|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
2-496 |
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: 957.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 2 LNIATDEICSLIRYRIQNYNSELKLNNVGVVFKVGDGIVRVFGLQGAMAGELLLFEEGSVGIAFNLEKNNIGVVLLGDCT 81
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 82 LIQEGMIVKGTGKIGEVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIG 161
Cdd:COG0056 81 GIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 162 RGQRELIIGDRQTGKTAVAIDTILNQKGKDVKCVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPY 241
Cdd:COG0056 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 242 SGTALAEYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDSLGGGSLTALPIVE 321
Cdd:COG0056 241 AGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 322 TQEGDVSAYIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAELEAFSQFAS 401
Cdd:COG0056 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 402 DLDQATQNQLARGKRLREILKQPQYSPLSLENQVGIIFAGTNGYLDKVSIENIPSYITSLTESLKNEKSKFGDVILSTKD 481
Cdd:COG0056 401 DLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGK 480
|
490
....*....|....*
gi 122233797 482 FTKDEENVLRNILEA 496
Cdd:COG0056 481 LDDEIEEKLKAAIEE 495
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
23-495 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 955.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 23 ELKLNNVGVVFKVGDGIVRVFGLQGAMAGELLLFEEGSVGIAFNLEKNNIGVVLLGDCTLIQEGMIVKGTGKIGEVPVGD 102
Cdd:CHL00059 1 EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 103 KFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGRGQRELIIGDRQTGKTAVAID 182
Cdd:CHL00059 81 AYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 183 TILNQKGKDVKCVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYSGTALAEYFMYNGSHALVVYD 262
Cdd:CHL00059 161 TILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 263 DLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDSLGGGSLTALPIVETQEGDVSAYIPTNVISITDGQ 342
Cdd:CHL00059 241 DLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 343 IFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAELEAFSQFASDLDQATQNQLARGKRLREILK 422
Cdd:CHL00059 321 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLK 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 122233797 423 QPQYSPLSLENQVGIIFAGTNGYLDKVSIENIPSYITSLTESLKNEKSKFGDVILSTKDFTKDEENVLRNILE 495
Cdd:CHL00059 401 QSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQ 473
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
2-496 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 949.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 2 LNIATDEICSLIRYRIQNYNSELKLNNVGVVFKVGDGIVRVFGLQGAMAGELLLFEEGSVGIAFNLEKNNIGVVLLGDCT 81
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 82 LIQEGMIVKGTGKIGEVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIG 161
Cdd:PRK09281 81 DIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 162 RGQRELIIGDRQTGKTAVAIDTILNQKGKDVKCVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPY 241
Cdd:PRK09281 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 242 SGTALAEYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDSLGGGSLTALPIVE 321
Cdd:PRK09281 241 AGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 322 TQEGDVSAYIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAELEAFSQFAS 401
Cdd:PRK09281 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 402 DLDQATQNQLARGKRLREILKQPQYSPLSLENQVGIIFAGTNGYLDKVSIENIPSYITSLTESLKNEKSKFGDVILSTKD 481
Cdd:PRK09281 401 DLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKD 480
|
490
....*....|....*
gi 122233797 482 FTKDEENVLRNILEA 496
Cdd:PRK09281 481 LSDEIEAKLKAAIEE 495
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
4-496 |
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: 816.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 4 IATDEICSLIRYRIQNYNSELKLNNVGVVFKVGDGIVRVFGLQGAMAGELLLFEEGSVGIAFNLEKNNIGVVLLGDCTLI 83
Cdd:TIGR00962 2 LKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 84 QEGMIVKGTGKIGEVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGRG 163
Cdd:TIGR00962 82 REGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 164 QRELIIGDRQTGKTAVAIDTILNQKGKDVKCVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYSG 243
Cdd:TIGR00962 162 QRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 244 TALAEYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDSLGGGSLTALPIVETQ 323
Cdd:TIGR00962 242 CTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIETQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 324 EGDVSAYIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAELEAFSQFASDL 403
Cdd:TIGR00962 322 AGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASDL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 404 DQATQNQLARGKRLREILKQPQYSPLSLENQVGIIFAGTNGYLDKVSIENIPSYITSLTESLKNEKSKFGDVILSTKDFT 483
Cdd:TIGR00962 402 DEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKLT 481
|
490
....*....|...
gi 122233797 484 KDEENVLRNILEA 496
Cdd:TIGR00962 482 EELEAKLKEALKN 494
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
2-496 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 769.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 2 LNIATDEICSLIRYRIQNYNSELKLNNVGVVFKVGDGIVRVFGLQGAMAGELLLFEEGSVGIAFNLEKNNIGVVLLGDCT 81
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 82 LIQEGMIVKGTGKIGEVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIG 161
Cdd:PRK13343 81 DILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 162 RGQRELIIGDRQTGKTAVAIDTILNQKGKDVKCVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPY 241
Cdd:PRK13343 161 RGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 242 SGTALAEYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDSLGGGSLTALPIVE 321
Cdd:PRK13343 241 AGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 322 TQEGDVSAYIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAELEAFSQFAS 401
Cdd:PRK13343 321 TLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 402 DLDQATQNQLARGKRLREILKQPQYSPLSLENQVGIIFAGTNGYLDKVSIENIPSYITSLTESLKNEKSKFGDVILSTKD 481
Cdd:PRK13343 401 LLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRE 480
|
490
....*....|....*
gi 122233797 482 FTKDEENVLRNILEA 496
Cdd:PRK13343 481 LDEAWLAALEEILRE 495
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
7-497 |
0e+00 |
|
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic species, including Methanosarcina barkeri, have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 alpha subunit of this apparent second ATP synthase.
