|
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: 1088.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 23 EVKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSE 102
Cdd:CHL00059 1 EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 103 DYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRELIIGDRQTGKTAVATD 182
Cdd:CHL00059 81 AYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 183 TILNQQGQNVICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLIIYD 262
Cdd:CHL00059 161 TILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 263 DPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQ 342
Cdd:CHL00059 241 DLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 343 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLK 422
Cdd:CHL00059 321 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 423 QSQSAPLTVAEQIITIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKETIPEQKESFL 502
Cdd:CHL00059 401 QSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQLELFL 480
|
....*
gi 1238819707 503 LQQQA 507
Cdd:CHL00059 481 LQEQT 485
|
|
| 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: 961.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 3 TIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLM 82
Cdd:PRK09281 2 QINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 83 IQEGSSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGR 162
Cdd:PRK09281 82 IKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 163 GQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYT 242
Cdd:PRK09281 162 GQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 243 GAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVET 322
Cdd:PRK09281 242 GCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIET 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 323 QSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASD 402
Cdd:PRK09281 322 QAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 403 LDKATQNQLARGQRLRELLKQSQSAPLTVAEQIITIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTF 482
Cdd:PRK09281 402 LDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKDL 481
|
490 500
....*....|....*....|
gi 1238819707 483 TEEAEALLKETIPEQKESFL 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: 956.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 3 TIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLM 82
Cdd:COG0056 2 QIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 83 IQEGSSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGR 162
Cdd:COG0056 82 IKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 163 GQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYT 242
Cdd:COG0056 162 GQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 243 GAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVET 322
Cdd:COG0056 242 GCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIET 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 323 QSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASD 402
Cdd:COG0056 322 QAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 403 LDKATQNQLARGQRLRELLKQSQSAPLTVAEQIITIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTF 482
Cdd:COG0056 402 LDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGKL 481
|
490
....*....|....*....
gi 1238819707 483 TEEAEALLKETIPEQKESF 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: 823.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 3 TIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLM 82
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 83 IQEGSSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGR 162
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 163 GQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYT 242
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 243 GAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVET 322
Cdd:TIGR00962 241 GCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 323 QSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASD 402
Cdd:TIGR00962 321 QAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 403 LDKATQNQLARGQRLRELLKQSQSAPLTVAEQIITIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTF 482
Cdd:TIGR00962 401 LDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKL 480
|
490
....*....|....*....
gi 1238819707 483 TEEAEALLKETIPEQKESF 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: 744.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 4 IRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMI 83
Cdd:PRK13343 3 SNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 84 QEGSSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRG 163
Cdd:PRK13343 83 LAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 164 QRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTG 243
Cdd:PRK13343 163 QRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 244 AALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVETQ 323
Cdd:PRK13343 243 CAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 324 SGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDL 403
Cdd:PRK13343 323 AGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 404 DKATQNQLARGQRLRELLKQSQSAPLTVAEQIITIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFT 483
Cdd:PRK13343 403 DAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRELD 482
|
490
....*....|....*...
gi 1238819707 484 EEAEALLKETIPEQKESF 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: 575.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 95 IAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRELIIGDRQT 174
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 175 GKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRE 254
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 255 RHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVETQSGDVSAYIPTN 334
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 1238819707 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: 551.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 7 DEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEG 86
Cdd:TIGR03324 6 DKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 87 SSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRE 166
Cdd:TIGR03324 86 DEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 167 LIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTGAAL 246
Cdd:TIGR03324 166 LILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 247 AEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVETQSGD 326
Cdd:TIGR03324 246 GEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 327 VSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKA 406
Cdd:TIGR03324 326 ISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDEN 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1238819707 407 TQNQLARGQRLRELLKQSQSAPLTVAEQIITIYTGTNGYLDSLEIGQV 454
Cdd:TIGR03324 406 TRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAM 453
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
62-457 |
9.64e-118 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 358.20 E-value: 9.64e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 62 GIALNLESNN-VGVVLMGDGLMIQEGSSVKATGKIAQIPVSEDYLGRVINALAKPIDgRGEISASESRL--------IES 132
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVP-VGLLTRSRALLeseqtlgkVDA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 133 PAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQQGQN--------VICVYVAIGQKAS 204
Cdd:PTZ00185 159 GAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINqqilsknaVISIYVSIGQRCS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 205 SVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGR 284
Cdd:PTZ00185 239 NVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 285 EAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISV 364
Cdd:PTZ00185 319 EAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSV 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 365 SRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATqnqLARGQRLRELLKQSQsaPLTVAEQIITIYTGTNG 444
Cdd:PTZ00185 399 SRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNALVSLYACLNG 473
|
410
....*....|...
