 364
Cdd:PTZ00185 319 EAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSV 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 365 SRVGSAAQIKAMKQVAGKSKLELAQFAELEAFAQFASDLDKATqnqLARGQRLRELLKQSQaaPLRVEEQVATIYTGANG 444
Cdd:PTZ00185 399 SRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNALVSLYACLNG 473
|
410
....*....|...
gi 190358244 445 YLDSLEIGQVKKF 457
Cdd:PTZ00185 474 YLDDVKVNYAKLY 486
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
150-365 |
1.23e-112 |
|
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: 332.01 E-value: 1.23e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 150 GLIAIDSMIPIGRGQRELIIGDRQTGKTAVAtDTILNQKGQNViCVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETA 229
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 230 DSSATLQYLAPYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRl 309
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGK- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 190358244 310 gEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVS 365
Cdd:pfam00006 158 -GGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
97-423 |
4.29e-104 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 320.77 E-value: 4.29e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 97 QIPVSESYLGRVINALAKPIDGRGEISASESRLI-ESP----APGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGD 171
Cdd:PRK07165 72 KVKTSKEYFGKIIDIDGNIIYPEAQNPLSKKFLPnTSSifnlAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGD 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 172 RQTGKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATlQYLAPYTGAALAEYFM 251
Cdd:PRK07165 152 RQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAENIS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 252 YRErHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSssrLGEGSMTALPIVETQSGDVSAYI 331
Cdd:PRK07165 231 YND-DVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKF---KNRKTITALPILQTVDNDITSLI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 332 PTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGK-SKLeLAQFAELEAFAQFASDLDKATQNQ 410
Cdd:PRK07165 307 SSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEiSKI-YRAYKRQLKLSMLDYDLNKETSDL 385
|
330
....*....|...
gi 190358244 411 LARGQRLRELLKQ 423
Cdd:PRK07165 386 LFKGKMIEKMFNQ 398
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
97-367 |
5.58e-103 |
|
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: 309.77 E-value: 5.58e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 97 QIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 177 TAVATDTILNQKGQNV-ICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTGAALAEYFMYRER 255
Cdd:cd19476 81 TVLAMQLARNQAKAHAgVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 256 HTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSrlGEGSMTALPIVETQSGDVSAYIPTNV 335
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 190358244 336 ISITDGQIFLSADLFNAGIRPAINVGISVSRV 367
Cdd:cd19476 239 FAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
376-501 |
4.39e-58 |
|
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: 188.34 E-value: 4.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 376 MKQVAGKSKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQAAPLRVEEQVATIYTGANGYLDSLEIGQVK 455
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 190358244 456 KFLVQLRTHLKTNKPQFQEIISSTKTLTGDAEALLKEAIQEQLELF 501
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
372-496 |
3.84e-56 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 183.41 E-value: 3.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 372 QIKAMKQVAGKSKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQAAPLRVEEQVATIYTGANGYLDSLEI 451
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 190358244 452 GQVKKFLVQLRTHLKTNKPQFQEIISSTKTLTGDAEALLKEAIQE 496
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEE 125
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
97-367 |
2.55e-49 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 170.43 E-value: 2.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 97 QIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 177 TavatdTILNQKGQNV---ICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTGAALAEYFMYR 253
Cdd:cd01136 81 S-----TLLGMIARNTdadVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 254 ERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsrlgEGSMTALPIVETQSGDVSAYIPT 333
Cdd:cd01136 156 GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGE----KGSITAFYTVLVEGDDFNDPIAD 231
|
250 260 270
....*....|....*....|....*....|....
gi 190358244 334 NVISITDGQIFLSADLFNAGIRPAINVGISVSRV 367
Cdd:cd01136 232 EVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
15-389 |
1.41e-48 |
|
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: 173.29 E-value: 1.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 15 ERIEQYNREIK----IVNTGTVLQVGDGIARIHGLD--------------EVMAGELVEFEEGTigialnlessnvgVVL 76
Cdd:COG1157 2 DRLARLLARLEelppVRVSGRVTRVVGLLIEAVGPDasigelceietadgRPVLAEVVGFRGDR-------------VLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 77 M--GDGLMIQEGSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAI 154
Cdd:COG1157 69 MplGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 155 DSMIPIGRGQReliIGdr---qtGKTavatdTILNQKGQNV---ICVyVA-IGqkassvaqvvttfqERG---------- 217
Cdd:COG1157 149 DGLLTVGRGQR---IGifagsgvGKS-----TLLGMIARNTeadVNV-IAlIG--------------ERGrevrefiedd 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 218 ----AMEYTIVVAETADSSATLQYLAPYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFY 293
Cdd:COG1157 206 lgeeGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 294 LHSRLLERAAKSssrlGEGSMTAL------------PIVETqsgdvsayiptnVISITDGQIFLSADLFNAGIRPAINVG 361
Cdd:COG1157 286 LLPRLLERAGNG----GKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVL 349
|
410 420
....*....|....*....|....*...
