|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
3-503 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 1021.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 3 SIRPDEISSILKQQITDYDQSVSVSNVGTVLQIGDGIARIYGLDQVMAGELLEFEDGTEGIALNLEDDNVGAVLMGEALG 82
Cdd:PRK09281 2 QINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 83 VQEGSNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGR 162
Cdd:PRK09281 82 IKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 163 GQRELIIGDRQTGKTAIAIDTIINQKGQDVVCVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAPYT 242
Cdd:PRK09281 162 GQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 243 GAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDDMGGGSMTALPIIET 322
Cdd:PRK09281 242 GCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIET 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 323 QAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQFDELAAFSQFASD 402
Cdd:PRK09281 322 QAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 403 LDEATQQQLERGKRLRELLKQAQFSPLNLAEQVAVVYAGVKGLIDEVPVEDVTKFAAELREYLKLNKAEFIEEILKEKKL 482
Cdd:PRK09281 402 LDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKDL 481
|
490 500
....*....|....*....|.
gi 500144929 483 NEGLETTLTEVIKEVKSSMLA 503
Cdd:PRK09281 482 SDEIEAKLKAAIEEFKKTFAA 502
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
3-504 |
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: 1017.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 3 SIRPDEISSILKQQITDYDQSVSVSNVGTVLQIGDGIARIYGLDQVMAGELLEFEDGTEGIALNLEDDNVGAVLMGEALG 82
Cdd:COG0056 2 QIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 83 VQEGSNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGR 162
Cdd:COG0056 82 IKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 163 GQRELIIGDRQTGKTAIAIDTIINQKGQDVVCVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAPYT 242
Cdd:COG0056 162 GQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 243 GAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDDMGGGSMTALPIIET 322
Cdd:COG0056 242 GCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIET 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 323 QAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQFDELAAFSQFASD 402
Cdd:COG0056 322 QAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 403 LDEATQQQLERGKRLRELLKQAQFSPLNLAEQVAVVYAGVKGLIDEVPVEDVTKFAAELREYLKLNKAEFIEEILKEKKL 482
Cdd:COG0056 402 LDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGKL 481
|
490 500
....*....|....*....|..
gi 500144929 483 NEGLETTLTEVIKEVKSSMLAT 504
Cdd:COG0056 482 DDEIEEKLKAAIEEFKKTFAAS 503
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
24-504 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 937.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 24 VSVSNVGTVLQIGDGIARIYGLDQVMAGELLEFEDGTEGIALNLEDDNVGAVLMGEALGVQEGSNVKSTGKIASVPVGEA 103
Cdd:CHL00059 2 VKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 104 MKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGKTAIAIDT 183
Cdd:CHL00059 82 YLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 184 IINQKGQDVVCVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAPYTGAAIAEHFMYQGKATLVIYDD 263
Cdd:CHL00059 162 ILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 264 LTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDDMGGGSMTALPIIETQAGDVSAYIPTNVISITDGQI 343
Cdd:CHL00059 242 LSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 344 FLSADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQFDELAAFSQFASDLDEATQQQLERGKRLRELLKQ 423
Cdd:CHL00059 322 FLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 424 AQFSPLNLAEQVAVVYAGVKGLIDEVPVEDVTKFAAELREYLKLNKAEFIEEILKEKKLNEGLETTLTEVIKEVKSSMLA 503
Cdd:CHL00059 402 SQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQLELFLL 481
|
.
gi 500144929 504 T 504
Cdd:CHL00059 482 Q 482
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
3-498 |
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: 864.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 3 SIRPDEISSILKQQITDYDQSVSVSNVGTVLQIGDGIARIYGLDQVMAGELLEFEDGTEGIALNLEDDNVGAVLMGEALG 82
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 83 VQEGSNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGR 162
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 163 GQRELIIGDRQTGKTAIAIDTIINQKGQDVVCVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAPYT 242
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 243 GAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDDMGGGSMTALPIIET 322
Cdd:TIGR00962 241 GCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 323 QAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQFDELAAFSQFASD 402
Cdd:TIGR00962 321 QAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 403 LDEATQQQLERGKRLRELLKQAQFSPLNLAEQVAVVYAGVKGLIDEVPVEDVTKFAAELREYLKLNKAEFIEEILKEKKL 482
Cdd:TIGR00962 401 LDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKL 480
|
490
....*....|....*.
gi 500144929 483 NEGLETTLTEVIKEVK 498
Cdd:TIGR00962 481 TEELEAKLKEALKNFK 496
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
7-498 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 776.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 7 DEISSILKQQITDYDQSVSVSNVGTVLQIGDGIARIYGLDQVMAGELLEFEDGTEGIALNLEDDNVGAVLMGEALGVQEG 86
Cdd:PRK13343 6 DEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 87 SNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRE 166
Cdd:PRK13343 86 TEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 167 LIIGDRQTGKTAIAIDTIINQKGQDVVCVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAPYTGAAI 246
Cdd:PRK13343 166 LIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 247 AEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDDMGGGSMTALPIIETQAGD 326
Cdd:PRK13343 246 AEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETLAGE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 327 VSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQFDELAAFSQFASDLDEA 406
Cdd:PRK13343 326 LSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLLDAG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 407 TQQQLERGKRLRELLKQAQFSPLNLAEQVAVVYAGVKGLIDEVPVEDVTKFAAELREYLKLNKAEFIEEILKEKKLNEGL 486
Cdd:PRK13343 406 TQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRELDEAW 485
|
490
....*....|..