gi 1238819707 445 YLDSLEIGQVRKF 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 |
2.29e-111 |
|
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: 328.55 E-value: 2.29e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 150 GLVAIDSMIPIGRGQRELIIGDRQTGKTAVAtDTILNQQGQNViCVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETA 229
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 230 DSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRl 309
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGK- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1238819707 310 gEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVS 365
Cdd:pfam00006 158 -GGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
97-478 |
1.03e-102 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 317.30 E-value: 1.03e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 97 QIPVSEDYLGRVINALAKPIDGRGEISASESRLI-ESP----APGIISRRSVYEPLQTGLVAIDSMIPIGRGQRELIIGD 171
Cdd:PRK07165 72 KVKTSKEYFGKIIDIDGNIIYPEAQNPLSKKFLPnTSSifnlAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGD 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 172 RQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATlQYLAPYTGAALAEYFM 251
Cdd:PRK07165 152 RQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAENIS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 252 YRErHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSssrLGEGSMTALPIVETQSGDVSAYI 331
Cdd:PRK07165 231 YND-DVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKF---KNRKTITALPILQTVDNDITSLI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 332 PTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQL 411
Cdd:PRK07165 307 SSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLL 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238819707 412 ARGQRLRELLKQSQSAPLTVAEQIITIYTGTNGYLDSL-EIGQVRKFLVELRTYLKTNKPQFQEIISS 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 |
4.92e-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: 307.07 E-value: 4.92e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 97 QIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 177 TAVATDTILNQQGQNV-ICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRER 255
Cdd:cd19476 81 TVLAMQLARNQAKAHAgVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 256 HTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSrlGEGSMTALPIVETQSGDVSAYIPTNV 335
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 1238819707 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 |
5.75e-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: 198.36 E-value: 5.75e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 376 MKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQSAPLTVAEQIITIYTGTNGYLDSLEIGQVR 455
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1238819707 456 KFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKETIPEQKESF 501
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
372-496 |
7.85e-59 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 190.35 E-value: 7.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 372 QIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQSAPLTVAEQIITIYTGTNGYLDSLEI 451
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1238819707 452 GQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKETIPE 496
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEE 125
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
13-443 |
6.66e-49 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 174.17 E-value: 6.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 13 IRERIEQYnrevkivnTGTVLQvgdgiARIHGldeVMAGELVEFEEGtiGIALNLESNNVGVVL-------MGDGLMIQE 85
Cdd:PRK06936 23 IRGRVTQV--------TGTILK-----AVVPG---VRIGELCYLRNP--DNSLSLQAEVIGFAQhqalltpLGEMYGISS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 86 GSSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQR 165
Cdd:PRK06936 85 NTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 166 ELIIGDRQTGKTAVATDTILNQQGQnvICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTGAA 245
Cdd:PRK06936 165 MGIFAAAGGGKSTLLASLIRSAEVD--VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 246 LAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsrlgEGSMTALPIVETQSG 325
Cdd:PRK06936 243 IAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSD----KGSITALYTVLVEGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 326 DVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQ---FASD 402
Cdd:PRK06936 319 DMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQigeYQKG 398
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1238819707 403 LDKATQNQLARGQRLRELLKQSQSAPLTVAEQIITIYTGTN 443
Cdd:PRK06936 399 QDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETLTQ 439
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
97-367 |
3.07e-48 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 167.35 E-value: 3.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 97 QIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 177 TavatdTILNQQGQNV---ICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYR 253
Cdd:cd01136 81 S-----TLLGMIARNTdadVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 254 ERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsrlgEGSMTALPIVETQSGDVSAYIPT 333
Cdd:cd01136 156 GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGE----KGSITAFYTVLVEGDDFNDPIAD 231
|
250 260 270
....*....|....*....|....*....|....
