|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
3-511 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 998.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 3 QLNPSEISEIIKGRIEKLDVASQARNEGTIVSVSDGIVRIYGLADVMYGEMIEFPGGVYGMALNLEQDSVGAVVLGEYQG 82
Cdd:PRK09281 2 QINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 83 LAEGMNAKCTGRILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGR 162
Cdd:PRK09281 82 IKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 163 GQRELIIGDRQIGKTALAVDAIINQKDSGIKCVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPYS 242
Cdd:PRK09281 162 GQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 243 GCTMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASRVSEEyvekftngavtGKT 322
Cdd:PRK09281 242 GCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDE-----------LGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 323 GSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIRTALAQYR 402
Cdd:PRK09281 311 GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 403 ELAAFAQFASDLDEATRKQLEHGQRVTELMKQKQYAPMSIAEMSLSLYAAERGFLQDVEIAKVGSFEQALISYFQREHAA 482
Cdd:PRK09281 391 ELEAFAQFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHAD 470
|
490 500
....*....|....*....|....*....
gi 15600749 483 LLAKINEKGDFNDEIDAGIKAGIEKFKAT 511
Cdd:PRK09281 471 LLEEIRETKDLSDEIEAKLKAAIEEFKKT 499
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
3-514 |
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: 981.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 3 QLNPSEISEIIKGRIEKLDVASQARNEGTIVSVSDGIVRIYGLADVMYGEMIEFPGGVYGMALNLEQDSVGAVVLGEYQG 82
Cdd:COG0056 2 QIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 83 LAEGMNAKCTGRILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGR 162
Cdd:COG0056 82 IKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 163 GQRELIIGDRQIGKTALAVDAIINQKDSGIKCVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPYS 242
Cdd:COG0056 162 GQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 243 GCTMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASRVSEEYvekftngavtgKT 322
Cdd:COG0056 242 GCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEL-----------GG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 323 GSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIRTALAQYR 402
Cdd:COG0056 311 GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 403 ELAAFAQFASDLDEATRKQLEHGQRVTELMKQKQYAPMSIAEMSLSLYAAERGFLQDVEIAKVGSFEQALISYFQREHAA 482
Cdd:COG0056 391 ELEAFAQFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPD 470
|
490 500 510
....*....|....*....|....*....|..
gi 15600749 483 LLAKINEKGDFNDEIDAGIKAGIEKFKATQTW 514
Cdd:COG0056 471 LLKEIRETGKLDDEIEEKLKAAIEEFKKTFAA 502
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
3-514 |
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: 860.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 3 QLNPSEISEIIKGRIEKLDVASQARNEGTIVSVSDGIVRIYGLADVMYGEMIEFPGGVYGMALNLEQDSVGAVVLGEYQG 82
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 83 LAEGMNAKCTGRILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGR 162
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 163 GQRELIIGDRQIGKTALAVDAIINQKDSGIKCVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPYS 242
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 243 GCTMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASRVSEEyvekftNGAvtgkt 322
Cdd:TIGR00962 241 GCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDE------KGG----- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 323 GSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIRTALAQYR 402
Cdd:TIGR00962 310 GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 403 ELAAFAQFASDLDEATRKQLEHGQRVTELMKQKQYAPMSIAEMSLSLYAAERGFLQDVEIAKVGSFEQALISYFQREHAA 482
Cdd:TIGR00962 390 ELEAFSQFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPD 469
|
490 500 510
....*....|....*....|....*....|..
gi 15600749 483 LLAKINEKGDFNDEIDAGIKAGIEKFKATQTW 514
Cdd:TIGR00962 470 ILEEINTTKKLTEELEAKLKEALKNFKKTFAW 501
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
3-514 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 759.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 3 QLNPSEISEIIKGRIEKLDVASQARNEGTIVSVSDGIVRIYGLADVMYGEMIEFPGGVYGMALNLEQDSVGAVVLGEYQG 82
Cdd:PRK13343 2 KSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 83 LAEGMNAKCTGRILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGR 162
Cdd:PRK13343 82 ILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 163 GQRELIIGDRQIGKTALAVDAIINQKDSGIKCVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPYS 242
Cdd:PRK13343 162 GQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 243 GCTMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASRVSEEYvekftngavtgKT 322
Cdd:PRK13343 242 GCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPEL-----------GG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 323 GSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIRTALAQYR 402
Cdd:PRK13343 311 GSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 403 ELAAFAQFASDLDEATRKQLEHGQRVTELMKQKQYAPMSIAEMSLSLYAAERGFLQDVEIAKVGSFEQALISYFQREHAA 482
Cdd:PRK13343 391 ELEAFTRFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAA 470
|
490 500 510
....*....|....*....|....*....|..
