|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-500 |
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: 1068.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 1 MNLRPEEISSIIKQQIKNYDNKIELTDTGSVLKVGDGIATVYGLENVMSSELLEFPGEVFGMALNLEEDVVGAVLFGDDS 80
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 81 GIKEGDIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIG 160
Cdd:COG0056 81 GIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 161 RGQRELIIGDRQTGKTSIAIDTILNQKGKDVICIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPY 240
Cdd:COG0056 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 241 AGAAMGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIE 320
Cdd:COG0056 241 AGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 321 TQAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSRVGGSAQIKSMKKVSGTLKLAYSQYRELASFSQFGS 400
Cdd:COG0056 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 401 DLDADTKRRLAQGERIVEVLKQGENAPLDVSDQVMIIFAVTNGFVDDIPVSELSRFESELFKFVDANYPELSEKILANKD 480
Cdd:COG0056 401 DLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGK 480
|
490 500
....*....|....*....|....
gi 494498175 481 FTTD----LTTAINEFKKTFVVEA 500
Cdd:COG0056 481 LDDEieekLKAAIEEFKKTFAASA 504
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-497 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 1055.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 1 MNLRPEEISSIIKQQIKNYDNKIELTDTGSVLKVGDGIATVYGLENVMSSELLEFPGEVFGMALNLEEDVVGAVLFGDDS 80
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 81 GIKEGDIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIG 160
Cdd:PRK09281 81 DIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 161 RGQRELIIGDRQTGKTSIAIDTILNQKGKDVICIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPY 240
Cdd:PRK09281 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 241 AGAAMGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIE 320
Cdd:PRK09281 241 AGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 321 TQAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSRVGGSAQIKSMKKVSGTLKLAYSQYRELASFSQFGS 400
Cdd:PRK09281 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 401 DLDADTKRRLAQGERIVEVLKQGENAPLDVSDQVMIIFAVTNGFVDDIPVSELSRFESELFKFVDANYPELSEKILANKD 480
Cdd:PRK09281 401 DLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKD 480
|
490 500
....*....|....*....|.
gi 494498175 481 FTTD----LTTAINEFKKTFV 497
Cdd:PRK09281 481 LSDEieakLKAAIEEFKKTFA 501
|
|
| 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: 872.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 3 LRPEEISSIIKQQIKNYDNKIELTDTGSVLKVGDGIATVYGLENVMSSELLEFPGEVFGMALNLEEDVVGAVLFGDDSGI 82
Cdd:TIGR00962 2 LKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 83 KEGDIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRG 162
Cdd:TIGR00962 82 REGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 163 QRELIIGDRQTGKTSIAIDTILNQKGKDVICIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPYAG 242
Cdd:TIGR00962 162 QRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 243 AAMGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIETQ 322
Cdd:TIGR00962 242 CTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIETQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 323 AGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSRVGGSAQIKSMKKVSGTLKLAYSQYRELASFSQFGSDL 402
Cdd:TIGR00962 322 AGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASDL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 403 DADTKRRLAQGERIVEVLKQGENAPLDVSDQVMIIFAVTNGFVDDIPVSELSRFESELFKFVDANYPELSEKILANKDFT 482
Cdd:TIGR00962 402 DEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKLT 481
|
490 500
....*....|....*....|
gi 494498175 483 ----TDLTTAINEFKKTFVV 498
Cdd:TIGR00962 482 eeleAKLKEALKNFKKTFAW 501
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-497 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 807.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 1 MNLRPEEISSIIKQQIKNYDNKIELTDTGSVLKVGDGIATVYGLENVMSSELLEFPGEVFGMALNLEEDVVGAVLFGDDS 80
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 81 GIKEGDIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIG 160
Cdd:PRK13343 81 DILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 161 RGQRELIIGDRQTGKTSIAIDTILNQKGKDVICIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPY 240
Cdd:PRK13343 161 RGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 241 AGAAMGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIE 320
Cdd:PRK13343 241 AGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 321 TQAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSRVGGSAQIKSMKKVSGTLKLAYSQYRELASFSQFGS 400
Cdd:PRK13343 321 TLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 401 DLDADTKRRLAQGERIVEVLKQGENAPLDVSDQVMIIFAVTNGFVDDIPVSELSRFESELFKFVDANYPELSEKILANKD 480
Cdd:PRK13343 401 LLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRE 480
|
490
....*....|....*..
gi 494498175 481 FTTDLTTAINEFKKTFV 497
Cdd:PRK13343 481 LDEAWLAALEEILREAG 497
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
23-500 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 805.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 23 IELTDTGSVLKVGDGIATVYGLENVMSSELLEFPGEVFGMALNLEEDVVGAVLFGDDSGIKEGDIVKRTGRIVEVPVGEA 102
Cdd:CHL00059 2 VKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 103 MIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGKTSIAIDT 182
Cdd:CHL00059 82 YLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 183 ILNQKGKDVICIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPYAGAAMGEEFMYNGKHVLIIYDD 262
Cdd:CHL00059 162 ILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 263 LSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIETQAGDVSAYIPTNVISITDGQI 342
Cdd:CHL00059 242 LSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 343 YLQPELFYSGVRPAVDPGISVSRVGGSAQIKSMKKVSGTLKLAYSQYRELASFSQFGSDLDADTKRRLAQGERIVEVLKQ 422
Cdd:CHL00059 322 FLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 423 GENAPLDVSDQVMIIFAVTNGFVDDIPVSELSRFESELFKFVDANYPELSEKILANKDFTTD----LTTAINEFKKTFVV 498
Cdd:CHL00059 402 SQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEaealLKEAIQEQLELFLL 481
|
..