gi 1238819707 334 NVISITDGQIFLSADLFNAGIRPAINVGISVSRV 367
Cdd:cd01136 232 EVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
9-424 |
1.95e-47 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 170.38 E-value: 1.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 9 ISNIIRERIEQYNREVK-IVNTGTVLQVGDGIARIhGLDEVMAGELVEFE-EGTIGIALNLESNNVGVVLMGDGLMIQEG 86
Cdd:PRK06820 9 LTPRLQQQLTRPSAPPEgLRYRGPIVEIGPTLLRA-SLPGVAQGELCRIEpQGMLAEVVSIEQEMALLSPFASSDGLRCG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 87 SSVKATGKIAQIPVSEDYLGRVINALAKPIDGrGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRE 166
Cdd:PRK06820 88 QWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 167 LIIGDRQTGKTAVATdTILNQQGQNVIcVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTGAAL 246
Cdd:PRK06820 167 GIFAAAGVGKSTLLG-MLCADSAADVM-VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 247 AEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsrlgEGSMTALPIVETQSGD 326
Cdd:PRK06820 245 AEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSD----RGSITAFYTVLVEGDD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 327 VSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQ---FASDL 403
Cdd:PRK06820 321 MNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRvgeYQAGE 400
|
410 420
....*....|....*....|.
gi 1238819707 404 DKATQNQLARGQRLRELLKQS 424
Cdd:PRK06820 401 DLQADEALQRYPAICAFLQQD 421
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
13-433 |
9.38e-47 |
|
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: 168.29 E-value: 9.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 13 IRERIEQYNRevkIVNTGTVLQVGDGIARIHGLDeVMAGELVEFEEGT--------IGIalnlesNNVGVVLM--GDGLM 82
Cdd:COG1157 7 LLARLEELPP---VRVSGRVTRVVGLLIEAVGPD-ASIGELCEIETADgrpvlaevVGF------RGDRVLLMplGDLEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 83 IQEGSSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGR 162
Cdd:COG1157 77 ISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 163 GQReliIGdr---qtGKTavatdTILNQQGQNV---ICVyVA-IGqkassvaqvvttfqER-R-------------AMEY 221
Cdd:COG1157 157 GQR---IGifagsgvGKS-----TLLGMIARNTeadVNV-IAlIG--------------ERgRevrefieddlgeeGLAR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 222 TIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLER 301
Cdd:COG1157 214 SVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLER 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 302 AAKSssrlGEGSMTAL------------PIVETqsgdvsayiptnVISITDGQIFLSADLFNAGIRPAINVGISVSRVGS 369
Cdd:COG1157 294 AGNG----GKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMP 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238819707 370 AAQIKAMKQVAGKLKLELAQFAELE------AFAQFAS-DLDKAtqnqLARGQRLRELLKQSQSAPLTVAE 433
Cdd:COG1157 358 DIVSPEHRALARRLRRLLARYEENEdlirigAYQPGSDpELDEA----IALIPAIEAFLRQGMDERVSFEE 424
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
95-366 |
5.09e-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: 156.61 E-value: 5.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 95 IAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRELIIGD--- 171
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGsgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 172 ----------RQTGktavatdtiLNQQGQNVICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPY 241
Cdd:cd01135 81 phnelaaqiaRQAG---------VVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 242 TGAALAEYFMY-RERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKSSSRlgEGSMTAL 317
Cdd:cd01135 152 MALTTAEYLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQI 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1238819707 318 PIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR 366
Cdd:cd01135 227 PILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
16-420 |
5.42e-43 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 158.45 E-value: 5.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 16 RIEQYNREVKivnTGTVLQVGDGIArihgldevmageLVEFEEGTIGIALnlesnnvgvvlmgdglmiqEGSSVKATGKI 95
Cdd:PRK04196 30 EIELPNGEKR---RGQVLEVSEDKA------------VVQVFEGTTGLDL-------------------KDTKVRFTGEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 96 AQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQR---------- 165
Cdd:PRK04196 76 LKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 166 --EL---IIgdRQTgktavatdTILNQQGQNVIcVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAP 240
Cdd:PRK04196 156 hnELaaqIA--RQA--------KVLGEEENFAV-VFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 241 YTGAALAEYFMY-RERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKSSSRlgEGSMTA 316
Cdd:PRK04196 225 RMALTAAEYLAFeKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 317 LPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVgsaaqikaMKQVAGKLKlelaqfaeleaf 396
Cdd:PRK04196 300 IPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRL--------MKDGIGEGK------------ 359
|
410 420
....*....|....*....|....*...