Pssm-ID: 132367 [Multi-domain] Cd Length: 497 Bit Score: 581.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 7 DEICSLIRYRIQNYNSELKLNNVGVVFKVGDGIVRVFGLQGAMAGELLLFEEGSVGIAFNLEKNNIGVVLLGDCTLIQEG 86
Cdd:TIGR03324 6 DKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 87 MIVKGTGKIGEVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGRGQRE 166
Cdd:TIGR03324 86 DEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 167 LIIGDRQTGKTAVAIDTILNQKGKDVKCVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYSGTAL 246
Cdd:TIGR03324 166 LILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 247 AEYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDSLGGGSLTALPIVETQEGD 326
Cdd:TIGR03324 246 GEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 327 VSAYIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAELEAFSQFASDLDQA 406
Cdd:TIGR03324 326 ISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDEN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 407 TQNQLARGKRLREILKQPQYSPLSLENQVGIIFAGTNGYLDKVSIENIPSYITSLTESLKNEKSKFGDVILSTKDFTKDE 486
Cdd:TIGR03324 406 TRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSDED 485
|
490
....*....|.
gi 122233797 487 ENVLRNILEAS 497
Cdd:TIGR03324 486 REQILDIARGA 496
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
95-368 |
0e+00 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 581.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 95 IGEVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGRGQRELIIGDRQT 174
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 175 GKTAVAIDTILNQKGKDVKCVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYSGTALAEYFMYNG 254
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 255 SHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDSLGGGSLTALPIVETQEGDVSAYIPTN 334
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 122233797 335 VISITDGQIFLSSDIFNAGFRPAINVGISVSRVG 368
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
60-457 |
5.02e-119 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 361.28 E-value: 5.02e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 60 SVGIAFNLEKNN-IGVVLLGDCTLIQEGMIVKGTGKIGEVPVGDKFLGRIVDSLANPIdgKGDIVSSQTRLIEPP----- 133
Cdd:PTZ00185 78 AAGLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEV--PVGLLTRSRALLESEqtlgk 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 134 ----APGIVDRRSVYEPLQTGITAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTILNQ--------KGKDVKCVYVAVGQ 201
Cdd:PTZ00185 156 vdagAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 202 KSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYSGTALAEYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRP 281
Cdd:PTZ00185 236 RCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 282 PGREAYPGDVFYLHSRLLERAAKLSDSLGGGSLTALPIVETQEGDVSAYIPTNVISITDGQIFLSSDIFNAGFRPAINVG 361
Cdd:PTZ00185 316 PGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 362 ISVSRVGSAAQPKAMKRVAGKLKLELAQFAELEAFSQFASdldQATQNQLARGKRLREILKQPQysPLSLENQVGIIFAG 441
Cdd:PTZ00185 396 LSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGS---QVQTVPMIRGARFVALFNQKN--PSFFMNALVSLYAC 470
|
410
....*....|....*.
gi 122233797 442 TNGYLDKVSIENIPSY 457
Cdd:PTZ00185 471 LNGYLDDVKVNYAKLY 486
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
150-365 |
2.90e-114 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 335.87 E-value: 2.90e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 150 GITAIDAMIPIGRGQRELIIGDRQTGKTAVAiDTILNQKGKDVkCVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAA 229
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 230 DTTATMQYIAPYSGTALAEYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDsl 309
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKG-- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 122233797 310 GGGSLTALPIVETQEGDVSAYIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVS 365
Cdd:pfam00006 157 KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
103-492 |
1.95e-109 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 334.25 E-value: 1.95e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 103 KFLGRIVDslanpIDGKGDIVSSQTRLIEPP----------APGIVDRRSVYEPLQTGITAIDAMIPIGRGQRELIIGDR 172
Cdd:PRK07165 78 EYFGKIID-----IDGNIIYPEAQNPLSKKFlpntssifnlAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 173 QTGKTAVAIDTILNQKGKDVKCVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAAdTTATMQYIAPYSGTALAEYFMY 252
Cdd:PRK07165 153 QTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPS-TSPYEQYLAPYVAMAHAENISY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 253 NgSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLsdsLGGGSLTALPIVETQEGDVSAYIP 332
Cdd:PRK07165 232 N-DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKF---KNRKTITALPILQTVDNDITSLIS 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 333 TNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAELEAFSQFASDLDQATQNQLA 412
Cdd:PRK07165 308 SNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLF 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 413 RGKRLREILKQPQYSPLSLEnqvgIIFAGTN----GYLDKVS-IENIPSYITSLTESLKNEKSKFgDVILSTKDFtkdEE 487
Cdd:PRK07165 388 KGKMIEKMFNQKGFSLYSYR----FVLLISKliswGLLKDVKdEQKALDFIDYLIENDPDAKKIF-NKIKNNEDV---DD 459
|
....*
gi 122233797 488 NVLRN 492
Cdd:PRK07165 460 ELMKN 464
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
98-367 |
5.74e-105 |
|
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: 314.39 E-value: 5.74e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 98 VPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGRGQRELIIGDRQTGKT 177
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 178 AVAIDTILNQKGKDVK-CVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYSGTALAEYFMYNGSH 256
Cdd:cd19476 82 VLAMQLARNQAKAHAGvVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 257 ALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDslGGGSLTALPIVETQEGDVSAYIPTNVI 336
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNTF 239
|
250 260 270
....*....|....*....|....*....|.