gi 494498175 499 EA 500
Cdd:CHL00059 482 QE 483
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
6-479 |
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: 616.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 6 EEISSIIKQQIKNYDNKIELTDTGSVLKVGDGIATVYGLENVMSSELLEFPGEVFGMALNLEEDVVGAVLFGDDSGIKEG 85
Cdd:TIGR03324 6 DKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 86 DIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRE 165
Cdd:TIGR03324 86 DEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 166 LIIGDRQTGKTSIAIDTILNQKGKDVICIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPYAGAAM 245
Cdd:TIGR03324 166 LILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 246 GEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIETQAGD 325
Cdd:TIGR03324 246 GEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 326 VSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSRVGGSAQIKSMKKVSGTLKLAYSQYRELASFSQFGSDLDAD 405
Cdd:TIGR03324 326 ISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDEN 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494498175 406 TKRRLAQGERIVEVLKQGENAPLDVSDQVMIIFAVTNGFVDDIPVSELSRFESELFKFVDANYPELSEKILANK 479
Cdd:TIGR03324 406 TRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGK 479
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
94-367 |
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: 604.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 94 IVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQT 173
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 174 GKTSIAIDTILNQKGKDVICIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPYAGAAMGEEFMYNG 253
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 254 KHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIETQAGDVSAYIPTN 333
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 494498175 334 VISITDGQIYLQPELFYSGVRPAVDPGISVSRVG 367
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
61-499 |
1.78e-124 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 375.15 E-value: 1.78e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 61 GMALNLEED-VVGAVLFGDDSGIKEGDIVKRTGRIVEVPVGEAMIGRVVSPLG------LPIDGKGPINTNKTR-PVESP 132
Cdd:PTZ00185 80 GLVFNLEKDgRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGhevpvgLLTRSRALLESEQTLgKVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 133 APGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGKTSIAIDTILNQ--------KGKDVICIYVAIGQKRST 204
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 205 VAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPYAGAAMGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGRE 284
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGRE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 285 AYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVS 364
Cdd:PTZ00185 320 AYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVS 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 365 RVGGSAQIKSMKKVSGTLKLAYSQYRELASFSQFGSDLDADTkrrLAQGERIVEVLKQGEnaPLDVSDQVMIIFAVTNGF 444
Cdd:PTZ00185 400 RVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNALVSLYACLNGY 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 494498175 445 VDDIPVselsrfeselfkfvdaNYPELSEKILANKDFTTDLTTAINEFKKTFVVE 499
Cdd:PTZ00185 475 LDDVKV----------------NYAKLYEYLLVNKDLSVMYGTATNKFFYMYVQQ 513
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
149-364 |
1.23e-118 |
|
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: 347.04 E-value: 1.23e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 149 GIKSIDSMIPIGRGQRELIIGDRQTGKTSIAiDTILNQKGKDViCIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATA 228
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 229 SESAPLQYLAPYAGAAMGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEl 308
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGK- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494498175 309 gGGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVS 364
Cdd:pfam00006 158 -GGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
97-366 |
6.59e-112 |
|
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: 332.11 E-value: 6.59e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 97 VPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGKT 176
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 177 SIAIDTILNQKGKDV-ICIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPYAGAAMGEEFMYNGKH 255
Cdd:cd19476 82 VLAMQLARNQAKAHAgVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 256 VLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelGGGSMTALPIIETQAGDVSAYIPTNVI 335
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNTF 239
|
250 260 270
....*....|....*....|....*....|.
gi 494498175 336 SITDGQIYLQPELFYSGVRPAVDPGISVSRV 366
Cdd:cd19476 240 AILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
115-494 |
1.06e-111 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 340.03 E-value: 1.06e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 115 IDGK--GPINTNKTR----PVESP----APGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGKTSIAIDTIL 184
Cdd:PRK07165 86 IDGNiiYPEAQNPLSkkflPNTSSifnlAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTII 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 185 NQKGKDVICIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSAtASESAPLQYLAPYAGAAMGEEFMYNgKHVLIIYDDLS 264
Cdd:PRK07165 166 NQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAENISYN-DDVLIVFDDLT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 265 KQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLsdeLGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIYL 344
Cdd:PRK07165 244 KHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKF---KNRKTITALPILQTVDNDITSLISSNIISITDGQIVT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 345 QPELFYSGVRPAVDPGISVSRVGGSAQIKSMKKVSGTLKLAYSQYRELASFSQFGSDLDADTKRRLAQGERIVEVLKQGE 424
Cdd:PRK07165 321 SSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKGKMIEKMFNQKG 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 425 NAPLDVSDQVMIIFAVTNGFVDDIpvselsRFESELFKFVDA---NYPE---LSEKILANKDFTTDLT-----TAINEFK 493
Cdd:PRK07165 401 FSLYSYRFVLLISKLISWGLLKDV------KDEQKALDFIDYlieNDPDakkIFNKIKNNEDVDDELMknyfaFLLNQYS 474
|
.