gi 190358244 362 ISVSRVgsaaqikaMKQVAGKSKLELAQ 389
Cdd:COG1157 350 ASISRV--------MPDIVSPEHRALAR 369
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
7-443 |
2.57e-47 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 169.93 E-value: 2.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 7 DEISNIIRERIEQyNREIKIvnTGTVLQVGDGIAR--IHGldeVMAGELVEFEEGtiGIALNLESSNVGVVL-------M 77
Cdd:PRK06936 5 DYIPHHLRHAIVG-SRLIQI--RGRVTQVTGTILKavVPG---VRIGELCYLRNP--DNSLSLQAEVIGFAQhqalltpL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 78 GDGLMIQEGSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSM 157
Cdd:PRK06936 77 GEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 158 IPIGRGQRELIIGDRQTGKTAVATDTIlnqKGQNV-ICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQ 236
Cdd:PRK06936 157 LTCGEGQRMGIFAAAGGGKSTLLASLI---RSAEVdVTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMER 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 237 YLAPYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsrlgEGSMTA 316
Cdd:PRK06936 234 AKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSD----KGSITA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 317 LPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELEAF 396
Cdd:PRK06936 310 LYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 190358244 397 AQ---FASDLDKATQNQLARGQRLRELLKQSQAAPLRVEEQVATIYTGAN 443
Cdd:PRK06936 390 LQigeYQKGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETLTQ 439
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
26-424 |
6.39e-45 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 163.40 E-value: 6.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 26 IVNTGTVLQVGDGIARIHGLDeVMAGELVEF--EEGTIGIALNLESSNVGVVLM---GDGLMIQEGSSVKATGRIAQIPV 100
Cdd:PRK09099 22 VRRTGKVVEVIGTLLRVSGLD-VTLGELCELrqRDGTLLQRAEVVGFSRDVALLspfGELGGLSRGTRVIGLGRPLSVPV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 101 SESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTava 180
Cdd:PRK09099 101 GPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKS--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 181 tdTILNQKGQNVIC---VYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTGAALAEYFMYRERHT 257
Cdd:PRK09099 178 --TLMGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 258 LIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSrlgeGSMTALPIV--ETQSGdvSAYIPTNV 335
Cdd:PRK09099 256 LLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGET----GSITALYTVlaEDESG--SDPIAEEV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 336 ISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELEAFAQ---FASDLDKATQNQLA 412
Cdd:PRK09099 330 RGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQvgeYRAGSDPVADEAIA 409
|
410
....*....|..
gi 190358244 413 RGQRLRELLKQS 424
Cdd:PRK09099 410 KIDAIRDFLSQR 421
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
9-424 |
9.80e-45 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 163.06 E-value: 9.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 9 ISNIIRERIEQYNREIK-IVNTGTVLQVGDGIARIhGLDEVMAGELVEFEEGTIG---IALNLESSNVGVVLMGDGLmiQ 84
Cdd:PRK06820 9 LTPRLQQQLTRPSAPPEgLRYRGPIVEIGPTLLRA-SLPGVAQGELCRIEPQGMLaevVSIEQEMALLSPFASSDGL--R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 85 EGSSVKATGRIAQIPVSESYLGRVINALAKPIDGrGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQ 164
Cdd:PRK06820 86 CGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 165 RELIIGDRQTGKTAVATdTILNQKGQNVIcVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTGA 244
Cdd:PRK06820 165 RIGIFAAAGVGKSTLLG-MLCADSAADVM-VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 245 ALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsrlgEGSMTALPIVETQS 324
Cdd:PRK06820 243 TIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSD----RGSITAFYTVLVEG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 325 GDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELEAFAQ---FAS 401
Cdd:PRK06820 319 DDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRvgeYQA 398
|
410 420
....*....|....*....|...
