|
Name |
Accession |
Description |
Interval |
E-value |
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
23-506 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 1096.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 23 EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSE 102
Cdd:CHL00059 1 EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 103 AYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 182
Cdd:CHL00059 81 AYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 183 TILNQQGQNVICVYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMFRERHTLIIYD 262
Cdd:CHL00059 161 TILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 263 DLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQ 342
Cdd:CHL00059 241 DLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 343 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLK 422
Cdd:CHL00059 321 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 423 QSQAAPLTVEEQIMTIYTGTNGYLDSLEIGQVRKFLVELRTYVKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQKERFL 502
Cdd:CHL00059 401 QSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQLELFL 480
|
....
gi 2127895048 503 LQEQ 506
Cdd:CHL00059 481 LQEQ 484
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
3-502 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 977.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 3 TIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLM 82
Cdd:PRK09281 2 QINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 83 IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR 162
Cdd:PRK09281 82 IKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 163 GQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPATLQYLAPYT 242
Cdd:PRK09281 162 GQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 243 GAALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVET 322
Cdd:PRK09281 242 GCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIET 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 323 QSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASD 402
Cdd:PRK09281 322 QAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 403 LDKATQNQLARGQRLRELLKQSQAAPLTVEEQIMTIYTGTNGYLDSLEIGQVRKFLVELRTYVKTNKPQFQEIISSTKTF 482
Cdd:PRK09281 402 LDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKDL 481
|
490 500
....*....|....*....|
gi 2127895048 483 TEEAEALLKEAIQEQKERFL 502
Cdd:PRK09281 482 SDEIEAKLKAAIEEFKKTFA 501
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
3-501 |
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: 973.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 3 TIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLM 82
Cdd:COG0056 2 QIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 83 IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR 162
Cdd:COG0056 82 IKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 163 GQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPATLQYLAPYT 242
Cdd:COG0056 162 GQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 243 GAALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVET 322
Cdd:COG0056 242 GCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIET 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 323 QSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASD 402
Cdd:COG0056 322 QAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 403 LDKATQNQLARGQRLRELLKQSQAAPLTVEEQIMTIYTGTNGYLDSLEIGQVRKFLVELRTYVKTNKPQFQEIISSTKTF 482
Cdd:COG0056 402 LDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGKL 481
|
490
....*....|....*....
gi 2127895048 483 TEEAEALLKEAIQEQKERF 501
Cdd:COG0056 482 DDEIEEKLKAAIEEFKKTF 500
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
3-501 |
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: 837.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 3 TIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLM 82
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 83 IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR 162
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 163 GQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPATLQYLAPYT 242
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 243 GAALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVET 322
Cdd:TIGR00962 241 GCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 323 QSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASD 402
Cdd:TIGR00962 321 QAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 403 LDKATQNQLARGQRLRELLKQSQAAPLTVEEQIMTIYTGTNGYLDSLEIGQVRKFLVELRTYVKTNKPQFQEIISSTKTF 482
Cdd:TIGR00962 401 LDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKL 480
|
490
....*....|....*....
gi 2127895048 483 TEEAEALLKEAIQEQKERF 501
Cdd:TIGR00962 481 TEELEAKLKEALKNFKKTF 499
|
|
| 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: 755.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 4 IRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMI 83
Cdd:PRK13343 3 SNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 84 QEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRG 163
Cdd:PRK13343 83 LAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 164 QRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPATLQYLAPYTG 243
Cdd:PRK13343 163 QRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 244 AALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVETQ 323
Cdd:PRK13343 243 CAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 324 SGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDL 403
Cdd:PRK13343 323 AGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 404 DKATQNQLARGQRLRELLKQSQAAPLTVEEQIMTIYTGTNGYLDSLEIGQVRKFLVELRTYVKTNKPQFQEIISSTKTFT 483
Cdd:PRK13343 403 DAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRELD 482
|
490
....*....|....*...
gi 2127895048 484 EEAEALLKEAIQEQKERF 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: 584.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 95 IAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQT 174
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 175 GKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMFRE 254
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 255 RHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVETQSGDVSAYIPTN 334
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 2127895048 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: 554.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 7 DEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEG 86
Cdd:TIGR03324 6 DKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 87 SSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRE 166
Cdd:TIGR03324 86 DEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 167 LIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPATLQYLAPYTGAAL 246
Cdd:TIGR03324 166 LILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 247 AEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVETQSGD 326
Cdd:TIGR03324 246 GEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 327 VSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKA 406
Cdd:TIGR03324 326 ISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDEN 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2127895048 407 TQNQLARGQRLRELLKQSQAAPLTVEEQIMTIYTGTNGYLDSLEIGQV 454
Cdd:TIGR03324 406 TRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAM 453
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
62-457 |
3.60e-120 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 364.36 E-value: 3.60e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 62 GIALNLESNN-VGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPI-----DGRGEIYASESRL--IESP 133
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVpvgllTRSRALLESEQTLgkVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 134 APGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQQGQN--------VICVYVAIGQKASS 205
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINqqilsknaVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 206 VAQVVNTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGRE 285
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGRE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 286 AYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVS 365
Cdd:PTZ00185 320 AYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVS 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 366 RVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATqnqLARGQRLRELLKQSQaaPLTVEEQIMTIYTGTNGY 445
Cdd:PTZ00185 400 RVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNALVSLYACLNGY 474
|
410
....*....|..