gi 15600749 483 LLAKINEKGDFNDEIDAGIKAGIEKFKATQTW 514
Cdd:PRK13343 471 LSLALESPRELDEAWLAALEEILREAGERFAA 502
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
28-512 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 673.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 28 NEGTIVSVSDGIVRIYGLADVMYGEMIEFPGGVYGMALNLEQDSVGAVVLGEYQGLAEGMNAKCTGRILEVPVGPELLGR 107
Cdd:CHL00059 6 NTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 108 VVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQRELIIGDRQIGKTALAVDAIINQ 187
Cdd:CHL00059 86 VVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 188 KDSGIKCVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPYSGCTMGEYFRDRGEDALIVYDDLSKQ 267
Cdd:CHL00059 166 KGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 268 AVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASRVSEEYVEkftngavtgktGSLTALPIIETQAGDVSAFVPTNVI 347
Cdd:CHL00059 246 AQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGE-----------GSMTALPIVETQAGDVSAYIPTNVI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 348 SITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAAFAQFASDLDEATRKQLEHGQR 427
Cdd:CHL00059 315 SITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 428 VTELMKQKQYAPMSIAEMSLSLYAAERGFLQDVEIAKVGSFEQALISYFQREHAALLAKINEKGDFNDEIDAGIKAGIEK 507
Cdd:CHL00059 395 LRELLKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQE 474
|
....*
gi 15600749 508 FKATQ 512
Cdd:CHL00059 475 QLELF 479
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
95-379 |
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: 530.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 95 ILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQRELIIGDRQI 174
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 175 GKTALAVDAIINQKDSGIKCVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPYSGCTMGEYFRDRG 254
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 255 EDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASRVSEEYvekftngavtgKTGSLTALPIIETQ 334
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEL-----------GGGSLTALPIIETQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15600749 335 AGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRVG 379
Cdd:cd01132 230 AGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
9-496 |
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: 529.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 9 ISEIIKGRIEKLDVASQA-------RNEGTIVSVSDGIVRIYGLADVMYGEMIEFPGGVYGMALNLEQDSVGAVVLGEYQ 81
Cdd:TIGR03324 1 LTEVLDKAFQQLDQARESfqpqltvQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 82 GLAEGMNAKCTGRILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVG 161
Cdd:TIGR03324 81 HLQAGDEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 162 RGQRELIIGDRQIGKTALAVDAIINQKDSGIKCVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPY 241
Cdd:TIGR03324 161 RGQRELILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 242 SGCTMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASRVSEEYvekftngavtgK 321
Cdd:TIGR03324 241 AATSIGEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEEL-----------G 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 322 TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIRTALAQY 401
Cdd:TIGR03324 310 GGSLTALPIIETEAQNISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 402 RELAAFAQFASDLDEATRKQLEHGQRVTELMKQKQYAPMSIAEMSLSLYAAERGFLQDVEIAKVGSFEQALISYFQREHA 481
Cdd:TIGR03324 390 EELETFARFGARLDENTRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPA 469
|
490
....*....|....*
gi 15600749 482 ALLAKINEKGDFNDE 496
Cdd:TIGR03324 470 DLRERLQSGKKLSDE 484
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
62-473 |
1.52e-108 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 334.70 E-value: 1.52e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 62 GMALNLEQDS-VGAVVLGEYQGLAEGMNAKCTGRILEVPVGPELLGRVVDALGNPID------GKGPIDAKAT-DAVEKV 133
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQTlGKVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 134 APGVIWRKSVDQPVQTGYKSVDAMIPVGRGQRELIIGDRQIGKTALAVDAIINQ--------KDSGIKCVYVAIGQKQST 205
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 206 IANVVRKLEENGALANTIVVAASASESAALQYLAPYSGCTMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGRE 285
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGRE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 286 AYPGDVFYLHSRLLERASRVSeeyvekftngavTGK-TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSG 364
Cdd:PTZ00185 320 AYPGDVFYLHSRLLERAAMLS------------PGKgGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 365 IRPAVNAGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAAFAQFASDLDEATrkqLEHGQRVTELMKQKQyaPMSIAE 444
Cdd:PTZ00185 388 QRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMN 462
|
410 420
....*....|....*....|....*....
gi 15600749 445 MSLSLYAAERGFLQDVEIAKVGSFEQALI 473
Cdd:PTZ00185 463 ALVSLYACLNGYLDDVKVNYAKLYEYLLV 491
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
103-497 |
5.14e-103 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 318.07 E-value: 5.14e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 103 ELLGRVVDALGNPIDGKGPIDAKATD-----AVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQRELIIGDRQIGKT 177
Cdd:PRK07165 78 EYFGKIIDIDGNIIYPEAQNPLSKKFlpntsSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 178 ALAVDAIINQKDSGIKCVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAAlQYLAPYSGCTMGE---YFrdrg 254
Cdd:PRK07165 158 HIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAEnisYN---- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 255 EDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASrvseeyveKFTNGAvtgktgSLTALPIIETQ 334
Cdd:PRK07165 233 DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAG--------KFKNRK------TITALPILQTV 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 335 AGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAAFAQFASDL 414
Cdd:PRK07165 299 DNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 415 DEATRKQLEHGQRVTELMKQKQYAPMSIAEMSLSLYAAERGFLQDV-EIAKVGSFEQALISYFQrEHAALLAKINEKGDF 493
Cdd:PRK07165 379 NKETSDLLFKGKMIEKMFNQKGFSLYSYRFVLLISKLISWGLLKDVkDEQKALDFIDYLIENDP-DAKKIFNKIKNNEDV 457
|
....
