|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-495 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 1038.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 1 MAINAQEISALIKKQIEDFQPNFDVTETGIVTYIGDGIARARGLDNAMSGELLEFSNGAYGMAQNLESNDVGIIILGDFS 80
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 81 EIREGDVVKRTGKIMEVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIG 160
Cdd:PRK09281 81 DIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 161 RGQRELIIGDRQTGKTSVAIDAILNQKGQDMICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPY 240
Cdd:PRK09281 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 241 AGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDALGGGSITALPFIE 320
Cdd:PRK09281 241 AGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 321 TQAGDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVSRVGGAAQIKAMKRVAGTLRLDLASYRELEAFTQFGS 400
Cdd:PRK09281 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 401 DLDAATQAKLNRGRRTVEVLKQPLHKPLPVEKQVVILYALTHGFLDDVPVNDILAFEEALYDYFDAHYDNLFETIRTTKD 480
Cdd:PRK09281 401 DLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKD 480
|
490
....*....|....*..
gi 446919357 481 LPEEAE--LDAAIQAFK 495
Cdd:PRK09281 481 LSDEIEakLKAAIEEFK 497
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-497 |
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: 1033.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 1 MAINAQEISALIKKQIEDFQPNFDVTETGIVTYIGDGIARARGLDNAMSGELLEFSNGAYGMAQNLESNDVGIIILGDFS 80
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 81 EIREGDVVKRTGKIMEVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIG 160
Cdd:COG0056 81 GIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 161 RGQRELIIGDRQTGKTSVAIDAILNQKGQDMICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPY 240
Cdd:COG0056 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 241 AGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDALGGGSITALPFIE 320
Cdd:COG0056 241 AGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 321 TQAGDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVSRVGGAAQIKAMKRVAGTLRLDLASYRELEAFTQFGS 400
Cdd:COG0056 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 401 DLDAATQAKLNRGRRTVEVLKQPLHKPLPVEKQVVILYALTHGFLDDVPVNDILAFEEALYDYFDAHYDNLFETIRTTKD 480
Cdd:COG0056 401 DLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGK 480
|
490
....*....|....*....
gi 446919357 481 LPEE--AELDAAIQAFKDQ 497
Cdd:COG0056 481 LDDEieEKLKAAIEEFKKT 499
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
2-495 |
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: 872.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 2 AINAQEISALIKKQIEDFQPNFDVTETGIVTYIGDGIARARGLDNAMSGELLEFSNGAYGMAQNLESNDVGIIILGDFSE 81
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 82 IREGDVVKRTGKIMEVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGR 161
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 162 GQRELIIGDRQTGKTSVAIDAILNQKGQDMICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPYA 241
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 242 GVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDALGGGSITALPFIET 321
Cdd:TIGR00962 241 GCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 322 QAGDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVSRVGGAAQIKAMKRVAGTLRLDLASYRELEAFTQFGSD 401
Cdd:TIGR00962 321 QAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 402 LDAATQAKLNRGRRTVEVLKQPLHKPLPVEKQVVILYALTHGFLDDVPVNDILAFEEALYDYFDAHYDNLFETIRTTKDL 481
Cdd:TIGR00962 401 LDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKL 480
|
490
....*....|....*.
gi 446919357 482 PEEAE--LDAAIQAFK 495
Cdd:TIGR00962 481 TEELEakLKEALKNFK 496
|
|
| 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: 783.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 1 MAINAQEISALIKKQIEDFQPNFDVTETGIVTYIGDGIARARGLDNAMSGELLEFSNGAYGMAQNLESNDVGIIILGDFS 80
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 81 EIREGDVVKRTGKIMEVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIG 160
Cdd:PRK13343 81 DILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 161 RGQRELIIGDRQTGKTSVAIDAILNQKGQDMICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPY 240
Cdd:PRK13343 161 RGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 241 AGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDALGGGSITALPFIE 320
Cdd:PRK13343 241 AGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 321 TQAGDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVSRVGGAAQIKAMKRVAGTLRLDLASYRELEAFTQFGS 400
Cdd:PRK13343 321 TLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 401 DLDAATQAKLNRGRRTVEVLKQPLHKPLPVEKQVVILYALTHGFLDDVPVNDILAFEEALYDYFDAHYDNLFETIRTTKD 480
Cdd:PRK13343 401 LLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRE 480
|
490
....*....|....*....