gi 494498175 494 K 494
Cdd:PRK07165 475 D 475
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
375-496 |
3.67e-64 |
|
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: 204.14 E-value: 3.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 375 MKKVSGTLKLAYSQYRELASFSQFGSDLDADTKRRLAQGERIVEVLKQGENAPLDVSDQVMIIFAVTNGFVDDIPVSELS 454
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 494498175 455 RFESELFKFVDANYPELSEKILANKDFTTD----LTTAINEFKKTF 496
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDEleekLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
371-496 |
1.55e-62 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 199.98 E-value: 1.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 371 QIKSMKKVSGTLKLAYSQYRELASFSQFGSDLDADTKRRLAQGERIVEVLKQGENAPLDVSDQVMIIFAVTNGFVDDIPV 450
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 494498175 451 SELSRFESELFKFVDANYPELSEKILANKDFTTDLTTAINEFKKTF 496
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
96-366 |
1.21e-52 |
|
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: 178.91 E-value: 1.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 96 EVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGK 175
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 176 TSIaIDTILNQKGKDVICIyVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPYAGAAMGEEFMYNGKH 255
Cdd:cd01136 81 STL-LGMIARNTDADVNVI-ALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 256 VLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSMTALPIIETQAGDVSAYIPTNVI 335
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----GSITAFYTVLVEGDDFNDPIADEVR 234
|
250 260 270
....*....|....*....|....*....|.
gi 494498175 336 SITDGQIYLQPELFYSGVRPAVDPGISVSRV 366
Cdd:cd01136 235 SILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
16-432 |
4.52e-47 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 169.06 E-value: 4.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 16 IKNYDNKIELTDT----GSVLKVGDGIATVYGLE-------NVMSSELLEFPGEVFGmalnLEEDVVGAVLFGDDSGIKE 84
Cdd:COG1157 4 LARLLARLEELPPvrvsGRVTRVVGLLIEAVGPDasigelcEIETADGRPVLAEVVG----FRGDRVLLMPLGDLEGISP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 85 GDIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQR 164
Cdd:COG1157 80 GARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 165 eliIGdr---qtGKTS---------------IA------------IDTILnqkGKDviciyvaiGQKRStvaqlvsrlen 214
Cdd:COG1157 160 ---IGifagsgvGKSTllgmiarnteadvnvIAligergrevrefIEDDL---GEE--------GLARS----------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 215 ggamdytIVVSATASESAPLQYLAPYAGAAMGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLH 294
Cdd:COG1157 215 -------VVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 295 SRLLERAAKlsdeLGGGSMTAL------------PIIETqagdvsayiptnVISITDGQIYLQPELFYSGVRPAVDPGIS 362
Cdd:COG1157 288 PRLLERAGN----GGKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLAS 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494498175 363 VSRVGGSAQIKSMKKVSGTLKLAYSQYRELASF-----SQFGSDLDADtkRRLAQGERIVEVLKQGENAPLDVSD 432
Cdd:COG1157 352 ISRVMPDIVSPEHRALARRLRRLLARYEENEDLirigaYQPGSDPELD--EAIALIPAIEAFLRQGMDERVSFEE 424
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
14-426 |
1.08e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 165.24 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 14 QQIKNYDNKIELTDT-GSVLKVGDGIATVYGLE-------NVMSSELLEfpgEVFGMALNLEEDVVGAVLFGDDSGIKEG 85
Cdd:PRK08472 4 ESLKNKLQKFNLSPRfGSITKISPTIIEADGLNpsvgdivKIESSDNGK---ECLGMVVVIEKEQFGISPFSFIEGFKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 86 DIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRE 165
Cdd:PRK08472 81 DKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 166 LIIGDRQTGKTSIAIDTILNQKGKdvICIYVAIGQKRSTVAQLVSRleN-GGAMDYTIVVSATASESAPLQYLAPYAGAA 244
Cdd:PRK08472 161 GIFAGSGVGKSTLMGMIVKGCLAP--IKVVALIGERGREIPEFIEK--NlGGDLENTVIVVATSDDSPLMRKYGAFCAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 245 MGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlsdELGGGSMTALPIIETQAG 324
Cdd:PRK08472 237 VAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTVLVEGD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 325 DVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSRVGGSAQIKSMKKVSGTLKLAYSQYRE------LASFsQF 398
Cdd:PRK08472 314 DMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKEnevlirIGAY-QK 392
|
410 420
....*....|....*....|....*...
