|
Name |
Accession |
Description |
Interval |
E-value |
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
23-505 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 1077.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 23 EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESKNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSE 102
Cdd:CHL00059 1 EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 103 AYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRELIIGDRQTGKTAVATD 182
Cdd:CHL00059 81 AYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 183 TILNQQGNNVICVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPYTGAALAEYFMYRERHTLIIYD 262
Cdd:CHL00059 161 TILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 263 DPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQ 342
Cdd:CHL00059 241 DLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 343 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFSSDLDKATQNQLARGQRLRELLK 422
Cdd:CHL00059 321 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 423 QSQAKPLTVAEQILTIYTGTNGYLDSFEIAQVRKFLDELRDYVKTRKPQFEEIISSTKIFTEEAQALLKDAIQEQKELFL 502
Cdd:CHL00059 401 QSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQLELFL 480
|
...
gi 169143037 503 VQE 505
Cdd:CHL00059 481 LQE 483
|
|
| 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: 964.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 3 TIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESKNVGVVLMGDGLM 82
Cdd:PRK09281 2 QINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 83 IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGR 162
Cdd:PRK09281 82 IKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 163 GQRELIIGDRQTGKTAVATDTILNQQGNNVICVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPYT 242
Cdd:PRK09281 162 GQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 243 GAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSRLGEGSMTALPIVET 322
Cdd:PRK09281 242 GCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIET 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 323 QSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFSSD 402
Cdd:PRK09281 322 QAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 403 LDKATQNQLARGQRLRELLKQSQAKPLTVAEQILTIYTGTNGYLDSFEIAQVRKFLDELRDYVKTRKPQFEEIISSTKIF 482
Cdd:PRK09281 402 LDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKDL 481
|
490 500
....*....|....*....|
gi 169143037 483 TEEAQALLKDAIQEQKELFL 502
Cdd:PRK09281 482 SDEIEAKLKAAIEEFKKTFA 501
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
3-505 |
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: 962.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 3 TIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESKNVGVVLMGDGLM 82
Cdd:COG0056 2 QIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 83 IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGR 162
Cdd:COG0056 82 IKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 163 GQRELIIGDRQTGKTAVATDTILNQQGNNVICVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPYT 242
Cdd:COG0056 162 GQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 243 GAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSRLGEGSMTALPIVET 322
Cdd:COG0056 242 GCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIET 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 323 QSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFSSD 402
Cdd:COG0056 322 QAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 403 LDKATQNQLARGQRLRELLKQSQAKPLTVAEQILTIYTGTNGYLDSFEIAQVRKFLDELRDYVKTRKPQFEEIISSTKIF 482
Cdd:COG0056 402 LDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGKL 481
|
490 500
....*....|....*....|...
gi 169143037 483 TEEAQALLKDAIQEQKELFLVQE 505
Cdd:COG0056 482 DDEIEEKLKAAIEEFKKTFAASA 504
|
|
| 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: 826.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 3 TIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESKNVGVVLMGDGLM 82
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 83 IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGR 162
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 163 GQRELIIGDRQTGKTAVATDTILNQQGNNVICVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPYT 242
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 243 GAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSRLGEGSMTALPIVET 322
Cdd:TIGR00962 241 GCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 323 QSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFSSD 402
Cdd:TIGR00962 321 QAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 403 LDKATQNQLARGQRLRELLKQSQAKPLTVAEQILTIYTGTNGYLDSFEIAQVRKFLDELRDYVKTRKPQFEEIISSTKIF 482
Cdd:TIGR00962 401 LDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKL 480
|
490
....*....|....*....
gi 169143037 483 TEEAQALLKDAIQEQKELF 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: 748.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 4 IRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESKNVGVVLMGDGLMI 83
Cdd:PRK13343 3 SNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 84 QEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRG 163
Cdd:PRK13343 83 LAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 164 QRELIIGDRQTGKTAVATDTILNQQGNNVICVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPYTG 243
Cdd:PRK13343 163 QRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 244 AALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSRLGEGSMTALPIVETQ 323
Cdd:PRK13343 243 CAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 324 SGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFSSDL 403
Cdd:PRK13343 323 AGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 404 DKATQNQLARGQRLRELLKQSQAKPLTVAEQILTIYTGTNGYLDSFEIAQVRKFLDELRDYVKTRKPQFEEIISSTKIFT 483
Cdd:PRK13343 403 DAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRELD 482
|
490
....*....|....*...
