|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-500 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 1060.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 1 MAIKAEEISALLRSQIENYESEMSVTDVGTVLQIGDGIALIHGLNDVMAGELVEFHNGVLGLAQNLEESNVGVVILGPYT 80
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 81 GITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIG 160
Cdd:PRK09281 81 DIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 161 RGQRELIIGDRQTGKTTIAIDTILNQKDQGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPY 240
Cdd:PRK09281 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 241 SGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDDLGGGSITALPIIE 320
Cdd:PRK09281 241 AGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 321 TQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFGS 400
Cdd:PRK09281 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 401 DLDEFTASKLERGKRTVEVLKQDQNKPLPVEHQVLIIYALTKGYLDDIPVVDITRFEDELNHWAESNATELLNEIRETGG 480
Cdd:PRK09281 401 DLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKD 480
|
490 500
....*....|....*....|..
gi 119367964 481 LPD--AEKFDTAINEFKKSFSK 500
Cdd:PRK09281 481 LSDeiEAKLKAAIEEFKKTFAA 502
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-502 |
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: 1056.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 1 MAIKAEEISALLRSQIENYESEMSVTDVGTVLQIGDGIALIHGLNDVMAGELVEFHNGVLGLAQNLEESNVGVVILGPYT 80
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 81 GITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIG 160
Cdd:COG0056 81 GIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 161 RGQRELIIGDRQTGKTTIAIDTILNQKDQGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPY 240
Cdd:COG0056 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 241 SGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDDLGGGSITALPIIE 320
Cdd:COG0056 241 AGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 321 TQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFGS 400
Cdd:COG0056 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 401 DLDEFTASKLERGKRTVEVLKQDQNKPLPVEHQVLIIYALTKGYLDDIPVVDITRFEDELNHWAESNATELLNEIRETGG 480
Cdd:COG0056 401 DLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGK 480
|
490 500
....*....|....*....|....
gi 119367964 481 LPDA--EKFDTAINEFKKSFSKSE 502
Cdd:COG0056 481 LDDEieEKLKAAIEEFKKTFAASA 504
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
2-499 |
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: 886.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 2 AIKAEEISALLRSQIENYESEMSVTDVGTVLQIGDGIALIHGLNDVMAGELVEFHNGVLGLAQNLEESNVGVVILGPYTG 81
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 82 ITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGR 161
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 162 GQRELIIGDRQTGKTTIAIDTILNQKDQGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYS 241
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 242 GVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDDLGGGSITALPIIET 321
Cdd:TIGR00962 241 GCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 322 QAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFGSD 401
Cdd:TIGR00962 321 QAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 402 LDEFTASKLERGKRTVEVLKQDQNKPLPVEHQVLIIYALTKGYLDDIPVVDITRFEDELNHWAESNATELLNEIRETGGL 481
Cdd:TIGR00962 401 LDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKL 480
|
490 500
....*....|....*....|
gi 119367964 482 PD--AEKFDTAINEFKKSFS 499
Cdd:TIGR00962 481 TEelEAKLKEALKNFKKTFA 500
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-500 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 795.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 1 MAIKAEEISALLRSQIENYESEMSVTDVGTVLQIGDGIALIHGLNDVMAGELVEFHNGVLGLAQNLEESNVGVVILGPYT 80
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 81 GITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIG 160
Cdd:PRK13343 81 DILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 161 RGQRELIIGDRQTGKTTIAIDTILNQKDQGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPY 240
Cdd:PRK13343 161 RGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 241 SGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDDLGGGSITALPIIE 320
Cdd:PRK13343 241 AGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 321 TQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFGS 400
Cdd:PRK13343 321 TLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 401 DLDEFTASKLERGKRTVEVLKQDQNKPLPVEHQVLIIYALTKGYLDDIPVVDITRFEDELNHWAESNATELLNEIRETGG 480
Cdd:PRK13343 401 LLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRE 480
|
490 500
....*....|....*....|..
gi 119367964 481 LPDA--EKFDTAINEFKKSFSK 500
Cdd:PRK13343 481 LDEAwlAALEEILREAGERFAA 502
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
22-502 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 769.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 22 EMSVTDVGTVLQIGDGIALIHGLNDVMAGELVEFHNGVLGLAQNLEESNVGVVILGPYTGITEGDEVKRTGRIMEVPVGE 101
Cdd:CHL00059 1 EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 102 ELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTIAID 181
Cdd:CHL00059 81 AYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 182 TILNQKDQGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTMGEEFMFNGKHVLIVYD 261
Cdd:CHL00059 161 TILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 262 DLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDDLGGGSITALPIIETQAGDISAYVPTNVISITDGQ 341
Cdd:CHL00059 241 DLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 342 IFLQSDLFFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFGSDLDEFTASKLERGKRTVEVLK 421
Cdd:CHL00059 321 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 422 QDQNKPLPVEHQVLIIYALTKGYLDDIPVVDITRFEDELNHWAESNATELLNEIRETGGL-PDAEK-FDTAINEFKKSFS 499
Cdd:CHL00059 401 QSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFtEEAEAlLKEAIQEQLELFL 480
|
...