gi 2127895048 446 LDSLEIGQVRKF 457
Cdd:PTZ00185 475 LDDVKVNYAKLY 486
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
150-365 |
3.99e-113 |
|
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: 333.17 E-value: 3.99e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 150 GLIAIDSMIPIGRGQRELIIGDRQTGKTAVAtDTILNQQGQNViCVYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETA 229
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 230 DSPATLQYLAPYTGAALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSll 309
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKG-- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2127895048 310 GEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVS 365
Cdd:pfam00006 157 KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
97-478 |
1.05e-105 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 325.00 E-value: 1.05e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 97 QIPVSEAYLGRVINALAKPIDGRGEIYASESRLI-ESP----APGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGD 171
Cdd:PRK07165 72 KVKTSKEYFGKIIDIDGNIIYPEAQNPLSKKFLPnTSSifnlAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGD 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 172 RQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPATlQYLAPYTGAALAEYFM 251
Cdd:PRK07165 152 RQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAENIS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 252 FRErHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlssLLGEGSMTALPIVETQSGDVSAYI 331
Cdd:PRK07165 231 YND-DVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGK---FKNRKTITALPILQTVDNDITSLI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 332 PTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQL 411
Cdd:PRK07165 307 SSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLL 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127895048 412 ARGQRLRELLKQSQAAPLTVEEQIMTIYTGTNGYLDSL-EIGQVRKFLVELRTYVKTNKPQFQEIISS 478
Cdd:PRK07165 387 FKGKMIEKMFNQKGFSLYSYRFVLLISKLISWGLLKDVkDEQKALDFIDYLIENDPDAKKIFNKIKNN 454
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
97-367 |
4.46e-102 |
|
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: 307.46 E-value: 4.46e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 97 QIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 177 TAVATDTILNQQGQNV-ICVYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMFRER 255
Cdd:cd19476 81 TVLAMQLARNQAKAHAgVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 256 HTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSllGEGSMTALPIVETQSGDVSAYIPTNV 335
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 2127895048 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 |
1.01e-62 |
|
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: 200.28 E-value: 1.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 376 MKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQAAPLTVEEQIMTIYTGTNGYLDSLEIGQVR 455
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2127895048 456 KFLVELRTYVKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQKERF 501
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
372-496 |
7.64e-60 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 193.04 E-value: 7.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 372 QIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQAAPLTVEEQIMTIYTGTNGYLDSLEI 451
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2127895048 452 GQVRKFLVELRTYVKTNKPQFQEIISSTKTFTEEAEALLKEAIQE 496
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEE 125
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
97-367 |
1.21e-50 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 173.90 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 97 QIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 177 TavatdTILNQQGQNV---ICVYVAIGQKASSVAQ-VVNTLQERGaMEYTIVVAETADSPATLQYLAPYTGAALAEYFMF 252
Cdd:cd01136 81 S-----TLLGMIARNTdadVNVIALIGERGREVREfIEKDLGEEG-LKRSVLVVATSDESPLLRVRAAYTATAIAEYFRD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 253 RERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSsllgEGSMTALPIVETQSGDVSAYIP 332
Cdd:cd01136 155 QGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGE----KGSITAFYTVLVEGDDFNDPIA 230
|
250 260 270
....*....|....*....|....*....|....*
gi 2127895048 333 TNVISITDGQIFLSADLFNAGIRPAINVGISVSRV 367
Cdd:cd01136 231 DEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
29-433 |
1.66e-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: 172.91 E-value: 1.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 29 TGTVLQVGDgIARIYGLD-EVMAGELVEFEEGTigialnlesnnvgVVLM--GDGLMIQEGSSVKATGRIAQIPVSEAYL 105
Cdd:COG1157 34 VGPDASIGE-LCEIETADgRPVLAEVVGFRGDR-------------VLLMplGDLEGISPGARVVPTGRPLSVPVGDGLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 106 GRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQReliIGdr---qtGKTavatd 182