gi 446919357 481 LPEE--AELDAAIQAFKDQ 497
Cdd:PRK13343 481 LDEAwlAALEEILREAGER 499
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
25-496 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 756.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 25 VTETGIVTYIGDGIARARGLDNAMSGELLEFSNGAYGMAQNLESNDVGIIILGDFSEIREGDVVKRTGKIMEVPVGEAMI 104
Cdd:CHL00059 4 IVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 105 GRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTSVAIDAIL 184
Cdd:CHL00059 84 GRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 185 NQKGQDMICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPYAGVAMAEEFMYNGKHVLIVYDDLS 264
Cdd:CHL00059 164 NQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 265 KQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDALGGGSITALPFIETQAGDISAYIATNVISITDGQIFL 344
Cdd:CHL00059 244 KQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 345 QENLFNSGIRPAIDAGSSVSRVGGAAQIKAMKRVAGTLRLDLASYRELEAFTQFGSDLDAATQAKLNRGRRTVEVLKQPL 424
Cdd:CHL00059 324 SADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQ 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446919357 425 HKPLPVEKQVVILYALTHGFLDDVPVNDILAFEEALYDYFDAHYDNLFETIRTTKDLPEEAE--LDAAIQAFKD 496
Cdd:CHL00059 404 SAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEalLKEAIQEQLE 477
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
6-484 |
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: 592.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 6 QEISALIKKQIEDFQPNFDVTETGIVTYIGDGIARARGLDNAMSGELLEFSNGAYGMAQNLESNDVGIIILGDFSEIREG 85
Cdd:TIGR03324 6 DKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 86 DVVKRTGKIMEVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRE 165
Cdd:TIGR03324 86 DEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 166 LIIGDRQTGKTSVAIDAILNQKGQDMICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPYAGVAM 245
Cdd:TIGR03324 166 LILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 246 AEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDALGGGSITALPFIETQAGD 325
Cdd:TIGR03324 246 GEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 326 ISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVSRVGGAAQIKAMKRVAGTLRLDLASYRELEAFTQFGSDLDAA 405
Cdd:TIGR03324 326 ISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDEN 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446919357 406 TQAKLNRGRRTVEVLKQPLHKPLPVEKQVVILYALTHGFLDDVPVNDILAFEEALYDYFDAHYDNLFETIRTTKDLPEE 484
Cdd:TIGR03324 406 TRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSDE 484
|
|
| 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: 562.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 94 IMEVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQT 173
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 174 GKTSVAIDAILNQKGQDMICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPYAGVAMAEEFMYNG 253
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 254 KHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDALGGGSITALPFIETQAGDISAYIATN 333
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 446919357 334 VISITDGQIFLQENLFNSGIRPAIDAGSSVSRVG 367
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
59-469 |
1.02e-121 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 368.21 E-value: 1.02e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 59 AYGMAQNLESND-VGIIILGDFSEIREGDVVKRTGKIMEVPVGEAMIGRVVNPLGQPVD--------GLGEIETTATRpV 129
Cdd:PTZ00185 78 AAGLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrsrALLESEQTLGK-V 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 130 ETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTSVAIDAILNQ--------KGQDMICIYVAIGQK 201
Cdd:PTZ00185 157 DAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQR 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 202 ESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPYAGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPP 281
Cdd:PTZ00185 237 CSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 282 GREAYPGDVFYLHSRLLERSAKVSDALGGGSITALPFIETQAGDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGS 361
Cdd:PTZ00185 317 GREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGL 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 362 SVSRVGGAAQIKAMKRVAGTLRLDLASYRELEAFTQFGSDLDAatqAKLNRGRRTVEVLKQplHKPLPVEKQVVILYALT 441
Cdd:PTZ00185 397 SVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQT---VPMIRGARFVALFNQ--KNPSFFMNALVSLYACL 471
|
410 420
....*....|....*....|....*...
gi 446919357 442 HGFLDDVPVNDIlafeeALYDYFDAHYD 469
Cdd:PTZ00185 472 NGYLDDVKVNYA-----KLYEYLLVNKD 494
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
149-364 |
2.68e-109 |
|
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: 323.15 E-value: 2.68e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 149 GLKAIDALVPIGRGQRELIIGDRQTGKTSVAiDAILNQKGQDmICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASA 228
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD-VVVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 229 SQPSPLLFIAPYAGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDal 308
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKG-- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446919357 309 GGGSITALPFIETQAGDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVS 364
Cdd:pfam00006 157 KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
97-366 |
3.05e-102 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 307.46 E-value: 3.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 97 VPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKT 176
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 177 SVAIDAILNQKGQD-MICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPYAGVAMAEEFMYNGKH 255
Cdd:cd19476 82 VLAMQLARNQAKAHaGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 256 VLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDalGGGSITALPFIETQAGDISAYIATNVI 335
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNTF 239
|
250 260 270
....*....|....*....|....*....|.
gi 446919357 336 SITDGQIFLQENLFNSGIRPAIDAGSSVSRV 366
Cdd:cd19476 240 AILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
133-484 |
7.59e-102 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 314.60 E-value: 7.59e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 133 APGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTSVAIDAILNQKGQDMICIYVAIGQKESTVRTQVETL 212
Cdd:PRK07165 114 AHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 213 RKYGALDYTIVVTASASQPSPlLFIAPYAGVAMAEEFMYNgKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFY 292
Cdd:PRK07165 194 KEHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAENISYN-DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFF 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 293 LHSRLLERSAKVsdaLGGGSITALPFIETQAGDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVSRVGGAAQI 372
Cdd:PRK07165 272 AHSKLLERAGKF---KNRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQS 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 373 KAMKRVAGTLRLDLASYRELEAFTQFGSDLDAATQAKLNRGRRTVEVLKQPLHKPLPVEKQVVILYALTHGFLDDVP-VN 451
Cdd:PRK07165 349 KTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKGKMIEKMFNQKGFSLYSYRFVLLISKLISWGLLKDVKdEQ 428
|
330 340 350
....*....|....*....|....*....|...