gi 500144929 487 ETTLTEVIKEVK 498
Cdd:PRK13343 486 LAALEEILREAG 497
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
95-368 |
0e+00 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 582.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 95 IASVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRELIIGDRQT 174
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 175 GKTAIAIDTIINQKGQDVVCVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAPYTGAAIAEHFMYQG 254
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 255 KATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDDMGGGSMTALPIIETQAGDVSAYIPTN 334
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 500144929 335 VISITDGQIFLSADLFNSGLRPAINVGISVSRVG 368
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
7-484 |
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: 581.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 7 DEISSILKQQITDYDQSVSVSNVGTVLQIGDGIARIYGLDQVMAGELLEFEDGTEGIALNLEDDNVGAVLMGEALGVQEG 86
Cdd:TIGR03324 6 DKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 87 SNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRE 166
Cdd:TIGR03324 86 DEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 167 LIIGDRQTGKTAIAIDTIINQKGQDVVCVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAPYTGAAI 246
Cdd:TIGR03324 166 LILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 247 AEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDDMGGGSMTALPIIETQAGD 326
Cdd:TIGR03324 246 GEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 327 VSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQFDELAAFSQFASDLDEA 406
Cdd:TIGR03324 326 ISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDEN 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500144929 407 TQQQLERGKRLRELLKQAQFSPLNLAEQVAVVYAGVKGLIDEVPVEDVTKFAAELREYLKLNKAEFIEEILKEKKLNE 484
Cdd:TIGR03324 406 TRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSD 483
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
62-469 |
8.09e-119 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 360.89 E-value: 8.09e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 62 GIALNLEDDN-VGAVLMGEALGVQEGSNVKSTGKIASVPVGEAMKGRVVNPLGQpidgkgEIP----TSDNRLIEEM--- 133
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGH------EVPvgllTRSRALLESEqtl 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 134 ------APGIIKRRSVHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGKTAIAIDTIINQ--------KGQDVVCVYVAI 199
Cdd:PTZ00185 154 gkvdagAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 200 GQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAPYTGAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLR 279
Cdd:PTZ00185 234 GQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 280 RPPGREAYPGDVFYCHSRLLERAAKLSDDMGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAIN 359
Cdd:PTZ00185 314 RPPGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVN 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 360 VGISVSRVGGAAQTKAIKKIAGTLKLELAQFDELAAFSQFASDLDEATqqqLERGKRLRELLKQAQfsPLNLAEQVAVVY 439
Cdd:PTZ00185 394 IGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNALVSLY 468
|
410 420 430
....*....|....*....|....*....|
gi 500144929 440 AGVKGLIDEVPVEdvtkfAAELREYLKLNK 469
Cdd:PTZ00185 469 ACLNGYLDDVKVN-----YAKLYEYLLVNK 493
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
150-365 |
4.91e-114 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 335.48 E-value: 4.91e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 150 GITSIDAMIPVGRGQRELIIGDRQTGKTAIAiDTIINQKGQDVvCVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGA 229
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 230 SEAAALQYLAPYTGAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDdm 309
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKG-- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500144929 310 GGGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVS 365
Cdd:pfam00006 157 KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
113-431 |
1.42e-108 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 332.32 E-value: 1.42e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 113 GQPIDGKGEI--PTSDNRLIEEM----------APGIIKRRSVHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGKTAIA 180
Cdd:PRK07165 81 GKIIDIDGNIiyPEAQNPLSKKFlpntssifnlAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 181 IDTIINQKGQDVVCVYVAIGQKSASVANVVEVLREKGALDYTVVVSAgASEAAALQYLAPYTGAAIAEHFMYQGKAtLVI 260
Cdd:PRK07165 161 LNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAENISYNDDV-LIV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 261 YDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLsddMGGGSMTALPIIETQAGDVSAYIPTNVISITD 340
Cdd:PRK07165 239 FDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKF---KNRKTITALPILQTVDNDITSLISSNIISITD 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 341 GQIFLSADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQFDELAAFSQFASDLDEATQQQLERGKRLREL 420
Cdd:PRK07165 316 GQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKGKMIEKM 395
|
330
....*....|.
gi 500144929 421 LKQAQFSPLNL 431
Cdd:PRK07165 396 FNQKGFSLYSY 406
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
97-367 |
2.18e-103 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 310.54 E-value: 2.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 97 SVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGK 176
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 177 TAIAIDTIINQKGQDV-VCVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAPYTGAAIAEHFMYQGK 255
Cdd:cd19476 81 TVLAMQLARNQAKAHAgVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 256 ATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDdmGGGSMTALPIIETQAGDVSAYIPTNV 335
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 500144929 336 ISITDGQIFLSADLFNSGLRPAINVGISVSRV 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 ... |
376-500 |
5.31e-63 |
|
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: 201.06 E-value: 5.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 376 IKKIAGTLKLELAQFDELAAFSQFASDLDEATQQQLERGKRLRELLKQAQFSPLNLAEQVAVVYAGVKGLIDEVPVEDVT 455
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 500144929 456 KFAAELREYLKLNKAEFIEEILKEKKLNEGLETTLTEVIKEVKSS 500
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKS 125
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
372-496 |
1.39e-61 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 197.28 E-value: 1.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 372 QTKAIKKIAGTLKLELAQFDELAAFSQFASDLDEATQQQLERGKRLRELLKQAQFSPLNLAEQVAVVYAGVKGLIDEVPV 451
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 500144929 452 EDVTKFAAELREYLKLNKAEFIEEILKEKKLNEGLETTLTEVIKE 496
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEE 125
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
97-367 |
5.90e-51 |
|
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: 174.67 E-value: 5.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 97 SVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGK 176
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 177 TAIaIDTIINQKGQDVVcVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAPYTGAAIAEHFMYQGKA 256
Cdd:cd01136 81 STL-LGMIARNTDADVN-VIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 257 TLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDdmggGSMTALPIIETQAGDVSAYIPTNVI 336
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----GSITAFYTVLVEGDDFNDPIADEVR 234
|
250 260 270
....*....|....*....|....*....|.