gi 15600749 494 NDEI 497
Cdd:PRK07165 458 DDEL 461
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
150-376 |
4.10e-102 |
|
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: 305.43 E-value: 4.10e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 150 GYKSVDAMIPVGRGQRELIIGDRQIGKTALAvDAIINQKDSGIkCVYVAIGQKQSTIANVVRKLEENGALANTIVVAASA 229
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 230 SESAALQYLAPYSGCTMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAsrvseey 309
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERA------- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600749 310 vekftnGAVTGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVS 376
Cdd:pfam00006 152 ------GRVKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
98-378 |
8.50e-102 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 306.69 E-value: 8.50e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 98 VPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQRELIIGDRQIGKT 177
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 178 ALAVDAIINQ-KDSGIKCVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPYSGCTMGEYFRDRGED 256
Cdd:cd19476 82 VLAMQLARNQaKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 257 ALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASRVseeyvekftngaVTGKtGSLTALPIIETQAG 336
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKV------------KDGG-GSITAIPAVSTPGD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15600749 337 DVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRV 378
Cdd:cd19476 229 DLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
387-511 |
2.27e-61 |
|
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: 197.20 E-value: 2.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 387 IKKLSGGIRTALAQYRELAAFAQFASDLDEATRKQLEHGQRVTELMKQKQYAPMSIAEMSLSLYAAERGFLQDVEIAKVG 466
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15600749 467 SFEQALISYFQREHAALLAKINEKGDFNDEIDAGIKAGIEKFKAT 511
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKS 125
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
383-508 |
4.71e-60 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 193.81 E-value: 4.71e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 383 QTKIIKKLSGGIRTALAQYRELAAFAQFASDLDEATRKQLEHGQRVTELMKQKQYAPMSIAEMSLSLYAAERGFLQDVEI 462
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15600749 463 AKVGSFEQALISYFQREHAALLAKINEKGDFNDEIDAGIKAGIEKF 508
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
19-420 |
1.93e-43 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 159.55 E-value: 1.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 19 KLDVASQARNEGTIVSVSDGIVRIYGLaDVMYGEMIEFPGG---------VYGMALNLEQDSVgavvLGEYQGLAEGMNA 89
Cdd:PRK09099 15 ELAALPAVRRTGKVVEVIGTLLRVSGL-DVTLGELCELRQRdgtllqraeVVGFSRDVALLSP----FGELGGLSRGTRV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 90 KCTGRILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQRELII 169
Cdd:PRK09099 90 IGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 170 GDRQIGKTALavdaiINQKDSGIKC---VYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPYSGCTM 246
Cdd:PRK09099 170 APAGVGKSTL-----MGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 247 GEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASRvseeyvekftngavtGKTGSLT 326
Cdd:PRK09099 245 AEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM---------------GETGSIT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 327 ALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAA 406
Cdd:PRK09099 310 ALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVET 389
|
410 420
....*....|....*....|.
gi 15600749 407 FAQF-----ASD--LDEATRK 420
Cdd:PRK09099 390 LLQVgeyraGSDpvADEAIAK 410
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
77-452 |
1.17e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 157.22 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 77 LGEYQGLAEGMNAKCTGRILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDA 156
Cdd:PRK06936 76 LGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 157 MIPVGRGQRELIIGDRQIGKTALaVDAIINQKDSGIkCVYVAIGQKQSTIANVV-RKLEENGaLANTIVVAASASESAAL 235
Cdd:PRK06936 156 LLTCGEGQRMGIFAAAGGGKSTL-LASLIRSAEVDV-TVLALIGERGREVREFIeSDLGEEG-LRKAVLVVATSDRPSME 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 236 QYLAPYSGCTMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASRvseeyvekftn 315
Cdd:PRK06936 233 RAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ----------- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 316 gavtGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIR 395
Cdd:PRK06936 302 ----SDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLR 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 396 TALAQYRE---LAAFAQFASDLDEATRKQLEHGQRVTELMKQKQYAPMSIAEMSLSLYAA 452
Cdd:PRK06936 378 ELLAKYEEvelLLQIGEYQKGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETL 437
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
97-378 |
2.80e-42 |
|
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: 151.56 E-value: 2.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 97 EVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQRELIIGDRQIGK 176
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 177 TALaVDAIINQKDSGIKcVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPYSGCTMGEYFRDRGED 256
Cdd:cd01136 81 STL-LGMIARNTDADVN-VIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 257 ALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAsrvseeyvekftnGAvtGKTGSLTALPIIETQAG 336
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERA-------------GN--GEKGSITAFYTVLVEGD 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15600749 337 DVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRV 378
Cdd:cd01136 224 DFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
11-385 |
4.08e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 152.92 E-value: 4.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 11 EIIKGRIEKLDVASQArneGTIVSVSDGIVRIYGL----ADVMYGEMIEFPGGVYGMALNLEQDSVGAVVLGEYQGLAEG 86
Cdd:PRK08472 4 ESLKNKLQKFNLSPRF---GSITKISPTIIEADGLnpsvGDIVKIESSDNGKECLGMVVVIEKEQFGISPFSFIEGFKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 87 MNAKCTGRILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQRE 166
Cdd:PRK08472 81 DKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 167 LIIGDRQIGKTALaVDAIINQKDSGIKCVYVaIGQKQSTIANVVRKlEENGALANTIVVAASASESAALQYLAPYSGCTM 246