gi 446919357 452 DILAFEEALYDYfDAHYDNLFETIRTTKDLPEE 484
Cdd:PRK07165 429 KALDFIDYLIEN-DPDAKKIFNKIKNNEDVDDE 460
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
375-497 |
2.44e-66 |
|
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: 209.53 E-value: 2.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 375 MKRVAGTLRLDLASYRELEAFTQFGSDLDAATQAKLNRGRRTVEVLKQPLHKPLPVEKQVVILYALTHGFLDDVPVNDIL 454
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446919357 455 AFEEALYDYFDAHYDNLFETIRTTKDLPEEAE--LDAAIQAFKDQ 497
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEekLKEAIEEFKKS 125
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
371-494 |
5.88e-66 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 208.84 E-value: 5.88e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 371 QIKAMKRVAGTLRLDLASYRELEAFTQFGSDLDAATQAKLNRGRRTVEVLKQPLHKPLPVEKQVVILYALTHGFLDDVPV 450
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446919357 451 NDILAFEEALYDYFDAHYDNLFETIRTTKDLPEE--AELDAAIQAF 494
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDEleEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
96-366 |
1.32e-53 |
|
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: 181.60 E-value: 1.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 96 EVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 176 tSVAIDAILNQKGQDMICIyVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPYAGVAMAEEFMYNGKH 255
Cdd:cd01136 81 -STLLGMIARNTDADVNVI-ALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 256 VLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKvsdaLGGGSITALPFIETQAGDISAYIATNVI 335
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN----GEKGSITAFYTVLVEGDDFNDPIADEVR 234
|
250 260 270
....*....|....*....|....*....|.
gi 446919357 336 SITDGQIFLQENLFNSGIRPAIDAGSSVSRV 366
Cdd:cd01136 235 SILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
74-443 |
7.68e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 176.45 E-value: 7.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 74 IILGDFSEIRE---GDVVKRTGKIMEVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGL 150
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 151 KAIDALVPIGRGQRELIIGDRQTGKtSVAIDAILNQKGQDMICIYVaIGQKESTVRTQVEtlRKYGA--LDYTIVVTASA 228
Cdd:PRK07721 147 RAIDSLLTVGKGQRVGIFAGSGVGK-STLMGMIARNTSADLNVIAL-IGERGREVREFIE--RDLGPegLKRSIVVVATS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 229 SQPSPLLFIAPYAGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAkvsdAL 308
Cdd:PRK07721 223 DQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG----TN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 309 GGGSITALPFIETQAGDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVSRVGGAAQIKAMKRVAGTLRLDLAS 388
Cdd:PRK07721 299 ASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLST 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446919357 389 YRELEAFTQFGS-------DLDAATQAKlnrgRRTVEVLKQPLHKPLPVEKQVVILYALTHG 443
Cdd:PRK07721 379 YQNSEDLINIGAykrgssrEIDEAIQFY----PQIISFLKQGTDEKATFEESIQALLSLFGK 436
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
12-405 |
1.84e-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: 1.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 12 IKKQIEDFQPnfdVTETGIVTYIGDGIARARGLDNAMsGELLEF--SNGAYGMAQ--NLESNDVGIIILGDFSEIREGDV 87
Cdd:COG1157 7 LLARLEELPP---VRVSGRVTRVVGLLIEAVGPDASI-GELCEIetADGRPVLAEvvGFRGDRVLLMPLGDLEGISPGAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 88 VKRTGKIMEVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQReli 167
Cdd:COG1157 83 VVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 168 IGdr---qtGKTSvaidaILNqkgqdMIC-------IYVA-IGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLF 236
Cdd:COG1157 160 IGifagsgvGKST-----LLG-----MIArnteadvNVIAlIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 237 IAPYAGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVsdalGGGSITAL 316
Cdd:COG1157 230 RAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNG----GKGSITAF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 317 PFIETQAGDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVSRVggAAQI--KAMKRVAGTLRLDLASYRELE- 393
Cdd:COG1157 306 YTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRV--MPDIvsPEHRALARRLRRLLARYEENEd 383
|
410
....*....|....*....