gi 500144929 337 SITDGQIFLSADLFNSGLRPAINVGISVSRV 367
Cdd:cd01136 235 SILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
12-433 |
1.89e-49 |
|
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: 175.22 E-value: 1.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 12 ILKQQITDYDQSVSVSNVGTVLQIGDGIARIYGLDqVMAGELLEFEDGTEGIAL----NLEDDNVgaVLM--GEALGVQE 85
Cdd:COG1157 3 RLARLLARLEELPPVRVSGRVTRVVGLLIEAVGPD-ASIGELCEIETADGRPVLaevvGFRGDRV--LLMplGDLEGISP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 86 GSNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQR 165
Cdd:COG1157 80 GARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 166 eliIGdr---qtGKTAIaIDTIINQKGQDVVcVyVA-IGQKSASVANVVE-VLREKGaLDYTVVVSAGASEAAALQYLAP 240
Cdd:COG1157 160 ---IGifagsgvGKSTL-LGMIARNTEADVN-V-IAlIGERGREVREFIEdDLGEEG-LARSVVVVATSDEPPLMRLRAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 241 YTGAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKlsddMGGGSMTAL--- 317
Cdd:COG1157 233 YTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN----GGKGSITAFytv 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 318 ---------PIIETqagdvsayiptnVISITDGQIFLSADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELA 388
Cdd:COG1157 309 lvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLA 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 500144929 389 QFDE------LAAFsQFASD--LDEAtqqqLERGKRLRELLKQAQFSPLNLAE 433
Cdd:COG1157 377 RYEEnedlirIGAY-QPGSDpeLDEA----IALIPAIEAFLRQGMDERVSFEE 424
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
48-443 |
3.38e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 172.24 E-value: 3.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 48 VMAGELLEFEDGTEgiALNLEDDNVG-----AVL--MGEALGVQEGSNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKG 120
Cdd:PRK06936 42 VRIGELCYLRNPDN--SLSLQAEVIGfaqhqALLtpLGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 121 EIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGKTAIaIDTIInqKGQDV-VCVYVAI 199
Cdd:PRK06936 120 PPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTL-LASLI--RSAEVdVTVLALI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 200 GQKSASVANVVEV-LREKGaLDYTVVVSAGASEAAALQYLAPYTGAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLL 278
Cdd:PRK06936 197 GERGREVREFIESdLGEEG-LRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 279 RRPPGREAYPGDVFYCHSRLLERAAKlSDDmggGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAI 358
Cdd:PRK06936 276 GEPPTRRGYPPSVFAALPRLMERAGQ-SDK---GSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 359 NVGISVSRVGGAAQTKAIKKIAGTLKLELAQFDE---LAAFSQFASDLDEATQQQLERGKRLRELLKQAQFSPLNLAEQV 435
Cdd:PRK06936 352 DVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEvelLLQIGEYQKGQDKEADQAIERIGAIRGFLRQGTHELSHFNETL 431
|
....*...
gi 500144929 436 AVVYAGVK 443
Cdd:PRK06936 432 NLLETLTQ 439
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
9-429 |
4.59e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 171.92 E-value: 4.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 9 ISSILKQQITDYDQSVS-VSNVGTVLQIGDGIARIyGLDQVMAGELLEFE-DGTEGIALNLEDDNVGAVLMGEALGVQEG 86
Cdd:PRK06820 9 LTPRLQQQLTRPSAPPEgLRYRGPIVEIGPTLLRA-SLPGVAQGELCRIEpQGMLAEVVSIEQEMALLSPFASSDGLRCG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 87 SNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGkGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRE 166
Cdd:PRK06820 88 QWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 167 LIIGDRQTGKTAIaIDTIINQKGQDVVcVYVAIGQKSASVANVVEVLREKGALDYTVVVSAgASEAAALQYL-APYTGAA 245
Cdd:PRK06820 167 GIFAAAGVGKSTL-LGMLCADSAADVM-VLALIGERGREVREFLEQVLTPEARARTVVVVA-TSDRPALERLkGLSTATT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 246 IAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDdmggGSMTALPIIETQAG 325
Cdd:PRK06820 244 IAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDR----GSITAFYTVLVEGD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 326 DVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQFDE---LAAFSQFASD 402
Cdd:PRK06820 320 DMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEielLVRVGEYQAG 399
|
410 420
....*....|....*....|....*....