gi 169143037 484 EEAQALLKDAIQEQKELF 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: 580.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 95 IAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRELIIGDRQT 174
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 175 GKTAVATDTILNQQGNNVICVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPYTGAALAEYFMYRE 254
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 255 RHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSRLGEGSMTALPIVETQSGDVSAYIPTN 334
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 169143037 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 ... |
7-492 |
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: 556.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 7 DEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESKNVGVVLMGDGLMIQEG 86
Cdd:TIGR03324 6 DKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 87 SSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRE 166
Cdd:TIGR03324 86 DEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 167 LIIGDRQTGKTAVATDTILNQQGNNVICVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPYTGAAL 246
Cdd:TIGR03324 166 LILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 247 AEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSRLGEGSMTALPIVETQSGD 326
Cdd:TIGR03324 246 GEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 327 VSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFSSDLDKA 406
Cdd:TIGR03324 326 ISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDEN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 407 TQNQLARGQRLRELLKQSQAKPLTVAEQILTIYTGTNGYLDSFEIAQVRKFLDELRDYVKTRKPQFEEIISSTKIFTEEA 486
Cdd:TIGR03324 406 TRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSDED 485
|
....*.
gi 169143037 487 QALLKD 492
Cdd:TIGR03324 486 REQILD 491
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
62-457 |
2.61e-119 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 362.05 E-value: 2.61e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 62 GIALNLESKN-VGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDgRGEISSSESRL--------IES 132
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVP-VGLLTRSRALLeseqtlgkVDA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 133 PAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRELIIGDRQTGKTAVATDTILNQ--------QGNNVICVYVAIGQKAS 204
Cdd:PTZ00185 159 GAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 205 SVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGR 284
Cdd:PTZ00185 239 NVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 285 EAYPGDVFYLHSRLLERAAKLSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISV 364
Cdd:PTZ00185 319 EAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSV 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 365 SRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFSSDLDKATqnqLARGQRLRELLKQSQakPLTVAEQILTIYTGTNG 444
Cdd:PTZ00185 399 SRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNALVSLYACLNG 473
|
410
....*....|...
gi 169143037 445 YLDSFEIAQVRKF 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 |
7.03e-110 |
|
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: 324.69 E-value: 7.03e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 150 GLIAIDAMIPIGRGQRELIIGDRQTGKTAVAtDTILNQQGNNViCVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAA 229
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 230 DSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSRl 309
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGK- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 169143037 310 gEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVS 365
Cdd:pfam00006 158 -GGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
97-478 |
1.15e-105 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 324.62 E-value: 1.15e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 97 QIPVSEAYLGRVINALAKPIDGRGEISSSESRLI-ESP----APGIISRRSVYEPLQTGLIAIDAMIPIGRGQRELIIGD 171
Cdd:PRK07165 72 KVKTSKEYFGKIIDIDGNIIYPEAQNPLSKKFLPnTSSifnlAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGD 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 172 RQTGKTAVATDTILNQQGNNVICVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATlQYLAPYTGAALAEYFM 251
Cdd:PRK07165 152 RQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAENIS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 252 YRErHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLssrLGEGSMTALPIVETQSGDVSAYI 331
Cdd:PRK07165 231 YND-DVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKF---KNRKTITALPILQTVDNDITSLI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 332 PTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFSSDLDKATQNQL 411
Cdd:PRK07165 307 SSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLL 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169143037 412 ARGQRLRELLKQSQAKPLTVAEQILTIYTGTNGYL-DSFEIAQVRKFLDELRDYVKTRKPQFEEIISS 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 |
2.06e-101 |
|
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: 305.53 E-value: 2.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 97 QIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRELIIGDRQTGK 176
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 177 TAVATDTILNQQGNNV-ICVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPYTGAALAEYFMYRER 255
Cdd:cd19476 81 TVLAMQLARNQAKAHAgVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 256 HTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSrlGEGSMTALPIVETQSGDVSAYIPTNV 335
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 169143037 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 |
1.58e-60 |
|
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: 194.51 E-value: 1.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 376 MKQVAGKLKLELAQFAELEAFAQFSSDLDKATQNQLARGQRLRELLKQSQAKPLTVAEQILTIYTGTNGYLDSFEIAQVR 455
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 169143037 456 KFLDELRDYVKTRKPQFEEIISSTKIFTEEAQALLKDAIQEQKELF 501
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
372-496 |
5.22e-57 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 185.72 E-value: 5.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 372 QIKAMKQVAGKLKLELAQFAELEAFAQFSSDLDKATQNQLARGQRLRELLKQSQAKPLTVAEQILTIYTGTNGYLDSFEI 451
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 169143037 452 AQVRKFLDELRDYVKTRKPQFEEIISSTKIFTEEAQALLKDAIQE 496