gi 119367964 500 KSE 502
Cdd:CHL00059 481 LQE 483
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
6-477 |
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: 609.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 6 EEISALLRSQIENYESEMSVTDVGTVLQIGDGIALIHGLNDVMAGELVEFHNGVLGLAQNLEESNVGVVILGPYTGITEG 85
Cdd:TIGR03324 6 DKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 86 DEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRE 165
Cdd:TIGR03324 86 DEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 166 LIIGDRQTGKTTIAIDTILNQKDQGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTM 245
Cdd:TIGR03324 166 LILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 246 GEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDDLGGGSITALPIIETQAGD 325
Cdd:TIGR03324 246 GEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 326 ISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFGSDLDEF 405
Cdd:TIGR03324 326 ISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDEN 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119367964 406 TASKLERGKRTVEVLKQDQNKPLPVEHQVLIIYALTKGYLDDIPVVDITRFEDELnhwaESNATELLNEIRE 477
Cdd:TIGR03324 406 TRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAI----RAAVTSLPADLRE 473
|
|
| 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: 574.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 94 IMEVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQT 173
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 174 GKTTIAIDTILNQKDQGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTMGEEFMFNG 253
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 254 KHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDDLGGGSITALPIIETQAGDISAYVPTN 333
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 119367964 334 VISITDGQIFLQSDLFFSGVRPAINAGQSVSRVG 367
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
61-462 |
2.83e-120 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 364.36 E-value: 2.83e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 61 GLAQNLE-ESNVGVVILGPYTGITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIdgqgPIN-TTKTR----------P 128
Cdd:PTZ00185 80 GLVFNLEkDGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEV----PVGlLTRSRalleseqtlgK 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 129 VEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTIAIDTILNQ--------KDQGTICIYVAIGQ 200
Cdd:PTZ00185 156 VDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 201 KDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLRRP 280
Cdd:PTZ00185 236 RCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 281 PGREAYPGDVFYLHSRLLERAAKLNDDLGGGSITALPIIETQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAG 360
Cdd:PTZ00185 316 PGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 361 QSVSRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFGSDLDEFtasKLERGKRTVEVLKQDQnkPLPVEHQVLIIYAL 440
Cdd:PTZ00185 396 LSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTV---PMIRGARFVALFNQKN--PSFFMNALVSLYAC 470
|
410 420
....*....|....*....|..
gi 119367964 441 TKGYLDDIPVVDITRFEDELNH 462
Cdd:PTZ00185 471 LNGYLDDVKVNYAKLYEYLLVN 492
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
149-364 |
7.41e-116 |
|
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: 340.10 E-value: 7.41e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 149 GIKAIDALVPIGRGQRELIIGDRQTGKTTIAiDTILNQKDQGtICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASA 228
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD-VVVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 229 SEPSPLLYIAPYSGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDdl 308
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKG-- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 119367964 309 GGGSITALPIIETQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVS 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 |
1.71e-107 |
|
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: 320.94 E-value: 1.71e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 97 VPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKT 176
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 177 TIAIDTILNQ-KDQGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTMGEEFMFNGKH 255
Cdd:cd19476 82 VLAMQLARNQaKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 256 VLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDdlGGGSITALPIIETQAGDISAYVPTNVI 335
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNTF 239
|
250 260 270
....*....|....*....|....*....|.
gi 119367964 336 SITDGQIFLQSDLFFSGVRPAINAGQSVSRV 366
Cdd:cd19476 240 AILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
85-414 |
9.89e-107 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 327.32 E-value: 9.89e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 85 GDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQGPINTTK-----TRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPI 159
Cdd:PRK07165 61 NDELIELNNTNKVKTSKEYFGKIIDIDGNIIYPEAQNPLSKkflpnTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 160 GRGQRELIIGDRQTGKTTIAIDTILNQKDQGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPlLYIAP 239
Cdd:PRK07165 141 GKGQRELIIGDRQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSPYE-QYLAP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 240 YSGVTMGEEFMFNgKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLnddLGGGSITALPII 319
Cdd:PRK07165 220 YVAMAHAENISYN-DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKF---KNRKTITALPIL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 320 ETQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFG 399
Cdd:PRK07165 296 QTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLD 375
|
330
....*....|....*
gi 119367964 400 SDLDEFTASKLERGK 414
Cdd:PRK07165 376 YDLNKETSDLLFKGK 390
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
375-498 |
1.92e-62 |
|
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349748 [Multi-domain] Cd Length: 126 Bit Score: 199.51 E-value: 1.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 375 MKKVAGTLRLDLASYRELESFAQFGSDLDEFTASKLERGKRTVEVLKQDQNKPLPVEHQVLIIYALTKGYLDDIPVVDIT 454
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 119367964 455 RFEDELNHWAESNATELLNEIRETGGLPDA--EKFDTAINEFKKSF 498
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDEleEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
371-494 |
1.11e-61 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 197.66 E-value: 1.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 371 QIKAMKKVAGTLRLDLASYRELESFAQFGSDLDEFTASKLERGKRTVEVLKQDQNKPLPVEHQVLIIYALTKGYLDDIPV 450
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 119367964 451 VDITRFEDELNHWAESNATELLNEIRETGGLPD--AEKFDTAINEF 494
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDelEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
96-366 |
2.23e-55 |
|
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: 186.23 E-value: 2.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 96 EVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 176 TTIAIDTILNQKdqGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTMGEEFMFNGKH 255
Cdd:cd01136 81 STLLGMIARNTD--ADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 256 VLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDdlggGSITALPIIETQAGDISAYVPTNVI 335
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----GSITAFYTVLVEGDDFNDPIADEVR 234
|
250 260 270
....*....|....*....|....*....|.