gi 446919357 394 -----AFTQfGSD--LDAA 405
Cdd:COG1157 384 lirigAYQP-GSDpeLDEA 401
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
76-441 |
2.27e-49 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 175.33 E-value: 2.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 76 LGDFSEIREGDVVKRTGKIMEVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDA 155
Cdd:PRK06936 76 LGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 156 LVPIGRGQRELIIGDRQTGKTSVAIDAIlnqKGQDM-ICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPL 234
Cdd:PRK06936 156 LLTCGEGQRMGIFAAAGGGKSTLLASLI---RSAEVdVTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSME 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 235 LFIAPYAGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERsAKVSDAlggGSIT 314
Cdd:PRK06936 233 RAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMER-AGQSDK---GSIT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 315 ALPFIETQAGDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVSRVGGAAQIKAMKRVAGTLRLDLASYRELEA 394
Cdd:PRK06936 309 ALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVEL 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446919357 395 FTQFGS---DLDAATQAKLNRGRRTVEVLKQPLHKPLPVEKQVVILYALT 441
Cdd:PRK06936 389 LLQIGEyqkGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETLT 438
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-440 |
5.84e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 171.54 E-value: 5.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 29 GIVTYIGDGIARArGLDNAMSGELLEFSNgaygmaQNLESNDVGI----IILGDFSE---IREGDVVKRTGKIMEVPVGE 101
Cdd:PRK06820 31 GPIVEIGPTLLRA-SLPGVAQGELCRIEP------QGMLAEVVSIeqemALLSPFASsdgLRCGQWVTPLGHMHQVQVGA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 102 AMIGRVVNPLGQPVDGlGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKtSVAID 181
Cdd:PRK06820 104 DLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGK-STLLG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 182 AILNQKGQDMIcIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPYAGVAMAEEFMYNGKHVLIVYD 261
Cdd:PRK06820 182 MLCADSAADVM-VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMAD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 262 DLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDalggGSITALPFIETQAGDISAYIATNVISITDGQ 341
Cdd:PRK06820 261 SLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDR----GSITAFYTVLVEGDDMNEPVADEVRSLLDGH 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 342 IFLQENLFNSGIRPAIDAGSSVSRVGGAAQIKAMKRVAGTLRLDLASYRELEAFTQFG---SDLDAATQAKLNRGRRTVE 418
Cdd:PRK06820 337 IVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGeyqAGEDLQADEALQRYPAICA 416
|
410 420
....*....|....*....|..
gi 446919357 419 VLKQPLHKPLPVEKQVVILYAL 440
Cdd:PRK06820 417 FLQQDHSETAHLETTLEHLAQV 438
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
25-441 |
4.98e-46 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 166.48 E-value: 4.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 25 VTETGIVTYIGDGIARARGLDNAMsGELLEFSNGAYGMAQNLE----SNDVGIII-LGDFSEIREGDVVKRTGKIMEVPV 99
Cdd:PRK09099 22 VRRTGKVVEVIGTLLRVSGLDVTL-GELCELRQRDGTLLQRAEvvgfSRDVALLSpFGELGGLSRGTRVIGLGRPLSVPV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 100 GEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTSVA 179
Cdd:PRK09099 101 GPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 180 idAILNQKGQDMICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPYAGVAMAEEFMYNGKHVLIV 259
Cdd:PRK09099 181 --GMFARGTQCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 260 YDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERsAKVSDAlggGSITALPFIETQAGDISAYIATNVISITD 339
Cdd:PRK09099 259 MDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLER-AGMGET---GSITALYTVLAEDESGSDPIAEEVRGILD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 340 GQIFLQENLFNSGIRPAIDAGSSVSRVGGAAQIKAMKRVAGTLRLDLASYRELEAFTQFG---SDLDAATQAKLNRGRRT 416
Cdd:PRK09099 335 GHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVGeyrAGSDPVADEAIAKIDAI 414
|
410 420
....*....|....*....|....*
gi 446919357 417 VEVLKQPLHKPLPVEKQVVILYALT 441
Cdd:PRK09099 415 RDFLSQRTDEYSDPDATLAALAELS 439
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
87-399 |
6.05e-43 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 157.46 E-value: 6.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 87 VVKRTGKIMEVPVGEAMIGRVVNPLGQPVDGLGEIETTAT----RPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRG 162
Cdd:PRK08149 72 VLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVGPiseeRVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 163 QRELIIGDRQTGKTSVaIDAILNQKGQDmicIYVA--IGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPY 240
Cdd:PRK08149 152 QRMGIFASAGCGKTSL-MNMLIEHSEAD---VFVIglIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 241 AGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAkvsdALGGGSITALPFIE 320
Cdd:PRK08149 228 VATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPG----ATLAGSITAFYTVL 303
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446919357 321 TQAGDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVSRVGGAAQIKAMKRVAGTLRLDLASYRELEAFTQFG 399
Cdd:PRK08149 304 LESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLG 382
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
29-409 |
4.21e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 155.61 E-value: 4.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 29 GIVTYIGDGIARARGLDNAMSG----ELLEFSNGAYGMAQNLESNDVGIIILGDFSEIREGDVVKRTGKIMEVPVGEAMI 104
Cdd:PRK08472 20 GSITKISPTIIEADGLNPSVGDivkiESSDNGKECLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 105 GRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTSVAIDAIL 184
Cdd:PRK08472 100 GRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 185 NQKGQdmICIYVAIGQKEstvRTQVETLRKY--GALDYTIVVTASaSQPSPLLF-IAPYAGVAMAEEFMYNGKHVLIVYD 261