gi 494498175 399 GSDLDADTKrrLAQGERIVEVLKQGENA 426
Cdd:PRK08472 393 GNDKELDEA--ISKKEFMEQFLKQNPNE 418
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
64-442 |
9.56e-45 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 163.00 E-value: 9.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 64 LNLEEDVVG-----AVL--FGDDSGIKEGDIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGI 136
Cdd:PRK06936 57 LSLQAEVIGfaqhqALLtpLGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 137 MARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGKTSIAIDTIlnqKGKDV-ICIYVAIGQKRSTVAQLVSRLENG 215
Cdd:PRK06936 137 MSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLI---RSAEVdVTVLALIGERGREVREFIESDLGE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 216 GAMDYTIVVSATASESAPLQYLAPYAGAAMGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHS 295
Cdd:PRK06936 214 EGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALP 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 296 RLLERAAKlSDElggGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSRVGGSAQIKSM 375
Cdd:PRK06936 294 RLMERAGQ-SDK---GSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEH 369
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494498175 376 KKVSGTLKLAYSQYRELASFSQF-----GSDLDADTKrrLAQGERIVEVLKQGENAPLDVSDQVMIIFAVTN 442
Cdd:PRK06936 370 KTWAGRLRELLAKYEEVELLLQIgeyqkGQDKEADQA--IERIGAIRGFLRQGTHELSHFNETLNLLETLTQ 439
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-433 |
7.87e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 157.67 E-value: 7.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 29 GSVLKVGDGIATVyGLENVMSSELLEF-PGEVFGMALNLEEDVVGAVLFGDDSGIKEGDIVKRTGRIVEVPVGEAMIGRV 107
Cdd:PRK06820 31 GPIVEIGPTLLRA-SLPGVAQGELCRIePQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 108 VSPLGLPIDGkGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGKTSIaIDTILNQK 187
Cdd:PRK06820 110 LDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTL-LGMLCADS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 188 GKDVIcIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATaSESAPLQYL-APYAGAAMGEEFMYNGKHVLIIYDDLSKQ 266
Cdd:PRK06820 188 AADVM-VLALIGERGREVREFLEQVLTPEARARTVVVVAT-SDRPALERLkGLSTATTIAEYFRDRGKKVLLMADSLTRY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 267 AVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlSDElggGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLQP 346
Cdd:PRK06820 266 ARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGN-SDR---GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 347 ELFYSGVRPAVDPGISVSRVGGSAQIKSMKKVSGTLKLAYSQYRELASF-----SQFGSDLDADTKrrLAQGERIVEVLK 421
Cdd:PRK06820 342 RLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLvrvgeYQAGEDLQADEA--LQRYPAICAFLQ 419
|
410
....*....|....
gi 494498175 422 Q--GENAPLDVSDQ 433
Cdd:PRK06820 420 QdhSETAHLETTLE 433
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
28-399 |
5.56e-42 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 155.31 E-value: 5.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 28 TGSVLKVGDGIATVYGLENVMSS--ELLEFPGEVFGMAlnleeDVVG-----AVL--FGDDSGIKEGDIVKRTGRIVEVP 98
Cdd:PRK09099 25 TGKVVEVIGTLLRVSGLDVTLGElcELRQRDGTLLQRA-----EVVGfsrdvALLspFGELGGLSRGTRVIGLGRPLSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 99 VGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGKTsi 178
Cdd:PRK09099 100 VGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKS-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 179 aidTILNQKGKDVIC---IYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPYAGAAMGEEFMYNGKH 255
Cdd:PRK09099 178 ---TLMGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 256 VLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsdeLGG-GSMTALPIIETQAGDVSAYIPTNV 334
Cdd:PRK09099 255 VLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-----MGEtGSITALYTVLAEDESGSDPIAEEV 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494498175 335 ISITDGQIYLQPELFYSGVRPAVDPGISVSRVGGSAQIKSMKKVSGTLKLAYSQYRELASFSQFG 399
Cdd:PRK09099 330 RGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVG 394
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
62-435 |
4.13e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 150.24 E-value: 4.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 62 MALNLEEDVVGavlFGDD----------SGIKEGDIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVES 131
Cdd:PRK08972 55 MAGELEAEVVG---FDGDllylmpieelRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 132 PAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGKtSIAIDTILNQKGKDVICIYVaIGQKRSTVAQLVSR 211
Cdd:PRK08972 132 PPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGK-SVLLGMMTRGTTADVIVVGL-VGERGREVKEFIEE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 212 L--ENGGAMdyTIVVSATASESAPLQYLAPYAGAAMGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGD 289
Cdd:PRK08972 210 IlgEEGRAR--SVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPS 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 290 VFYLHSRLLERAAKLSDelGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSRVG-- 367
Cdd:PRK08972 288 VFAKLPALVERAGNGGP--GQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMpm 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494498175 368 --GSAQIKSMKKVSGTLKLaYSQYRELASFSQF--GSDLDADTKRRLAqgERIVEVLKQG--ENAPLDVSDQVM 435
Cdd:PRK08972 366 viSEEHLEAMRRVKQVYSL-YQQNRDLISIGAYkqGSDPRIDNAIRLQ--PAMNAFLQQTmkEAVPYDMSVNML 436
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
28-432 |
9.93e-40 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 148.95 E-value: 9.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 28 TGSVLKVGDGIATVYgLENVMSSELLEF-PGEVFGMALNLEEDVVGAVLFGDDSGIKEGDIVKRTGRIVEVPVGEAMIGR 106
Cdd:PRK07594 22 WGRIQDVSATLLNAW-LPGVFMGELCCIkPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 107 VVSPLGLPIDGKgPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGKTSIaIDTILNQ 186
Cdd:PRK07594 101 VIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLCNA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 187 KGKDViCIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPYAGAAMGEEFMYNGKHVLIIYDDLSKQ 266
Cdd:PRK07594 179 PDADS-NVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 267 AVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsdeLGG-GSMTALPIIETQAGDVSAYIPTNVISITDGQIYLQ 345
Cdd:PRK07594 258 ARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 346 PELFYSGVRPAVDPGISVSRVGGSAQIKSMKKVSGTLKLAYSQYRE---LASFSQFGSDLDADTKRRLAQGERIVEVLKQ 422
Cdd:PRK07594 333 RRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEvelLIRIGEYQRGVDTDTDKAIDTYPDICTFLRQ 412
|
410
....*....|
gi 494498175 423 GENAPLDVSD 432
Cdd:PRK07594 413 SKDEVCGPEL 422
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
94-370 |