gi 190358244 402 DLDKATQNQLARGQRLRELLKQS 424
Cdd:PRK06820 399 GEDLQADEALQRYPAICAFLQQD 421
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
95-366 |
1.25e-44 |
|
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: 158.54 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 95 IAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGD--- 171
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGsgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 172 ----------RQTGktavatdtiLNQKGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPY 241
Cdd:cd01135 81 phnelaaqiaRQAG---------VVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 242 TGAALAEYFMY-RERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKSSSRlgEGSMTAL 317
Cdd:cd01135 152 MALTTAEYLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQI 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 190358244 318 PIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR 366
Cdd:cd01135 227 PILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
16-420 |
2.11e-43 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 159.61 E-value: 2.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 16 RIEQYNREIKivnTGTVLQVGDGIArihgldevmageLVEFEEGTIGIALnlessnvgvvlmgdglmiqEGSSVKATGRI 95
Cdd:PRK04196 30 EIELPNGEKR---RGQVLEVSEDKA------------VVQVFEGTTGLDL-------------------KDTKVRFTGEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 96 AQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR---------- 165
Cdd:PRK04196 76 LKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 166 --EL---IIgdRQTgktavatdTILNQKGQNVIcVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAP 240
Cdd:PRK04196 156 hnELaaqIA--RQA--------KVLGEEENFAV-VFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 241 YTGAALAEYFMY-RERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKSSSRlgEGSMTA 316
Cdd:PRK04196 225 RMALTAAEYLAFeKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 317 LPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVgsaaqikaMKQVAGKSKlelaqfaeleaf 396
Cdd:PRK04196 300 IPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRL--------MKDGIGEGK------------ 359
|
410 420
....*....|....*....|....*...
gi 190358244 397 aqfASDLDKATQNQL----ARGQRLREL 420
Cdd:PRK04196 360 ---TREDHKDVANQLyaayARGKDLREL 384
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
13-424 |
7.90e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 154.84 E-value: 7.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 13 IRERIEQYNREIKIvntGTVLQVGDGIARIHGLdEVMAGELVEFEEG-----TIGIALNLESSNVGVVLMG--DGLMIqe 85
Cdd:PRK08472 6 LKNKLQKFNLSPRF---GSITKISPTIIEADGL-NPSVGDIVKIESSdngkeCLGMVVVIEKEQFGISPFSfiEGFKI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 86 GSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR 165
Cdd:PRK08472 80 GDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 166 ELIIGDRQTGKTAVATDTILNQKGQnvICVYVAIGQKASSVAQvvttFQER---GAMEYTIVVAETADSSATLQYLAPYT 242
Cdd:PRK08472 160 LGIFAGSGVGKSTLMGMIVKGCLAP--IKVVALIGERGREIPE----FIEKnlgGDLENTVIVVATSDDSPLMRKYGAFC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 243 GAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsrlGEGSMTALPIVET 322
Cdd:PRK08472 234 AMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEE---GKGSITAFFTVLV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 323 QSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELEAFAQFAS- 401
Cdd:PRK08472 311 EGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAy 390
|
410 420
....*....|....*....|....*
gi 190358244 402 --DLDKATQNQLARGQRLRELLKQS 424
Cdd:PRK08472 391 qkGNDKELDEAISKKEFMEQFLKQN 415
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
86-379 |
5.62e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 147.15 E-value: 5.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 86 GSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR 165
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 166 ELIIGDRQTGKTaVATDTILNQKGQNVICVYVaIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTGAA 245
Cdd:PRK08972 165 MGLFAGSGVGKS-VLLGMMTRGTTADVIVVGL-VGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 246 LAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSrlGEGSMTALPIVETQSG 325
Cdd:PRK08972 243 IAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVLTEGD 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 190358244 326 DVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVG----SAAQIKAMKQV 379
Cdd:PRK08972 321 DLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMpmviSEEHLEAMRRV 378
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
41-426 |
3.95e-38 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 144.37 E-value: 3.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 41 RIHG------LDEVMAGELVE-----FEEGTIGIA--LNLESSNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSESYLGR 107
Cdd:PRK08149 12 RIQGpiieaeLPDVAIGEICEiragwHSNEVIARAqvVGFQRERTILSLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 108 VINALAKpIDGR-----GEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATd 182
Cdd:PRK08149 92 VLDPTGK-IVERfdappTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMN- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 183 tILNQKGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTGAALAEYFMYRERHTLIIYD 262
Cdd:PRK08149 170 -MLIEHSEADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFID 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 263 DLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERaaksSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQ 342
Cdd:PRK08149 249 SMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLER----PGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 343 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELEAFAQFA-------SDLDKATQNQlargQ 415
Cdd:PRK08149 325 IYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGeyrrgenADNDRAMDKR----P 400
|
410
....*....|.