gi 119367964 336 SITDGQIFLQSDLFFSGVRPAINAGQSVSRV 366
Cdd:cd01136 235 SILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
28-393 |
1.45e-53 |
|
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: 186.39 E-value: 1.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 28 VGTVLQIGDGIALIHGLNDVMAGELVEFHNGvlglaqnleesNVGVVILGPYTGITEGDEVKRTGRIMEVPVGEELIGRV 107
Cdd:COG1157 34 VGPDASIGELCEIETADGRPVLAEVVGFRGD-----------RVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGLLGRV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 108 VNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQReliIGdr---qtGKTT----IAi 180
Cdd:COG1157 103 LDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR---IGifagsgvGKSTllgmIA- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 181 dtilnqkdQGTIC--IYVA-IGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTMGEEFMFNGKHVL 257
Cdd:COG1157 179 --------RNTEAdvNVIAlIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 258 IVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAklNDdlGGGSITAL------------PIIETqagd 325
Cdd:COG1157 251 LLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAG--NG--GKGSITAFytvlvegddmndPIADA---- 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119367964 326 isayvptnVISITDGQIFLQSDLFFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYRELE 393
Cdd:COG1157 323 --------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENE 382
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
29-431 |
2.18e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 177.96 E-value: 2.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 29 GTVLQIGDGIALIHGLNdVMAGELVEFHNG-----VLGLAQNLEESNVGVVILGPYTGITEGDEVKRTGRIMEVPVGEEL 103
Cdd:PRK08472 20 GSITKISPTIIEADGLN-PSVGDIVKIESSdngkeCLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 104 IGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTIAIDTI 183
Cdd:PRK08472 99 LGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 184 LNQKDQgtICIYVAIGQKDSTVRANVEKlRQAGALDYTIVVAASaSEPSPLL--YIApYSGVTMGEEFMFNGKHVLIVYD 261
Cdd:PRK08472 179 KGCLAP--IKVVALIGERGREIPEFIEK-NLGGDLENTVIVVAT-SDDSPLMrkYGA-FCAMSVAEYFKNQGLDVLFIMD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 262 DLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKlndDLGGGSITALPIIETQAGDISAYVPTNVISITDGQ 341
Cdd:PRK08472 254 SVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 342 IFLQSDLFFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFGS-------DLDEFTASKlergK 414
Cdd:PRK08472 331 IVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAyqkgndkELDEAISKK----E 406
|
410
....*....|....*..
gi 119367964 415 RTVEVLKQDQNKPLPVE 431
Cdd:PRK08472 407 FMEQFLKQNPNELFPFE 423
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
74-431 |
1.10e-49 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 176.16 E-value: 1.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 74 VILGPYT---GITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGqGPINTTKTRPVEKKATGVMDRKSVDEPLQTGI 150
Cdd:PRK06820 73 ALLSPFAssdGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 151 KAIDALVPIGRGQRELIIGDRQTGKTTIAidTILNQKDQGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASE 230
Cdd:PRK06820 152 RAIDGILSCGEGQRIGIFAAAGVGKSTLL--GMLCADSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 231 PSPLLYIAPYSGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAklNDDLgg 310
Cdd:PRK06820 230 PALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG--NSDR-- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 311 GSITALPIIETQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYR 390
Cdd:PRK06820 306 GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQ 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 119367964 391 ELESFAQFG---SDLDEFTASKLERGKRTVEVLKQDQNKPLPVE 431
Cdd:PRK06820 386 EIELLVRVGeyqAGEDLQADEALQRYPAICAFLQQDHSETAHLE 429
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
6-442 |
1.30e-49 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 176.10 E-value: 1.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 6 EEISALLRSQIEN---YESEMSVTDV-GTVLQigdgiALIHGlndVMAGELVEFHNG---------VLGLAQNleesnVG 72
Cdd:PRK06936 5 DYIPHHLRHAIVGsrlIQIRGRVTQVtGTILK-----AVVPG---VRIGELCYLRNPdnslslqaeVIGFAQH-----QA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 73 VVI-LGPYTGITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIK 151
Cdd:PRK06936 72 LLTpLGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 152 AIDALVPIGRGQRELIIGDRQTGKTTIAIDTILNQkdQGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEP 231
Cdd:PRK06936 152 VIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSA--EVDVTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 232 SPLLYIAPYSGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKlNDDlggG 311
Cdd:PRK06936 230 SMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ-SDK---G 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 312 SITALPIIETQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYRE 391
Cdd:PRK06936 306 SITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEE 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 119367964 392 LESFAQFGS---DLDEFTASKLERGKRTVEVLKQDQNKPLPVEHQVLIIYALTK 442
Cdd:PRK06936 386 VELLLQIGEyqkGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETLTQ 439
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
28-399 |
2.02e-49 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 175.73 E-value: 2.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 28 VGTVLQIGdgialihGLnDVMAGELVEFHNGVLGLAQNLEEsnVG----VVILGPY---TGITEGDEVKRTGRIMEVPVG 100
Cdd:PRK09099 32 IGTLLRVS-------GL-DVTLGELCELRQRDGTLLQRAEV--VGfsrdVALLSPFgelGGLSRGTRVIGLGRPLSVPVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 101 EELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTtiai 180
Cdd:PRK09099 102 PALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKS---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 181 dTILNQKDQGTIC---IYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTMGEEFMFNGKHVL 257
Cdd:PRK09099 178 -TLMGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 258 IVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAklnddLGG-GSITALPIIETQAGDISAYVPTNVIS 336