1.21e-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: 141.98 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 94 IVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGD--- 170
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGsgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 171 ----------RQTGktsiaidtiLNQKGKDVICIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPY 240
Cdd:cd01135 81 phnelaaqiaRQAG---------VVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 241 AGAAMGEEFMY-NGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSDElgGGSMTAL 316
Cdd:cd01135 152 MALTTAEYLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQI 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 494498175 317 PIIETQAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSRVGGSA 370
Cdd:cd01135 227 PILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSG 280
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
82-391 |
5.32e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 141.40 E-value: 5.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 82 IKEGDIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGR 161
Cdd:PRK07721 78 IAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 162 GQRELIIGDRQTGKTSIaIDTILNQKGKDVICIYVaIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPYA 241
Cdd:PRK07721 158 GQRVGIFAGSGVGKSTL-MGMIARNTSADLNVIAL-IGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 242 GAAMGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDELggGSMTALPIIET 321
Cdd:PRK07721 236 ATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG--TNAS--GSITAFYTVLV 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 322 QAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSRVGGSAQIKSMKKVSGTLKLAYSQYRE 391
Cdd:PRK07721 312 DGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQN 381
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
29-428 |
1.69e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 140.13 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 29 GSVLKVGDGIATVYGL-ENVMSSELLEFP---GEVFGMALNLEEDVVGAVLFGDDSGIKEGDIVKRTGRIVEVPvGEAMI 104
Cdd:PRK06002 28 GTVSEVTASHYRVRGLsRFVRLGDFVAIRadgGTHLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGPLRIRP-DPSWK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 105 GRVVSPLGLPIDGKGPINT-NKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGKTSI----- 178
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLlamla 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 179 ---AIDTIlnqkgkdVICIyvaIGQKRSTVAQLvsrLEN--GGAMDYTIVVSATASESAPLQYLAPYAGAAMGEEFMYNG 253
Cdd:PRK06002 187 radAFDTV-------VIAL---VGERGREVREF---LEDtlADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 254 KHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelGGGSMTALPIIETQAGDVSAYIPTN 333
Cdd:PRK06002 254 ENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLVDGDDHNDPVADS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 334 VISITDGQIYLQPELFYSGVRPAVDPGISVSRVGGSAQIKSMKKVSGTLKLAYSQYRE-----LASFSQFGSDLDADtkR 408
Cdd:PRK06002 332 IRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdlrLIGGYRAGSDPDLD--Q 409
|
410 420
....*....|....*....|
gi 494498175 409 RLAQGERIVEVLKQGENAPL 428
Cdd:PRK06002 410 AVDLVPRIYEALRQSPGDPP 429
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
75-366 |
1.97e-36 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 139.74 E-value: 1.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 75 LFGDDSGIKEGDIVKRTGRIVEVPVGEAMIGRVVSPLG---LPIDGKGPINTN-KTRPVESPAPGIMARRSVYEPLQTGI 150
Cdd:PRK08149 60 LIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGkivERFDAPPTVGPIsEERVIDVAPPSYAERRPIREPLITGV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 151 KSIDSMIPIGRGQRELIIGDRQTGKTSIaIDTILNQKGKDVICIYVaIGQKRSTVAQLVSRLENGGAMDYTIVVSATASE 230
Cdd:PRK08149 140 RAIDGLLTCGVGQRMGIFASAGCGKTSL-MNMLIEHSEADVFVIGL-IGERGREVTEFVESLRASSRREKCVLVYATSDF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 231 SAPLQYLAPYAGAAMGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelgg 310
Cdd:PRK08149 218 SSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA---- 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 494498175 311 GSMTALPIIETQAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSRV 366
Cdd:PRK08149 294 GSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
41-462 |
2.64e-35 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 137.26 E-value: 2.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 41 VYGLENVMSSELLEF---PGEVF-GMALNLEEDVVGAVLFGDDSGIKEGDI-VKRTGRIVEVPVGEAMIGRVVSPLGLPI 115
Cdd:PRK04196 17 VEGVEGVAYGEIVEIelpNGEKRrGQVLEVSEDKAVVQVFEGTTGLDLKDTkVRFTGEPLKLPVSEDMLGRIFDGLGRPI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 116 DGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQR------------EL---IIgdRQTgktsiai 180
Cdd:PRK04196 97 DGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnELaaqIA--RQA------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 181 dTILNQKGKDVIcIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPYAGAAMGEEFMYN-GKHVLII 259
Cdd:PRK04196 168 -KVLGEEENFAV-VFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFEkGMHVLVI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 260 YDDLSKQAVAYREMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSDElgGGSMTALPIIETQAGDVSAYIPTNVIS 336
Cdd:PRK04196 246 LTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHPIPDLTGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 337 ITDGQIYLQPELFYSGVRPAVDPGISVSRVGGSAQIKSM-----KKVSGTLKLAYSQYRELASFSQF-G----SDLDadt 406
Cdd:PRK04196 321 ITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKtredhKDVANQLYAAYARGKDLRELAAIvGeealSERD--- 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494498175 407 KRRLAQGERI-VEVLKQGENAP------LDVSDQVMIIFavtngfvddiPVSELSRFESELFK 462
Cdd:PRK04196 398 RKYLKFADAFeREFVNQGFDENrsieetLDLGWELLSIL----------PESELKRIKDEYIE 450
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
96-431 |
3.62e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 136.17 E-value: 3.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 96 EVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGK 175
Cdd:PRK07196 89 ELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 176 tSIAIDTILNQKGKDVICIYVaIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPYAGAAMGEEFMYNGKH 255
Cdd:PRK07196 169 -SVLLGMITRYTQADVVVVGL-IGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHD 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 256 VLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsDELGGGSMTALPIIETQAGDVSAYIPTNVI 335
Cdd:PRK07196 247 VLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQDPIVDCAR 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 336 SITDGQIYLQPELFYSGVRPAVDPGISVSR----VGGSAQIKSMKKVSGTLKlAYSQYRELASFSQFGSDLDADTKRRLA 411
Cdd:PRK07196 324 AVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCYA-DYMAIKPLIPLGGYVAGADPMADQAVH 402
|
330 340
....*....|....*....|..