gi 122233797 337 SITDGQIFLSSDIFNAGFRPAINVGISVSRV 367
Cdd:cd19476 240 AILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
376-496 |
4.98e-59 |
|
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: 190.65 E-value: 4.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 376 MKRVAGKLKLELAQFAELEAFSQFASDLDQATQNQLARGKRLREILKQPQYSPLSLENQVGIIFAGTNGYLDKVSIENIP 455
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 122233797 456 SYITSLTESLKNEKSKFGDVILSTKDFTKDEENVLRNILEA 496
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEE 121
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
372-496 |
7.05e-58 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 187.65 E-value: 7.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 372 QPKAMKRVAGKLKLELAQFAELEAFSQFASDLDQATQNQLARGKRLREILKQPQYSPLSLENQVGIIFAGTNGYLDKVSI 451
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 122233797 452 ENIPSYITSLTESLKNEKSKFGDVILSTKDFTKDEENVLRNILEA 496
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEE 125
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
97-367 |
1.76e-49 |
|
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: 170.43 E-value: 1.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 97 EVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGRGQRELIIGDRQTGK 176
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 177 TaVAIDTILNQKGKDVKcVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYSGTALAEYFMYNGSH 256
Cdd:cd01136 81 S-TLLGMIARNTDADVN-VIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 257 ALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDslggGSLTALPIVETQEGDVSAYIPTNVI 336
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----GSITAFYTVLVEGDDFNDPIADEVR 234
|
250 260 270
....*....|....*....|....*....|.
gi 122233797 337 SITDGQIFLSSDIFNAGFRPAINVGISVSRV 367
Cdd:cd01136 235 SILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
30-428 |
1.64e-47 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 170.33 E-value: 1.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 30 GVVFKVGDGIVRVFGLQGAMaGEL--LLFEEGSVGIAFNLEKNNIGVVLL---GDCTLIQEGMIVKGTGKIGEVPVGDKF 104
Cdd:PRK09099 26 GKVVEVIGTLLRVSGLDVTL-GELceLRQRDGTLLQRAEVVGFSRDVALLspfGELGGLSRGTRVIGLGRPLSVPVGPAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 105 LGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGRGQRELIIGDRQTGKTavaidTI 184
Cdd:PRK09099 105 LGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKS-----TL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 185 LNQKGKDVKC---VYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYSGTALAEYFMYNGSHALVVY 261
Cdd:PRK09099 180 MGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 262 DDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAkLSDSlggGSLTALPIVETQEGDVSAYIPTNVISITDG 341
Cdd:PRK09099 260 DSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-MGET---GSITALYTVLAEDESGSDPIAEEVRGILDG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 342 QIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAELEAFSQ---FASDLDQATQNQLARGKRLR 418
Cdd:PRK09099 336 HMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQvgeYRAGSDPVADEAIAKIDAIR 415
|
410
....*....|..
gi 122233797 419 EILKQP--QYSP 428
Cdd:PRK09099 416 DFLSQRtdEYSD 427
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
29-432 |
3.05e-46 |
|
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: 166.74 E-value: 3.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 29 VGVVFKVGDGIVRVFGLQGAMaGELLLFEEGS--------VGIafnlEKNNIGVVLLGDCTLIQEGMIVKGTGKIGEVPV 100
Cdd:COG1157 20 SGRVTRVVGLLIEAVGPDASI-GELCEIETADgrpvlaevVGF----RGDRVLLMPLGDLEGISPGARVVPTGRPLSVPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 101 GDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGRGQReliIGdr---qtGKT 177
Cdd:COG1157 95 GDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR---IGifagsgvGKS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 178 avaidTILNQKGKDVKC-VYVavgqksssIAQV------VT-----TLQDKGaLDYTILVSAAADTTATMQYIAPYSGTA 245
Cdd:COG1157 172 -----TLLGMIARNTEAdVNV--------IALIgergreVRefiedDLGEEG-LARSVVVVATSDEPPLMRLRAAYTATA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 246 LAEYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlsdsLGGGSLTAL-------- 317
Cdd:COG1157 238 IAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN----GGKGSITAFytvlvegd 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 318 ----PIVETqegdvsayiptnVISITDGQIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAEL 393
Cdd:COG1157 314 dmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEEN 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 122233797 394 E------AFsQFASD--LDQAtqnqLARGKRLREILKQPQYSPLSLE 432
Cdd:COG1157 382 EdlirigAY-QPGSDpeLDEA----IALIPAIEAFLRQGMDERVSFE 423
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
30-423 |
1.67e-45 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 164.99 E-value: 1.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 30 GVVFKVGDGIVRVfGLQGAMAGELLLFE-EGSVGIAFNLEKNNIGVVLLGDCTLIQEGMIVKGTGKIGEVPVGDKFLGRI 108
Cdd:PRK06820 31 GPIVEIGPTLLRA-SLPGVAQGELCRIEpQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 109 VDSLANPIDGkGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGRGQRELIIGDRQTGKTAVaIDTILNQK 188
Cdd:PRK06820 110 LDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTL-LGMLCADS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 189 GKDVkCVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYSGTALAEYFMYNGSHALVVYDDLSKQA 268
Cdd:PRK06820 188 AADV-MVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 269 QAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlSDSlggGSLTALPIVETQEGDVSAYIPTNVISITDGQIFLSSD 348
Cdd:PRK06820 267 RAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGN-SDR---GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRR 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 122233797 349 IFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAELEAFSQ---FASDLDQATQNQLARGKRLREILKQ 423