Cdd:PRK08472 161 GIFAGSGVGKSTL-MGMIVKGCLAPIKVVAL-IGERGREIPEFIEK-NLGGDLENTVIVVATSDDSPLMRKYGAFCAMSV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 247 GEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASRvsEEyvekftngavtGKtGSLT 326
Cdd:PRK08472 238 AEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK--EE-----------GK-GSIT 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600749 327 ALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTK 385
Cdd:PRK08472 304 AFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
17-444 |
1.37e-40 |
|
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: 151.34 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 17 IEKLDVASQARNEGTIVSVSDGIVRIYGLaDVMYGE--MIEFPGG--VYGMALNLEQDSVGAVVLGEYQGLAEGMNAKCT 92
Cdd:COG1157 8 LARLEELPPVRVSGRVTRVVGLLIEAVGP-DASIGElcEIETADGrpVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 93 GRILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQReliIGdr 172
Cdd:COG1157 87 GRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR---IG-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 173 qI------GKTALaVDAIINQKDSGIkcvyvaigqkqstiaNVV---------------RKLEENGaLANTIVVAASASE 231
Cdd:COG1157 162 -IfagsgvGKSTL-LGMIARNTEADV---------------NVIaligergrevrefieDDLGEEG-LARSVVVVATSDE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 232 SAALQYLAPYSGCTMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAsrvseeyve 311
Cdd:COG1157 224 PPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERA--------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 312 kftnGavTGKTGSLTAL------------PIIETqagdvsafvptnVISITDGQIFLESAMFNSGIRPAVNAGISVSRVG 379
Cdd:COG1157 295 ----G--NGGKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVM 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600749 380 GAAQTKIIKKLSGGIRTALAQYRE------LAAFAQFAS-DLDEATRKQlehgQRVTELMKQKQYAPMSIAE 444
Cdd:COG1157 357 PDIVSPEHRALARRLRRLLARYEEnedlirIGAYQPGSDpELDEAIALI----PAIEAFLRQGMDERVSFEE 424
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
75-444 |
1.71e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 148.72 E-value: 1.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 75 VVLGEYQGLAE---GMNAKCTGRILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGY 151
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 152 KSVDAMIPVGRGQRELIIGDRQIGKTALAvdAIINQKDSGIKCVYVAIGQKQSTIANVV-RKLEENGaLANTIVVAASAS 230
Cdd:PRK07721 147 RAIDSLLTVGKGQRVGIFAGSGVGKSTLM--GMIARNTSADLNVIALIGERGREVREFIeRDLGPEG-LKRSIVVVATSD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 231 ESAALQYLAPYSGCTMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASrvseeyv 310
Cdd:PRK07721 224 QPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 311 ekftngavTGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTKIIKKL 390
Cdd:PRK07721 297 --------TNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEA 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600749 391 SGGIRTALAQYRE------LAAFAQFAS-DLDEATRKQlehgQRVTELMKQKQYAPMSIAE 444
Cdd:PRK07721 369 ANRFRELLSTYQNsedlinIGAYKRGSSrEIDEAIQFY----PQIISFLKQGTDEKATFEE 425
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
1-435 |
2.38e-39 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 148.42 E-value: 2.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 1 MQQLNPSEISEIIKGRIEK-LDVASQARNEGTIVSVSDGIVRIyGLADVMYGEM--IEfPGGVYGMALNLEQDSVGAVVL 77
Cdd:PRK06820 1 MKLPDIARLTPRLQQQLTRpSAPPEGLRYRGPIVEIGPTLLRA-SLPGVAQGELcrIE-PQGMLAEVVSIEQEMALLSPF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 78 GEYQGLAEGMNAKCTGRILEVPVGPELLGRVVDALGNPIDGkGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAM 157
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 158 IPVGRGQRELIIGDRQIGKTALaVDAIINQKDSGIkCVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQY 237
Cdd:PRK06820 158 LSCGEGQRIGIFAAAGVGKSTL-LGMLCADSAADV-MVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 238 LAPYSGCTMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASrvseeyvekftnga 317
Cdd:PRK06820 236 KGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG-------------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 318 vTGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIRTA 397
Cdd:PRK06820 302 -NSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRM 380
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15600749 398 LAQYRE---LAAFAQFASDLDEATRKQLEHGQRVTELMKQK 435
Cdd:PRK06820 381 LACYQEielLVRVGEYQAGEDLQADEALQRYPAICAFLQQD 421
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
27-442 |
5.40e-33 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 130.46 E-value: 5.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 27 RNEGTIVSVSDGIVRIYgLADVMYGEMIEF-PGGVYGMALNLEQDSVGAVVLGEYQGLAEGMNAKCTGRILEVPVGPELL 105
Cdd:PRK07594 20 CRWGRIQDVSATLLNAW-LPGVFMGELCCIkPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 106 GRVVDALGNPIDGKGPIDAKATDaVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQRELIIGDRQIGKTALaVDAII 185
Cdd:PRK07594 99 GRVIDGFGRPLDGRELPDVCWKD-YDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 186 NQKDSGIKcVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPYSGCTMGEYFRDRGEDALIVYDDLS 265
Cdd:PRK07594 177 NAPDADSN-VLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 266 KQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASrvseeyvekftngavTGKTGSLTALPIIETQAGDVSAFVPTN 345
Cdd:PRK07594 256 RYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG---------------MGEKGSITAFYTVLVEGDDMNEPLADE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 346 VISITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIRTALAQYRE---LAAFAQFASDLDEATRKQL 422
Cdd:PRK07594 321 VRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEvelLIRIGEYQRGVDTDTDKAI 400
|
410 420
....*....|....*....|
gi 15600749 423 EHGQRVTELMKQKQYAPMSI 442
Cdd:PRK07594 401 DTYPDICTFLRQSKDEVCGP 420
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
98-378 |
2.10e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 129.05 E-value: 2.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 98 VPVGPELLGRVVDALGNPIDGKGPI--DAKATDAVEKVAPgvIWRKSVDQPVQTGYKSVDAMIPVGRGQRELIIGDRQIG 175
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIytDQRASRHSPPINP--LSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 176 KTALAvdAIINQKDSGIKCVYVAIGQKQSTIANVVRK-LEENGaLANTIVVAASASESAALQYLAPYSGCTMGEYFRDRG 254
Cdd:PRK08972 175 KSVLL--GMMTRGTTADVIVVGLVGERGREVKEFIEEiLGEEG-RARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 255 EDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASrvseeyvekftNGAvtGKTGSLTALPIIETQ 334