gi 1238819707 397 aqfASDLDKATQNQL----ARGQRLREL 420
Cdd:PRK04196 360 ---TREDHKDVANQLyaayARGKDLREL 384
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
5-424 |
6.06e-43 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 158.01 E-value: 6.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 5 RADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIHGLDeVMAGELVEF--EEGTIGIALNLESNNVGVVLM---GD 79
Cdd:PRK09099 1 ALAELSRLADALERELAALPAVRRTGKVVEVIGTLLRVSGLD-VTLGELCELrqRDGTLLQRAEVVGFSRDVALLspfGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 80 GLMIQEGSSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIP 159
Cdd:PRK09099 80 LGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 160 IGRGQRELIIGDRQTGKTavatdTILNQQGQNVIC---VYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQ 236
Cdd:PRK09099 160 LGEGQRMGIFAPAGVGKS-----TLMGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 237 YLAPYTGAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSrlgeGSMTA 316
Cdd:PRK09099 235 AKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGET----GSITA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 317 LPIV--ETQSGdvSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELE 394
Cdd:PRK09099 311 LYTVlaEDESG--SDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVE 388
|
410 420 430
....*....|....*....|....*....|...
gi 1238819707 395 AFAQ---FASDLDKATQNQLARGQRLRELLKQS 424
Cdd:PRK09099 389 TLLQvgeYRAGSDPVADEAIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
83-435 |
2.51e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 151.03 E-value: 2.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 83 IQEGSSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGR 162
Cdd:PRK07721 78 IAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 163 GQRELIIGDRQTGKTAVATDTILNQQGQ-NVICVyvaIGQKASSVAQvvttFQER----RAMEYTIVVAETADSPATLQY 237
Cdd:PRK07721 158 GQRVGIFAGSGVGKSTLMGMIARNTSADlNVIAL---IGERGREVRE----FIERdlgpEGLKRSIVVVATSDQPALMRI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 238 LAPYTGAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSrlgeGSMTAL 317
Cdd:PRK07721 231 KGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS----GSITAF 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 318 PIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELE--- 394
Cdd:PRK07721 307 YTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEdli 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1238819707 395 ---AFAQFAS-DLDKATQNQLArgqrLRELLKQSQSAPLTVAEQI 435
Cdd:PRK07721 387 nigAYKRGSSrEIDEAIQFYPQ----IISFLKQGTDEKATFEESI 427
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
30-427 |
9.59e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 149.07 E-value: 9.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 30 GTVLQVGDGIARIHGLdEVMAGELVEFEEG-----TIGIALNLESNNVGVVLMG--DGLMIqeGSSVKATGKIAQIPVSE 102
Cdd:PRK08472 20 GSITKISPTIIEADGL-NPSVGDIVKIESSdngkeCLGMVVVIEKEQFGISPFSfiEGFKI--GDKVFISKEGLNIPVGR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 103 DYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRELIIGDRQTGKTAVATD 182
Cdd:PRK08472 97 NLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 183 TILNQQGQnvICVYVAIGQKASSVAQvvttFQERRA---MEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLI 259
Cdd:PRK08472 177 IVKGCLAP--IKVVALIGERGREIPE----FIEKNLggdLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLF 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 260 IYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsrlGEGSMTALPIVETQSGDVSAYIPTNVISIT 339
Cdd:PRK08472 251 IMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEE---GKGSITAFFTVLVEGDDMSDPIADQSRSIL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 340 DGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFAS---DLDKATQNQLARGQR 416
Cdd:PRK08472 328 DGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAyqkGNDKELDEAISKKEF 407
|
410
....*....|.