Cdd:COG1157 100 GRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR---IGifagsgvGKS----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 183 TILNQQGQNV---ICVyVA-IGqkassvaqvvntlqERG--------------AMEYTIVVAETADSPATLQYLAPYTGA 244
Cdd:COG1157 172 TLLGMIARNTeadVNV-IAlIG--------------ERGrevrefieddlgeeGLARSVVVVATSDEPPLMRLRAAYTAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 245 ALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlsslLGEGSMTAL------- 317
Cdd:COG1157 237 AIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN----GGKGSITAFytvlveg 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 318 -----PIVETqsgdvsayiptnVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAE 392
Cdd:COG1157 313 ddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEE 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2127895048 393 LE------AFAQFAS-DLDKAtqnqLARGQRLRELLKQSQAAPLTVEE 433
Cdd:COG1157 381 NEdlirigAYQPGSDpELDEA----IALIPAIEAFLRQGMDERVSFEE 424
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
77-443 |
9.42e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 171.09 E-value: 9.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 77 MGDGLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDS 156
Cdd:PRK06936 76 LGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 157 MIPIGRGQRELIIGDRQTGKTAVATDTILNQQGQnvICVYVAIGQKASSVAQVV-NTLQERGaMEYTIVVAETADSPATL 235
Cdd:PRK06936 156 LLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVD--VTVLALIGERGREVREFIeSDLGEEG-LRKAVLVVATSDRPSME 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 236 QYLAPYTGAALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSsllgEGSMT 315
Cdd:PRK06936 233 RAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSD----KGSIT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 316 ALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEA 395
Cdd:PRK06936 309 ALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVEL 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2127895048 396 FAQ---FASDLDKATQNQLARGQRLRELLKQSQAAPLTVEEQIMTIYTGTN 443
Cdd:PRK06936 389 LLQigeYQKGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETLTQ 439
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
9-424 |
1.10e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 168.45 E-value: 1.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 9 ISNIIRERIEQYNREVK-IVNTGTVLQVGDGIARIyGLDEVMAGELVEFE-EGTIGIALNLESNNVGVVLMGDGLMIQEG 86
Cdd:PRK06820 9 LTPRLQQQLTRPSAPPEgLRYRGPIVEIGPTLLRA-SLPGVAQGELCRIEpQGMLAEVVSIEQEMALLSPFASSDGLRCG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 87 SSVKATGRIAQIPVSEAYLGRVINALAKPIDGrGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRE 166
Cdd:PRK06820 88 QWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 167 LIIGDRQTGKTAVATdTILNQQGQNVIcVYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPATLQYLAPYTGAAL 246
Cdd:PRK06820 167 GIFAAAGVGKSTLLG-MLCADSAADVM-VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 247 AEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSsllgEGSMTALPIVETQSGD 326
Cdd:PRK06820 245 AEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSD----RGSITAFYTVLVEGDD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 327 VSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQ---FASDL 403
Cdd:PRK06820 321 MNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRvgeYQAGE 400
|
410 420
....*....|....*....|.
gi 2127895048 404 DKATQNQLARGQRLRELLKQS 424
Cdd:PRK06820 401 DLQADEALQRYPAICAFLQQD 421
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
5-424 |
2.28e-44 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 161.86 E-value: 2.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 5 RADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIYGLDeVMAGELVEF--EEGTIGIALNLESNNVGVVLM---GD 79
Cdd:PRK09099 1 ALAELSRLADALERELAALPAVRRTGKVVEVIGTLLRVSGLD-VTLGELCELrqRDGTLLQRAEVVGFSRDVALLspfGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 80 GLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIP 159
Cdd:PRK09099 80 LGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 160 IGRGQRELIIGDRQTGKTavatdTILNQQGQNVIC---VYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPATLQ 236
Cdd:PRK09099 160 LGEGQRMGIFAPAGVGKS-----TLMGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 237 YLAPYTGAALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsslLGE-GSMT 315
Cdd:PRK09099 235 AKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-----MGEtGSIT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 316 ALPIV--ETQSGdvSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAEL 393
Cdd:PRK09099 310 ALYTVlaEDESG--SDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREV 387
|
410 420 430
....*....|....*....|....*....|....