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEE 125
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
97-367 |
4.99e-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: 166.97 E-value: 4.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 97 QIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRELIIGDRQTGK 176
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 177 TavatdTILNQQGNNV---ICVYVAIGQKASSVAQ-VVNALQERGaMEYTIVVAEAADSPATLQYLAPYTGAALAEYFMY 252
Cdd:cd01136 81 S-----TLLGMIARNTdadVNVIALIGERGREVREfIEKDLGEEG-LKRSVLVVATSDESPLLRVRAAYTATAIAEYFRD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 253 RERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSsrlgEGSMTALPIVETQSGDVSAYIP 332
Cdd:cd01136 155 QGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGE----KGSITAFYTVLVEGDDFNDPIA 230
|
250 260 270
....*....|....*....|....*....|....*
gi 169143037 333 TNVISITDGQIFLSADLFNAGIRPAINVGISVSRV 367
Cdd:cd01136 231 DEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
7-443 |
6.75e-47 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 168.78 E-value: 6.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 7 DEISNIIRERIEQyNREVKIvnTGTVLQVGDGIARIYgLDEVMAGELVEFEEGtiGIALNLESKNVGVVL-------MGD 79
Cdd:PRK06936 5 DYIPHHLRHAIVG-SRLIQI--RGRVTQVTGTILKAV-VPGVRIGELCYLRNP--DNSLSLQAEVIGFAQhqalltpLGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 80 GLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIP 159
Cdd:PRK06936 79 MYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 160 IGRGQRELIIGDRQTGKTAVATDTILNQQGNnvICVYVAIGQKASSVAQVVNA-LQERGaMEYTIVVAEAADSPATLQYL 238
Cdd:PRK06936 159 CGEGQRMGIFAAAGGGKSTLLASLIRSAEVD--VTVLALIGERGREVREFIESdLGEEG-LRKAVLVVATSDRPSMERAK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 239 APYTGAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlSSRlgeGSMTALP 318
Cdd:PRK06936 236 AGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ-SDK---GSITALY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 319 IVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQ 398
Cdd:PRK06936 312 TVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQ 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 169143037 399 ---FSSDLDKATQNQLARGQRLRELLKQSQAKPLTVAEQILTIYTGTN 443
Cdd:PRK06936 392 igeYQKGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETLTQ 439
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
29-433 |
2.56e-45 |
|
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: 164.43 E-value: 2.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 29 TGTVLQVGDgIARIYGLD-EVMAGELVEFEEGTigialnlesknvgVVLM--GDGLMIQEGSSVKATGRIAQIPVSEAYL 105
Cdd:COG1157 34 VGPDASIGE-LCEIETADgRPVLAEVVGFRGDR-------------VLLMplGDLEGISPGARVVPTGRPLSVPVGDGLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 106 GRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQReliIGdr---qtGKTavatd 182
Cdd:COG1157 100 GRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR---IGifagsgvGKS----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 183 TILNQQGNNV---ICVyVA-IGqkassvaqvvnalqERG--------------AMEYTIVVAEAADSPATLQYLAPYTGA 244
Cdd:COG1157 172 TLLGMIARNTeadVNV-IAlIG--------------ERGrevrefieddlgeeGLARSVVVVATSDEPPLMRLRAAYTAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 245 ALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlssrLGEGSMTAL------- 317
Cdd:COG1157 237 AIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN----GGKGSITAFytvlveg 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 318 -----PIVETqsgdvsayiptnVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAE 392
Cdd:COG1157 313 ddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEE 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 169143037 393 LE------AFAQFSS-DLDKAtqnqLARGQRLRELLKQSQAKPLTVAE 433
Cdd:COG1157 381 NEdlirigAYQPGSDpELDEA----IALIPAIEAFLRQGMDERVSFEE 424
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
9-424 |
4.44e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 161.14 E-value: 4.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 9 ISNIIRERIEQYNREVK-IVNTGTVLQVGDGIARIyGLDEVMAGELVEFE-EGTIGIALNLESKNVGVVLMGDGLMIQEG 86
Cdd:PRK06820 9 LTPRLQQQLTRPSAPPEgLRYRGPIVEIGPTLLRA-SLPGVAQGELCRIEpQGMLAEVVSIEQEMALLSPFASSDGLRCG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 87 SSVKATGRIAQIPVSEAYLGRVINALAKPIDGrGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRE 166
Cdd:PRK06820 88 QWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 167 LIIGDRQTGKTAVATdTILNQQGNNVIcVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPYTGAAL 246
Cdd:PRK06820 167 GIFAAAGVGKSTLLG-MLCADSAADVM-VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 247 AEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSsrlgEGSMTALPIVETQSGD 326
Cdd:PRK06820 245 AEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSD----RGSITAFYTVLVEGDD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 327 VSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQ---FSSDL 403
Cdd:PRK06820 321 MNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRvgeYQAGE 400
|
410 420
....*....|....*....|.
gi 169143037 404 DKATQNQLARGQRLRELLKQS 424
Cdd:PRK06820 401 DLQADEALQRYPAICAFLQQD 421
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
16-420 |
1.29e-43 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 160.38 E-value: 1.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 16 RIEQYNREVKivnTGTVLQVGDGIAriygldevmageLVEFEEGTIGIALnlesknvgvvlmgdglmiqEGSSVKATGRI 95
Cdd:PRK04196 30 EIELPNGEKR---RGQVLEVSEDKA------------VVQVFEGTTGLDL-------------------KDTKVRFTGEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 96 AQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQR---------- 165
Cdd:PRK04196 76 LKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 166 --EL---IIgdRQTgktavatdTILNQQGNNVIcVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAP 240
Cdd:PRK04196 156 hnELaaqIA--RQA--------KVLGEEENFAV-VFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 241 YTGAALAEYFMY-RERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSSRlgEGSMTA 316
Cdd:PRK04196 225 RMALTAAEYLAFeKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 317 LPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVgsaaqikaMKQVAGKLKlelaqfaeleaf 396
Cdd:PRK04196 300 IPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRL--------MKDGIGEGK------------ 359
|
410 420
....*....|....*....|....*...