gi 500144929 403 LDEATQQQLERGKRLRELLKQA--QFSPL 429
Cdd:PRK06820 400 EDLQADEALQRYPAICAFLQQDhsETAHL 428
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
26-423 |
4.39e-44 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 161.09 E-value: 4.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 26 VSNVGTVLQIGDGIARIYGLDqVMAGELLEFEDGtEGiALNLEDDNVG-----AVL--MGEALGVQEGSNVKSTGKIASV 98
Cdd:PRK09099 22 VRRTGKVVEVIGTLLRVSGLD-VTLGELCELRQR-DG-TLLQRAEVVGfsrdvALLspFGELGGLSRGTRVIGLGRPLSV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 99 PVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGKTa 178
Cdd:PRK09099 99 PVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKS- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 179 iaidTIINQKGQDVVC---VYVAIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAPYTGAAIAEHFMYQGK 255
Cdd:PRK09099 178 ----TLMGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 256 ATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAklsddMGG-GSMTALPIIETQAGDVSAYIPTN 334
Cdd:PRK09099 254 RVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-----MGEtGSITALYTVLAEDESGSDPIAEE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 335 VISITDGQIFLSADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQFDELAAFSQ---FASDLDEATQQQL 411
Cdd:PRK09099 329 VRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQvgeYRAGSDPVADEAI 408
|
410
....*....|..
gi 500144929 412 ERGKRLRELLKQ 423
Cdd:PRK09099 409 AKIDAIRDFLSQ 420
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
97-423 |
8.20e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 152.15 E-value: 8.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 97 SVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGK 176
Cdd:PRK08472 91 NIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 177 TAIAIDTIINQKGQdvVCVYVAIGQKSASVANVVEVlREKGALDYTVVVSAGASEAAALQYLAPYTGAAIAEHFMYQGKA 256
Cdd:PRK08472 171 STLMGMIVKGCLAP--IKVVALIGERGREIPEFIEK-NLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 257 TLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKlsdDMGGGSMTALPIIETQAGDVSAYIPTNVI 336
Cdd:PRK08472 248 VLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTVLVEGDDMSDPIADQSR 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 337 SITDGQIFLSADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQFDE------LAAFSQFA-SDLDEAtqq 409
Cdd:PRK08472 325 SILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKEnevlirIGAYQKGNdKELDEA--- 401
|
330
....*....|....
gi 500144929 410 qLERGKRLRELLKQ 423
Cdd:PRK08472 402 -ISKKEFMEQFLKQ 414
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
47-367 |
2.11e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 151.01 E-value: 2.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 47 QVMAGELlefedgtEGIALNLEDDNVGAVLMGEALGVQEGSNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIPTSD 126
Cdd:PRK08972 53 ETMAGEL-------EAEVVGFDGDLLYLMPIEELRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 127 N--RLIEEMAPgiIKRRSVHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGKTaIAIDTIINQKGQDVVCVYVaIGQKSA 204
Cdd:PRK08972 126 RasRHSPPINP--LSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKS-VLLGMMTRGTTADVIVVGL-VGERGR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 205 SVANVVE-VLREKGaLDYTVVVSAGASEAAALQYLAPYTGAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPG 283
Cdd:PRK08972 202 EVKEFIEeILGEEG-RARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 284 REAYPGDVFYCHSRLLERAAKLSDdmGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGIS 363
Cdd:PRK08972 281 TKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEAS 358
|
....
gi 500144929 364 VSRV 367
Cdd:PRK08972 359 ISRV 362
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
76-396 |
6.05e-40 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 149.37 E-value: 6.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 76 LMGEALGVQEGSNVKSTGKIASVPVGEAMKGRVVNPLGQpIDGKGEIPTSDN-----RLIEEMAPGIIKRRSVHEPMQTG 150
Cdd:PRK08149 60 LIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGK-IVERFDAPPTVGpiseeRVIDVAPPSYAERRPIREPLITG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 151 ITSIDAMIPVGRGQRELIIGDRQTGKTAIaIDTIINQKGQDVvCVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGAS 230
Cdd:PRK08149 139 VRAIDGLLTCGVGQRMGIFASAGCGKTSL-MNMLIEHSEADV-FVIGLIGERGREVTEFVESLRASSRREKCVLVYATSD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 231 EAAALQYLAPYTGAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDdmg 310
Cdd:PRK08149 217 FSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA--- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 311 gGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQF 390
Cdd:PRK08149 294 -GSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRL 372
|
....*.