Cdd:PRK06820 343 LAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRvgeYQAGEDLQADEALQRYPAICAFLQQ 420
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
77-435 |
5.43e-45 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 163.38 E-value: 5.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 77 LGDCTLIQEGMIVKGTGKIGEVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDA 156
Cdd:PRK06936 76 LGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 157 MIPIGRGQRELIIGDRQTGKTAVaIDTILNQKGKDVkCVYVAVGQKSSSIAQVVTtlQDKGA--LDYTILVSAAADTTAT 234
Cdd:PRK06936 156 LLTCGEGQRMGIFAAAGGGKSTL-LASLIRSAEVDV-TVLALIGERGREVREFIE--SDLGEegLRKAVLVVATSDRPSM 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 235 MQYIAPYSGTALAEYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlSDSlggGSL 314
Cdd:PRK06936 232 ERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ-SDK---GSI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 315 TALPIVETQEGDVSAYIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAELE 394
Cdd:PRK06936 308 TALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVE 387
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 122233797 395 AFSQ---FASDLDQATQNQLARGKRLREILKQPQYSPLSLENQV 435
Cdd:PRK06936 388 LLLQigeYQKGQDKEADQAIERIGAIRGFLRQGTHELSHFNETL 431
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
83-444 |
1.39e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 151.41 E-value: 1.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 83 IQEGMIVKGTGKIGEVPVGDKFLGRIVDSLANPIDG----KGDIVSSQTRliEPPAPgiVDRRSVYEPLQTGITAIDAMI 158
Cdd:PRK07721 78 IAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGsalpKGLAPVSTDQ--DPPNP--LKRPPIREPMEVGVRAIDSLL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 159 PIGRGQRELIIGDRQTGKTAVaIDTILNQKGKDVKcVYVAVGQKSSSIAQVVTtlQDKGA--LDYTILVSAAADTTATMQ 236
Cdd:PRK07721 154 TVGKGQRVGIFAGSGVGKSTL-MGMIARNTSADLN-VIALIGERGREVREFIE--RDLGPegLKRSIVVVATSDQPALMR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 237 YIAPYSGTALAEYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsdSLGGGSLTA 316
Cdd:PRK07721 230 IKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG----TNASGSITA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 317 LPIVETQEGDVSAYIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAELE-- 394
Cdd:PRK07721 306 FYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEdl 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 122233797 395 ----AFSQFAS-DLDQATQNQlargKRLREILKQPQYSPLSLENQVGIIFAGTNG 444
Cdd:PRK07721 386 inigAYKRGSSrEIDEAIQFY----PQIISFLKQGTDEKATFEESIQALLSLFGK 436
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
97-381 |
2.66e-39 |
|
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: 143.90 E-value: 2.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 97 EVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGRGQRELIIGD----- 171
Cdd:cd01135 3 KLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGsglph 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 172 --------RQTGktavaidtiLNQKGKDVKCVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYSG 243
Cdd:cd01135 83 nelaaqiaRQAG---------VVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 244 TALAEYFMY-NGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSDSlgGGSLTALPI 319
Cdd:cd01135 154 LTTAEYLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPI 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 122233797 320 VETQEGDVSAYIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVgsaaqpkaMKRVAG 381
Cdd:cd01135 229 LTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRL--------MKSGIG 282
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
98-379 |
4.34e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 147.54 E-value: 4.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 98 VPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGRGQR-----------E 166
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRmglfagsgvgkS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 167 LIIGDRQTGKTA-VAIDTILNQKGKDVKcvyvavgqksSSIAQVvttLQDKGaLDYTILVSAAADTTATMQYIAPYSGTA 245
Cdd:PRK08972 177 VLLGMMTRGTTAdVIVVGLVGERGREVK----------EFIEEI---LGEEG-RARSVVVAAPADTSPLMRLKGCETATT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 246 LAEYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDslGGGSLTALPIVETQEG 325
Cdd:PRK08972 243 IAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVLTEGD 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 122233797 326 DVSAYIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVG----SAAQPKAMKRV 379
Cdd:PRK08972 321 DLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMpmviSEEHLEAMRRV 378
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
98-423 |
4.85e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 144.06 E-value: 4.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 98 VPVGDKFLGRIVDSLANPIDGKGDI-VSSQTRLIEPPAP----GIVDrrsvyEPLQTGITAIDAMIPIGRGQRELIIGDR 172
Cdd:PRK08472 92 IPVGRNLLGRVVDPLGRPIDGKGAIdYERYAPIMKAPIAamkrGLID-----EVFSVGVKSIDGLLTCGKGQKLGIFAGS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 173 QTGKTAVaIDTILNQKGKDVKCVYVaVGQKSSSIAQVVTTlQDKGALDYTILVSAAADTTATMQYIAPYSGTALAEYFMY 252
Cdd:PRK08472 167 GVGKSTL-MGMIVKGCLAPIKVVAL-IGERGREIPEFIEK-NLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 253 NGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlsdSLGGGSLTALPIVETQEGDVSAYIP 332
Cdd:PRK08472 244 QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTVLVEGDDMSDPIA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 333 TNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAELEAFSQFAS-------DLDQ 405
Cdd:PRK08472 321 DQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAyqkgndkELDE 400
|
330
....*....|....*...