gi 169143037 397 aqfSSDLDKATQNQL----ARGQRLREL 420
Cdd:PRK04196 360 ---TREDHKDVANQLyaayARGKDLREL 384
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
5-424 |
3.82e-43 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 158.78 E-value: 3.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 5 RADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIYGLDeVMAGELVEF--EEGTIGIALNLESKNVGVVLM---GD 79
Cdd:PRK09099 1 ALAELSRLADALERELAALPAVRRTGKVVEVIGTLLRVSGLD-VTLGELCELrqRDGTLLQRAEVVGFSRDVALLspfGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 80 GLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIP 159
Cdd:PRK09099 80 LGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 160 IGRGQRELIIGDRQTGKTavatdTILNQQGNNVIC---VYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQ 236
Cdd:PRK09099 160 LGEGQRMGIFAPAGVGKS-----TLMGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 237 YLAPYTGAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklssrLGE-GSMT 315
Cdd:PRK09099 235 AKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-----MGEtGSIT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 316 ALPIV--ETQSGdvSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAEL 393
Cdd:PRK09099 310 ALYTVlaEDESG--SDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREV 387
|
410 420 430
....*....|....*....|....*....|....
gi 169143037 394 EAFAQ---FSSDLDKATQNQLARGQRLRELLKQS 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 |
1.01e-42 |
|
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: 153.15 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 95 IAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRELIIGD--- 171
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGsgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 172 ----------RQTGktavatdtiLNQQGNNVICVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPY 241
Cdd:cd01135 81 phnelaaqiaRQAG---------VVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 242 TGAALAEYFMY-RERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSSRlgEGSMTAL 317
Cdd:cd01135 152 MALTTAEYLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQI 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 169143037 318 PIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR 366
Cdd:cd01135 227 PILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
83-435 |
2.50e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 147.95 E-value: 2.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 83 IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGR 162
Cdd:PRK07721 78 IAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 163 GQRELIIGDRQTGKTAVATDTILNQQGN-NVICVyvaIGQKASSVAQVV-NALQERGaMEYTIVVAEAADSPATLQYLAP 240
Cdd:PRK07721 158 GQRVGIFAGSGVGKSTLMGMIARNTSADlNVIAL---IGERGREVREFIeRDLGPEG-LKRSIVVVATSDQPALMRIKGA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 241 YTGAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSrlgeGSMTALPIV 320
Cdd:PRK07721 234 YTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS----GSITAFYTV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 321 ETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELE------ 394
Cdd:PRK07721 310 LVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEdlinig 389
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 169143037 395 AFAQFSS-DLDKATQNQLArgqrLRELLKQSQAKPLTVAEQI 435
Cdd:PRK07721 390 AYKRGSSrEIDEAIQFYPQ----IISFLKQGTDEKATFEESI 427
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
30-424 |
9.42e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 143.67 E-value: 9.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 30 GTVLQVGDGIARIYGLdEVMAGELVEFEEG-----TIGIALNLESKNVGVVLMG--DGLMIqeGSSVKATGRIAQIPVSE 102
Cdd:PRK08472 20 GSITKISPTIIEADGL-NPSVGDIVKIESSdngkeCLGMVVVIEKEQFGISPFSfiEGFKI--GDKVFISKEGLNIPVGR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 103 AYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRELIIGDRQTGKTAVATD 182
Cdd:PRK08472 97 NLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 183 TILNQQGNnvICVYVAIGQKASSVAQVVNAlQERGAMEYT-IVVAEAADSPATLQYLApYTGAALAEYFMYRERHTLIIY 261
Cdd:PRK08472 177 IVKGCLAP--IKVVALIGERGREIPEFIEK-NLGGDLENTvIVVATSDDSPLMRKYGA-FCAMSVAEYFKNQGLDVLFIM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 262 DDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSsrlGEGSMTALPIVETQSGDVSAYIPTNVISITDG 341
Cdd:PRK08472 253 DSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEE---GKGSITAFFTVLVEGDDMSDPIADQSRSILDG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 342 QIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQ---FSSDLDKATQNQLARGQRLR 418
Cdd:PRK08472 330 HIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRigaYQKGNDKELDEAISKKEFME 409
|
....*.