gi 500144929 391 DELAAF 396
Cdd:PRK08149 373 EELQLF 378
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
68-436 |
8.18e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 149.50 E-value: 8.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 68 EDDNVGAVLMGEALGVQEGSNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRlieEMAPGII---KRRSVH 144
Cdd:PRK05688 73 SGDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWV---PMDGPTInplNRHPIS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 145 EPMQTGITSIDAMIPVGRGQRELIIGDRQTGKTAIaIDTIINQKGQDVVCVYVaIGQKSASVANVVE-VLREKGaLDYTV 223
Cdd:PRK05688 150 EPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVL-LGMMTRFTEADIIVVGL-IGERGREVKEFIEhILGEEG-LKRSV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 224 VVSAGASEAAALQYLAPYTGAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAA 303
Cdd:PRK05688 227 VVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 304 klSDDMGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTL 383
Cdd:PRK05688 307 --NAEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRF 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 500144929 384 KLELAQFDE---LAAFSQFASDLDEATQQQLERGKRLRELLKQAQFSPLNLAEQVA 436
Cdd:PRK05688 385 KQLWSRYQQsrdLISVGAYVAGGDPETDLAIARFPHLVQFLRQGLRENVSLAQSRE 440
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
75-437 |
1.02e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 149.10 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 75 VLMGEALGVQE---GSNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGI 151
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 152 TSIDAMIPVGRGQRELIIGDRQTGKTAIaIDTIINQKGQDVvCVYVAIGQKSASVANVVEV-LREKGaLDYTVVVSAGAS 230
Cdd:PRK07721 147 RAIDSLLTVGKGQRVGIFAGSGVGKSTL-MGMIARNTSADL-NVIALIGERGREVREFIERdLGPEG-LKRSIVVVATSD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 231 EAAALQYLAPYTGAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKlsddMG 310
Cdd:PRK07721 224 QPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGT----NA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 311 GGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQF 390
Cdd:PRK07721 300 SGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTY 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 500144929 391 DE------LAAFSQFAS-DLDEATQQQlergKRLRELLKQAQFSPLNLAEQVAV 437
Cdd:PRK07721 380 QNsedlinIGAYKRGSSrEIDEAIQFY----PQIISFLKQGTDEKATFEESIQA 429
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
30-428 |
5.00e-39 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 147.02 E-value: 5.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 30 GTVLQIGDGIARIYgLDQVMAGELLEFEDGtEGIA--LNLEDDNVGAVLMGEALGVQEGSNVKSTGKIASVPVGEAMKGR 107
Cdd:PRK07594 23 GRIQDVSATLLNAW-LPGVFMGELCCIKPG-EELAevVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 108 VVNPLGQPIDGKgEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGKTAIaIDTIINQ 187
Cdd:PRK07594 101 VIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLCNA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 188 KGQDVVcVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAPYTGAAIAEHFMYQGKATLVIYDDLTKQ 267
Cdd:PRK07594 179 PDADSN-VLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 268 AQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAklsddMGG-GSMTALPIIETQAGDVSAYIPTNVISITDGQIFLS 346
Cdd:PRK07594 258 ARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 347 ADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQFDE---LAAFSQFASDLDEATQQQLERGKRLRELLKQ 423
Cdd:PRK07594 333 RRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEvelLIRIGEYQRGVDTDTDKAIDTYPDICTFLRQ 412
|
....*
gi 500144929 424 AQFSP 428
Cdd:PRK07594 413 SKDEV 417
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
95-366 |
1.17e-38 |
|
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: 142.36 E-value: 1.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 95 IASVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRELIIGDrqT 174
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSG--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 175 GKTA------IAIDTIINQKGQDVVCVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAPYTGAAIAE 248
Cdd:cd01135 79 GLPHnelaaqIARQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 249 HFMYQ-GKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDDmgGGSMTALPIIETQAGDV 327
Cdd:cd01135 159 YLAYEkGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGR--KGSITQIPILTMPNDDI 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 500144929 328 SAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSR 366
Cdd:cd01135 237 THPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
13-429 |
3.36e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 142.44 E-value: 3.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 13 LKQQITDYDQSV-SVSNVGTVLQIGDGIARIYGLDQ-VMAGELLEFEDGTE---GIALNLEDDNVGAVLMGEALGVQEGS 87
Cdd:PRK06002 10 LAALVERYAAPEpLVRIGGTVSEVTASHYRVRGLSRfVRLGDFVAIRADGGthlGEVVRVDPDGVTVKPFEPRIEIGLGD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 88 NVKSTGKIASVPvGEAMKGRVVNPLGQPIDGKGEIPTSDNRL-IEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRE 166
Cdd:PRK06002 90 AVFRKGPLRIRP-DPSWKGRVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 167 LIIGDRQTGKT--------AIAIDTiinqkgqdvvcVYVA-IGQKSASVANVVE-VLRekGALDYTVVVSAGASEAAALQ 236
Cdd:PRK06002 169 GIFAGSGVGKStllamlarADAFDT-----------VVIAlVGERGREVREFLEdTLA--DNLKKAVAVVATSDESPMMR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 237 YLAPYTGAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDdmGGGSMTA 316
Cdd:PRK06002 236 RLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 317 LPIIETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSRVGGAAQTKAIKKIAGTLKLELAQFDE---- 392
Cdd:PRK06002 314 IFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdl 393
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 500144929 393 --LAAFSQFA-SDLDEATQQQlergKRLRELLKQAQFSPL 429
Cdd:PRK06002 394 rlIGGYRAGSdPDLDQAVDLV----PRIYEALRQSPGDPP 429
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
30-366 |
2.50e-36 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 139.96 E-value: 2.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 30 GTVLQIGDGIARIygldQVmagelleFEdGTEGIALnleddnvgavlmgealgvqEGSNVKSTGKIASVPVGEAMKGRVV 109
Cdd:PRK04196 41 GQVLEVSEDKAVV----QV-------FE-GTTGLDL-------------------KDTKVRFTGEPLKLPVSEDMLGRIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 110 NPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQR------------EL---IIgdRQT 174
Cdd:PRK04196 90 DGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnELaaqIA--RQA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 175 gktaiaidTIINQKGQDVVcVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAPYTGAAIAEHFMYQ- 253
Cdd:PRK04196 168 --------KVLGEEENFAV-VFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFEk 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 254 GKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGdvfYCHSRL---LERAAKLSDDmgGGSMTALPIIETQAGDVSAY 330
Cdd:PRK04196 239 GMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHP 313
|
330 340 350
....*....|....*....|....*....|....*.