Cdd:PRK09099 257 LMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-----MGEtGSITALYTVLAEDESGSDPIAEEVRG 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119367964 337 ITDGQIFLQSDLFFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFG 399
Cdd:PRK09099 332 ILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVG 394
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
34-443 |
5.76e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 168.75 E-value: 5.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 34 IGDgIALIH---GLNDVMAGELVEFHngvlglaqnlEESnvgvVILGPYTGITE---GDEVKRTGRIMEVPVGEELIGRV 107
Cdd:PRK07721 39 IGD-VCYIHtkgGGDKAIKAEVVGFK----------DEH----VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 108 VNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTT----IAIDTi 183
Cdd:PRK07721 104 LDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTlmgmIARNT- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 184 lnQKDQGTICIyvaIGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTMGEEFMFNGKHVLIVYDDL 263
Cdd:PRK07721 183 --SADLNVIAL---IGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 264 TKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKlNddlGGGSITALPIIETQAGDISAYVPTNVISITDGQIF 343
Cdd:PRK07721 258 TRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGT-N---ASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 344 LQSDLFFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFGS-------DLDEftasKLERGKRT 416
Cdd:PRK07721 334 LDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAykrgssrEIDE----AIQFYPQI 409
|
410 420
....*....|....*....|....*..
gi 119367964 417 VEVLKQDQNKPLPVEHQVLIIYALTKG 443
Cdd:PRK07721 410 ISFLKQGTDEKATFEESIQALLSLFGK 436
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
94-380 |
2.06e-42 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 152.38 E-value: 2.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 94 IMEVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDrqT 173
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSG--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 174 G------KTTIAIDTILNQKDQGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTMGE 247
Cdd:cd01135 79 GlphnelAAQIARQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 248 EFMF-NGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLNDDlgGGSITALPIIETQA 323
Cdd:cd01135 159 YLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTMPN 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 119367964 324 GDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSRVggsaqikaMKKVAG 380
Cdd:cd01135 234 DDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRL--------MKSGIG 282
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
74-399 |
1.47e-40 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 151.26 E-value: 1.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 74 VILGPYT---GITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQgPINTTKTRPVEKKATGVMDRKSVDEPLQTGI 150
Cdd:PRK07594 65 ALLSPFTstiGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 151 KAIDALVPIGRGQRELIIGDRQTGKTTIAidTILNQKDQGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASE 230
Cdd:PRK07594 144 RAIDSVATCGEGQRVGIFSAPGVGKSTLL--AMLCNAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 231 PSPLLYIAPYSGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAklnddLGG 310
Cdd:PRK07594 222 PALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-----MGE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 311 -GSITALPIIETQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASY 389
Cdd:PRK07594 297 kGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALY 376
|
330
....*....|
gi 119367964 390 RELESFAQFG 399
Cdd:PRK07594 377 QEVELLIRIG 386
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
30-365 |
1.97e-40 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 151.52 E-value: 1.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 30 TVLQIGDGIALIHGLNDVMAGELVEF--HNGVLGLAQNLEESNVGVVI--LGPYTGI-TEGDEVKRTGRIMEVPVGEELI 104
Cdd:PRK04196 6 TVSEIKGPLLFVEGVEGVAYGEIVEIelPNGEKRRGQVLEVSEDKAVVqvFEGTTGLdLKDTKVRFTGEPLKLPVSEDML 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 105 GRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQR------------EL---IIg 169
Cdd:PRK04196 86 GRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnELaaqIA- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 170 dRQTgkttiaidTILNQKDQGTIcIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTMGEEF 249
Cdd:PRK04196 165 -RQA--------KVLGEEENFAV-VFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 250 MFN-GKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLNDDlgGGSITALPIIETQAGD 325
Cdd:PRK04196 235 AFEkGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDD 309
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 119367964 326 ISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSR 365
Cdd:PRK04196 310 ITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
46-366 |
5.83e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 149.85 E-value: 5.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 46 DVMAGELVEfhnGVLGLAQNLeesnvgvVILGP---YTGITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQGPIN 122
Cdd:PRK08972 53 ETMAGELEA---EVVGFDGDL-------LYLMPieeLRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIY 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 123 TTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTtiaidTILNQKDQGT---ICIYVAIG 199
Cdd:PRK08972 123 TDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKS-----VLLGMMTRGTtadVIVVGLVG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 200 QKDSTVRANVEKLRQAGALDYTIVVAASAsEPSPLLYI-APYSGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLR 278
Cdd:PRK08972 198 ERGREVKEFIEEILGEEGRARSVVVAAPA-DTSPLMRLkGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 279 RPPGREAYPGDVFYLHSRLLERAAklNDDLGGGSITALPIIETQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAIN 358
Cdd:PRK08972 277 EPPATKGYPPSVFAKLPALVERAG--NGGPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAID 354
|
....*...