gi 169143037 419 ELLKQS 424
Cdd:PRK08472 410 QFLKQN 415
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
41-428 |
1.22e-36 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 140.51 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 41 RIYG------LDEVMAGELVE-----FEEGTIGIALNLESKNVGVVL--MGDGLMIQEGSSVKATGRIAQIPVSEAYLGR 107
Cdd:PRK08149 12 RIQGpiieaeLPDVAIGEICEiragwHSNEVIARAQVVGFQRERTILslIGNAQGLSRQVVLKPTGKPLSVWVGEALLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 108 VINALAKpIDGR-----GEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRELIIGDRQTGKTAVATD 182
Cdd:PRK08149 92 VLDPTGK-IVERfdappTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 183 TILNQQGNnvICVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPYTGAALAEYFMYRERHTLIIYD 262
Cdd:PRK08149 171 LIEHSEAD--VFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFID 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 263 DPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERaaklSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQ 342
Cdd:PRK08149 249 SMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLER----PGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 343 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQF-------SSDLDKATQNQlargQ 415
Cdd:PRK08149 325 IYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLgeyrrgeNADNDRAMDKR----P 400
|
410
....*....|...
gi 169143037 416 RLRELLKQSQAKP 428
Cdd:PRK08149 401 ALEAFLKQDVAEK 413
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
86-379 |
5.98e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 138.68 E-value: 5.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 86 GSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQR 165
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 166 ELIIGDRQTGKTaVATDTILNQQGNNVICVYVaIGQKASSVAQVVNA-LQERGaMEYTIVVAEAADSPATLQYLAPYTGA 244
Cdd:PRK08972 165 MGLFAGSGVGKS-VLLGMMTRGTTADVIVVGL-VGERGREVKEFIEEiLGEEG-RARSVVVAAPADTSPLMRLKGCETAT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 245 ALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSrlGEGSMTALPIVETQS 324
Cdd:PRK08972 242 TIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVLTEG 319
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 169143037 325 GDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVG----SAAQIKAMKQV 379
Cdd:PRK08972 320 DDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMpmviSEEHLEAMRRV 378
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-428 |
1.53e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 137.39 E-value: 1.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 29 TGTVLQVGDGIARIYgLDEVMAGELVEFE-EGTIGIALNLESKNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGR 107
Cdd:PRK07594 22 WGRIQDVSATLLNAW-LPGVFMGELCCIKpGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 108 VINALAKPIDGRgEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRELIIGDRQTGKTAVATdtILNQ 187
Cdd:PRK07594 101 VIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLA--MLCN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 188 QGNNVICVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDPSKQ 267
Cdd:PRK07594 178 APDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 268 AQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklssrLGE-GSMTALPIVETQSGDVSAYIPTNVISITDGQIFLS 346
Cdd:PRK07594 258 ARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 347 ADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAF---AQFSSDLDKATQNQLARGQRLRELLKQ 423
Cdd:PRK07594 333 RRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLiriGEYQRGVDTDTDKAIDTYPDICTFLRQ 412
|
....*
gi 169143037 424 SQAKP 428
Cdd:PRK07594 413 SKDEV 417
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
17-429 |
2.31e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 137.05 E-value: 2.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 17 IEQYNREVKIVNT-GTVLQVGDGIARIYGL-DEVMAGELVEFEEGT---IGIALNLESKNVGVVLMGDGLMIQEGSSVKA 91
Cdd:PRK06002 14 VERYAAPEPLVRIgGTVSEVTASHYRVRGLsRFVRLGDFVAIRADGgthLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 92 TGRiAQIPVSEAYLGRVINALAKPIDGRGEISSSESRL-IESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRELIIG 170
Cdd:PRK06002 94 KGP-LRIRPDPSWKGRVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 171 DRQTGKTavatdTILnqqgnnvicvyvAIGQKASSVAQVVNAL-QERG-------------AMEYTIVVAEAADSPATLQ 236
Cdd:PRK06002 173 GSGVGKS-----TLL------------AMLARADAFDTVVIALvGERGrevrefledtladNLKKAVAVVATSDESPMMR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 237 YLAPYTGAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSSRLGEGSMTA 316
Cdd:PRK06002 236 RLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAG--PGAEGGGSITG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 317 LPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAE---L 393
Cdd:PRK06002 314 IFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdL 393
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 169143037 394 EAFAQF----SSDLDKAtqnqLARGQRLRELLKQSQAKPL 429
Cdd:PRK06002 394 RLIGGYragsDPDLDQA----VDLVPRIYEALRQSPGDPP 429
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
25-376 |
1.83e-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: 134.85 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 25 KIVNtgtvLQVGDGIARIYGLDEVMAGE-LVEFEEGTIGIalnlESKNvgvvlmgdglmiqegSSVKATGRIAQIPVSEA 103
Cdd:TIGR01040 25 EIVN----LTLPDGTVRSGQVLEVSGNKaVVQVFEGTSGI----DAKK---------------TTCEFTGDILRTPVSED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 104 YLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRELIIGD------------ 171
Cdd:TIGR01040 82 MLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAaglphneiaaqi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 172 -RQTGKTAVATDTILNQQGNNVICVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPYTGAALAEYF 250
Cdd:TIGR01040 162 cRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 251 MY-RERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSRlgEGSMTALPIVETQSGDVSA 329
Cdd:TIGR01040 242 AYqCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR--NGSITQIPILTMPNDDITH 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 169143037 330 YIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAM 376
Cdd:TIGR01040 320 PIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
86-435 |
1.06e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 129.63 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 86 GSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQR 165
Cdd:PRK07196 78 GARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 166 ELIIGDRQTGKTaVATDTILNQQGNNVICVYVaIGQKASSVAQVV-NALQERGAMEYTIVVAEAADSPaTLQYLAPYTGA 244
Cdd:PRK07196 158 VGLMAGSGVGKS-VLLGMITRYTQADVVVVGL-IGERGREVKEFIeHSLQAAGMAKSVVVAAPADESP-LMRIKATELCH 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 245 ALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsSRLGEGSMTALPIVETQS 324
Cdd:PRK07196 235 AIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 325 GDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAE---LEAFAQFSS 401
Cdd:PRK07196 312 DDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAikpLIPLGGYVA 391
|
330 340 350
....*....|....*....|....*....|....