gi 500144929 331 IPTNVISITDGQIFLSADLFNSGLRPAINVGISVSR 366
Cdd:PRK04196 314 IPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
82-436 |
5.90e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 138.49 E-value: 5.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 82 GVQEGSNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIpTSDNRLIEEMAP-GIIKRRSVHEPMQTGITSIDAMIPV 160
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQL-GGSTPLQQQLPQiHPLQRRAVDTPLDVGVNAINGLLTI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 161 GRGQRELIIGDRQTGKTAIaIDTIINQKGQDVVCVYVaIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAP 240
Cdd:PRK07196 153 GKGQRVGLMAGSGVGKSVL-LGMITRYTQADVVVVGL-IGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKAT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 241 YTGAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAklsDDMGGGSMTALPII 320
Cdd:PRK07196 231 ELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 321 ETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSR----VGGAAQTKAIKKIAGTLKlELAQFDELAAF 396
Cdd:PRK07196 308 LAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCYA-DYMAIKPLIPL 386
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 500144929 397 SQFASDLDEATQQQLERGKRLRELLKQAQFSPLNLAEQVA 436
Cdd:PRK07196 387 GGYVAGADPMADQAVHYYPAITQFLRQEVGHPALFSASVE 426
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
24-366 |
4.31e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 125.09 E-value: 4.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 24 VSVSNVGTVLQIGDGIARIYGLDQVMAGELLEFEDGTegialnleddnvgAVLM--GEALGVQEGSNVKSTGKIASVPVG 101
Cdd:PRK08927 29 VEVAGPIHALSVGARIVVETRGGRPVPCEVVGFRGDR-------------ALLMpfGPLEGVRRGCRAVIANAAAAVRPS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 102 EAMKGRVVNPLGQPIDGKGEIPTSD-NRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGKTAIa 180
Cdd:PRK08927 96 RAWLGRVVNALGEPIDGKGPLPQGPvPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVL- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 181 IDTIINQKGQDVVcVYVAIGQKSASVANVVE-VLREKGaLDYTVVVSAGASEAAALQYLAPYTGAAIAEHFMYQGKATLV 259
Cdd:PRK08927 175 LSMLARNADADVS-VIGLIGERGREVQEFLQdDLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 260 IYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAklSDDMGGGSMTALPIIETQAGDVSAYIPTNVISIT 339
Cdd:PRK08927 253 LMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVDGDDHNEPVADAVRGIL 330
|
330 340
....*....|....*....|....*..
gi 500144929 340 DGQIFLSADLFNSGLRPAINVGISVSR 366
Cdd:PRK08927 331 DGHIVMERAIAERGRYPAINVLKSVSR 357
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
63-481 |
1.96e-30 |
|
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: 123.29 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 63 IALNLEDDNVGAVLMGEALGVQEGSNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRS 142
Cdd:TIGR01039 43 VAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQST 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 143 VHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGKTAIAIDTIIN-QKGQDVVCVYVAIGQKSASVANVVEVLREKGALDY 221
Cdd:TIGR01039 123 KVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 222 TVVVSAGASEAAALQYLAPYTGAAIAEHFM-YQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYpgdvfychsrlle 300
Cdd:TIGR01039 203 TALVYGQMNEPPGARMRVALTGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGY------------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 301 rAAKLSDDMG----------GGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSR---- 366
Cdd:TIGR01039 270 -QPTLATEMGelqeritstkTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRlldp 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 367 -VGGAAQTKAIKKIAGTLK--------LELAQFDELaafsqfaSDLDEATqqqLERGKRLRELLKQAQFsplnlaeqVAV 437
Cdd:TIGR01039 349 sVVGEEHYDVARGVQQILQrykelqdiIAILGMDEL-------SEEDKLT---VERARRIQRFLSQPFF--------VAE 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 500144929 438 VYAGVKGliDEVPVED-VTKFAAELR-EYLKLNKAEF-----IEEILKEKK 481
Cdd:TIGR01039 411 VFTGQPG--KYVPLKDtIRGFKEILEgKYDHLPEQAFymvgtIEEVVEKAK 459
|
|
| 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 |
6.84e-30 |
|
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: 111.39 E-value: 6.84e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500144929 28 NVGTVLQIGDGIARIYGLDQVMAGELLEFEDGTEGIALNLEDDNVGAVLMGEALGVQEGSNVKSTGK 94
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
86-367 |
3.44e-28 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 116.81 E-value: 3.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 86 GSNVKSTGKiaSVPVGEAMKGRVVNPLGQPIDGkgeIPTSDNrliEEMAPGI------IKRRSVHEPMQTGITSIDAMIP 159
Cdd:PRK07960 100 SGEGLQSGK--QLPLGPALLGRVLDGSGKPLDG---LPAPDT---GETGALItppfnpLQRTPIEHVLDTGVRAINALLT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 160 VGRGQRELIIGDRQTGKTAIaIDTIINQKGQDVVCVYVaIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLA 239
Cdd:PRK07960 172 VGRGQRMGLFAGSGVGKSVL-LGMMARYTQADVIVVGL-IGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 240 PYTGAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDdmGGGSMTALPI 319
Cdd:PRK07960 250 AAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYT 327
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 500144929 320 IETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSRV 367
Cdd:PRK07960 328 VLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRA 375
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
87-367 |
2.79e-26 |
|