Cdd:PRK08472 180 GCLAP--IKVVALIGERG---REIPEFIEKNlgGDLENTVIVVAT-SDDSPLMRkYGAFCAMSVAEYFKNQGLDVLFIMD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 262 DLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSdalGGGSITALPFIETQAGDISAYIATNVISITDGQ 341
Cdd:PRK08472 254 SVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEE---GKGSITAFFTVLVEGDDMSDPIADQSRSILDGH 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446919357 342 IFLQENLFNSGIRPAIDAGSSVSRVGGAAQIKAMKRVAGTLRLDLASYRELEAFTQFGS-------DLDAATQAK 409
Cdd:PRK08472 331 IVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAyqkgndkELDEAISKK 405
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
28-399 |
1.39e-41 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 153.96 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 28 TGIVTYIGDGIARARgLDNAMSGELLEFSNGAyGMAQ--NLESNDVGIIILGDFSEIREGDVVKRTGKIMEVPVGEAMIG 105
Cdd:PRK07594 22 WGRIQDVSATLLNAW-LPGVFMGELCCIKPGE-ELAEvvGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 106 RVVNPLGQPVDGLgEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTSVaIDAILN 185
Cdd:PRK07594 100 RVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLCN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 186 QKGQDmICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPYAGVAMAEEFMYNGKHVLIVYDDLSK 265
Cdd:PRK07594 178 APDAD-SNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 266 QAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDalggGSITALPFIETQAGDISAYIATNVISITDGQIFLQ 345
Cdd:PRK07594 257 YARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEK----GSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLS 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 446919357 346 ENLFNSGIRPAIDAGSSVSRVGGAAQIKAMKRVAGTLRLDLASYRELEAFTQFG 399
Cdd:PRK07594 333 RRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIG 386
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
94-380 |
8.79e-40 |
|
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: 145.06 E-value: 8.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 94 IMEVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDrqT 173
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSG--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 174 G------KTSVAIDAILNQKGQDMICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPYAGVAMAE 247
Cdd:cd01135 79 GlphnelAAQIARQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 248 EFMY-NGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERSAKVSDAlgGGSITALPFIETQA 323
Cdd:cd01135 159 YLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTMPN 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446919357 324 GDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVSRVggaaqikaMKRVAG 380
Cdd:cd01135 234 DDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRL--------MKSGIG 282
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
96-397 |
9.19e-39 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 146.85 E-value: 9.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 96 EVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 176 tSVAIDAILNQKGQDMICIYVaIGQKESTVRTQVETLRKYGALDYTIVVTASASQpSPLLFI--APYAgVAMAEEFMYNG 253
Cdd:PRK07960 189 -SVLLGMMARYTQADVIVVGL-IGERGREVKDFIENILGAEGRARSVVIAAPADV-SPLLRMqgAAYA-TRIAEDFRDRG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 254 KHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDalGGGSITALPFIETQAGDISAYIATN 333
Cdd:PRK07960 265 QHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGDDQQDPIADS 342
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446919357 334 VISITDGQIFLQENLFNSGIRPAIDAGSSVSRvggaaqikAMkrvagTLRLDLASYRELEAFTQ 397
Cdd:PRK07960 343 ARAILDGHIVLSRRLAEAGHYPAIDIEASISR--------AM-----TALIDEQHYARVRQFKQ 393
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
97-440 |
1.84e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 145.61 E-value: 1.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 97 VPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKt 176
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGK- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 177 SVAIDAILNQKGQDMICIYVaIGQKESTVRTQVETLRKYGALDYTIVVTASASQpSPLLFI-APYAGVAMAEEFMYNGKH 255
Cdd:PRK08972 176 SVLLGMMTRGTTADVIVVGL-VGERGREVKEFIEEILGEEGRARSVVVAAPADT-SPLMRLkGCETATTIAEYFRDQGLN 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 256 VLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDalGGGSITALPFIETQAGDISAYIATNVI 335
Cdd:PRK08972 254 VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVLTEGDDLQDPIADASR 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 336 SITDGQIFLQENLFNSGIRPAIDAGSSVSRVG----GAAQIKAMKRVAGTLRL-----DLASyreLEAFTQfGSD--LDA 404
Cdd:PRK08972 332 AILDGHIVLSRELADSGHYPAIDIEASISRVMpmviSEEHLEAMRRVKQVYSLyqqnrDLIS---IGAYKQ-GSDprIDN 407
|
330 340 350
....*....|....*....|....*....|....*...
gi 446919357 405 A--TQAKLNrgrrtvEVLKQPLHKPLPVEKQVVILYAL 440
Cdd:PRK08972 408 AirLQPAMN------AFLQQTMKEAVPYDMSVNMLKQL 439
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
95-366 |
1.62e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 134.86 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 95 MEVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTG 174
Cdd:PRK05688 101 GRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 175 KtSVAIDAILNQKGQDMICIYVaIGQKESTVRTQVETLRKYGALDYTIVVtASASQPSPL--LFIAPYAgVAMAEEFMYN 252
Cdd:PRK05688 181 K-SVLLGMMTRFTEADIIVVGL-IGERGREVKEFIEHILGEEGLKRSVVV-ASPADDAPLmrLRAAMYC-TRIAEYFRDK 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 253 GKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAkvSDALGGGSITALPFIETQAGDISAYIAT 332
Cdd:PRK05688 257 GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEGDDQQDPIAD 334
|
250 260 270
....*....|....*....|....*....|....