gi 494498175 412 QGERIVEVLKQ--GENAPLDVS 431
Cdd:PRK07196 403 YYPAITQFLRQevGHPALFSAS 424
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
65-439 |
3.37e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 134.09 E-value: 3.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 65 NLEEDVVGavlFGDD----------SGIKEGDIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAP 134
Cdd:PRK05688 64 QVEAEVMG---FSGDkvflmpvgsvAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 135 GIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGKtSIAIDTILNQKGKDVICIYVaIGQKRSTVAQLVSRLEN 214
Cdd:PRK05688 141 NPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK-SVLLGMMTRFTEADIIVVGL-IGERGREVKEFIEHILG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 215 GGAMDYTIVVSATAsESAPLQYLApyagAAM-----GEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGD 289
Cdd:PRK05688 219 EEGLKRSVVVASPA-DDAPLMRLR----AAMyctriAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPS 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 290 VFYLHSRLLERAAklSDELGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSRVGGS 369
Cdd:PRK05688 294 VFAKLPKLVERAG--NAEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQ 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494498175 370 AQIKSMKKVSGTLKLAYSQY---RELASFSQFGSDLDADTKRRLAQGERIVEVLKQG--ENAPLDVS-DQVMIIFA 439
Cdd:PRK05688 372 VVDPEHLRRAQRFKQLWSRYqqsRDLISVGAYVAGGDPETDLAIARFPHLVQFLRQGlrENVSLAQSrEQLAAIFA 447
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
27-93 |
1.21e-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: 118.71 E-value: 1.21e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494498175 27 DTGSVLKVGDGIATVYGLENVMSSELLEFPGEVFGMALNLEEDVVGAVLFGDDSGIKEGDIVKRTGR 93
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
50-423 |
2.47e-32 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 128.75 E-value: 2.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 50 SELLEFPGE-VFGMAL-NLEEDVVGAVLFGDDSGIKEgdivKRTGRivEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTR 127
Cdd:PRK07960 67 SEVVGFNGQrLFLMPLeEVEGILPGARVYARNISGEG----LQSGK--QLPLGPALLGRVLDGSGKPLDGLPAPDTGETG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 128 PVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGKtSIAIDTILNQKGKDVICIYVaIGQKRSTVAQ 207
Cdd:PRK07960 141 ALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK-SVLLGMMARYTQADVIVVGL-IGERGREVKD 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 208 LVSRLENGGAMDYTIVVSATASESaPLQYL--APYAgAAMGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREA 285
Cdd:PRK07960 219 FIENILGAEGRARSVVIAAPADVS-PLLRMqgAAYA-TRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKG 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 286 YPGDVFYLHSRLLERAAKLSDelGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSR 365
Cdd:PRK07960 297 YPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISR 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494498175 366 VGGS-------AQIKSMKKvsgtLKLAYSQYRELASFSQFGSDLDADTKRRLAQGERIVEVLKQG 423
Cdd:PRK07960 375 AMTAlideqhyARVRQFKQ----LLSSFQRNRDLVSVGAYAKGSDPMLDKAIALWPQLEAFLQQG 435
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
93-365 |
8.22e-29 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 118.47 E-value: 8.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 93 RIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQ 172
Cdd:PRK05922 88 RPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 173 TGKTSIaIDTIlnQKG-KDVICIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPYAGAAMGEEFMY 251
Cdd:PRK05922 168 SGKSSL-LSTI--AKGsKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 252 NGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlSDElggGSMTALPIIETQAGDVSAYIP 331
Cdd:PRK05922 245 QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-NDK---GSITALYAILHYPNHPDIFTD 320
|
250 260 270
....*....|....*....|....*....|....*.