gi 1238819707 417 LRELLKQSQSA 427
Cdd:PRK08472 408 MEQFLKQNPNE 418
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
41-425 |
3.04e-38 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 144.75 E-value: 3.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 41 RIHG------LDEVMAGELVE-----FEEGTIGIALNLESNNVGVVL--MGDGLMIQEGSSVKATGKIAQIPVSEDYLGR 107
Cdd:PRK08149 12 RIQGpiieaeLPDVAIGEICEiragwHSNEVIARAQVVGFQRERTILslIGNAQGLSRQVVLKPTGKPLSVWVGEALLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 108 VINALAKpIDGR-----GEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRELIIGDRQTGKTAVATd 182
Cdd:PRK08149 92 VLDPTGK-IVERfdappTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMN- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 183 tILNQQGQNVICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLIIYD 262
Cdd:PRK08149 170 -MLIEHSEADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFID 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 263 DPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERaaksSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQ 342
Cdd:PRK08149 249 SMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLER----PGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 343 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFA-------SDLDKATQNQlargQ 415
Cdd:PRK08149 325 IYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGeyrrgenADNDRAMDKR----P 400
|
410
....*....|
gi 1238819707 416 RLRELLKQSQ 425
Cdd:PRK08149 401 ALEAFLKQDV 410
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
17-429 |
2.26e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 140.13 E-value: 2.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 17 IEQYNREVKIVNT-GTVLQVGDGIARIHGL-DEVMAGELVEFEEGT---IGIALNLESNNVGVVLMGDGLMIQEGSSVKA 91
Cdd:PRK06002 14 VERYAAPEPLVRIgGTVSEVTASHYRVRGLsRFVRLGDFVAIRADGgthLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 92 TGKiAQIPVSEDYLGRVINALAKPIDGRGEISASESRL-IESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRELIIG 170
Cdd:PRK06002 94 KGP-LRIRPDPSWKGRVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 171 DRQTGKT--------AVATDTilnqqgqnvicVYVA-IGQKASSVAQvvttFQE---RRAMEYTIVVAETADSPATLQYL 238
Cdd:PRK06002 173 GSGVGKStllamlarADAFDT-----------VVIAlVGERGREVRE----FLEdtlADNLKKAVAVVATSDESPMMRRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 239 APYTGAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSrlGEGSMTALP 318
Cdd:PRK06002 238 APLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 319 IVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAE---LEA 395
Cdd:PRK06002 316 SVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdLRL 395
|
410 420 430
....*....|....*....|....*....|....*...
gi 1238819707 396 FAQFA----SDLDKAtqnqLARGQRLRELLKQSQSAPL 429
Cdd:PRK06002 396 IGGYRagsdPDLDQA----VDLVPRIYEALRQSPGDPP 429
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
86-379 |
3.79e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 139.45 E-value: 3.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 86 GSSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQR 165
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 166 ELIIGDRQTGKTaVATDTILNQQGQNVICVYVaIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTGAA 245
Cdd:PRK08972 165 MGLFAGSGVGKS-VLLGMMTRGTTADVIVVGL-VGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 246 LAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSrlGEGSMTALPIVETQSG 325
Cdd:PRK08972 243 IAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVLTEGD 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1238819707 326 DVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVG----SAAQIKAMKQV 379
Cdd:PRK08972 321 DLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMpmviSEEHLEAMRRV 378
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
87-376 |
4.91e-36 |
|
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: 139.47 E-value: 4.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 87 SSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRE 166
Cdd:TIGR01040 65 TTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 167 LIIGD-------------RQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPA 233
Cdd:TIGR01040 145 PIFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 234 TLQYLAPYTGAALAEYFMY-RERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRlgEG 312
Cdd:TIGR01040 225 IERIITPRLALTTAEYLAYqCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR--NG 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238819707 313 SMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAM 376
Cdd:TIGR01040 303 SITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-428 |
8.79e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 135.47 E-value: 8.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 29 TGTVLQVGDGIARIHgLDEVMAGELVEFE-EGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEDYLGR 107
Cdd:PRK07594 22 WGRIQDVSATLLNAW-LPGVFMGELCCIKpGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 108 VINALAKPIDGRgEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRELIIGDRQTGKTAVATdTILNQ 187
Cdd:PRK07594 101 VIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLA-MLCNA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 188 QGQNViCVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDPSKQ 267