gi 446919357 333 NVISITDGQIFLQENLFNSGIRPAIDAGSSVSRV 366
Cdd:PRK05688 335 SARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV 368
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
20-365 |
1.19e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 132.43 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 20 QPNFDVTETGIVTYIGDGIARARGL-DNAMSGELLEFS--NGAY-GMAQNLESNDVGIIILGDFSEIREGDVVKRTGKiM 95
Cdd:PRK06002 19 APEPLVRIGGTVSEVTASHYRVRGLsRFVRLGDFVAIRadGGTHlGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGP-L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 96 EVPVGEAMIGRVVNPLGQPVDGLGEIET-TATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTG 174
Cdd:PRK06002 98 RIRPDPSWKGRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 175 KTSVAidAILNQ-KGQDMICIYVaIGQKESTVRTQVE-TLRkyGALDYTIVVTASaSQPSPLLF-IAPYAGVAMAEEFMY 251
Cdd:PRK06002 178 KSTLL--AMLARaDAFDTVVIAL-VGERGREVREFLEdTLA--DNLKKAVAVVAT-SDESPMMRrLAPLTATAIAEYFRD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 252 NGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDalGGGSITALPFIETQAGDISAYIA 331
Cdd:PRK06002 252 RGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLVDGDDHNDPVA 329
|
330 340 350
....*....|....*....|....*....|....
gi 446919357 332 TNVISITDGQIFLQENLFNSGIRPAIDAGSSVSR 365
Cdd:PRK06002 330 DSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISR 363
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
96-440 |
2.16e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 128.47 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 96 EVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:PRK07196 89 ELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 176 tSVAIDAILNQKGQDMICIYVaIGQKESTVRTQVETLRKYGALDYTIVVTASASQpSPLLFI-APYAGVAMAEEFMYNGK 254
Cdd:PRK07196 169 -SVLLGMITRYTQADVVVVGL-IGERGREVKEFIEHSLQAAGMAKSVVVAAPADE-SPLMRIkATELCHAIATYYRDKGH 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 255 HVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAkvsDALGGGSITALPFIETQAGDISAYIATNV 334
Cdd:PRK07196 246 DVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQDPIVDCA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 335 ISITDGQIFLQENLFNSGIRPAIDAGSSVSR----VGGAAQIKAMKRVAGTLRlDLASYRELEAFTQFGSDLDAATQAKL 410
Cdd:PRK07196 323 RAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCYA-DYMAIKPLIPLGGYVAGADPMADQAV 401
|
330 340 350
....*....|....*....|....*....|
gi 446919357 411 NRGRRTVEVLKQPLHKPLPVEKQVVILYAL 440
Cdd:PRK07196 402 HYYPAITQFLRQEVGHPALFSASVEQLTGM 431
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
13-428 |
8.90e-32 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 126.94 E-value: 8.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 13 KKQIEDFQPnfdVTETGIVTYIGDGIARARGLdNAMSGELLEFSNGAYgmaQNLESNDVGI-------IILGDFSEIREG 85
Cdd:PRK05922 8 KLLIHQWQP---YRECGLLSRVSGNLLEAQGL-SACLGELCQISLSKS---PPILAEVIGFhnrttllMSLSPIHYVALG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 86 DVVKRTGKIMEVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRE 165
Cdd:PRK05922 81 AEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 166 LIIGDRQTGKTSVAidAILNQKGQDMICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPYAGVAM 245
Cdd:PRK05922 161 GVFSEPGSGKSSLL--STIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 246 AEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDalggGSITALPFIETQAG- 324
Cdd:PRK05922 239 AEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDK----GSITALYAILHYPNh 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 325 -DIsayIATNVISITDGQIFL--QENLFNSgirPAIDAGSSVSRVGGAAQIKAMKRVAGTLRLDLASYRELEAFTQFGSd 401
Cdd:PRK05922 315 pDI---FTDYLKSLLDGHFFLtpQGKALAS---PPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGA- 387
|
410 420
....*....|....*....|....*..