gi 494498175 332 TnVISITDGQIYLQPE--LFYSgvrPAVDPGISVSR 365
Cdd:PRK05922 321 Y-LKSLLDGHFFLTPQgkALAS---PPIDILTSLSR 352
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
69-432 |
5.35e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 115.85 E-value: 5.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 69 DVVG-----AVL--FGDDSGIKEGDIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKT-RPVESPAPGIMARR 140
Cdd:PRK08927 57 EVVGfrgdrALLmpFGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVpYPLRAPPPPAHSRA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 141 SVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGKtSIAIDTILNQKGKDVICIYVaIGQKRSTVAQLVSRLENGGAMDY 220
Cdd:PRK08927 137 RVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGK-SVLLSMLARNADADVSVIGL-IGERGREVQEFLQDDLGPEGLAR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 221 TIVVSATASESAPLQYLAPYAGAAMGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLER 300
Cdd:PRK08927 215 SVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLER 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 301 AAklSDELGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSR-VGGSAQIKSMKKVS 379
Cdd:PRK08927 295 AG--PGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRtMPGCNDPEENPLVR 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 494498175 380 GTLKL--AYSQYRELASFSQF--GSDLDADTKRRLAqgERIVEVLKQGENAPLDVSD 432
Cdd:PRK08927 373 RARQLmaTYADMEELIRLGAYraGSDPEVDEAIRLN--PALEAFLRQGKDEATSLAE 427
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
63-392 |
8.42e-28 |
|
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: 115.59 E-value: 8.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 63 ALNLEEDVVGAVLFGDDSGIKEGDIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSV 142
Cdd:TIGR01039 44 AQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 143 YEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGKTSIAIDTILN-QKGKDVICIYVAIGQKRSTVAQLVSRLENGGAMDYT 221
Cdd:TIGR01039 124 VEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 222 IVVSATASESAPLQYLAPYAGAAMGEEFM-YNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLER 300
Cdd:TIGR01039 204 ALVYGQMNEPPGARMRVALTGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQER 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 301 AAKLSdelgGGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSR-----VGGSAQIKSM 375
Cdd:TIGR01039 284 ITSTK----TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRlldpsVVGEEHYDVA 359
|
330
....*....|....*..
gi 494498175 376 KKVSGTLKlaysQYREL 392
Cdd:TIGR01039 360 RGVQQILQ----RYKEL 372
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
91-394 |
1.59e-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: 112.12 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 91 TGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGD 170
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 171 -------------RQTGKTSIAIDTILNQKGKDVICIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYL 237
Cdd:TIGR01040 150 aglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERII 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 238 APYAGAAMGEEFMYN-GKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLsdELGGGSMTAL 316
Cdd:TIGR01040 230 TPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV--EGRNGSITQI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 317 PIIETQAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSRVGGSAQIKSMKK-----VSGTLKLAYSQYRE 391
Cdd:TIGR01040 308 PILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRkdhsdVSNQLYACYAIGKD 387
|
...
gi 494498175 392 LAS 394
Cdd:TIGR01040 388 VQA 390
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
64-415 |
8.93e-25 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 106.66 E-value: 8.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 64 LNLEEDVVGAVLFGDDSGIKEGDIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTR---PVESPAPGIMARR 140
Cdd:PRK02118 43 IRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGEPIEiggPSVNPVKRIVPRE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 141 SVyeplQTGIKSIDSMIPIGRGQRELIIGDrqTGKTSIAI-DTILNQKGKDVIcIYVAIGQKRSTVAQLVSRLENGGAMD 219
Cdd:PRK02118 123 MI----RTGIPMIDVFNTLVESQKIPIFSV--SGEPYNALlARIALQAEADII-ILGGMGLTFDDYLFFKDTFENAGALD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 220 YTIVVSATASESAPLQYLAPYAGAAMGEEFMYNG-KHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDvfyLHSRLL 298
Cdd:PRK02118 196 RTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGS---LYSDLA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 299 ERAAKLSDELGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLQpelfysgvRPAVDPGISVSR----VGGSAQIKS 374
Cdd:PRK02118 273 SRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLR--------RGRIDPFGSLSRlkqlVIGKKTRED 344
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 494498175 375 MKKVSGTLKLAYSQYRELASFSQFGSDLDADTKRRLAQGER 415
Cdd:PRK02118 345 HGDLMNAMIRLYADSREAKEKMAMGFKLSNWDEKLLKFSEL 385
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
85-400 |
1.92e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 102.75 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 85 GDIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQR 164
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 165 ELIIGDRQTGKTSIAidTILNQKGKDVICIYVAIGQKRSTVAQLVSRLENGGAMDYTIVVSATASESAPLQYLAPYAGAA 244
Cdd:PRK06793 159 IGIFAGSGVGKSTLL--GMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATS 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 245 MGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPgreaYPGDVFYLHS---RLLERAAKLSDelggGSMTALPIIET 321
Cdd:PRK06793 237 IAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK----GSITGIYTVLV 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494498175 322 QAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSRVGGSAQIKSMKKVSGTLKLAYSQYRELASFSQFGS 400
Cdd:PRK06793 309 DGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGT 387