gi 122233797 406 AtqnqLARGKRLREILKQ 423
Cdd:PRK08472 401 A----ISKKEFMEQFLKQ 414
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
96-423 |
7.55e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 140.80 E-value: 7.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 96 GEVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGRGQRELIIGDRQTG 175
Cdd:PRK07196 88 GELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 176 KTaVAIDTILNQKGKDVKCVYVaVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYSGTALAEYFMYNGS 255
Cdd:PRK07196 168 KS-VLLGMITRYTQADVVVVGL-IGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGH 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 256 HALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsDSLGGGSLTALPIVETQEGDVSAYIPTNV 335
Cdd:PRK07196 246 DVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQDPIVDCA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 336 ISITDGQIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAE---LEAFSQFASDLDQATQNQLA 412
Cdd:PRK07196 323 RAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAikpLIPLGGYVAGADPMADQAVH 402
|
330
....*....|.
gi 122233797 413 RGKRLREILKQ 423
Cdd:PRK07196 403 YYPAITQFLRQ 413
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
30-394 |
1.03e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 140.47 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 30 GVVFKVGDGIVRVFgLQGAMAGELL-LFEEGSVGIAFNLEKNNIGVVLLGDCTLIQEGMIVKGTGKIGEVPVGDKFLGRI 108
Cdd:PRK07594 23 GRIQDVSATLLNAW-LPGVFMGELCcIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 109 VDSLANPIDGKGDIVSSQTRLIEPPAPGIVdRRSVYEPLQTGITAIDAMIPIGRGQRELIIGDRQTGKTAVaIDTILNQK 188
Cdd:PRK07594 102 IDGFGRPLDGRELPDVCWKDYDAMPPPAMV-RQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLCNAP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 189 GKDVKcVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYSGTALAEYFMYNGSHALVVYDDLSKQA 268
Cdd:PRK07594 180 DADSN-VLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 269 QAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsdsLGG-GSLTALPIVETQEGDVSAYIPTNVISITDGQIFLSS 347
Cdd:PRK07594 259 RAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSR 333
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 122233797 348 DIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAELE 394
Cdd:PRK07594 334 RLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVE 380
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
76-425 |
9.07e-36 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 137.82 E-value: 9.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 76 LLGDCTLIQEGMIVKGTGKIGEVPVGDKFLGRIVDSLANPIDGKGDIVSSQT----RLIEPPAPGIVDRRSVYEPLQTGI 151
Cdd:PRK08149 60 LIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVGPiseeRVIDVAPPSYAERRPIREPLITGV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 152 TAIDAMIPIGRGQRELIIGDRQTGKTAVaIDTILNQKGKDVkCVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADT 231
Cdd:PRK08149 140 RAIDGLLTCGVGQRMGIFASAGCGKTSL-MNMLIEHSEADV-FVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 232 TATMQYIAPYSGTALAEYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDslgg 311
Cdd:PRK08149 218 SSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA---- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 312 GSLTALPIVETQEGDVSAYIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFA 391
Cdd:PRK08149 294 GSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLE 373
|
330 340 350
....*....|....*....|....*....|....*..
gi 122233797 392 ELEAFSQFAS-DLDQATQNQLARGKR--LREILKQPQ 425
Cdd:PRK08149 374 ELQLFIDLGEyRRGENADNDRAMDKRpaLEAFLKQDV 410
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
54-420 |
1.14e-35 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 138.04 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 54 LLFEEGSVGIAFNlEKNNI---------GVVLL--GDCTLIQ----------EGMIVKGTGKIGEVPVGDKFLGRIVDSL 112
Cdd:PRK04196 14 LLFVEGVEGVAYG-EIVEIelpngekrrGQVLEvsEDKAVVQvfegttgldlKDTKVRFTGEPLKLPVSEDMLGRIFDGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 113 ANPIDGKGDIVSSQTRLI--EPPAPgiVDRRSVYEPLQTGITAIDAMIPIGRGQR------------ELiigdrqtgktA 178
Cdd:PRK04196 93 GRPIDGGPEIIPEKRLDIngAPINP--VAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnEL----------A 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 179 VAIDTILNQKGKDVK--CVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYSGTALAEYFMYN-GS 255
Cdd:PRK04196 161 AQIARQAKVLGEEENfaVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFEkGM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 256 HALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSDSlgGGSLTALPIVETQEGDVSAYIP 332
Cdd:PRK04196 241 HVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHPIP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 333 TNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVgsaaqpkaMKRVAGKLKlelaqfaeleafsqfASDLDQATQNQL- 411
Cdd:PRK04196 316 DLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRL--------MKDGIGEGK---------------TREDHKDVANQLy 372
|
410
....*....|..