gi 446919357 402 LDAATQAKLNRGRRTVEVLKQPLHKPL 428
Cdd:PRK05922 388 YVPGQDAHLDRAVKLLPSIKQFLSQPL 414
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
97-393 |
2.23e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 125.86 E-value: 2.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 97 VPVGEAMIGRVVNPLGQPVDGLGEI-ETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:PRK08927 92 VRPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 176 tSVAIDAILNQKGQDMICIYVaIGQKESTVRTQVE-TLRKYGaLDYTIVVTASASQPSPLLFIAPYAGVAMAEEFMYNGK 254
Cdd:PRK08927 172 -SVLLSMLARNADADVSVIGL-IGERGREVQEFLQdDLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGK 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 255 HVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAkvSDALGGGSITALPFIETQAGDISAYIATNV 334
Cdd:PRK08927 249 DVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVDGDDHNEPVADAV 326
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446919357 335 ISITDGQIFLQENLFNSGIRPAIDAGSSVSRVGGAAQIKAMKRVAGTLRLDLASYRELE 393
Cdd:PRK08927 327 RGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADME 385
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
50-365 |
6.78e-31 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 124.55 E-value: 6.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 50 GELLEF--SNGAYGMAQNLESND--VGIIILGDFSEIREGDV-VKRTGKIMEVPVGEAMIGRVVNPLGQPVDGLGEIETT 124
Cdd:PRK04196 26 GEIVEIelPNGEKRRGQVLEVSEdkAVVQVFEGTTGLDLKDTkVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 125 ATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQR------------EL---IIgdRQtgktsvaidAILNQKGQ 189
Cdd:PRK04196 106 KRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnELaaqIA--RQ---------AKVLGEEE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 190 DMICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPYAGVAMAEEFMYN-GKHVLIVYDDLSKQAV 268
Cdd:PRK04196 175 NFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFEkGMHVLVILTDMTNYCE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 269 AYRELSLLLRRPPGREAYPGdvfYLHSRL---LERSAKVSDAlgGGSITALPFIETQAGDISAYIATNVISITDGQIFLQ 345
Cdd:PRK04196 255 ALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLS 329
|
330 340
....*....|....*....|
gi 446919357 346 ENLFNSGIRPAIDAGSSVSR 365
Cdd:PRK04196 330 RELHRKGIYPPIDVLPSLSR 349
|
|
| 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 |
4.78e-29 |
|
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: 109.08 E-value: 4.78e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446919357 27 ETGIVTYIGDGIARARGLDNAMSGELLEFSNGAYGMAQNLESNDVGIIILGDFSEIREGDVVKRTGK 93
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
91-377 |
3.84e-28 |
|
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: 116.75 E-value: 3.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 91 TGKIMEVPVGEAMIGRVVNPLGQPVDG----LGE----IETTATRPVETPAPGVMqrksvfepLQTGLKAIDALVPIGRG 162
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKgppvLAEdyldINGQPINPYARIYPEEM--------IQTGISAIDVMNSIARG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 163 QRELIIGD-------------RQTGKTSVAIDAILNQKGQDMICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASAS 229
Cdd:TIGR01040 142 QKIPIFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLAN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 230 QPSPLLFIAPYAGVAMAEEFMYN-GKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDAl 308
Cdd:TIGR01040 222 DPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR- 300
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446919357 309 gGGSITALPFIETQAGDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVSRVGGAAQIKAMKR 377
Cdd:TIGR01040 301 -NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTR 368
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
28-365 |
1.71e-23 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 102.80 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 28 TGIVTYIGDGIA-RARGLDNamsGEL--LEFSNGA-YGMAQNLESNDVGIIILGDFSEIREGDVVKRTGKIMEVPVGEAM 103
Cdd:PRK02118 6 TKITDITGNVITvEAEGVGY---GELatVERKDGSsLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 104 IGRVVNPLGQPVDGLGEIEttaTRPVETPAPGV--MQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDrqTGKTSVAID 181
Cdd:PRK02118 83 LGRRFNGSGKPIDGGPELE---GEPIEIGGPSVnpVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSV--SGEPYNALL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 182 A-ILNQKGQDMIcIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPYAGVAMAEEFMYNG-KHVLIV 259
Cdd:PRK02118 158 ArIALQAEADII-ILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 260 YDDLSKQAVAYRELSLLLRRPPGREAYPGDvfyLHSRLLERSAKVSDALGGGSITALPFIETQAGDISAYIATNVISITD 339
Cdd:PRK02118 237 LTDMTNFADALKEISITMDQIPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITE 313
|
330 340
....*....|....*....|....*.
gi 446919357 340 GQIFLQENlfnsgirpAIDAGSSVSR 365
Cdd:PRK02118 314 GQFYLRRG--------RIDPFGSLSR 331
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-366 |
1.93e-23 |
|
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: 99.99 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 96 EVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 176 TSVAIDAILN-QKGQDMICIYVAIGQ------------KESTVrtqvetlRKYGALDYTIVVTASASQPSPLLFIAPYAG 242
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGErtregndlyhemKESGV-------INLDGLSKVALVYGQMNEPPGARARVALTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 243 VAMAEEFM-YNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKVSDalggGSITALPFIET 321
Cdd:cd01133 154 LTMAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKK----GSITSVQAVYV 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446919357 322 QAGDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVSRV 366
Cdd:cd01133 230 PADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
85-426 |
4.62e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 98.51 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 85 GDVVKRTGKIMEVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQRKSVFEPLQTGLKAIDALVPIGRGQR 164
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 165 ELIIGDRQTGKTSVAidAILNQKGQDMICIYVAIGQKESTVRTQVETLRKYGALDYTIVVTASASQPSPLLFIAPYAGVA 244
Cdd:PRK06793 159 IGIFAGSGVGKSTLL--GMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATS 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 245 MAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPgreaYPGDVFYLHS---RLLERSAKVSDalggGSITALPFIET 321
Cdd:PRK06793 237 IAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK----GSITGIYTVLV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 322 QAGDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVSRVGGAAQIKAMKRVAGTLRLDLASYRELEAFTQFGSD 401
Cdd:PRK06793 309 DGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTI 388
|
330 340
....*....|....*....|....*
gi 446919357 402 LDAATQAKLNRGRRTVEVLKQPLHK 426
Cdd:PRK06793 389 QENAENAYIFECKNKVEGINTFLKQ 413
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
64-393 |
1.60e-18 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 88.17 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 64 QNLESNDVGIIILGDFSEIREGDVVKRTGKIMEVPVGEAMIGRVVNPLGQPVDGLGEIETTATRPVETPAPGVMQ---RK 140
Cdd:CHL00060 63 QLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQldtKL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 141 SVFEplqTGLKAIDALVPIGRGQRELIIGDRQTGKTSVAIDAILN-QKGQDMICIYVAIGQ------------KESTVRT 207
Cdd:CHL00060 143 SIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGErtregndlymemKESGVIN 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 208 QVETLRKYGALDYtivvtASASQPSPLLFIAPYAGVAMAEEFM-YNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAY 286
Cdd:CHL00060 220 EQNIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRdVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 287 PGDVFYLHSRLLERSAKVSDalggGSITALPFIETQAGDISAYIATNVISITDGQIFLQENLFNSGIRPAIDAGSSVS-- 364
Cdd:CHL00060 295 QPTLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTStm 370
|
330 340 350
....*....|....*....|....*....|..