gi 2127895048 394 EAFAQ---FASDLDKATQNQLARGQRLRELLKQS 424
Cdd:PRK09099 388 ETLLQvgeYRAGSDPVADEAIAKIDAIRDFLSQR 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 |
3.97e-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: 157.00 E-value: 3.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 95 IAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGD--- 171
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGsgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 172 ----------RQTGktavatdtiLNQQGQNVICVYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPATLQYLAPY 241
Cdd:cd01135 81 phnelaaqiaRQAG---------VVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 242 TGAALAEYFMF-RERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSSLlgEGSMTAL 317
Cdd:cd01135 152 MALTTAEYLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQI 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2127895048 318 PIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR 366
Cdd:cd01135 227 PILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
16-420 |
4.10e-44 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 161.53 E-value: 4.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 16 RIEQYNREVKivnTGTVLQVGDGIAriygldevmageLVEFEEGTIGIALnlesnnvgvvlmgdglmiqEGSSVKATGRI 95
Cdd:PRK04196 30 EIELPNGEKR---RGQVLEVSEDKA------------VVQVFEGTTGLDL-------------------KDTKVRFTGEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 96 AQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR---------- 165
Cdd:PRK04196 76 LKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 166 --EL---IIgdRQTgktavatdTILNQQGQNVIcVYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPATLQYLAP 240
Cdd:PRK04196 156 hnELaaqIA--RQA--------KVLGEEENFAV-VFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 241 YTGAALAEYFMF-RERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSSLlgEGSMTA 316
Cdd:PRK04196 225 RMALTAAEYLAFeKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 317 LPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVgsaaqikaMKQVAGKLKlelaqfaeleaf 396
Cdd:PRK04196 300 IPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRL--------MKDGIGEGK------------ 359
|
410 420
....*....|....*....|....*...
gi 2127895048 397 aqfASDLDKATQNQL----ARGQRLREL 420
Cdd:PRK04196 360 ---TREDHKDVANQLyaayARGKDLREL 384
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
83-435 |
1.06e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 151.80 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 83 IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR 162
Cdd:PRK07721 78 IAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 163 GQRELIIGDRQTGKTAVATDTILNQQGQ-NVICVyvaIGQKASSVAQVV-NTLQERGaMEYTIVVAETADSPATLQYLAP 240
Cdd:PRK07721 158 GQRVGIFAGSGVGKSTLMGMIARNTSADlNVIAL---IGERGREVREFIeRDLGPEG-LKRSIVVVATSDQPALMRIKGA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 241 YTGAALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSllgeGSMTALPIV 320
Cdd:PRK07721 234 YTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS----GSITAFYTV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 321 ETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELE------ 394
Cdd:PRK07721 310 LVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEdlinig 389
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2127895048 395 AFAQFAS-DLDKATQNQLArgqrLRELLKQSQAAPLTVEEQI 435
Cdd:PRK07721 390 AYKRGSSrEIDEAIQFYPQ----IISFLKQGTDEKATFEESI 427
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
30-435 |
6.48e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 149.45 E-value: 6.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 30 GTVLQVGDGIARIYGLdEVMAGELVEFEEG-----TIGIALNLESNNVGVVLMG--DGLMIqeGSSVKATGRIAQIPVSE 102
Cdd:PRK08472 20 GSITKISPTIIEADGL-NPSVGDIVKIESSdngkeCLGMVVVIEKEQFGISPFSfiEGFKI--GDKVFISKEGLNIPVGR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 103 AYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 182
Cdd:PRK08472 97 NLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 183 TILNQQGQnvICVYVAIGQKASSVAQVVNTlQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMFRERHTLIIYD 262
Cdd:PRK08472 177 IVKGCLAP--IKVVALIGERGREIPEFIEK-NLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 263 DLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSsllGEGSMTALPIVETQSGDVSAYIPTNVISITDGQ 342
Cdd:PRK08472 254 SVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEE---GKGSITAFFTVLVEGDDMSDPIADQSRSILDGH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 343 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFAS---DLDKATQNQLARGQRLRE 419
Cdd:PRK08472 331 IVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAyqkGNDKELDEAISKKEFMEQ 410
|
410
....*....|....*.
gi 2127895048 420 LLKQSQAAPLTVEEQI 435
Cdd:PRK08472 411 FLKQNPNELFPFEQTF 426
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
41-433 |
4.44e-39 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 147.06 E-value: 4.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 41 RIYG------LDEVMAGELVE-----FEEGTIGIALNLESNNVGVVL--MGDGLMIQEGSSVKATGRIAQIPVSEAYLGR 107
Cdd:PRK08149 12 RIQGpiieaeLPDVAIGEICEiragwHSNEVIARAQVVGFQRERTILslIGNAQGLSRQVVLKPTGKPLSVWVGEALLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 108 VINALAKpIDGR-----GEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATd 182
Cdd:PRK08149 92 VLDPTGK-IVERfdappTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMN- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 183 tILNQQGQNVICVYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMFRERHTLIIYD 262
Cdd:PRK08149 170 -MLIEHSEADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFID 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 263 DLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSllgeGSMTALPIVETQSGDVSAYIPTNVISITDGQ 342
Cdd:PRK08149 249 SMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA----GSITAFYTVLLESEEEPDPIGDEIRSILDGH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 343 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFA-------SDLDKATQNQlargQ 415
Cdd:PRK08149 325 IYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGeyrrgenADNDRAMDKR----P 400
|
410
....*....|....*...