Cdd:PRK07594 179 PDADS-NVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 268 AQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAksssrLGE-GSMTALPIVETQSGDVSAYIPTNVISITDGQIFLS 346
Cdd:PRK07594 258 ARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 347 ADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAF---AQFASDLDKATQNQLARGQRLRELLKQ 423
Cdd:PRK07594 333 RRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLiriGEYQRGVDTDTDKAIDTYPDICTFLRQ 412
|
....*
gi 1238819707 424 SQSAP 428
Cdd:PRK07594 413 SKDEV 417
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
83-444 |
1.49e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 132.16 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 83 IQEGSSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGR 162
Cdd:PRK05688 88 IAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 163 GQRELIIGDRQTGKTAVAtdTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYT 242
Cdd:PRK05688 168 GQRLGLFAGTGVGKSVLL--GMMTRFTEADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 243 GAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAksSSRLGEGSMTALPIVET 322
Cdd:PRK05688 246 CTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 323 QSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVgsaaqikaMKQVAGKLKLELAQ-FAELEAFAQFAS 401
Cdd:PRK05688 324 EGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV--------MPQVVDPEHLRRAQrFKQLWSRYQQSR 395
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1238819707 402 DL----------DKATQNQLARGQRLRELLKQS--QSAPLT-VAEQIITIYTGTNG 444
Cdd:PRK05688 396 DLisvgayvaggDPETDLAIARFPHLVQFLRQGlrENVSLAqSREQLAAIFAPAAG 451
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
100-423 |
4.01e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 127.70 E-value: 4.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 100 VSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRELIIGDRQTGKTAV 179
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 180 AtdTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLI 259
Cdd:PRK07196 172 L--GMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 260 IYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsrlGEGSMTALPIVETQSGDVSAYIPTNVISIT 339
Cdd:PRK07196 250 LVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSS---GNGTMTAIYTVLAEGDDQQDPIVDCARAVL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 340 DGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAE---LEAFAQFASDLDKATQNQLARGQR 416
Cdd:PRK07196 327 DGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAikpLIPLGGYVAGADPMADQAVHYYPA 406
|
....*..
gi 1238819707 417 LRELLKQ 423
Cdd:PRK07196 407 ITQFLRQ 413
|
|
| 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 |
6.41e-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: 6.41e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238819707 28 NTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGK 94
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
31-394 |
6.96e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 124.32 E-value: 6.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 31 TVLQVGDGIARIHGLDEVMAGELVEFEEGTigialnlesnnvgVVLMG----DGlmIQEGSSVKATGKIAQIPVSEDYLG 106
Cdd:PRK08927 36 HALSVGARIVVETRGGRPVPCEVVGFRGDR-------------ALLMPfgplEG--VRRGCRAVIANAAAAVRPSRAWLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 107 RVINALAKPIDGRGEISASES-RLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRELIIGDRQTGKTavatdTIL 185
Cdd:PRK08927 101 RVVNALGEPIDGKGPLPQGPVpYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKS-----VLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 186 NQQGQNVIC---VYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLIIYD 262
Cdd:PRK08927 176 SMLARNADAdvsVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 263 DPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAksSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQ 342
Cdd:PRK08927 256 SVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGH 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1238819707 343 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELE 394
Cdd:PRK08927 334 IVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADME 385
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
60-450 |
8.80e-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: 109.81 E-value: 8.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 60 TIGIALNLESNNVGVVLMG--DGLmiQEGSSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGI 137
Cdd:TIGR01039 40 TLEVAQHLGDDTVRTIAMGstDGL--VRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 138 ISRRSVYEPLQTGLVAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN-QQGQNVICVYVAIGQKASSVAQVVTTFQER 216
Cdd:TIGR01039 118 EEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKES 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 217 RAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERH-TLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLH 295
Cdd:TIGR01039 198 GVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQdVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 296 SRLLERAAKSSsrlgEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQI-K 374
Cdd:TIGR01039 278 GELQERITSTK----TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVgE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 375 AMKQVAGKLKLELAQFAELEAFAQF-----ASDLDKATqnqLARGQRLRELLKQsqsaPLTVAEQiitiYTGTNGYLDSL 449
Cdd:TIGR01039 354 EHYDVARGVQQILQRYKELQDIIAIlgmdeLSEEDKLT---VERARRIQRFLSQ----PFFVAEV----FTGQPGKYVPL 422
|
.