gi 190358244 416 RLRELLKQSQA 426
Cdd:PRK08149 401 ALEAFLKQDVA 411
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
83-436 |
9.16e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 143.71 E-value: 9.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 83 IQEGSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR 162
Cdd:PRK07721 78 IAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 163 GQRELIIGDRQTGKTA----VATDTilnQKGQNVICVyvaIGQKASSVAQvvttFQERG----AMEYTIVVAETADSSAT 234
Cdd:PRK07721 158 GQRVGIFAGSGVGKSTlmgmIARNT---SADLNVIAL---IGERGREVRE----FIERDlgpeGLKRSIVVVATSDQPAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 235 LQYLAPYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSrlgeGSM 314
Cdd:PRK07721 228 MRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS----GSI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 315 TALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELE 394
Cdd:PRK07721 304 TAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSE 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 190358244 395 ------AFAQFAS-DLDKATQNQLArgqrLRELLKQSQAAPLRVEEQVA 436
Cdd:PRK07721 384 dlinigAYKRGSSrEIDEAIQFYPQ----IISFLKQGTDEKATFEESIQ 428
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
17-429 |
3.23e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 142.44 E-value: 3.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 17 IEQYNREIKIVNT-GTVLQVGDGIARIHGL-DEVMAGELVEFEEGT---IGIALNLESSNVGVVLMGDGLMIQEGSSVKA 91
Cdd:PRK06002 14 VERYAAPEPLVRIgGTVSEVTASHYRVRGLsRFVRLGDFVAIRADGgthLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 92 TGRiAQIPVSESYLGRVINALAKPIDGRGEISASESRL-IESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIG 170
Cdd:PRK06002 94 KGP-LRIRPDPSWKGRVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 171 DRQTGKT--------AVATDTilnqkgqnvicVYVA-IGQKASSVAQvvttFQE---RGAMEYTIVVAETADSSATLQYL 238
Cdd:PRK06002 173 GSGVGKStllamlarADAFDT-----------VVIAlVGERGREVRE----FLEdtlADNLKKAVAVVATSDESPMMRRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 239 APYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSrlGEGSMTALP 318
Cdd:PRK06002 238 APLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 319 IVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAE---LEA 395
Cdd:PRK06002 316 SVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdLRL 395
|
410 420 430
....*....|....*....|....*....|....*...
gi 190358244 396 FAQFA----SDLDKAtqnqLARGQRLRELLKQSQAAPL 429
Cdd:PRK06002 396 IGGYRagsdPDLDQA----VDLVPRIYEALRQSPGDPP 429
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
83-444 |
8.52e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 138.32 E-value: 8.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 83 IQEGSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR 162
Cdd:PRK05688 88 IAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 163 GQRELIIGDRQTGKTAVAtdTILNQKGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYT 242
Cdd:PRK05688 168 GQRLGLFAGTGVGKSVLL--GMMTRFTEADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 243 GAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAksSSRLGEGSMTALPIVET 322
Cdd:PRK05688 246 CTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 323 QSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVgsaaqikaMKQVAGKSKLELAQ-FAELEAFAQFAS 401
Cdd:PRK05688 324 EGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV--------MPQVVDPEHLRRAQrFKQLWSRYQQSR 395
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 190358244 402 DL----------DKATQNQLARGQRLRELLKQS--QAAPL-RVEEQVATIYTGANG 444
Cdd:PRK05688 396 DLisvgayvaggDPETDLAIARFPHLVQFLRQGlrENVSLaQSREQLAAIFAPAAG 451
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
87-376 |
1.04e-35 |
|
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: 138.70 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 87 SSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRE 166
Cdd:TIGR01040 65 TTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 167 LIIGD-------------RQTGKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSA 233
Cdd:TIGR01040 145 PIFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 234 TLQYLAPYTGAALAEYFMY-RERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRlgEG 312
Cdd:TIGR01040 225 IERIITPRLALTTAEYLAYqCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR--NG 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190358244 313 SMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAM 376
Cdd:TIGR01040 303 SITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
86-438 |
2.74e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 136.94 E-value: 2.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 86 GSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR 165
Cdd:PRK07196 78 GARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 166 ELIIGDRQTGKTAVAtdTILNQKGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTGAA 245
Cdd:PRK07196 158 VGLMAGSGVGKSVLL--GMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 246 LAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsrlGEGSMTALPIVETQSG 325
Cdd:PRK07196 236 IATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSS---GNGTMTAIYTVLAEGD 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 326 DVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSaaQIKAMKQVAGKSKLELA-----QFAELEAFAQFA 400
Cdd:PRK07196 313 DQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS--QVIGSQQAKAASLLKQCyadymAIKPLIPLGGYV 390
|
330 340 350
....*....|....*....|....*....|....*...