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: 111.35 E-value: 2.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 87 SNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRE 166
Cdd:TIGR01040 65 TTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 167 LIIGD-------------RQTGKTAIAIDTIINQKGQDVVCVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGASEAA 233
Cdd:TIGR01040 145 PIFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 234 ALQYLAPYTGAAIAEHFMYQ-GKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAKLSDDmgGG 312
Cdd:TIGR01040 225 IERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR--NG 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 500144929 313 SMTALPIIETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSRV 367
Cdd:TIGR01040 303 SITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 357
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
86-366 |
1.74e-25 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 108.84 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 86 GSNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQR 165
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 166 ELIIGDRQTGKTAIAidTIINQKGQDVVCVYVAIGQKSASVANVVEVLREKGALDYTVVVSAGASEAAALQYLAPYTGAA 245
Cdd:PRK05922 160 IGVFSEPGSGKSSLL--STIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 246 IAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFYCHSRLLERAAklSDDMggGSMTALPIIETQAG 325
Cdd:PRK05922 238 IAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG--NNDK--GSITALYAILHYPN 313
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 500144929 326 DVSAYIPTnVISITDGQIFLSADlFNSGLRPAINVGISVSR 366
Cdd:PRK05922 314 HPDIFTDY-LKSLLDGHFFLTPQ-GKALASPPIDILTSLSR 352
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
86-367 |
9.86e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 97.36 E-value: 9.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 86 GSNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGE-IPTSDNRLieeMAPGI--IKRRSVHEPMQTGITSIDAMIPVGR 162
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAEnIPLQKIKL---DAPPIhaFEREEITDVFETGIKSIDSMLTIGI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 163 GQRELIIGDRQTGKTAIAidTIINQKGQDVVCVYVAIGQKSASVANVV-EVLREKGaLDYTVVVSAGASEAAALQYLAPY 241
Cdd:PRK06793 156 GQKIGIFAGSGVGKSTLL--GMIAKNAKADINVISLVGERGREVKDFIrKELGEEG-MRKSVVVVATSDESHLMQLRAAK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 242 TGAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLRRPP--GR----EAYpgdvfycHSRLLERAAKLSDdmggGSMT 315
Cdd:PRK06793 233 LATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPigGKtllmESY-------MKKLLERSGKTQK----GSIT 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 500144929 316 ALPIIETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSRV 367
Cdd:PRK06793 302 GIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRI 353
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
65-352 |
4.16e-21 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 95.49 E-value: 4.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 65 LNLEDDNVGAVLMGEALGVQEGSNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIptsDNRLIEEMAPGI--IKRRS 142
Cdd:PRK02118 43 IRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPEL---EGEPIEIGGPSVnpVKRIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 143 VHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGKTAIAIdTIINQKGQDVVcVYVAIGQKSASVANVVEVLREKGALDYT 222
Cdd:PRK02118 120 PREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA-RIALQAEADII-ILGGMGLTFDDYLFFKDTFENAGALDRT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 223 VVVSAGASEAAALQYLAPYTGAAIAEHFMYQG-KATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYPGDVFychSRLLER 301
Cdd:PRK02118 198 VMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLY---SDLASR 274
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 500144929 302 AAKLSDDMGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIFL---SADLFNS 352
Cdd:PRK02118 275 YEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLrrgRIDPFGS 328
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
97-367 |
2.15e-19 |
|
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: 88.05 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 97 SVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGK 176
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 177 TAIAIDTIIN-QKGQDVVCVYVAIGQKSASVANVVEVLREKG-----ALDYTVVVSAGASEAAALQYLAPYTGAAIAEHF 250
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGERTREGNDLYHEMKESGvinldGLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 251 M-YQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAYpgdvfychsrllerAAKLSDDMG----------GGSMTALPI 319
Cdd:cd01133 161 RdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGY--------------QPTLATEMGslqeritstkKGSITSVQA 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 500144929 320 IETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSRV 367
Cdd:cd01133 227 VYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
25-366 |
5.67e-18 |
|
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: 86.30 E-value: 5.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 25 SVSNVGTVLQI----------GDGIARIYgldqvmagELLEFEDGTEG-----IALNLEDDNVGAVLMGEALGVQEGSNV 89
Cdd:COG0055 1 MAMNTGKIVQVigpvvdvefpEGELPAIY--------NALEVENEGGGelvleVAQHLGDNTVRCIAMDSTDGLVRGMEV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 90 KSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIKRRSVHEPMQTGITSIDAMIPVGRGQRELII 169