gi 122233797 412 ---ARGKRLREI 420
Cdd:PRK04196 373 aayARGKDLREL 384
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
83-444 |
1.18e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 132.16 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 83 IQEGMIVKGTGKIGEVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGR 162
Cdd:PRK05688 88 IAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 163 GQRELIIGDRQTGKTaVAIDTILNQKGKDVKCVYVaVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYS 242
Cdd:PRK05688 168 GQRLGLFAGTGVGKS-VLLGMMTRFTEADIIVVGL-IGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 243 GTALAEYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDSLGGGSLTALPIVET 322
Cdd:PRK05688 246 CTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 323 QEGDVSAYIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVgsaaqpkaMKRVAGKLKLELAQ-FAELEAFSQFAS 401
Cdd:PRK05688 324 EGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV--------MPQVVDPEHLRRAQrFKQLWSRYQQSR 395
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 122233797 402 DL----------DQATQNQLARGKRLREILKQPQYSPLSL---ENQVGIIFAGTNG 444
Cdd:PRK05688 396 DLisvgayvaggDPETDLAIARFPHLVQFLRQGLRENVSLaqsREQLAAIFAPAAG 451
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
106-432 |
2.19e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 131.66 E-value: 2.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 106 GRIVDSLANPIDGKGDIVS-SQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGRGQRELIIGDRQTGKTavaidTI 184
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKS-----TL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 185 LNQ--KGKDVKCVYVA-VGQKSSSIAQVVT-TLQDkgALDYTILVSAAADTTATMQYIAPYSGTALAEYFMYNGSHALVV 260
Cdd:PRK06002 182 LAMlaRADAFDTVVIAlVGERGREVREFLEdTLAD--NLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 261 YDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDslGGGSLTALPIVETQEGDVSAYIPTNVISITD 340
Cdd:PRK06002 260 VDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLVDGDDHNDPVADSIRGTLD 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 341 GQIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAE---LEAFSQFA----SDLDQAtqnqLAR 413
Cdd:PRK06002 338 GHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdLRLIGGYRagsdPDLDQA----VDL 413
|
330
....*....|....*....
gi 122233797 414 GKRLREILKQPQYSPLSLE 432
Cdd:PRK06002 414 VPRIYEALRQSPGDPPSDD 432
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
96-394 |
1.02e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 118.16 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 96 GEVPVGDKFLGRIVDSLANPIDGKGDI----VSSQTRLIEPPAPGivdRRSVYEPLQTGITAIDAMIPIGRGQRELIIGD 171
Cdd:PRK08927 90 AAVRPSRAWLGRVVNALGEPIDGKGPLpqgpVPYPLRAPPPPAHS---RARVGEPLDLGVRALNTFLTCCRGQRMGIFAG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 172 RQTGKTavaidTILNQKGKDVKC---VYVAVGQKSSSIAQVVT-TLQDKGaLDYTILVSAAADTTATMQYIAPYSGTALA 247
Cdd:PRK08927 167 SGVGKS-----VLLSMLARNADAdvsVIGLIGERGREVQEFLQdDLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAIA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 248 EYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDSLGGGSLTALPIVETQEGDV 327
Cdd:PRK08927 241 EYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVDGDDH 318
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 122233797 328 SAYIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAELE 394
Cdd:PRK08927 319 NEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADME 385
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
90-370 |
5.21e-28 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 116.04 E-value: 5.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 90 KGTGKigEVPVGDKFLGRIVDSLANPIDG-KGDIVSSQTRLIEPP-APgiVDRRSVYEPLQTGITAIDAMIPIGRGQREL 167
Cdd:PRK07960 104 LQSGK--QLPLGPALLGRVLDGSGKPLDGlPAPDTGETGALITPPfNP--LQRTPIEHVLDTGVRAINALLTVGRGQRMG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 168 IIGDRQTGKTaVAIDTILNQKGKDVKCVYVaVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYSGTALA 247
Cdd:PRK07960 180 LFAGSGVGKS-VLLGMMARYTQADVIVVGL-IGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 248 EYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDslGGGSLTALPIVETQEGDV 327
Cdd:PRK07960 258 EDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGDDQ 335
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 122233797 328 SAYIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVGSA 370
Cdd:PRK07960 336 QDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTA 378
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
92-378 |
6.83e-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: 115.97 E-value: 6.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 92 TGKIGEVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLI--EPPAPgivdRRSVY--EPLQTGITAIDAMIPIGRGQREL 167
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDIngQPINP----YARIYpeEMIQTGISAIDVMNSIARGQKIP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 168 IIGD-------------RQTGKTAVAIDTILNQKGKDVKCVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTAT 234
Cdd:TIGR01040 146 IFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 235 MQYIAPYSGTALAEYFMYN-GSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDSlgGGS 313