gi 169143037 402 DLDKATQNQLARGQRLRELLKQSQAKPLTVAEQI 435
Cdd:PRK07196 392 GADPMADQAVHYYPAITQFLRQEVGHPALFSASV 425
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
83-435 |
1.25e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 129.47 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 83 IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGR 162
Cdd:PRK05688 88 IAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 163 GQRELIIGDRQTGKTAVAtdTILNQQGNNVICVYVAIGQKASSVAQVV-NALQERGaMEYTIVVAEAADSPATLQYLAPY 241
Cdd:PRK05688 168 GQRLGLFAGTGVGKSVLL--GMMTRFTEADIIVVGLIGERGREVKEFIeHILGEEG-LKRSVVVASPADDAPLMRLRAAM 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 242 TGAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSSRLGEGSMTALPIVE 321
Cdd:PRK05688 245 YCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 322 TQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVgsaaqikaMKQVAGKLKLELAQ-FAELEAFAQFS 400
Cdd:PRK05688 323 SEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV--------MPQVVDPEHLRRAQrFKQLWSRYQQS 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 169143037 401 SDL----------DKATQNQLARGQRLRELLKQSQAKPLTVAEQI 435
Cdd:PRK05688 395 RDLisvgayvaggDPETDLAIARFPHLVQFLRQGLRENVSLAQSR 439
|
|
| 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 |
3.52e-32 |
|
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, in mitochondrial inner membranes, and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349740 [Multi-domain] Cd Length: 67 Bit Score: 117.55 E-value: 3.52e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169143037 28 NTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESKNVGVVLMGDGLMIQEGSSVKATGR 94
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
31-433 |
1.95e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 123.17 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 31 TVLQVGDGIARIYGLDEVMAGELVEFEEGTigialnlesknvgVVLMG----DGlmIQEGSSVKATGRIAQIPVSEAYLG 106
Cdd:PRK08927 36 HALSVGARIVVETRGGRPVPCEVVGFRGDR-------------ALLMPfgplEG--VRRGCRAVIANAAAAVRPSRAWLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 107 RVINALAKPIDGRGEISSSES-RLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRELIIGDRQTGKTavatdTIL 185
Cdd:PRK08927 101 RVVNALGEPIDGKGPLPQGPVpYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKS-----VLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 186 NQQGNNVIC---VYVAIGQKASSVAQVVNA-LQERGaMEYTIVVAEAADSPATLQYLAPYTGAALAEYFMYRERHTLIIY 261
Cdd:PRK08927 176 SMLARNADAdvsVIGLIGERGREVQEFLQDdLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 262 DDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDG 341
Cdd:PRK08927 255 DSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 342 QIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELE------AFAQFSS-DLDKATQNQlarg 414
Cdd:PRK08927 333 HIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEelirlgAYRAGSDpEVDEAIRLN---- 408
|
410
....*....|....*....
gi 169143037 415 QRLRELLKQSQAKPLTVAE 433
Cdd:PRK08927 409 PALEAFLRQGKDEATSLAE 427
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
28-444 |
1.46e-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: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 28 NTGTVLQV----------GDGIARIYGLDEVMAGELVEFeegTIGIALNLESKNVGVVLMG--DGLmiQEGSSVKATGRI 95
Cdd:TIGR01039 1 TKGKVVQVigpvvdvefeQGELPRIYNALKVQNRAESEL---TLEVAQHLGDDTVRTIAMGstDGL--VRGLEVIDTGAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 96 AQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRELIIGDRQTG 175
Cdd:TIGR01039 76 ISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 176 KTAVATDTILN-QQGNNVICVYVAIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPYTGAALAEYFMYRE 254
Cdd:TIGR01039 156 KTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 255 RH-TLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSSRlgEGSMTALPIVETQSGDVSAYIPT 333
Cdd:TIGR01039 236 GQdVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERIT--STK--TGSITSVQAVYVPADDLTDPAPA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 334 NVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQI-KAMKQVAGKLKLELAQFAELEAFAQF-----SSDLDKAT 407
Cdd:TIGR01039 312 TTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVgEEHYDVARGVQQILQRYKELQDIIAIlgmdeLSEEDKLT 391
|
410 420 430
....*....|....*....|....*....|....*..