gi 190358244 401 SDLDKATQNQLARGQRLRELLKQSQAAPLRVEEQVATI 438
Cdd:PRK07196 391 AGADPMADQAVHYYPAITQFLRQEVGHPALFSASVEQL 428
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-432 |
2.03e-34 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 134.31 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 29 TGTVLQVGDGIARIHgLDEVMAGELVEFE-EGTIGIALNLESSNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSESYLGR 107
Cdd:PRK07594 22 WGRIQDVSATLLNAW-LPGVFMGELCCIKpGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 108 VINALAKPIDGRgEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATdTILNQ 187
Cdd:PRK07594 101 VIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLA-MLCNA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 188 KGQNViCVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTGAALAEYFMYRERHTLIIYDDLSKQ 267
Cdd:PRK07594 179 PDADS-NVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 268 AQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAksssrLGE-GSMTALPIVETQSGDVSAYIPTNVISITDGQIFLS 346
Cdd:PRK07594 258 ARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 347 ADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELEAF---AQFASDLDKATQNQLARGQRLRELLKQ 423
Cdd:PRK07594 333 RRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLiriGEYQRGVDTDTDKAIDTYPDICTFLRQ 412
|
....*....
gi 190358244 424 SQAAPLRVE 432
Cdd:PRK07594 413 SKDEVCGPE 421
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
28-94 |
1.44e-31 |
|
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: 116.01 E-value: 1.44e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190358244 28 NTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESSNVGVVLMGDGLMIQEGSSVKATGR 94
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
31-394 |
2.01e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 125.86 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 31 TVLQVGDGIARIHGLDEVMAGELVEFEEGTigiALNLESSNVGVVLMGDGLMIQEGSsvkatgriAQIPVSESYLGRVIN 110
Cdd:PRK08927 36 HALSVGARIVVETRGGRPVPCEVVGFRGDR---ALLMPFGPLEGVRRGCRAVIANAA--------AAVRPSRAWLGRVVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 111 ALAKPIDGRGEISASES-RLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTavatdTILNQKG 189
Cdd:PRK08927 105 ALGEPIDGKGPLPQGPVpYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKS-----VLLSMLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 190 QNVIC---VYVAIGQKASSVAQVVT-TFQERGaMEYTIVVAETADSSATLQYLAPYTGAALAEYFMYRERHTLIIYDDLS 265
Cdd:PRK08927 180 RNADAdvsVIGLIGERGREVQEFLQdDLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 266 KQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAksSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFL 345
Cdd:PRK08927 259 RFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVM 336
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 190358244 346 SADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELE 394
Cdd:PRK08927 337 ERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADME 385
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
97-378 |
4.97e-27 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 113.34 E-value: 4.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 97 QIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 177 TaVATDTILNQKGQNVICVYVaIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTGAALAEYFMYRERH 256
Cdd:PRK07960 189 S-VLLGMMARYTQADVIVVGL-IGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQH 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 257 TLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSrlGEGSMTALPIVETQSGDVSAYIPTNVI 336
Cdd:PRK07960 267 VLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGDDQQDPIADSAR 344
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 190358244 337 SITDGQIFLSADLFNAGIRPAINVGISVSRVGSA-------AQIKAMKQ 378
Cdd:PRK07960 345 AILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAlideqhyARVRQFKQ 393
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
86-385 |