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-366 |
2.43e-20 |
|
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: 90.74 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 96 EVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGK 175
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 176 TSIAIDTILN-QKGKDVICIYVAIGQKRSTVAQLV-----SRLENGGAMDYTIVVSATASESAPLQYLAPYAGAAMGEEF 249
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGERTREGNDLYhemkeSGVINLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 250 M-YNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSMTALPIIETQAGDVSA 328
Cdd:cd01133 161 RdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKK----GSITSVQAVYVPADDLTD 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 494498175 329 YIPTNVISITDGQIYLQPELFYSGVRPAVDPGISVSRV 366
Cdd:cd01133 237 PAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
58-162 |
2.39e-19 |
|
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: 90.53 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 58 EVfgmALNLEEDVVGAVLFGDDSGIKEGDIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIM 137
Cdd:COG0055 45 EV---AQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFE 121
|
90 100
....*....|....*....|....*
gi 494498175 138 ARRSVYEPLQTGIKSIDSMIPIGRG 162
Cdd:COG0055 122 EQSTKTEILETGIKVIDLLAPYAKG 146
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
28-92 |
9.48e-18 |
|
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: 77.20 E-value: 9.48e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494498175 28 TGSVLKVGDGIATVYGLENVMSSELLEFPGEVFGMALNLEEDVVGAVLFGDDSGIKEGDIVKRTG 92
Cdd:pfam02874 5 IGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
66-392 |
1.27e-14 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 76.23 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 66 LEEDVVGAVLFGDDSGIKEGDIVKRTGRIVEVPVGEAMIGRVVSPLGLPIDGKGPINTNKTRPVESPAPGIM---ARRSV 142
Cdd:CHL00060 65 LGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTKLSI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 143 YEplqTGIKSIDSMIPIGRGQRELIIGDRQTGKTSIAIDTILN-QKGKDVICIYVAIGQ------------KRSTVAQLV 209
Cdd:CHL00060 145 FE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGErtregndlymemKESGVINEQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 210 SRLENGGAMDY---------TIVVSATASesaplqylapyagaAMGEEFM-YNGKHVLIIYDDLSKQAVAYREMSLLLRR 279
Cdd:CHL00060 222 NIAESKVALVYgqmneppgaRMRVGLTAL--------------TMAEYFRdVNKQDVLLFIDNIFRFVQAGSEVSALLGR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 280 PPGREAYPGDVFYLHSRLLERAAKLSDelggGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLQPELFYSGVRPAVDP 359
Cdd:CHL00060 288 MPSAVGYQPTLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDP 363
|
330 340 350
....*....|....*....|....*....|....*...
gi 494498175 360 GISVS-----RVGGSAQIKSMKKVSGTLKlaysQYREL 392
Cdd:CHL00060 364 LDSTStmlqpRIVGEEHYETAQRVKQTLQ----RYKEL 397
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
375-442 |
1.63e-13 |
|
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: 65.54 E-value: 1.63e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 375 MKKVSGTLKLAYSQYRELASFSQFGSD--LDADTKRRLAQGERIVEVLKQGENAPLDVSDQVMIIFAVTN 442
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
128-365 |
7.11e-13 |
|
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: 69.14 E-value: 7.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 128 PVESPAPgIMARRSVYEPLQTGIKSIDSMIPIGRGQRELIIGDRQTGKTSIaIDTILNQKGKDVIcIYVAIGQKRSTVA- 206
Cdd:cd01134 43 PVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVI-SQSLSKWSNSDVV-IYVGCGERGNEMAe 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 207 ------QLVSRLENGGAMDYTIVVSATASESAPLQYLAPYAGAAMGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRP 280
Cdd:cd01134 120 vleefpELKDPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEM 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 281 PGREAYPGdvfYLHSRL---LERAAK---LSDELGGGSMTALPIIETQAGDVSAYIPTNVISITdgQIY--LQPELFYSG 352
Cdd:cd01134 200 PAEEGYPA---YLGARLaefYERAGRvrcLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRR 274
|
250
....*....|...
gi 494498175 353 VRPAVDPGISVSR 365
Cdd:cd01134 275 HFPSINWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
144-301 |
2.54e-07 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 53.25 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 144 EPLQTGIKSIDSMIPIGRGQRELIIGDRQTGKT----SIAidtilnqKGKDV-ICIYVAIGQKRSTVAQLVS---RLE-- 213
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTvtqhQLA-------KWADAdIVIYVGCGERGNEMTEVLEefpELIdp 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 214 -NGGA-MDYTIVVSAT------ASESAPlqylapYAGAAMGEEFMYNGKHVLIIYDDLSKQAVAYREMSLLLRRPPGREA 285
Cdd:PRK04192 282 kTGRPlMERTVLIANTsnmpvaAREASI------YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEG 355
|
170
....*....|....*....
gi 494498175 286 YPGdvfYLHSRL---LERA 301
Cdd:PRK04192 356 YPA---YLASRLaefYERA 371
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
192-337 |
2.21e-06 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 50.41 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494498175 192 ICIYVAIGQKRSTVAQLVSRLE-----NGGA--MDYTIVVSATASESAPLQYLAPYAGAAMGEEFMYNGKHVLIIYDDLS 264
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPklkdpKTGKplMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTS 763
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494498175 265 KQAVAYREMSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKLSDELGGGSMTALPIIETQAGDVSAYIPTNVISI 337
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRV 839
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
28-93 |
5.88e-03 |
|
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: 35.75 E-value: 5.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494498175 28 TGSVLKVGDGIATVYGLENVMSSELLEF-----PGEVFGMA--LNLEEDVVGAVLFGDDSGIKEGDIVKRTGR 93
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIergdgNNETVLKAevIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| |