gi 169143037 408 qnqLARGQRLRELLKQsqakPLTVAEQiltiYTGTNG 444
Cdd:TIGR01039 392 ---VERARRIQRFLSQ----PFFVAEV----FTGQPG 417
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
97-378 |
4.45e-26 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 110.64 E-value: 4.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 97 QIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRELIIGDRQTGK 176
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 177 TaVATDTILNQQGNNVICVYVaIGQKASSVAQVV-NALQERGAMEYTIVVAEAADSPATLQYLAPYtGAALAEYFMYRER 255
Cdd:PRK07960 189 S-VLLGMMARYTQADVIVVGL-IGERGREVKDFIeNILGAEGRARSVVIAAPADVSPLLRMQGAAY-ATRIAEDFRDRGQ 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 256 HTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSrlGEGSMTALPIVETQSGDVSAYIPTNV 335
Cdd:PRK07960 266 HVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGDDQQDPIADSA 343
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 169143037 336 ISITDGQIFLSADLFNAGIRPAINVGISVSRVGSA-------AQIKAMKQ 378
Cdd:PRK07960 344 RAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAlideqhyARVRQFKQ 393
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
86-435 |
3.53e-25 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 107.68 E-value: 3.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 86 GSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQR 165
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 166 ELIIGDRQTGKTA-VATDTILNQQGNNVICVyvaIGQKASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPYTGA 244
Cdd:PRK05922 160 IGVFSEPGSGKSSlLSTIAKGSKSTINVIAL---IGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAM 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 245 ALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSsrlgEGSMTALPIVetqs 324
Cdd:PRK05922 237 TIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND----KGSITALYAI---- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 325 gdvsAYIPTN-------VISITDGQIFLSADlFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAE---LE 394
Cdd:PRK05922 309 ----LHYPNHpdiftdyLKSLLDGHFFLTPQ-GKALASPPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEaldII 383
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 169143037 395 AFAQFSSDLDKatqnQLARGQRLRELLKQSQAKPLTVAEQI 435
Cdd:PRK05922 384 QLGAYVPGQDA----HLDRAVKLLPSIKQFLSQPLSSYCAL 420
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
86-396 |
1.52e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 96.97 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 86 GSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQR 165
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 166 ELIIGDRQTGKTAVATDTILNQQGN-NVICVyvaIGQKASSVAQVVNA-LQERGaMEYTIVVAEAADSPATLQYLAPYTG 243
Cdd:PRK06793 159 IGIFAGSGVGKSTLLGMIAKNAKADiNVISL---VGERGREVKDFIRKeLGEEG-MRKSVVVVATSDESHLMQLRAAKLA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 244 AALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPgreaYPGDVFYLHS---RLLERAAKLSsrlgEGSMTALPIV 320
Cdd:PRK06793 235 TSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQ----KGSITGIYTV 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169143037 321 ETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAF 396
Cdd:PRK06793 307 LVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELY 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 |
4.44e-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: 90.33 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 145 EPLQTGLIAIDAMIPIGRGQRELIIGDRQTGKTavatdtILNQQ----GNNVICVYVAIGQKASSVAQVVNALQE----- 215
Cdd:cd01134 58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKT------VISQSlskwSNSDVVIYVGCGERGNEMAEVLEEFPElkdpi 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 216 --RGAMEYTIVVAEAADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGdvfY 293
Cdd:cd01134 132 tgESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---Y 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 294 LHSRL---LERAAK---LSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITdgQIF--LSADLFNAGIRPAINVGISVS 365
Cdd:cd01134 209 LGARLaefYERAGRvrcLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYS 286
|
.