Cdd:TIGR01040 226 ERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR--NGS 303
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 122233797 314 LTALPIVETQEGDVSAYIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKR 378
Cdd:TIGR01040 304 ITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTR 368
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
28-94 |
1.61e-26 |
|
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: 101.76 E-value: 1.61e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 122233797 28 NVGVVFKVGDGIVRVFGLQGAMAGELLLFEEGSVGIAFNLEKNNIGVVLLGDCTLIQEGMIVKGTGK 94
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
98-435 |
2.69e-26 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 111.15 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 98 VPVGDKFLGRIVDSLANPIDGKGDIVSSQTR-LIEPPaPGIVDRRSVYEPLQTGITAIDAMIPIGRGQRELIIGDRQTGK 176
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKpLFSSP-PSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 177 TAVaIDTILNQKGKDVKcVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYSGTALAEYFMYNGSH 256
Cdd:PRK05922 171 SSL-LSTIAKGSKSTIN-VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 257 ALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlSDSlggGSLTALPIVetqegdvsAYIPTN-- 334
Cdd:PRK05922 249 VLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-NDK---GSITALYAI--------LHYPNHpd 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 335 -----VISITDGQIFLSSdIFNAGFRPAINVGISVSRVGSA-AQPK---AMKRVAGKLKL--ELAQFAELEAFSQ-FASD 402
Cdd:PRK05922 317 iftdyLKSLLDGHFFLTP-QGKALASPPIDILTSLSRSARQlALPHhyaAAEELRSLLKAyhEALDIIQLGAYVPgQDAH 395
|
330 340 350
....*....|....*....|....*....|...
gi 122233797 403 LDQATQNQlargKRLREILKQPQYSPLSLENQV 435
Cdd:PRK05922 396 LDRAVKLL----PSIKQFLSQPLSSYCALHNTL 424
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
83-424 |
3.62e-25 |
|
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: 107.88 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 83 IQEGMIVKGTGKIGEVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGR 162
Cdd:TIGR01039 63 LVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 163 GQRELIIGDRQTGKTAVAIDTILN-QKGKDVKCVYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPY 241
Cdd:TIGR01039 143 GGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVAL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 242 SGTALAEYFM-YNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsdSLGGGSLTALPIV 320
Cdd:TIGR01039 223 TGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERIT----STKTGSITSVQAV 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 321 ETQEGDVSAYIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVgsaAQPKAMK----RVAGKLKLELAQFAELEAF 396
Cdd:TIGR01039 299 YVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRL---LDPSVVGeehyDVARGVQQILQRYKELQDI 375
|
330 340 350
....*....|....*....|....*....|...
gi 122233797 397 SQF-----ASDLDQATqnqLARGKRLREILKQP 424
Cdd:TIGR01039 376 IAIlgmdeLSEEDKLT---VERARRIQRFLSQP 405
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
98-396 |
2.97e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 101.98 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 98 VPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGRGQRELIIGDRQTGKT 177
Cdd:PRK06793 91 IPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 178 avaidTILNQKGKDVKC---VYVAVGQKSSSIAQVVTTLQDKGALDYTILVSAAADTTATMQYIAPYSGTALAEYFMYNG 254
Cdd:PRK06793 171 -----TLLGMIAKNAKAdinVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 255 SHALVVYDDLSKQAQAYREMSLLLRRPPgreaYPGDVFYLHS---RLLERAAKLSDslggGSLTALPIVETQEGDVSAYI 331
Cdd:PRK06793 246 NNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK----GSITGIYTVLVDGDDLNGPV 317
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 122233797 332 PTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRVGSAAQPKAMKRVAGKLKLELAQFAELEAF 396
Cdd:PRK06793 318 PDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELY 382
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
376-443 |
7.64e-19 |
|
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: 80.57 E-value: 7.64e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 376 MKRVAGKLKLELAQFAELEAFSQFASD--LDQATQNQLARGKRLREILKQPQYSPLSLENQVGIIFAGTN 443
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
97-367 |
1.14e-18 |
|
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: 86.12 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 97 EVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGRGQRELIIGDRQTGK 176
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 177 TAVAIDTILN-QKGKDVKCVYVAVGQKSSS----IAQVVTT-LQDKGALDYTILVSAAADTTATMQYIAPYSGTALAEYF 250
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGERTREgndlYHEMKESgVINLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 251 M-YNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsdSLGGGSLTALPIVETQEGDVSA 329
Cdd:cd01133 161 RdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERIT----STKKGSITSVQAVYVPADDLTD 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 122233797 330 YIPTNVISITDGQIFLSSDIFNAGFRPAINVGISVSRV 367