gi 2127895048 416 RLRELLKQSQAAPLTVEE 433
Cdd:PRK08149 401 ALEAFLKQDVAEKSSFSD 418
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-440 |
1.88e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 145.48 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 29 TGTVLQVGDGIARIYgLDEVMAGELVEFE-EGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGR 107
Cdd:PRK07594 22 WGRIQDVSATLLNAW-LPGVFMGELCCIKpGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 108 VINALAKPIDGRgEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATdTILNQ 187
Cdd:PRK07594 101 VIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLA-MLCNA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 188 QGQNViCVYVAIGQKASSVAQVVN-TLQERGAMEYTIVVAeTADSPATLQYLAPYTGAALAEYFMFRERHTLIIYDDLSK 266
Cdd:PRK07594 179 PDADS-NVLVLIGERGREVREFIDfTLSEETRKRCVIVVA-TSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 267 QAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsslLGE-GSMTALPIVETQSGDVSAYIPTNVISITDGQIFL 345
Cdd:PRK07594 257 YARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 346 SADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAF---AQFASDLDKATQNQLARGQRLRELLK 422
Cdd:PRK07594 332 SRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLiriGEYQRGVDTDTDKAIDTYPDICTFLR 411
|
410 420
....*....|....*....|.
gi 2127895048 423 QSQAAPLTVE---EQIMTIYT 440
Cdd:PRK07594 412 QSKDEVCGPElliEKLHQILT 432
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
86-379 |
6.12e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 144.46 E-value: 6.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 86 GSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR 165
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 166 ELIIGDRQTGKTaVATDTILNQQGQNVICVYVaIGQKASSVAQVV-NTLQERGaMEYTIVVAETADSPATLQYLAPYTGA 244
Cdd:PRK08972 165 MGLFAGSGVGKS-VLLGMMTRGTTADVIVVGL-VGERGREVKEFIeEILGEEG-RARSVVVAAPADTSPLMRLKGCETAT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 245 ALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSllGEGSMTALPIVETQS 324
Cdd:PRK08972 242 TIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVLTEG 319
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2127895048 325 GDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVG----SAAQIKAMKQV 379
Cdd:PRK08972 320 DDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMpmviSEEHLEAMRRV 378
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
17-432 |
7.50e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 141.29 E-value: 7.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 17 IEQYNREVKIVNT-GTVLQVGDGIARIYGL-DEVMAGELVEFEEGT---IGIALNLESNNVGVVLMGDGLMIQEGSSVKA 91
Cdd:PRK06002 14 VERYAAPEPLVRIgGTVSEVTASHYRVRGLsRFVRLGDFVAIRADGgthLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 92 TGRiAQIPVSEAYLGRVINALAKPIDGRGEIYASESRL-IESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIG 170
Cdd:PRK06002 94 KGP-LRIRPDPSWKGRVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 171 DRQTGKT--------AVATDTilnqqgqnvicVYVA-IGQKASSVAQVV-NTLQerGAMEYTIVVAETADSPATLQYLAP 240
Cdd:PRK06002 173 GSGVGKStllamlarADAFDT-----------VVIAlVGERGREVREFLeDTLA--DNLKKAVAVVATSDESPMMRRLAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 241 YTGAALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSSLLGEGSMTALPIV 320
Cdd:PRK06002 240 LTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAG--PGAEGGGSITGIFSV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 321 ETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAE---LEAFA 397
Cdd:PRK06002 318 LVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdLRLIG 397
|
410 420 430
....*....|....*....|....*....|....*....
gi 2127895048 398 QFA----SDLDKAtqnqLARGQRLRELLKQSQAAPLTVE 432
Cdd:PRK06002 398 GYRagsdPDLDQA----VDLVPRIYEALRQSPGDPPSDD 432
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
87-376 |
3.81e-34 |
|
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: 134.08 E-value: 3.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 87 SSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRE 166
Cdd:TIGR01040 65 TTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 167 LIIGD-------------RQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPA 233
Cdd:TIGR01040 145 PIFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 234 TLQYLAPYTGAALAEYFMF-RERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSLlgEG 312
Cdd:TIGR01040 225 IERIITPRLALTTAEYLAYqCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR--NG 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127895048 313 SMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAM 376
Cdd:TIGR01040 303 SITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
83-444 |
5.76e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 133.32 E-value: 5.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 83 IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR 162
Cdd:PRK05688 88 IAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 163 GQRELIIGDRQTGKTAVAtdTILNQQGQNVICVYVAIGQKASSVAQVV-NTLQERGaMEYTIVVAETADSPATLQYLAPY 241
Cdd:PRK05688 168 GQRLGLFAGTGVGKSVLL--GMMTRFTEADIIVVGLIGERGREVKEFIeHILGEEG-LKRSVVVASPADDAPLMRLRAAM 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 242 TGAALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSllGEGSMTALPIVE 321
Cdd:PRK05688 245 YCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEP--GGGSITAFYTVL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 322 TQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVgsaaqikaMKQVAGKLKLELAQ-FAELEAFAQFA 400
Cdd:PRK05688 323 SEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV--------MPQVVDPEHLRRAQrFKQLWSRYQQS 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2127895048 401 SDL----------DKATQNQLARGQRLRELLKQS--QAAPLT-VEEQIMTIYTGTNG 444
Cdd:PRK05688 395 RDLisvgayvaggDPETDLAIARFPHLVQFLRQGlrENVSLAqSREQLAAIFAPAAG 451
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
86-428 |
9.45e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 129.63 E-value: 9.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 86 GSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR 165
Cdd:PRK07196 78 GARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 166 ELIIGDRQTGKTAVAtdTILNQQGQNVICVYVAIGQKASSVAQVV-NTLQERGaMEYTIVVAETADSPATLQYLAPYTGA 244
Cdd:PRK07196 158 VGLMAGSGVGKSVLL--GMITRYTQADVVVVGLIGERGREVKEFIeHSLQAAG-MAKSVVVAAPADESPLMRIKATELCH 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 245 ALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSsllGEGSMTALPIVETQS 324
Cdd:PRK07196 235 AIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSS---GNGTMTAIYTVLAEG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 325 GDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAE---LEAFAQFAS 401
Cdd:PRK07196 312 DDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAikpLIPLGGYVA 391
|
330 340
....*....|....*....|....*..