gi 119367964 359 AGQSVSRV 366
Cdd:PRK08972 355 IEASISRV 362
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
44-399 |
1.13e-38 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 145.91 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 44 LNDVMAGELVE-----FHNGVLGLAQ--NLEESNVGVVILGPYTGITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQ--- 113
Cdd:PRK08149 22 LPDVAIGEICEiragwHSNEVIARAQvvGFQRERTILSLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKive 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 114 PIDGQGPINT-TKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTIaIDTILNQKDqGTI 192
Cdd:PRK08149 102 RFDAPPTVGPiSEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSL-MNMLIEHSE-ADV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 193 CIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRE 272
Cdd:PRK08149 180 FVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 273 LSLLLRRPPGREAYPGDVFYLHSRLLERAAKlnddLGGGSITALPIIETQAGDISAYVPTNVISITDGQIFLQSDLFFSG 352
Cdd:PRK08149 260 VALAAGELPARRGYPASVFDSLPRLLERPGA----TLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKG 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 119367964 353 VRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFG 399
Cdd:PRK08149 336 HYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLG 382
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
12-428 |
1.38e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 143.21 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 12 LRSQIENY-ESEMSVTDVGTVLQIGDGIALIHGLN-DVMAGELVEFHNG---VLGLAQNLEESNVGVVILGPYTGITEGD 86
Cdd:PRK06002 10 LAALVERYaAPEPLVRIGGTVSEVTASHYRVRGLSrFVRLGDFVAIRADggtHLGEVVRVDPDGVTVKPFEPRIEIGLGD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 87 EVKRTGRiMEVPVGEELIGRVVNPLGQPIDGQGPINT-TKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRE 165
Cdd:PRK06002 90 AVFRKGP-LRIRPDPSWKGRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 166 LIIGDRQTGKTTI--------AIDTILnqkdqgticiyVA-IGQKDSTVRANVEKLrQAGALDYTIVVAASASEpSPLLY 236
Cdd:PRK06002 169 GIFAGSGVGKSTLlamlaradAFDTVV-----------IAlVGERGREVREFLEDT-LADNLKKAVAVVATSDE-SPMMR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 237 -IAPYSGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDdlGGGSITA 315
Cdd:PRK06002 236 rLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 316 LPIIETQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYRE---- 391
Cdd:PRK06002 314 IFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdl 393
|
410 420 430
....*....|....*....|....*....|....*...
gi 119367964 392 -LESFAQFGSDLDEFTASKLErgKRTVEVLKQDQNKPL 428
Cdd:PRK06002 394 rLIGGYRAGSDPDLDQAVDLV--PRIYEALRQSPGDPP 429
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
67-366 |
4.21e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 142.18 E-value: 4.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 67 EESNVGVVILGPYTGITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPL 146
Cdd:PRK05688 73 SGDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 147 QTGIKAIDALVPIGRGQRELIIGDRQTGKTTI-AIDTILNQKDqgtICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVA 225
Cdd:PRK05688 153 DVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLlGMMTRFTEAD---IIVVGLIGERGREVKEFIEHILGEEGLKRSVVVA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 226 ASASEpSPLLYI-APYSGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAkl 304
Cdd:PRK05688 230 SPADD-APLMRLrAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG-- 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119367964 305 NDDLGGGSITALPIIETQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSRV 366
Cdd:PRK05688 307 NAEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV 368
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
81-429 |
2.97e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 139.26 E-value: 2.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 81 GITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIG 160
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 161 RGQRELIIGDRQTGKTTIAidTILNQKDQGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEpSPLLYI-AP 239
Cdd:PRK07196 154 KGQRVGLMAGSGVGKSVLL--GMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADE-SPLMRIkAT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 240 YSGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAklnDDLGGGSITALPII 319
Cdd:PRK07196 231 ELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 320 ETQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSR----VGGSAQIKAMKKVAGTLRlDLASYRELESF 395
Cdd:PRK07196 308 LAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCYA-DYMAIKPLIPL 386
|
330 340 350
....*....|....*....|....*....|....