6.03e-26 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 109.99 E-value: 6.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 86 GSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR 165
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 166 ELIIGDRQTGKTAVAtdTILNQKGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTGAA 245
Cdd:PRK05922 160 IGVFSEPGSGKSSLL--STIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 246 LAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsrlgEGSMTALPIVetqsg 325
Cdd:PRK05922 238 IAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND----KGSITALYAI----- 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190358244 326 dvsAYIPTN-------VISITDGQIFLSADlFNAGIRPAINVGISVSRvgSAAQIKAMKQVAGKSKL 385
Cdd:PRK05922 309 ---LHYPNHpdiftdyLKSLLDGHFFLTPQ-GKALASPPIDILTSLSR--SARQLALPHHYAAAEEL 369
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
60-450 |
2.12e-24 |
|
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: 105.96 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 60 TIGIALNLESSNVGVVLMG--DGLmiQEGSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGI 137
Cdd:TIGR01039 40 TLEVAQHLGDDTVRTIAMGstDGL--VRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 138 ISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN-QKGQNVICVYVAIGQKASSVAQVVTTFQER 216
Cdd:TIGR01039 118 EEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKES 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 217 GAMEYTIVVAETADSSATLQYLAPYTGAALAEYFMYRERH-TLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLH 295
Cdd:TIGR01039 198 GVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQdVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 296 SRLLERAAKSSsrlgEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQI-K 374
Cdd:TIGR01039 278 GELQERITSTK----TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVgE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 375 AMKQVAGKSKLELAQFAELEAFAQF-----ASDLDKATqnqLARGQRLRELLKQsqaaPLRVEEQvatiYTGANGYLDSL 449
Cdd:TIGR01039 354 EHYDVARGVQQILQRYKELQDIIAIlgmdeLSEEDKLT---VERARRIQRFLSQ----PFFVAEV----FTGQPGKYVPL 422
|
.
gi 190358244 450 E 450
Cdd:TIGR01039 423 K 423
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
86-367 |
1.53e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 102.75 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 86 GSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR 165
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 166 ELIIGDRQTGKTAVATDTILNQKGQ-NVICVyvaIGQKASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTGA 244
Cdd:PRK06793 159 IGIFAGSGVGKSTLLGMIAKNAKADiNVISL---VGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLAT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 245 ALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPgreaYPGDVFYLHS---RLLERAAKSSsrlgEGSMTALPIVE 321
Cdd:PRK06793 236 SIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQ----KGSITGIYTVL 307
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 190358244 322 TQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRV 367
Cdd:PRK06793 308 VDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRI 353
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
145-366 |
1.77e-19 |
|
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: 88.79 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 145 EPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTaVATDTILNQKGQNVIcVYVAIGQKASSVAQVVTTFQE-------RG 217
Cdd:cd01134 58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKT-VISQSLSKWSNSDVV-IYVGCGERGNEMAEVLEEFPElkdpitgES 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 218 AMEYTIVVAET-----ADSSATLqylapYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvf 292
Cdd:cd01134 136 LMERTVLIANTsnmpvAAREASI-----YTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA--- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 293 YLHSRL---LERAAK-----SSSRlgEGSMTALPIVETQSGDVSAYIPTNVISITdgQIF--LSADLFNAGIRPAINVGI 362
Cdd:cd01134 208 YLGARLaefYERAGRvrclgSPGR--EGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLI 283
|
....