Cdd:PRK08972 252 LNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAG-----------NGG--PGQGSITAFYTVLTE 318
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15600749 335 AGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRV 378
Cdd:PRK08972 319 GDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRV 362
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
30-403 |
4.26e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 128.19 E-value: 4.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 30 GTIVSVSDGIVRIYGLA-DVMYGEMIEFPGGvygmalnlEQDSVGAVVLGEyqglAEGMNAKCTGRILEVPVG------- 101
Cdd:PRK06002 28 GTVSEVTASHYRVRGLSrFVRLGDFVAIRAD--------GGTHLGEVVRVD----PDGVTVKPFEPRIEIGLGdavfrkg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 102 -------PELLGRVVDALGNPIDGKGPIdAKATD--AVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQRELIIGDR 172
Cdd:PRK06002 96 plrirpdPSWKGRVINALGEPIDGLGPL-APGTRpmSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 173 QIGKTALAvdAIINQKDSGIKCVYVAIGQKqstiANVVRK-LEEN--GALANTIVVAASASESAALQYLAPYSGCTMGEY 249
Cdd:PRK06002 175 GVGKSTLL--AMLARADAFDTVVIALVGER----GREVREfLEDTlaDNLKKAVAVVATSDESPMMRRLAPLTATAIAEY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 250 FRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAsrvseeyvekftnGAVTGKTGSLTALP 329
Cdd:PRK06002 249 FRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERA-------------GPGAEGGGSITGIF 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600749 330 IIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIRTALAQYRE 403
Cdd:PRK06002 316 SVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEE 389
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
95-377 |
5.36e-32 |
|
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: 124.26 E-value: 5.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 95 ILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQRELIIGDRQI 174
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 175 GKTALAV----DAIINQKDSGIKCVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPYSGCTMGEYF 250
Cdd:cd01135 81 PHNELAAqiarQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 251 R-DRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGdvfYLHSRL---LERASRVSeeyvekftngavtGKTGSLT 326
Cdd:cd01135 161 AyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVE-------------GRKGSIT 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15600749 327 ALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSR 377
Cdd:cd01135 225 QIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
64-378 |
1.49e-31 |
|
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: 126.76 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 64 ALNLEQDSVGAVVLGEYQGLAEGMNAKCTGRILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSV 143
Cdd:TIGR01039 44 AQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 144 DQPVQTGYKSVDAMIPVGRGQRELIIGDRQIGKTALAVDAI--INQKDSGIKcVYVAIGQKQSTIANVVRKLEENGALAN 221
Cdd:TIGR01039 124 VEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELInnIAKEHGGYS-VFAGVGERTREGNDLYHEMKESGVIDK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 222 TIVVAASASESAALQYLAPYSGCTMGEYFRD-RGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLE 300
Cdd:TIGR01039 203 TALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQE 282
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600749 301 RASrvseeyvekftngavTGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRV 378
Cdd:TIGR01039 283 RIT---------------STKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRL 345
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
31-444 |
1.93e-31 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 126.48 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 31 TIVSVSDGIVRIYGLADVMYGEM--IEFPGG--VYGMALNLEQDSVGAVVLGEYQGLA-EGMNAKCTGRILEVPVGPELL 105
Cdd:PRK04196 6 TVSEIKGPLLFVEGVEGVAYGEIveIELPNGekRRGQVLEVSEDKAVVQVFEGTTGLDlKDTKVRFTGEPLKLPVSEDML 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 106 GRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQR------------ELIIgdrQ 173
Cdd:PRK04196 86 GRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnELAA---Q 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 174 IgktalAVDAIINQKDSGIKCVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPYSGCTMGEYFR-D 252
Cdd:PRK04196 163 I-----ARQAKVLGEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 253 RGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGdvfYLHSRL---LERAsrvseeyvekftnGAVTGKTGSLTALP 329
Cdd:PRK04196 238 KGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERA-------------GRIKGKKGSITQIP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 330 IIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSR-----VGGAAQTKIIKKLSGGIRTALAQYREL 404
Cdd:PRK04196 302 ILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRlmkdgIGEGKTREDHKDVANQLYAAYARGKDL 381
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15600749 405 AAFAQF--ASDLDEATRKQLEHGQRV-TELMKQKQYAPMSIAE 444
Cdd:PRK04196 382 RELAAIvgEEALSERDRKYLKFADAFeREFVNQGFDENRSIEE 424
|
|
| 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 |
9.64e-30 |
|
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, in mitochondrial inner membranes, and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349740 [Multi-domain] Cd Length: 67 Bit Score: 111.01 E-value: 9.64e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600749 28 NEGTIVSVSDGIVRIYGLADVMYGEMIEFPGGVYGMALNLEQDSVGAVVLGEYQGLAEGMNAKCTGR 94
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
82-434 |
5.59e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 118.84 E-value: 5.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 82 GLAEGMNAKCTGRILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVG 161
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 162 RGQRELIIGDRQIGKTALAvdAIINQKDSGIKCVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPY 241
Cdd:PRK07196 154 KGQRVGLMAGSGVGKSVLL--GMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 242 SGCTMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASrvseeyvekftNGAvtgK 321
Cdd:PRK07196 232 LCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG-----------NSS---G 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 322 TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSR----VGGAAQTKIIKKLSGGIrTA 397
Cdd:PRK07196 298 NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCY-AD 376
|
330 340 350
....*....|....*....|....*....|....*..