gi 1238819707 450 E 450
Cdd:TIGR01039 423 K 423
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
97-378 |
1.79e-25 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 109.10 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 97 QIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 177 TaVATDTILNQQGQNVICVYVaIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERH 256
Cdd:PRK07960 189 S-VLLGMMARYTQADVIVVGL-IGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQH 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 257 TLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSrlGEGSMTALPIVETQSGDVSAYIPTNVI 336
Cdd:PRK07960 267 VLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGDDQQDPIADSAR 344
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1238819707 337 SITDGQIFLSADLFNAGIRPAINVGISVSRVGSA-------AQIKAMKQ 378
Cdd:PRK07960 345 AILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAlideqhyARVRQFKQ 393
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
86-435 |
1.89e-24 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 105.76 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 86 GSSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQR 165
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 166 ELIIGDRQTGKTA-VATDTILNQQGQNVICVyvaIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTGA 244
Cdd:PRK05922 160 IGVFSEPGSGKSSlLSTIAKGSKSTINVIAL---IGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAM 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 245 ALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsrlgEGSMTALPIVetqs 324
Cdd:PRK05922 237 TIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND----KGSITALYAI---- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 325 gdvsAYIPTN-------VISITDGQIFLSADlFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFA 397
Cdd:PRK05922 309 ----LHYPNHpdiftdyLKSLLDGHFFLTPQ-GKALASPPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDII 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1238819707 398 QFAS-------DLDKATqnqlargqRLRELLKQSQSAPLTVAEQI 435
Cdd:PRK05922 384 QLGAyvpgqdaHLDRAV--------KLLPSIKQFLSQPLSSYCAL 420
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
86-396 |
7.12e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 100.82 E-value: 7.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 86 GSSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQR 165
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 166 ELIIGDRQTGKTavatdTILNQQGQNV---ICVYVAIGQKASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYT 242
Cdd:PRK06793 159 IGIFAGSGVGKS-----TLLGMIAKNAkadINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 243 GAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPgreaYPGDVFYLHS---RLLERAAKSSsrlgEGSMTALPI 319
Cdd:PRK06793 234 ATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQ----KGSITGIYT 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238819707 320 VETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAF 396
Cdd:PRK06793 306 VLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELY 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 |
1.00e-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: 92.25 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 145 EPLQTGLVAIDSMIPIGRGQRELIIGDRQTGKTavatdtILNQQ----GQNVICVYVAIGQKASSVAQVVTTFQE----- 215
Cdd:cd01134 58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKT------VISQSlskwSNSDVVIYVGCGERGNEMAEVLEEFPElkdpi 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 216 --RRAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGdvfY 293
Cdd:cd01134 132 tgESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---Y 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 294 LHSRL---LERAAK-----SSSRlgEGSMTALPIVETQSGDVSAYIPTNVISITdgQIF--LSADLFNAGIRPAINVGIS 363
Cdd:cd01134 209 LGARLaefYERAGRvrclgSPGR--EGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLIS 284
|
...