gi 190358244 363 SVSR 366
Cdd:cd01134 284 SYSK 287
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
51-345 |
1.77e-18 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 87.78 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 51 GELVEFEE---GTIGIALNLESSNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEIsasES 127
Cdd:PRK02118 26 GELATVERkdgSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPEL---EG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 128 RLIE------SPAPGIISRRSVyeplQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATdTILNQKGQNVIcVYVAIGQ 201
Cdd:PRK02118 103 EPIEiggpsvNPVKRIVPREMI----RTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA-RIALQAEADII-ILGGMGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 202 KASSVAQVVTTFQERGAMEYTIVVAETADSSATLQYLAPYTGAALAEYFMYRE-RHTLIIYDDLSKQAQAYRQMSLLLRR 280
Cdd:PRK02118 177 TFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLTDMTNFADALKEISITMDQ 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190358244 281 PPGREAYPGDvfyLHSRLLERAAKSSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFL 345
Cdd:PRK02118 257 IPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
97-367 |
1.59e-17 |
|
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: 82.65 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 97 QIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 177 TAVATDTILN-QKGQNVICVYVAIGQKASSVAQVVTTFQERGameytiVVAETADSSATLQY-----------LAPYTGA 244
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGERTREGNDLYHEMKESG------VINLDGLSKVALVYgqmneppgaraRVALTGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 245 ALAEYFMYRE-RHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSssrlGEGSMTALPIVETQ 323
Cdd:cd01133 155 TMAEYFRDEEgQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST----KKGSITSVQAVYVP 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 190358244 324 SGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRV 367
Cdd:cd01133 231 ADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
376-443 |
3.23e-17 |
|
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: 75.94 E-value: 3.23e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 376 MKQVAGKSKLELAQFAELEAFAQFASD--LDKATQNQLARGQRLRELLKQSQAAPLRVEEQVATIYTGAN 443
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
29-93 |
3.55e-16 |
|
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: 72.96 E-value: 3.55e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190358244 29 TGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESSNVGVVLMGDGLMIQEGSSVKATG 93
Cdd:pfam02874 5 IGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
145-366 |
3.56e-14 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 74.82 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 145 EPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTavatdtILNQ---KGQNV-ICVYVAIGQKASSVAQVVTTFQE----- 215
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT------VTQHqlaKWADAdIVIYVGCGERGNEMTEVLEEFPElidpk 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 216 --RGAMEYTIVVAETadSS-------ATLqylapYTGAALAEYfmYRE--RHTLIIYDDLSKQAQAYRQMSLLLRRPPGR 284
Cdd:PRK04192 283 tgRPLMERTVLIANT--SNmpvaareASI-----YTGITIAEY--YRDmgYDVLLMADSTSRWAEALREISGRLEEMPGE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 285 EAYPGdvfYLHSRL---LERAAKSSSRLG-EGSMTALPIVETQSGDVSAYIPTNVISITdgQIF--LSADLFNAGIRPAI 358
Cdd:PRK04192 354 EGYPA---YLASRLaefYERAGRVKTLGGeEGSVTIIGAVSPPGGDFSEPVTQNTLRIV--KVFwaLDAELADRRHFPAI 428
|
....*...
gi 190358244 359 NVGISVSR 366
Cdd:PRK04192 429 NWLTSYSL 436
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
79-163 |
9.21e-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: 70.12 E-value: 9.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 79 DGLmiQEGSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMI 158
Cdd:COG0055 64 DGL--VRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLA 141
|
....*
gi 190358244 159 PIGRG 163
Cdd:COG0055 142 PYAKG 146
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
29-94 |
6.28e-12 |
|
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: 61.17 E-value: 6.28e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190358244 29 TGTVLQVGDGIARIHGLDEVMAGELVEFEEG-------TIGIALNLESSNVGVVLMGDGLMIQEGSSVKATGR 94
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGdgnnetvLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
193-372 |
7.90e-12 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 68.12 E-value: 7.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 193 ICVYVAIGQKASSVAQVVTTFQE-------RGAMEYTIVVAETADSSATLQYLAPYTGAALAEYFMYRERHTLIIYDDLS 265
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 266 KQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKSSSRLGEGSMTALPIVETQSGDVSAYIPTNVISIT 339
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVV 840
|
170 180 190
....*....|....*....|....*....|...
gi 190358244 340 DGQIFLSADLFNAGIRPAINVGISVSRVGSAAQ 372
Cdd:PRK14698 841 KVFWALDADLARRRHFPAINWLTSYSLYVDAVK 873
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
79-359 |
1.36e-10 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 63.52 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 79 DGLMiqEGSSVKATGRIAQIPVSESYLGRVINALAKPIDGRGEISASESRLIESPAPGII---SRRSVYEplqTGLIAID 155
Cdd:CHL00060 79 DGLM--RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTKLSIFE---TGIKVVD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 156 SMIPIGRGQRELIIGDRQTGKTAVATDTILN-QKGQNVICVYVAIGQKASSVAQVVTTFQERGameyTIVVAETADSSAT 234
Cdd:CHL00060 154 LLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGERTREGNDLYMEMKESG----VINEQNIAESKVA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190358244 235 LQY-----------LAPYTGAALAEYFM-YRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERA 302
Cdd:CHL00060 230 LVYgqmneppgarmRVGLTALTMAEYFRdVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 190358244 303 AKSSsrlgEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAIN 359
Cdd:CHL00060 310 TSTK----EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 362
|
|
| |