gi 15600749 398 LAQYRELAAFAQFASDLDEATRKQLEHGQRVTELMKQ 434
Cdd:PRK07196 377 YMAIKPLIPLGGYVAGADPMADQAVHYYPAITQFLRQ 413
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
77-407 |
7.13e-29 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 118.56 E-value: 7.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 77 LGEYQGLAEGMNAKCTGRILEVPVGPELLGRVVDALGNPIDGKGPIDAKATD----AVEKVAPGVIWRKSVDQPVQTGYK 152
Cdd:PRK08149 61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVGPIseerVIDVAPPSYAERRPIREPLITGVR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 153 SVDAMIPVGRGQRELIIGDRQIGKTALaVDAIINQKDSGIkCVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASES 232
Cdd:PRK08149 141 AIDGLLTCGVGQRMGIFASAGCGKTSL-MNMLIEHSEADV-FVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 233 AALQYLAPYSGCTMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASRVseeyvek 312
Cdd:PRK08149 219 SVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT------- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 313 ftngavtgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSG 392
Cdd:PRK08149 292 --------LAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAA 363
|
330
....*....|....*
gi 15600749 393 GIRTALAQYRELAAF 407
Cdd:PRK08149 364 AFRKLLTRLEELQLF 378
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
97-472 |
6.77e-27 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 113.34 E-value: 6.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 97 EVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQRELIIGDRQIGK 176
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 177 TAL-AVDAIINQKDSgikCVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPYSGCTMGEYFRDRGE 255
Cdd:PRK07960 189 SVLlGMMARYTQADV---IVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQ 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 256 DALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASrvseeyvekftNGAVTGktGSLTALPIIETQA 335
Cdd:PRK07960 266 HVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG-----------NGISGG--GSITAFYTVLTEG 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 336 GDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRvggaAQTKIIKKlsggirtalAQYRELAAFAQFASDLd 415
Cdd:PRK07960 333 DDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISR----AMTALIDE---------QHYARVRQFKQLLSSF- 398
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600749 416 eatrkqlehgQRVTELMKQKQYAPMS--IAEMSLSLYAAERGFLQDvEIAKVGSFEQAL 472
Cdd:PRK07960 399 ----------QRNRDLVSVGAYAKGSdpMLDKAIALWPQLEAFLQQ-GIFERADWEDSL 446
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
77-378 |
7.55e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 112.90 E-value: 7.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 77 LGEYQGLAEGMNAKCTGRILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDA 156
Cdd:PRK05688 82 VGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSING 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 157 MIPVGRGQRELIIGDRQIGKTALaVDAIINQKDSGIKCVYVaIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQ 236
Cdd:PRK05688 162 LLTVGRGQRLGLFAGTGVGKSVL-LGMMTRFTEADIIVVGL-IGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 237 YLAPYSGCTMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASrvseeyvekftNG 316
Cdd:PRK05688 240 LRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG-----------NA 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600749 317 AVTGktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRV 378
Cdd:PRK05688 309 EPGG--GSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV 368
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
87-378 |
3.51e-26 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 111.35 E-value: 3.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 87 MNAKC--TGRILEVPVGPELLGRVVDALGNPIDgKGP---------IDAKATDAVEKVAPgviwrksvDQPVQTGYKSVD 155
Cdd:TIGR01040 63 KKTTCefTGDILRTPVSEDMLGRVFNGSGKPID-KGPpvlaedyldINGQPINPYARIYP--------EEMIQTGISAID 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 156 AMIPVGRGQRELIIGD-------------RQIGKTALAVDAIINQKDSGIKCVYVAIGQKQSTIANVVRKLEENGALANT 222
Cdd:TIGR01040 134 VMNSIARGQKIPIFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 223 IVVAASASESAALQYLAPYSGCTMGEYFR-DRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLER 301
Cdd:TIGR01040 214 CLFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYER 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600749 302 ASRVseeyvekftngavTGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRV 378
Cdd:TIGR01040 294 AGRV-------------EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 357
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
40-419 |
2.60e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 105.45 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 40 VRIYGLADVMYGEMIEFPGGVYGMAL-------NLEQDSVGAVVLGEYQGLA--------EGMNAKCTGRILE----VPV 100
Cdd:PRK08927 15 LVIYGRVVAVRGLLVEVAGPIHALSVgarivveTRGGRPVPCEVVGFRGDRAllmpfgplEGVRRGCRAVIANaaaaVRP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 101 GPELLGRVVDALGNPIDGKGPIDAKATD-AVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQRELIIGDRQIGKTAL 179
Cdd:PRK08927 95 SRAWLGRVVNALGEPIDGKGPLPQGPVPyPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 180 ------AVDAIINqkdsgikcVYVAIGQKQSTIANVVRK-LEENGaLANTIVVAASASESAALQYLAPYSGCTMGEYFRD 252
Cdd:PRK08927 175 lsmlarNADADVS--------VIGLIGERGREVQEFLQDdLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 253 RGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAsrvseeyvekftnGAVTGKTGSLTALPIIE 332
Cdd:PRK08927 246 QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERA-------------GPGPIGEGTITGLFTVL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 333 TQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIRTALAQYRE------LAA 406
Cdd:PRK08927 313 VDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADmeelirLGA 392
|
410
....*....|....