gi 446919357 365 ---RVGGAAQIKAMKRVAGTLRldlaSYRELE 393
Cdd:CHL00060 371 lqpRIVGEEHYETAQRVKQTLQ----RYKELQ 398
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
128-365 |
3.28e-16 |
|
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: 79.16 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 128 PVETPAPgVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTsVAIDAILNQKGQDMIcIYVAIGQKESTVrt 207
Cdd:cd01134 43 PVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKT-VISQSLSKWSNSDVV-IYVGCGERGNEM-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 208 qVETLRKYGAL----------DYTIVVTASASQPSPLLFIAPYAGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLL 277
Cdd:cd01134 118 -AEVLEEFPELkdpitgeslmERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 278 RRPPGREAYPGdvfYLHSRL---LERSAKVSdALGG----GSITALPFIETQAGDISAYIATNVISITdgQIF--LQENL 348
Cdd:cd01134 197 EEMPAEEGYPA---YLGARLaefYERAGRVR-CLGSpgreGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKL 270
|
250
....*....|....*..
gi 446919357 349 FNSGIRPAIDAGSSVSR 365
Cdd:cd01134 271 AQRRHFPSINWLISYSK 287
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
27-92 |
1.72e-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: 71.04 E-value: 1.72e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446919357 27 ETGIVTYIGDGIARARGLDNAMSGELLEFSNGAYGMAQNLESNDVGIIILGDFSEIREGDVVKRTG 92
Cdd:pfam02874 4 VIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
375-441 |
4.34e-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: 64.39 E-value: 4.34e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446919357 375 MKRVAGTLRLDLASYRELEAFTQFGSD--LDAATQAKLNRGRRTVEVLKQPLHKPLPVEKQVVILYALT 441
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIK 69
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
128-315 |
3.95e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 59.03 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 128 PVETPAPgVMQRKSVFEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTsVAIDAILNQKGQDmICIYVAIGQKESTVrt 207
Cdd:PRK04192 194 PVRRPRP-YKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT-VTQHQLAKWADAD-IVIYVGCGERGNEM-- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 208 qVETLRKYGAL----------DYTIVVTASASQPspllfIAP-----YAGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRE 272
Cdd:PRK04192 269 -TEVLEEFPELidpktgrplmERTVLIANTSNMP-----VAAreasiYTGITIAEYYRDMGYDVLLMADSTSRWAEALRE 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446919357 273 LSLLLRRPPGREAYPGdvfYLHSRL---LERSAKVSdALGG--GSITA 315
Cdd:PRK04192 343 ISGRLEEMPGEEGYPA---YLASRLaefYERAGRVK-TLGGeeGSVTI 386
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
192-364 |
1.27e-07 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 54.64 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 192 ICIYVAIGQKESTVRTQVETLRKYG-------ALDYTIVVTASASQPSPLLFIAPYAGVAMAEEFMYNGKHVLIVYDDLS 264
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPKLKdpktgkpLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446919357 265 KQAVAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERSAKVSdALGG----GSITALPFIETQAGDISAYIATNVISI 337
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPA---YLASKLaefYERAGRVV-TLGSdyrvGSVSVIGAVSPPGGDFSEPVVQNTLRV 839
|
170 180
....*....|....*....|....*..
gi 446919357 338 TDGQIFLQENLFNSGIRPAIDAGSSVS 364
Cdd:PRK14698 840 VKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| 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 |
1.38e-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: 37.29 E-value: 1.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446919357 28 TGIVTYIGDGIARARGLDNAMSGELLEF-----SNGAYGMAQ--NLESNDVGIIILGDFSEIREGDVVKRTGK 93
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIergdgNNETVLKAEviGFRGDRAILQLFESTRGLSRGALVEPTGR 73
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