gi 169143037 366 R 366
Cdd:cd01134 287 K 287
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
51-345 |
1.71e-17 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 84.70 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 51 GELVEFEE---GTIGIALNLESKNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIsssES 127
Cdd:PRK02118 26 GELATVERkdgSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPEL---EG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 128 RLIE------SPAPGIISRRSVyeplQTGLIAIDAMIPIGRGQRELIIGDRQTGKTAVATdTILNQQGNNVIcVYVAIGQ 201
Cdd:PRK02118 103 EPIEiggpsvNPVKRIVPREMI----RTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA-RIALQAEADII-ILGGMGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 202 KASSVAQVVNALQERGAMEYTIVVAEAADSPATLQYLAPYTGAALAEYFMYRE-RHTLIIYDDPSKQAQAYRQMSLLLRR 280
Cdd:PRK02118 177 TFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLTDMTNFADALKEISITMDQ 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169143037 281 PPGREAYPGDvfyLHSRLLERAAKLSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFL 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 |
8.78e-17 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 74.79 E-value: 8.78e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 376 MKQVAGKLKLELAQFAELEAFAQFSSD--LDKATQNQLARGQRLRELLKQSQAKPLTVAEQILTIYTGTN 443
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
97-367 |
9.02e-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: 9.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 97 QIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMIPIGRGQRELIIGDRQTGK 176
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 177 TAVATDTILN-QQGNNVICVYVAIGQKASSVAQVVNALQERGameytiVVAEAADSPATLQY-----------LAPYTGA 244
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGERTREGNDLYHEMKESG------VINLDGLSKVALVYgqmneppgaraRVALTGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 245 ALAEYFMYRE-RHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSSRlgEGSMTALPIVETQ 323
Cdd:cd01133 155 TMAEYFRDEEgQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERIT--STK--KGSITSVQAVYVP 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 169143037 324 SGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRV 367
Cdd:cd01133 231 ADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
29-93 |
9.82e-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: 9.82e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169143037 29 TGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESKNVGVVLMGDGLMIQEGSSVKATG 93
Cdd:pfam02874 5 IGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
79-163 |
3.77e-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: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 79 DGLmiQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDAMI 158
Cdd:COG0055 64 DGL--VRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLA 141
|
....*
gi 169143037 159 PIGRG 163
Cdd:COG0055 142 PYAKG 146
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
145-366 |
1.25e-12 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 70.20 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 145 EPLQTGLIAIDAMIPIGRGQRELIIGDRQTGKTavatdtILNQQ----GNNVICVYVAIGQKASSVAQVVNALQE----- 215
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT------VTQHQlakwADADIVIYVGCGERGNEMTEVLEEFPElidpk 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 216 --RGAMEYTIVVAEAADSP-----ATLqylapYTGAALAEYfmYRE--RHTLIIYDDPSKQAQAYRQMSLLLRRPPGREA 286
Cdd:PRK04192 283 tgRPLMERTVLIANTSNMPvaareASI-----YTGITIAEY--YRDmgYDVLLMADSTSRWAEALREISGRLEEMPGEEG 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 287 YPGdvfYLHSRL---LERAAKLSSRLG-EGSMTALPIVETQSGDVSAYIPTNVISITdgQIF--LSADLFNAGIRPAINV 360
Cdd:PRK04192 356 YPA---YLASRLaefYERAGRVKTLGGeEGSVTIIGAVSPPGGDFSEPVTQNTLRIV--KVFwaLDAELADRRHFPAINW 430
|
....*.
gi 169143037 361 GISVSR 366
Cdd:PRK04192 431 LTSYSL 436
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
193-372 |
2.36e-12 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 69.67 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 193 ICVYVAIGQKASSVAQVVNALQE-------RGAMEYTIVVAEAADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDPS 265
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 266 KQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKLSSRLGEGSMTALPIVETQSGDVSAYIPTNVISIT 339
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVV 840
|
170 180 190
....*....|....*....|....*....|...
gi 169143037 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 |
3.26e-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: 58.86 E-value: 3.26e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169143037 29 TGTVLQVGDGIARIYGLDEVMAGELVEFEE-------GTIGIALNLESKNVGVVLMGDGLMIQEGSSVKATGR 94
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERgdgnnetVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
79-444 |
5.00e-10 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 61.60 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 79 DGLMiqEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGII---SRRSVYEplqTGLIAID 155
Cdd:CHL00060 79 DGLM--RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTKLSIFE---TGIKVVD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 156 AMIPIGRGQRELIIGDRQTGKTAVATDTIlnqqgNNV------ICVYVAIGQ------------KASSVAQVVNALQERG 217
Cdd:CHL00060 154 LLAPYRRGGKIGLFGGAGVGKTVLIMELI-----NNIakahggVSVFGGVGErtregndlymemKESGVINEQNIAESKV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 218 AMEYtivvAEAADSPATLQYLApYTGAALAEYFM-YRERHTLIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHS 296
Cdd:CHL00060 229 ALVY----GQMNEPPGARMRVG-LTALTMAEYFRdVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169143037 297 RLLERAAKLSsrlgEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR------VG-- 368
Cdd:CHL00060 304 SLQERITSTK----EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTmlqpriVGee 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169143037 369 --SAAQikAMKQVAGKLKlELAQFAELEAFAQFSSDlDKATqnqLARGQRLRELLKQsqakPLTVAEqiltIYTGTNG 444
Cdd:CHL00060 380 hyETAQ--RVKQTLQRYK-ELQDIIAILGLDELSEE-DRLT---VARARKIERFLSQ----PFFVAE----VFTGSPG 442
|
|
| |