gi 15600749 407 FAQFAS-DLDEATR 419
Cdd:PRK08927 393 YRAGSDpEVDEAIR 406
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
98-377 |
4.93e-23 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 101.52 E-value: 4.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 98 VPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQRELIIGDRQIGKT 177
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 178 ALaVDAIINQKDSGIKcVYVAIGQKQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPYSGCTMGEYFRDRGEDA 257
Cdd:PRK05922 172 SL-LSTIAKGSKSTIN-VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 258 LIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERASrvseeyvekftngavTGKTGSLTALPIIETQAGD 337
Cdd:PRK05922 250 LFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG---------------NNDKGSITALYAILHYPNH 314
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15600749 338 VSAFVPTnVISITDGQIFL---ESAMFNsgirPAVNAGISVSR 377
Cdd:PRK05922 315 PDIFTDY-LKSLLDGHFFLtpqGKALAS----PPIDILTSLSR 352
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
97-378 |
1.44e-20 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 91.51 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 97 EVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQRELIIGDRQIGK 176
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 177 TALAVDAIIN-QKDSGIKCVYVAIGQKQSTIANVVRKLEENGalantiVVAASASESAALQY-----------LAPYSGC 244
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGERTREGNDLYHEMKESG------VINLDGLSKVALVYgqmneppgaraRVALTGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 245 TMGEYFRD-RGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERasrvseeyvekftngAVTGKTG 323
Cdd:cd01133 155 TMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQER---------------ITSTKKG 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15600749 324 SLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRV 378
Cdd:cd01133 220 SITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
98-403 |
1.29e-19 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 91.19 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 98 VPVGPELLGRVVDALGNPID--------GKGPIDAKATDAVEkvapgviwRKSVDQPVQTGYKSVDAMIPVGRGQRELII 169
Cdd:PRK06793 91 IPRGNHLLGKVLSANGEVLNeeaeniplQKIKLDAPPIHAFE--------REEITDVFETGIKSIDSMLTIGIGQKIGIF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 170 GDRQIGKTALaVDAIINQKDSGIKCVYVaIGQKQSTIANVVRK-LEENGaLANTIVVAASASESAALQYLAPYSGCTMGE 248
Cdd:PRK06793 163 AGSGVGKSTL-LGMIAKNAKADINVISL-VGERGREVKDFIRKeLGEEG-MRKSVVVVATSDESHLMQLRAAKLATSIAE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 249 YFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPgreaYPGDVFYLHS---RLLERASRVseeyvekftngavtgKTGSL 325
Cdd:PRK06793 240 YFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKT---------------QKGSI 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600749 326 TALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSRVGGAAQTKIIKKLSGGIRTALAQYRE 403
Cdd:PRK06793 301 TGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKE 378
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
25-404 |
1.94e-18 |
|
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439825 [Multi-domain] Cd Length: 468 Bit Score: 87.84 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 25 QARNEGTIVSVSDGIVriyglaDVmygemiEFPGG----VY---------GMALNLE------QDSVGAVVLGEYQGLAE 85
Cdd:COG0055 1 MAMNTGKIVQVIGPVV------DV------EFPEGelpaIYnalevenegGGELVLEvaqhlgDNTVRCIAMDSTDGLVR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 86 GMNAKCTGRILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGYKSVDAMIPVGRGQR 165
Cdd:COG0055 69 GMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 166 ELIIGDRQIGKTALAVDAIIN--QKDSGIkCVYVAIGQKQSTIANVVRKLEENGALANTIVVaasasesaalqY------ 237
Cdd:COG0055 149 IGLFGGAGVGKTVLIMELIHNiaKEHGGV-SVFAGVGERTREGNDLYREMKESGVLDKTALV-----------Fgqmnep 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 238 -----LAPYSGCTMGEYFRD-RGEDALIVYDDLSK--QAVAyrQISLLLRRPPGREAY-P---GDVfylhSRLLER-ASR 304
Cdd:COG0055 217 pgarlRVALTALTMAEYFRDeEGQDVLLFIDNIFRftQAGS--EVSALLGRMPSAVGYqPtlaTEM----GALQERiTST 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 305 vseeyvekftngavtgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVSR------V 378
Cdd:COG0055 291 ----------------KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRildpliV 354
|
410 420 430
....*....|....*....|....*....|
gi 15600749 379 G----GAAQtkiikklsgGIRTALAQYREL 404
Cdd:COG0055 355 GeehyRVAR---------EVQRILQRYKEL 375
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
96-377 |
8.58e-17 |
|
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: 80.70 E-value: 8.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 96 LEVPVGPELLGRVVDALGNPID----------GKGpIDA------KATDAVEKVAPgviwrksvDQPVQTGYKSVDAMIP 159
Cdd:cd01134 2 LSVELGPGLLGSIFDGIQRPLEviaetgsifiPRG-VNVqrwpvrQPRPVKEKLPP--------NVPLLTGQRVLDTLFP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 160 VGRGQRELIIGDRQIGKTALAvDAIINQKDSGIkCVYVAIGQKQSTIANVVRKLEE-------NGALANTIVVAASASES 232