gi 1238819707 364 VSR 366
Cdd:cd01134 285 YSK 287
|
|
| 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 |
3.58e-18 |
|
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: 78.64 E-value: 3.58e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 376 MKQVAGKLKLELAQFAELEAFAQFASD--LDKATQNQLARGQRLRELLKQSQSAPLTVAEQIITIYTGTN 443
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
51-345 |
2.07e-17 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 84.32 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 51 GELVEFEE---GTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEIsasES 127
Cdd:PRK02118 26 GELATVERkdgSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPEL---EG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 128 RLIE------SPAPGIISRRSVyeplQTGLVAIDSMIPIGRGQRELIIGDRQTGKTAVATdTILNQQGQNVIcVYVAIGQ 201
Cdd:PRK02118 103 EPIEiggpsvNPVKRIVPREMI----RTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA-RIALQAEADII-ILGGMGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 202 KASSVAQVVTTFQERRAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRE-RHTLIIYDDPSKQAQAYRQMSLLLRR 280
Cdd:PRK02118 177 TFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLTDMTNFADALKEISITMDQ 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238819707 281 PPGREAYPGDvfyLHSRLLERAAKSSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFL 345
Cdd:PRK02118 257 IPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
29-93 |
9.40e-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: 74.50 E-value: 9.40e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238819707 29 TGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATG 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 |
1.03e-15 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 77.26 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 97 QIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 177 TAVATDTILN-QQGQNVICVYVAIGqkassvaqvvttfqER--------RAMEYTIVVAETADSPATLQY---------- 237
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVG--------------ERtregndlyHEMKESGVINLDGLSKVALVYgqmneppgar 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 238 -LAPYTGAALAEYFMYRE-RHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSssrlGEGSMT 315
Cdd:cd01133 147 aRVALTGLTMAEYFRDEEgQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST----KKGSIT 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1238819707 316 ALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRV 367
Cdd:cd01133 223 SVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
145-366 |
3.15e-15 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 78.29 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 145 EPLQTGLVAIDSMIPIGRGQRELIIGDRQTGKTavatdtILNQQ----GQNVICVYVAIGQKASSVAQVVTTFQE----- 215
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT------VTQHQlakwADADIVIYVGCGERGNEMTEVLEEFPElidpk 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 216 --RRAMEYTIVVAETADSP-----ATLqylapYTGAALAEYfmYRE--RHTLIIYDDPSKQAQAYRQMSLLLRRPPGREA 286
Cdd:PRK04192 283 tgRPLMERTVLIANTSNMPvaareASI-----YTGITIAEY--YRDmgYDVLLMADSTSRWAEALREISGRLEEMPGEEG 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 287 YPGdvfYLHSRL---LERAAKSSSRLG-EGSMTALPIVETQSGDVSAYIPTNVISITdgQIF--LSADLFNAGIRPAINV 360
Cdd:PRK04192 356 YPA---YLASRLaefYERAGRVKTLGGeEGSVTIIGAVSPPGGDFSEPVTQNTLRIV--KVFwaLDAELADRRHFPAINW 430
|
....*.
gi 1238819707 361 GISVSR 366
Cdd:PRK04192 431 LTSYSL 436
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
54-163 |
4.57e-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: 71.27 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 54 VEFEEGTI-------------GIALNLE------SNNVGVVLMG--DGLmiQEGSSVKATGKIAQIPVSEDYLGRVINAL 112
Cdd:COG0055 18 VEFPEGELpaiynalevenegGGELVLEvaqhlgDNTVRCIAMDstDGL--VRGMEVIDTGAPISVPVGEATLGRIFNVL 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1238819707 113 AKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLVAIDSMIPIGRG 163
Cdd:COG0055 96 GEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKG 146
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
193-372 |
7.58e-13 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 71.21 E-value: 7.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 193 ICVYVAIGQKASSVAQVVTTFQE-------RRAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDPS 265
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 266 KQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKSSSRLGEGSMTALPIVETQSGDVSAYIPTNVISIT 339
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVV 840
|
170 180 190
....*....|....*....|....*....|...
gi 1238819707 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 |
2.90e-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: 61.94 E-value: 2.90e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238819707 29 TGTVLQVGDGIARIHGLDEVMAGELVEFEEG-------TIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGK 94
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGdgnnetvLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
67-186 |
2.76e-09 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 59.28 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238819707 67 LESNNVGVVLMG--DGLMiqEGSSVKATGKIAQIPVSEDYLGRVINALAKPIDGRGEISASESRLIESPAPGII---SRR 141
Cdd:CHL00060 65 LGNNRVRAVAMSatDGLM--RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTKL 142
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1238819707 142 SVYEplqTGLVAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN 186
Cdd:CHL00060 143 SIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINN 184
|
|
| |