gi 2127895048 402 DLDKATQNQLARGQRLRELLKQSQAAP 428
Cdd:PRK07196 392 GADPMADQAVHYYPAITQFLRQEVGHP 418
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
31-394 |
2.34e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 128.56 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 31 TVLQVGDGIARIYGLDEVMAGELVEFEEGTigialnlesnnvgVVLMG----DGlmIQEGSSVKATGRIAQIPVSEAYLG 106
Cdd:PRK08927 36 HALSVGARIVVETRGGRPVPCEVVGFRGDR-------------ALLMPfgplEG--VRRGCRAVIANAAAAVRPSRAWLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 107 RVINALAKPIDGRGEIYASES-RLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTavatdTIL 185
Cdd:PRK08927 101 RVVNALGEPIDGKGPLPQGPVpYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKS-----VLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 186 NQQGQNVIC---VYVAIGQKASSVAQVV-NTLQERGaMEYTIVVAETADSPATLQYLAPYTGAALAEYFMFRERHTLIIY 261
Cdd:PRK08927 176 SMLARNADAdvsVIGLIGERGREVQEFLqDDLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 262 DDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSSLLGEGSMTALPIVETQSGDVSAYIPTNVISITDG 341
Cdd:PRK08927 255 DSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDG 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2127895048 342 QIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELE 394
Cdd:PRK08927 333 HIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADME 385
|
|
| 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 |
5.67e-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: 116.78 E-value: 5.67e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2127895048 28 NTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGR 94
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
28-450 |
1.33e-26 |
|
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: 112.12 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 28 NTGTVLQV----------GDGIARIYGLDEVMAGELVEFeegTIGIALNLESNNVGVVLMG--DGLmiQEGSSVKATGRI 95
Cdd:TIGR01039 1 TKGKVVQVigpvvdvefeQGELPRIYNALKVQNRAESEL---TLEVAQHLGDDTVRTIAMGstDGL--VRGLEVIDTGAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 96 AQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTG 175
Cdd:TIGR01039 76 ISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 176 KTAVATDTILN-QQGQNVICVYVAIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMFRE 254
Cdd:TIGR01039 156 KTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 255 RH-TLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSsllgEGSMTALPIVETQSGDVSAYIPT 333
Cdd:TIGR01039 236 GQdVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTK----TGSITSVQAVYVPADDLTDPAPA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 334 NVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQI-KAMKQVAGKLKLELAQFAELEAFAQF-----ASDLDKAT 407
Cdd:TIGR01039 312 TTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVgEEHYDVARGVQQILQRYKELQDIIAIlgmdeLSEEDKLT 391
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2127895048 408 qnqLARGQRLRELLKQsqaaPLTVEEQimtiYTGTNGYLDSLE 450
Cdd:TIGR01039 392 ---VERARRIQRFLSQ----PFFVAEV----FTGQPGKYVPLK 423
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
97-378 |
2.82e-26 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 111.41 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 97 QIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 177 TaVATDTILNQQGQNVICVYVaIGQKASSVAQVV-NTLQERGaMEYTIVVAETADSPATLQYLAPYTGAALAEYFMFRER 255
Cdd:PRK07960 189 S-VLLGMMARYTQADVIVVGL-IGERGREVKDFIeNILGAEG-RARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQ 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 256 HTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSSLLGEGSMTALPIVETQSGDVSAYIPTNV 335
Cdd:PRK07960 266 HVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG--NGISGGGSITAFYTVLTEGDDQQDPIADSA 343
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2127895048 336 ISITDGQIFLSADLFNAGIRPAINVGISVSRVGSA-------AQIKAMKQ 378
Cdd:PRK07960 344 RAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAlideqhyARVRQFKQ 393
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
86-435 |
1.93e-25 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 108.45 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 86 GSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR 165
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 166 ELIIGDRQTGKTA-VATDTILNQQGQNVICVyvaIGQKASSVAQVVNTLQERGAMEYTIVVAETADSPATLQYLAPYTGA 244
Cdd:PRK05922 160 IGVFSEPGSGKSSlLSTIAKGSKSTINVIAL---IGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAM 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 245 ALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSsllgEGSMTALPIVetqs 324
Cdd:PRK05922 237 TIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND----KGSITALYAI---- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 325 gdvsAYIPTN-------VISITDGQIFLSADlFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFA 397
Cdd:PRK05922 309 ----LHYPNHpdiftdyLKSLLDGHFFLTPQ-GKALASPPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDII 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2127895048 398 QFAS-------DLDKATqnqlargqRLRELLKQSQAAPLTVEEQI 435
Cdd:PRK05922 384 QLGAyvpgqdaHLDRAV--------KLLPSIKQFLSQPLSSYCAL 420
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
86-396 |