gi 119367964 396 AQFGSDLDEFTASKLERGKRTVEVLKQDQNKPLP 429
Cdd:PRK07196 387 GGYVAGADPMADQAVHYYPAITQFLRQEVGHPAL 420
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
46-428 |
7.33e-36 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 138.50 E-value: 7.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 46 DVMAgELVEFHNGVLGLaqnleesnvgvVILGPYTGITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQGPINTTK 125
Cdd:PRK05922 53 PILA-EVIGFHNRTTLL-----------MSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 126 TRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTIaIDTILnQKDQGTICIYVAIGQKDSTV 205
Cdd:PRK05922 121 LKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSL-LSTIA-KGSKSTINVIALIGERGREV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 206 RANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREA 285
Cdd:PRK05922 199 REYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHH 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 286 YPGDVFYLHSRLLERAAklNDDlgGGSITALPIIETQAG--DI-SAYVPtnviSITDGQIFL--QSDLFFSgvrPAINAG 360
Cdd:PRK05922 279 YAASVFHHVSEFTERAG--NND--KGSITALYAILHYPNhpDIfTDYLK----SLLDGHFFLtpQGKALAS---PPIDIL 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119367964 361 QSVSRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFGSDLDEFTAsKLERGKRTVEVLKQDQNKPL 428
Cdd:PRK05922 348 TSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAYVPGQDA-HLDRAVKLLPSIKQFLSQPL 414
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
59-449 |
9.47e-36 |
|
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: 138.31 E-value: 9.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 59 VLGLAQNLEESNVGVVILGPYTGITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMD 138
Cdd:TIGR01039 40 TLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 139 RKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTIAIDTILN-QKDQGTICIYVAIGQKdsTVRAN--VEKLRQA 215
Cdd:TIGR01039 120 QSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGER--TREGNdlYHEMKES 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 216 GALDYTIVVAASASEPSPLLYIAPYSGVTMGEEFM-FNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLH 294
Cdd:TIGR01039 198 GVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 295 SRLLERAAKLNddlgGGSITALPIIETQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSR-----VGGS 369
Cdd:TIGR01039 278 GELQERITSTK----TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRlldpsVVGE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 370 AQIKAMKKVAGTLRldlaSYRELES-FAQFG----SDLDEFTASKLERGKR-------TVEVLKQDQNKPLPVEHQVLII 437
Cdd:TIGR01039 354 EHYDVARGVQQILQ----RYKELQDiIAILGmdelSEEDKLTVERARRIQRflsqpffVAEVFTGQPGKYVPLKDTIRGF 429
|
410
....*....|..
gi 119367964 438 YALTKGYLDDIP 449
Cdd:TIGR01039 430 KEILEGKYDHLP 441
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
96-397 |
1.86e-35 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 137.61 E-value: 1.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 96 EVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 176 TTIAidTILNQKDQGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASAsEPSPLLYIAPYSGVT-MGEEFMFNGK 254
Cdd:PRK07960 189 SVLL--GMMARYTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPA-DVSPLLRMQGAAYATrIAEDFRDRGQ 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 255 HVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAklNDDLGGGSITALPIIETQAGDISAYVPTNV 334
Cdd:PRK07960 266 HVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG--NGISGGGSITAFYTVLTEGDDQQDPIADSA 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119367964 335 ISITDGQIFLQSDLFFSGVRPAINAGQSVSRvggsaqikAMkkvagTLRLDLASYRELESFAQ 397
Cdd:PRK07960 344 RAILDGHIVLSRRLAEAGHYPAIDIEASISR--------AM-----TALIDEQHYARVRQFKQ 393
|
|
| 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 |
2.29e-31 |
|
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: 115.24 E-value: 2.29e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119367964 27 DVGTVLQIGDGIALIHGLNDVMAGELVEFHNGVLGLAQNLEESNVGVVILGPYTGITEGDEVKRTGR 93
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
30-399 |
2.02e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 123.17 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 30 TVLQIGDGIALIHGLNDVMAGELVEFHNGvlglaqnleesNVGVVILGPYTGITEGDEVKRTGRIMEVPVGEELIGRVVN 109
Cdd:PRK08927 36 HALSVGARIVVETRGGRPVPCEVVGFRGD-----------RALLMPFGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 110 PLGQPIDGQGPI-NTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTIAidTILNQKD 188
Cdd:PRK08927 105 ALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLL--SMLARNA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 189 QGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTMGEEFMFNGKHVLIVYDDLTKQAA 268
Cdd:PRK08927 183 DADVSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 269 AYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKlnDDLGGGSITALPIIETQAGDISAYVPTNVISITDGQIFLQSDL 348
Cdd:PRK08927 263 AQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGP--GPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAI 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 119367964 349 FFSGVRPAINAGQSVSRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFG 399
Cdd:PRK08927 341 AERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLG 391