Cdd:COG0055 73 IDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 170 GDRQTGKTAIAIDTIINqkgqdvvcvyVAIGQKSASV-ANVVEVLRE----------KGALDYTVVV------SAGASEA 232
Cdd:COG0055 153 GGAGVGKTVLIMELIHN----------IAKEHGGVSVfAGVGERTREgndlyremkeSGVLDKTALVfgqmnePPGARLR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 233 AALqylapyTGAAIAEHFM-YQGKATLVIYDDLTKQAQAYRQMSLLLRRPPGREAY-PgdvfychsrlleraaKLSDDMG 310
Cdd:COG0055 223 VAL------TALTMAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYqP---------------TLATEMG 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500144929 311 ----------GGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAINVGISVSR 366
Cdd:COG0055 282 alqeritstkKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSR 347
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
377-443 |
2.20e-16 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 73.63 E-value: 2.20e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500144929 377 KKIAGTLKLELAQFDELAAFSQFASD--LDEATQQQLERGKRLRELLKQAQFSPLNLAEQVAVVYAGVK 443
Cdd:cd01429 2 KAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
26-93 |
2.03e-15 |
|
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: 70.65 E-value: 2.03e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500144929 26 VSNVGTVLQIGDGIARIYGLDQVMAGELLEFEDGTEGIALNLEDDNVGAVLMGEALGVQEGSNVKSTG 93
Cdd:pfam02874 2 VQVIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
137-366 |
7.37e-15 |
|
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: 74.92 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 137 IIKRRSVHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGKTAIaIDTIINQKGQDVVcVYVAIGQKsasvAN-VVEVLRE 215
Cdd:cd01134 50 VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVI-SQSLSKWSNSDVV-IYVGCGER----GNeMAEVLEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 216 ----------KGALDYTVVVS------AGASEAAAlqylapYTGAAIAEHFMYQGKATLVIYDDLTKQAQAYRQMSLLLR 279
Cdd:cd01134 124 fpelkdpitgESLMERTVLIAntsnmpVAAREASI------YTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 280 RPPGREAYPGdvfYCHSRL---LERAAK---LSDDMGGGSMTALPIIETQAGDVSAYIPTNVISITdgQIF--LSADLFN 351
Cdd:cd01134 198 EMPAEEGYPA---YLGARLaefYERAGRvrcLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQ 272
|
250
....*....|....*
gi 500144929 352 SGLRPAINVGISVSR 366
Cdd:cd01134 273 RRHFPSINWLISYSK 287
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
67-359 |
6.56e-13 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 70.84 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 67 LEDDNVGAVLMGEALGVQEGSNVKSTGKIASVPVGEAMKGRVVNPLGQPIDGKGEIPTSDNRLIEEMAPGIIK---RRSV 143
Cdd:CHL00060 65 LGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQldtKLSI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 144 HEpmqTGITSIDAMIPVGRGQRELIIGDRQTGKTAIAIDTIIN-QKGQDVVCVYVAIGQ------------KSASVANVV 210
Cdd:CHL00060 145 FE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGErtregndlymemKESGVINEQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 211 EVLREKGALDY-TVVVSAGASEAAALqylapyTGAAIAEHFMYQGKA-TLVIYDDLTKQAQAYRQMSLLLRRPPGREAYp 288
Cdd:CHL00060 222 NIAESKVALVYgQMNEPPGARMRVGL------TALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGY- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 289 gdvfychsrllerAAKLSDDMGG----------GSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSADLFNSGLRPAI 358
Cdd:CHL00060 295 -------------QPTLSTEMGSlqeritstkeGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAV 361
|
.
gi 500144929 359 N 359
Cdd:CHL00060 362 D 362
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
193-359 |
9.67e-11 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 64.66 E-value: 9.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 193 VCVYVAIGQKSASVANVVEVLRE-------KGALDYTVVVSAGASEAAALQYLAPYTGAAIAEHFMYQGKATLVIYDDLT 265
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 266 KQAQAYRQMSLLLRRPPGREAYPGdvfYCHSRLLE------RAAKLSDDMGGGSMTALPIIETQAGDVSAYIPTNVISIT 339
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVV 840
|
170 180
....*....|....*....|
gi 500144929 340 DGQIFLSADLFNSGLRPAIN 359
Cdd:PRK14698 841 KVFWALDADLARRRHFPAIN 860
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
30-94 |
1.21e-08 |
|
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: 51.54 E-value: 1.21e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500144929 30 GTVLQIGDGIARIYGLDQVMAGELLEFE-------DGTEGIALNLEDDNVGAVLMGEALGVQEGSNVKSTGK 94
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIGEVCEIErgdgnneTVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
70-302 |
1.00e-07 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 54.40 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 70 DNVGAvlmGEALG-VQEGSNVksTGKIAsVPVGeaMKGRVVNplgqpIDGKGE---------IPTSDNRLIE-EMA---- 134
Cdd:PRK04192 128 DKVEA---GDILGtVQETPSI--EHKIM-VPPG--VSGTVKE-----IVSEGDytvddtiavLEDEDGEGVElTMMqkwp 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 135 ---PGIIKRR-SVHEPMQTGITSIDAMIPVGRGQRELIIGDRQTGKT----AIAidtiinqKGQDV-VCVYVAIGQKsas 205
Cdd:PRK04192 195 vrrPRPYKEKlPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTvtqhQLA-------KWADAdIVIYVGCGER--- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500144929 206 vAN-VVEVLRE----------KGALDYTVVVS------AGASEAAAlqylapYTGAAIAEHFMYQGKATLVIYDDLTKQA 268
Cdd:PRK04192 265 -GNeMTEVLEEfpelidpktgRPLMERTVLIAntsnmpVAAREASI------YTGITIAEYYRDMGYDVLLMADSTSRWA 337
|
250 260 270
....*....|....*....|....*....|....*..
gi 500144929 269 QAYRQMSLLLRRPPGREAYPGdvfYCHSRL---LERA 302
Cdd:PRK04192 338 EALREISGRLEEMPGEEGYPA---YLASRLaefYERA 371
|
|
| |