1.24e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 100.05 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 86 GSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR 165
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 166 ELIIGDRQTGKTavatdTILNQQGQNV---ICVYVAIGQKASSVAQVV-NTLQERGaMEYTIVVAETADSPATLQYLAPY 241
Cdd:PRK06793 159 IGIFAGSGVGKS-----TLLGMIAKNAkadINVISLVGERGREVKDFIrKELGEEG-MRKSVVVVATSDESHLMQLRAAK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 242 TGAALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPgreaYPGDVFYLHS---RLLERAAKLSsllgEGSMTALP 318
Cdd:PRK06793 233 LATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQ----KGSITGIY 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127895048 319 IVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAF 396
Cdd:PRK06793 305 TVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELY 382
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
145-366 |
2.76e-20 |
|
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: 91.10 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 145 EPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTavatdtILNQQ----GQNVICVYVAIGQKASSVAQVVN-------TL 213
Cdd:cd01134 58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKT------VISQSlskwSNSDVVIYVGCGERGNEMAEVLEefpelkdPI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 214 QERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMFRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfY 293
Cdd:cd01134 132 TGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---Y 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 294 LHSRL---LERAAK---LSSLLGEGSMTALPIVETQSGDVSAYIPTNVISITdgQIF--LSADLFNAGIRPAINVGISVS 365
Cdd:cd01134 209 LGARLaefYERAGRvrcLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYS 286
|
.
gi 2127895048 366 R 366
Cdd:cd01134 287 K 287
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
51-345 |
6.19e-20 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 92.02 E-value: 6.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 51 GELVEFEE---GTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIyasES 127
Cdd:PRK02118 26 GELATVERkdgSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPEL---EG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 128 RLIE------SPAPGIISRRSVyeplQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATdTILNQQGQNVIcVYVAIGQ 201
Cdd:PRK02118 103 EPIEiggpsvNPVKRIVPREMI----RTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA-RIALQAEADII-ILGGMGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 202 KASSVAQVVNTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMFRE-RHTLIIYDDLSKQAQAYRQMSLLLRR 280
Cdd:PRK02118 177 TFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLTDMTNFADALKEISITMDQ 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127895048 281 PPGREAYPGDvfyLHSRLLERAAKLSSLLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFL 345
Cdd:PRK02118 257 IPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| 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 |
2.05e-19 |
|
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: 82.11 E-value: 2.05e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 376 MKQVAGKLKLELAQFAELEAFAQFASD--LDKATQNQLARGQRLRELLKQSQAAPLTVEEQIMTIYTGTN 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 |
3.64e-17 |
|
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: 75.66 E-value: 3.64e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127895048 29 TGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATG 93
Cdd:pfam02874 5 IGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
97-367 |
9.62e-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: 80.34 E-value: 9.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 97 QIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 177 TAVATDTILN-QQGQNVICVYVAIGQKASSVAQVVNTLQERGameytiVVAETADSPATLQY-----------LAPYTGA 244
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGERTREGNDLYHEMKESG------VINLDGLSKVALVYgqmneppgaraRVALTGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 245 ALAEYFMFRE-RHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlsslLGEGSMTALPIVETQ 323
Cdd:cd01133 155 TMAEYFRDEEgQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITS----TKKGSITSVQAVYVP 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2127895048 324 SGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRV 367
Cdd:cd01133 231 ADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
145-366 |
1.60e-14 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 75.97 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 145 EPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTavatdtILNQQ----GQNVICVYVAIGQKASSVAQVVNTLQE----- 215
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT------VTQHQlakwADADIVIYVGCGERGNEMTEVLEEFPElidpk 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 216 --RGAMEYTIVVAETADSP-----ATLqylapYTGAALAEYFmfRE--RHTLIIYDDLSKQAQAYRQMSLLLRRPPGREA 286
Cdd:PRK04192 283 tgRPLMERTVLIANTSNMPvaareASI-----YTGITIAEYY--RDmgYDVLLMADSTSRWAEALREISGRLEEMPGEEG 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 287 YPGdvfYLHSRL---LERAAKLSSLLG-EGSMTALPIVETQSGDVSAYIPTNVISITdgQIF--LSADLFNAGIRPAINV 360
Cdd:PRK04192 356 YPA---YLASRLaefYERAGRVKTLGGeEGSVTIIGAVSPPGGDFSEPVTQNTLRIV--KVFwaLDAELADRRHFPAINW 430
|
....*.