Cdd:cd01134 73 VAKGGTAAIPGPFGCGKTVIS-QSLSKWSNSDV-VIYVGCGERGNEMAEVLEEFPElkdpitgESLMERTVLIANTSNMP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 233 AALQYLAPYSGCTMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGdvfYLHSRL---LERASRVSeey 309
Cdd:cd01134 151 VAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYERAGRVR--- 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 310 vekfTNGAvTGKTGSLTALPIIETQAGDVSAFVPTNVISITdgQIF--LESAMFNSGIRPAVNAGISVSR 377
Cdd:cd01134 225 ----CLGS-PGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
30-93 |
3.47e-15 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 70.27 E-value: 3.47e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600749 30 GTIVSVSDGIVRIYGLADVMYGEMIEFPGGVYGMALNLEQDSVGAVVLGEYQGLAEGMNAKCTG 93
Cdd:pfam02874 6 GPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
48-356 |
5.39e-15 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 77.00 E-value: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 48 VMYGEM--IEFP-GGVYGMALNLEQDSVGAVVLGEYQGLAEGMNAKCTGRILEVPVGPELLGRVVDALGNPIDGKGPIDA 124
Cdd:PRK02118 23 VGYGELatVERKdGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 125 katDAVEKVAPGV--IWRKSVDQPVQTGYKSVDAMIPVGRGQRELIIGDRqiGKTALAVDA-IINQKDSGIkCVYVAIGQ 201
Cdd:PRK02118 103 ---EPIEIGGPSVnpVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVS--GEPYNALLArIALQAEADI-IILGGMGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 202 KQSTIANVVRKLEENGALANTIVVAASASESAALQYLAPYSGCTMGEYFR-DRGEDALIVYDDLSKQAVAYRQISLLLRR 280
Cdd:PRK02118 177 TFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQ 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600749 281 PPGREAYPGDvfyLHSRLlerASRVsEEYVEkFTNGavtgktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFL 356
Cdd:PRK02118 257 IPSNRGYPGS---LYSDL---ASRY-EKAVD-FEDG------GSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
72-404 |
9.43e-13 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 70.45 E-value: 9.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 72 VGAVVLGEYQGLAEGMNAKCTGRILEVPVGPELLGRVVDALGNPIDGKGPIDAKATDAVEKVAPGVIWRKSVDQPVQTGY 151
Cdd:CHL00060 70 VRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 152 KSVDAMIPVGRGQRELIIGDRQIGKTALAVDAIIN-QKDSGIKCVYVAIGQ------------KQSTIANvvrklEENGA 218
Cdd:CHL00060 150 KVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGErtregndlymemKESGVIN-----EQNIA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 219 LANTIVVAASASESAALQYLAPYSGCTMGEYFRD-RGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSR 297
Cdd:CHL00060 225 ESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 298 LLERASRVseeyvekftngavtgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESAMFNSGIRPAVNAGISVS- 376
Cdd:CHL00060 305 LQERITST---------------KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSt 369
|
330 340 350
....*....|....*....|....*....|..
gi 15600749 377 ----RVGGAAQTKIIKKlsggIRTALAQYREL 404
Cdd:CHL00060 370 mlqpRIVGEEHYETAQR----VKQTLQRYKEL 397
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
241-327 |
1.67e-11 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 66.73 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 241 YSGCTMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAYPGdvfYLHSRL---LERASRVSeeyvekfTNGa 317
Cdd:PRK04192 310 YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASRLaefYERAGRVK-------TLG- 378
|
90
....*....|
gi 15600749 318 vtGKTGSLTA 327
Cdd:PRK04192 379 --GEEGSVTI 386
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
388-444 |
3.25e-10 |
|
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: 55.91 E-value: 3.25e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600749 388 KKLSGGIRTALAQYRELAAFAQFASD--LDEATRKQLEHGQRVTELMKQKQYAPMSIAE 444
Cdd:cd01429 2 KAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIED 60
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
195-370 |
1.25e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 60.81 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 195 VYVAIGQKQSTIANVVR---KLEENGA----LANTIVVAASASESAALQYLAPYSGCTMGEYFRDRGEDALIVYDDLSKQ 267
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEefpKLKDPKTgkplMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600749 268 AVAYRQISLLLRRPPGREAYPGdvfYLHSRL---LERASRVseeyvekFTNGAvTGKTGSLTALPIIETQAGDVSAFVPT 344
Cdd:PRK14698 766 AEALREISGRLEEMPGEEGYPA---YLASKLaefYERAGRV-------VTLGS-DYRVGSVSVIGAVSPPGGDFSEPVVQ 834
|
170 180
....*....|....*....|....*.
gi 15600749 345 NVISITDGQIFLESAMFNSGIRPAVN 370
Cdd:PRK14698 835 NTLRVVKVFWALDADLARRRHFPAIN 860
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
30-94 |
9.36e-04 |
|
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: 38.06 E-value: 9.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600749 30 GTIVSVSDGIVRIYGLADVMYGEMIEF-------PGGVYGMALNLEQDSVGAVVLGEYQGLAEGMNAKCTGR 94
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIGEVCEIergdgnnETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
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