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
83-375 |
3.71e-30 |
|
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: 122.52 E-value: 3.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 83 TEGDEVKR-----TGRIMEVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALV 157
Cdd:TIGR01040 57 TSGIDAKKttcefTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 158 PIGRGQRELIIGD-------------RQTGKTTIAIDTILNQKDQGTICIYVAIGQKDSTVRANVEKLRQAGALDYTIVV 224
Cdd:TIGR01040 137 SIARGQKIPIFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLF 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 225 AASASEPSPLLYIAPYSGVTMGEEFMFN-GKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAK 303
Cdd:TIGR01040 217 LNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGR 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119367964 304 LNDDlgGGSITALPIIETQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSRVGGSAQIKAM 375
Cdd:TIGR01040 297 VEGR--NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-366 |
8.56e-26 |
|
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: 106.53 E-value: 8.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 96 EVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 176 TTIAIDTILN-QKDQGTICIYVAIGQKdsTVRAN------VE-KLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTMGE 247
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGER--TREGNdlyhemKEsGVINLDGLSKVALVYGQMNEPPGARARVALTGLTMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 248 EFM-FNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLNDdlggGSITALPIIETQAGDI 326
Cdd:cd01133 159 YFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKK----GSITSVQAVYVPADDL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 119367964 327 SAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVSRV 366
Cdd:cd01133 235 TDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
50-347 |
2.09e-25 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 108.58 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 50 GELVEFHNGVLG-LAQ--NLEESNVGVVILGPYTGITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQG------- 119
Cdd:PRK02118 26 GELATVERKDGSsLAQviRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPelegepi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 120 PINTTKTRPVEKKATGVMDRksvdeplqTGIKAIDALVPIGRGQRELIIGDrqTGKTTIAI-DTILNQKDQGTIcIYVAI 198
Cdd:PRK02118 106 EIGGPSVNPVKRIVPREMIR--------TGIPMIDVFNTLVESQKIPIFSV--SGEPYNALlARIALQAEADII-ILGGM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 199 GQKDSTVRANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTMGEEFMFNG-KHVLIVYDDLTKQAAAYRELSLLL 277
Cdd:PRK02118 175 GLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLTDMTNFADALKEISITM 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 278 RRPPGREAYPGDvfyLHSRLLERAAKLNDDLGGGSITALPIIETQAGDISAYVPTNVISITDGQIFLQSD 347
Cdd:PRK02118 255 DQIPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLRRG 321
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
47-400 |
1.27e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 106.22 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 47 VMAGElvefhNGVLGLAQNLEESNVGVVILGPYTGITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQGPINTTKT 126
Cdd:PRK06793 46 CFVGE-----HNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 127 RPVEKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTIAidTILNQKDQGTICIYVAIGQKDSTVR 206
Cdd:PRK06793 121 IKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLL--GMIAKNAKADINVISLVGERGREVK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 207 ANVEKLRQAGALDYTIVVAASASEPSPLLYIAPYSGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELSLLLRRPPgreaY 286
Cdd:PRK06793 199 DFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----I 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 287 PGDVFYLHS---RLLERAAKLNDdlggGSITALPIIETQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSV 363
Cdd:PRK06793 275 GGKTLLMESymkKLLERSGKTQK----GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSV 350
|
330 340 350
....*....|....*....|....*....|....*..
gi 119367964 364 SRVGGSAQIKAMKKVAGTLRLDLASYRELESFAQFGS 400
Cdd:PRK06793 351 SRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGT 387
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
59-365 |
4.73e-24 |
|
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: 104.79 E-value: 4.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 59 VLGLAQNLEESNVGVVILGPYTGITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMD 138
Cdd:COG0055 43 VLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 139 RKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTIAIDTILN-QKDQGTICIYVAIGQKdsTVRAN--VEKLRQA 215
Cdd:COG0055 123 QSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNiAKEHGGVSVFAGVGER--TREGNdlYREMKES 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 216 GALDYTIVVAASASEPSPLLYIAPYSGVTMGEEFM-FNGKHVLIVYDDLTK--QAAAyrELSLLLRRPPGREAY-Pgdvf 291
Cdd:COG0055 201 GVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRdEEGQDVLLFIDNIFRftQAGS--EVSALLGRMPSAVGYqP---- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 292 ylhsrlleraaKLNDDLG----------GGSITALPIIETQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQ 361
Cdd:COG0055 275 -----------TLATEMGalqeritstkKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLD 343
|
....