Cdd:cd01133 237 PAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
97-366 |
1.60e-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: 85.70 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 97 EVPVGDKFLGRIVDSLANPID----------GKGdiVSSQTRLIEPPAPgIVDRRSVYEPLQTGITAIDAMIPIGRGQRE 166
Cdd:cd01134 3 SVELGPGLLGSIFDGIQRPLEviaetgsifiPRG--VNVQRWPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 167 LIIGDRQTGKTavaidtILNQ---KGKDVKCV-YVAVGQKSSSIAQVVT---TLQD----KGALDYTILVSaaadTTATM 235
Cdd:cd01134 80 AIPGPFGCGKT------VISQslsKWSNSDVViYVGCGERGNEMAEVLEefpELKDpitgESLMERTVLIA----NTSNM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 236 QYIAP----YSGTALAEYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSdS 308
Cdd:cd01134 150 PVAAReasiYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYERAGRVR-C 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 122233797 309 LGG----GSLTALPIVETQEGDVSAYIPTNVISITdgQIF--LSSDIFNAGFRPAINVGISVSR 366
Cdd:cd01134 226 LGSpgreGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
89-348 |
7.42e-17 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 82.77 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 89 VKGTGKIGEVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEP---PAPGIVDRRSVyeplQTGITAIDAMIPIGRGQR 165
Cdd:PRK02118 67 VVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGEPIEIGGPsvnPVKRIVPREMI----RTGIPMIDVFNTLVESQK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 166 ELIIGDRQTGKTAVAIdTILNQKGKDVkCVYVAVGQKSSSIAQVVTTLQDKGALDYTIL-VSAAADTTATMQYIaPYSGT 244
Cdd:PRK02118 143 IPIFSVSGEPYNALLA-RIALQAEADI-IILGGMGLTFDDYLFFKDTFENAGALDRTVMfIHTASDPPVECLLV-PDMAL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 245 ALAEYFMYNGS-HALVVYDDLSKQAQAYREMSLLLRRPPGREAYPGDvfyLHSRLLERAAKLSDSLGGGSLTALPIVETQ 323
Cdd:PRK02118 220 AVAEKFALEGKkKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMP 296
|
250 260
....*....|....*....|....*
gi 122233797 324 EGDVSAYIPTNVISITDGQIFLSSD 348
Cdd:PRK02118 297 GDDVTHPVPDNTGYITEGQFYLRRG 321
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
86-163 |
4.03e-15 |
|
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: 77.44 E-value: 4.03e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 122233797 86 GMIVKGTGKIGEVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVDRRSVYEPLQTGITAIDAMIPIGRG 163
Cdd:COG0055 69 GMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKG 146
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
145-328 |
5.69e-11 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 64.80 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 145 EPLQTGITAIDAMIPIGRGQRELIIGDRQTGKTavaidtILNQ---KGKDVKCV-YVAVGQKSSSIAQVVTT---LQD-- 215
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT------VTQHqlaKWADADIViYVGCGERGNEMTEVLEEfpeLIDpk 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 216 --KGALDYTILVSaaadTTATMqyiaP--------YSGTALAEYFMYNGSHALVVYDDLSKQAQAYREMSLLLRRPPGRE 285
Cdd:PRK04192 283 tgRPLMERTVLIA----NTSNM----PvaareasiYTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEE 354
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 122233797 286 AYPGdvfYLHSRL---LERAAKLSdSLGG--GSLTALPIVETQEGDVS 328
Cdd:PRK04192 355 GYPA---YLASRLaefYERAGRVK-TLGGeeGSVTIIGAVSPPGGDFS 398
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
195-372 |
1.13e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 64.27 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 195 VYVAVGQKSSSIAQVVT---TLQD----KGALDYTILVSAAADTTATMQYIAPYSGTALAEYFMYNGSHALVVYDDLSKQ 267
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEefpKLKDpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 268 AQAYREMSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKLSDSLGGGSLTALPIVETQEGDVSAYIPTNVISITDG 341
Cdd:PRK14698 766 AEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKV 842
|
170 180 190
....*....|....*....|....*....|.
gi 122233797 342 QIFLSSDIFNAGFRPAINVGISVSRVGSAAQ 372
Cdd:PRK14698 843 FWALDADLARRRHFPAINWLTSYSLYVDAVK 873
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
83-186 |
3.79e-10 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 61.98 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122233797 83 IQEGMIVKGTGKIGEVPVGDKFLGRIVDSLANPIDGKGDIVSSQTRLIEPPAPGIVD---RRSVYEplqTGITAIDAMIP 159
Cdd:CHL00060 81 LMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQldtKLSIFE---TGIKVVDLLAP 157
|
90 100
....*....|....*....|....*..
gi 122233797 160 IGRGQRELIIGDRQTGKTAVAIDTILN 186
Cdd:CHL00060 158 YRRGGKIGLFGGAGVGKTVLIMELINN 184
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
29-93 |
1.10e-09 |
|
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: 54.47 E-value: 1.10e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 122233797 29 VGVVFKVGDGIVRVFGLQGAMAGELLLFEEGSVGIAFNLEKNNIGVVLLGDCTLIQEGMIVKGTG 93
Cdd:pfam02874 5 IGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
30-94 |
1.13e-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: 37.68 E-value: 1.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 122233797 30 GVVFKVGDGIVRVFGLQGAMAGELLLFEEGSV-------GIAFNLEKNNIGVVLLGDCTLIQEGMIVKGTGK 94
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIGEVCEIERGDGnnetvlkAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| |