gi 2127895048 361 GISVSR 366
Cdd:PRK04192 431 LTSYSL 436
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
28-163 |
3.32e-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: 71.66 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 28 NTGTVLQV----------GDGIARIYGLDEVmagELVEFEEGTIGIALNLESNNVGVVLMG--DGLmiQEGSSVKATGRI 95
Cdd:COG0055 4 NTGKIVQVigpvvdvefpEGELPAIYNALEV---ENEGGGELVLEVAQHLGDNTVRCIAMDstDGL--VRGMEVIDTGAP 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127895048 96 AQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRG 163
Cdd:COG0055 79 ISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKG 146
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
193-372 |
8.48e-13 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 71.21 E-value: 8.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 193 ICVYVAIGQKASSVAQVVNTLQE-------RGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMFRERHTLIIYDDLS 265
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 266 KQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSSLLGE---GSMTALPIVETQSGDVSAYIPTNVISIT 339
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPA---YLASKLaefYERAGRVVTLGSDyrvGSVSVIGAVSPPGGDFSEPVVQNTLRVV 840
|
170 180 190
....*....|....*....|....*....|...
gi 2127895048 340 DGQIFLSADLFNAGIRPAINVGISVSRVGSAAQ 372
Cdd:PRK14698 841 KVFWALDADLARRRHFPAINWLTSYSLYVDAVK 873
|
|
| 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 |
2.69e-11 |
|
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: 59.25 E-value: 2.69e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127895048 29 TGTVLQVGDGIARIYGLDEVMAGELVEFEE-------GTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGR 94
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERgdgnnetVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
67-359 |
7.21e-10 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 61.21 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 67 LESNNVGVVLMG--DGLMiqEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIYASESRLIESPAPGII---SRR 141
Cdd:CHL00060 65 LGNNRVRAVAMSatDGLM--RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTKL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 142 SVYEplqTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN-QQGQNVICVYVAIGQ------------KASSVAQ 208
Cdd:CHL00060 143 SIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGErtregndlymemKESGVIN 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 209 VVNTLQERGAMEYtivvAETADSPATLQYLApYTGAALAEYFM-FRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAY 287
Cdd:CHL00060 220 EQNIAESKVALVY----GQMNEPPGARMRVG-LTALTMAEYFRdVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGY 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127895048 288 PGDVFYLHSRLLERAAKLSsllgEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAIN 359
Cdd:CHL00060 295 QPTLSTEMGSLQERITSTK----EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 362
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
122-366 |
3.74e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 39.68 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 122 IYASESRLIESPAPGIISRrsvyeplqtgliAIDSMIPIGRGQRELIIGDRQTGKTavatdTILNQQGQnvicvyvAIGQ 201
Cdd:PRK12608 104 LHPRERLRLETGSDDLSMR------------VVDLVAPIGKGQRGLIVAPPRAGKT-----VLLQQIAA-------AVAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 202 KASSVAQVVNTLQERGA----MEYTI---VVAETADSPatlqylaPYTGAALAEYFMFRERH-------TLIIYDDLSKQ 267
Cdd:PRK12608 160 NHPEVHLMVLLIDERPEevtdMRRSVkgeVYASTFDRP-------PDEHIRVAELVLERAKRlveqgkdVVILLDSLTRL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127895048 268 AQAYRQMSlllrRPPGREAYPGdvfyLHSRLLERAAKL--SSLLGE--GSMT--ALPIVETQSgDVSAYIPTNVISITDG 341
Cdd:PRK12608 233 ARAYNNEV----ESSGRTLSGG----VDARALQRPKRLfgAARNIEegGSLTiiATALVDTGS-RMDEVIFEEFKGTGNM 303
|
250 260
....*....|....*....|....*
gi 2127895048 342 QIFLSADLFNAGIRPAINVGISVSR 366
Cdd:PRK12608 304 EIVLDRELADKRVFPAIDIAKSGTR 328
|
|
| |