gi 119367964 362 SVSR 365
Cdd:COG0055 344 STSR 347
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
64-412 |
5.21e-18 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 86.63 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 64 QNLEESNVGVVILGPYTGITEGDEVKRTGRIMEVPVGEELIGRVVNPLGQPIDGQGPINTTKTRPVEKKATGVMDRKSVD 143
Cdd:CHL00060 63 QLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 144 EPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTIAIDTILN-QKDQGTICIYVAIGQ------------KDSTVrANVE 210
Cdd:CHL00060 143 SIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGErtregndlymemKESGV-INEQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 211 KLRQAG-ALDYtivvaASASEPSPLLYIAPYSGVTMGEEFM-FNGKHVLIVYDDLTKQAAAYRELSLLLRRPPGREAYPG 288
Cdd:CHL00060 222 NIAESKvALVY-----GQMNEPPGARMRVGLTALTMAEYFRdVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQP 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 289 DVFYLHSRLLERAAKLNDdlggGSITALPIIETQAGDISAYVPTNVISITDGQIFLQSDLFFSGVRPAINAGQSVS---- 364
Cdd:CHL00060 297 TLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTStmlq 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 119367964 365 -RVGGSAQIKAMKKVAGTLRldlaSYRELESF-AQFGsdLDEFT---------ASKLER 412
Cdd:CHL00060 373 pRIVGEEHYETAQRVKQTLQ----RYKELQDIiAILG--LDELSeedrltvarARKIER 425
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
127-365 |
7.61e-18 |
|
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: 83.78 E-value: 7.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 127 RPVEKKATGvmdrksvDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTIAidTILNQKDQGTICIYVAIGQkdstvR 206
Cdd:cd01134 48 RPVKEKLPP-------NVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVIS--QSLSKWSNSDVVIYVGCGE-----R 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 207 AN--VEKLRQAGAL----------DYTIVVAASASEPSPLLYIAPYSGVTMGEEFMFNGKHVLIVYDDLTKQAAAYRELS 274
Cdd:cd01134 114 GNemAEVLEEFPELkdpitgeslmERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREIS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 275 LLLRRPPGREAYPGdvfYLHSRL---LERAAK---LNDDLGGGSITALPIIETQAGDISAYVPTNVISITdgQIF--LQS 346
Cdd:cd01134 194 GRLEEMPAEEGYPA---YLGARLaefYERAGRvrcLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDK 268
|
250
....*....|....*....
gi 119367964 347 DLFFSGVRPAINAGQSVSR 365
Cdd:cd01134 269 KLAQRRHFPSINWLISYSK 287
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
28-92 |
1.73e-17 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 76.81 E-value: 1.73e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119367964 28 VGTVLQIGDGIALIHGLNDVMAGELVEFHNGVLGLAQNLEESNVGVVILGPYTGITEGDEVKRTG 92
Cdd:pfam02874 5 IGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
375-442 |
2.11e-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: 65.16 E-value: 2.11e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 375 MKKVAGTLRLDLASYRELESFAQFGSD--LDEFTASKLERGKRTVEVLKQDQNKPLPVEHQVLIIYALTK 442
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
192-358 |
5.39e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 61.96 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 192 ICIYVAIGQKDSTVRANVE---KLRQAGA----LDYTIVVAASASEPSPLLYIAPYSGVTMGEEFMFNGKHVLIVYDDLT 264
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEefpKLKDPKTgkplMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 265 KQAAAYRELSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKLNDDLGGGSITALPIIETQAGDISAYVPTNVISIT 338
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVV 840
|
170 180
....*....|....*....|
gi 119367964 339 DGQIFLQSDLFFSGVRPAIN 358
Cdd:PRK14698 841 KVFWALDADLARRRHFPAIN 860
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
128-315 |
3.97e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 59.03 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 128 PVeKKATGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTtiaidtILNQK-------DqgtICIYVAIGQ 200
Cdd:PRK04192 194 PV-RRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT------VTQHQlakwadaD---IVIYVGCGE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 201 kdstvRAN--VEKLRQ---------AGAL-DYTIVVA------ASASEPSpllyIapYSGVTMGEEFMFNGKHVLIVYDD 262
Cdd:PRK04192 264 -----RGNemTEVLEEfpelidpktGRPLmERTVLIAntsnmpVAAREAS----I--YTGITIAEYYRDMGYDVLLMADS 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 119367964 263 LTKQAAAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERA--AKLNDDlGGGSITA 315
Cdd:PRK04192 333 TSRWAEALREISGRLEEMPGEEGYPA---YLASRLaefYERAgrVKTLGG-EEGSVTI 386
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
29-93 |
2.30e-06 |
|
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: 45.38 E-value: 2.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119367964 29 GTVLQIGDGIALIHGLNDVMAGELVEFH-----NGVLGLAQ--NLEESNVGVVILGPYTGITEGDEVKRTGR 93
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIGEVCEIErgdgnNETVLKAEviGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
151-270 |
2.59e-03 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 39.50 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119367964 151 KAIDALVPIGRGQRELIIGDRQTGKTT----IAIDTILNQKDqgTICIYVAIGQKDSTVranVEKLRQAGAldytIVVAA 226
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTllqnIANAIAKNHPE--VELIVLLIDERPEEV---TDMRRSVKG----EVVAS 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 119367964 227 SASEPspllyiaPYSGVTMGEEFM-------FNGKHVLIVYDDLTKQAAAY 270
Cdd:cd01128 76 TFDEP-------PERHVQVAEMVIekakrlvEHGKDVVILLDSITRLARAY 119
|
|
| |
