|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
7-510 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 984.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 7 PTEVSSILEERIKGVSDEANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKE 86
Cdd:PRK09281 5 PEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 87 GELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQR 166
Cdd:PRK09281 85 GDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 167 ELIIGDRQTGKTAVALDTILNQKrwnngsdeSKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQY 246
Cdd:PRK09281 165 ELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 247 LAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTAL 326
Cdd:PRK09281 237 LAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 327 PVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFA 406
Cdd:PRK09281 317 PIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 407 QFGSDLDASTKQTLVRGERLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYLKSNHNELLTEIR 486
Cdd:PRK09281 397 QFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIR 476
|
490 500
....*....|....*....|....
gi 300193115 487 EKGELSKELLASLKSATESFVATF 510
Cdd:PRK09281 477 ETKDLSDEIEAKLKAAIEEFKKTF 500
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
7-510 |
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: 983.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 7 PTEVSSILEERIKGVSDEANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKE 86
Cdd:COG0056 5 PEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEGIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 87 GELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQR 166
Cdd:COG0056 85 GDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 167 ELIIGDRQTGKTAVALDTILNQKrwnngsdeSKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQY 246
Cdd:COG0056 165 ELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 247 LAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTAL 326
Cdd:COG0056 237 IAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 327 PVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFA 406
Cdd:COG0056 317 PIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 407 QFGSDLDASTKQTLVRGERLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYLKSNHNELLTEIR 486
Cdd:COG0056 397 QFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIR 476
|
490 500
....*....|....*....|....
gi 300193115 487 EKGELSKELLASLKSATESFVATF 510
Cdd:COG0056 477 ETGKLDDEIEEKLKAAIEEFKKTF 500
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
7-510 |
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: 819.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 7 PTEVSSILEERIKGVSDEANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKE 86
Cdd:TIGR00962 4 LEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 87 GELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQR 166
Cdd:TIGR00962 84 GSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 167 ELIIGDRQTGKTAVALDTILNQKrwnngsdeSKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQY 246
Cdd:TIGR00962 164 ELIIGDRQTGKTAVAIDTIINQK--------DSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 247 LAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTAL 326
Cdd:TIGR00962 236 LAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 327 PVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFA 406
Cdd:TIGR00962 316 PIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 407 QFGSDLDASTKQTLVRGERLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYLKSNHNELLTEIR 486
Cdd:TIGR00962 396 QFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEIN 475
|
490 500
....*....|....*....|....
gi 300193115 487 EKGELSKELLASLKSATESFVATF 510
Cdd:TIGR00962 476 TTKKLTEELEAKLKEALKNFKKTF 499
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
24-510 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 751.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 24 EANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGP 103
Cdd:CHL00059 1 EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 104 GLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALD 183
Cdd:CHL00059 81 AYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 184 TILNQKrwnngsdeSKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNG 263
Cdd:CHL00059 161 TILNQK--------GQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 264 KHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTALPVIETQGGDVSAYIPTN 343
Cdd:CHL00059 233 RHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 344 VISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRG 423
Cdd:CHL00059 313 VISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 424 ERLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYLKSNHNELLTEIREKGELSKELLASLKSAT 503
Cdd:CHL00059 393 QRLRELLKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAI 472
|
....*..
gi 300193115 504 ESFVATF 510
Cdd:CHL00059 473 QEQLELF 479
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
9-510 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 727.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 9 EVSSILEERIKGVSDEANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKEGE 88
Cdd:PRK13343 7 EWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILAGT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 89 LVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQREL 168
Cdd:PRK13343 87 EVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQREL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 169 IIGDRQTGKTAVALDTILNQKrwnngsdeSKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLA 248
Cdd:PRK13343 167 IIGDRQTGKTAIAIDAIINQK--------DSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 249 PFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTALPV 328
Cdd:PRK13343 239 PFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 329 IETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQF 408
Cdd:PRK13343 319 IETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 409 GSDLDASTKQTLVRGERLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYLKSNHNELLTEIREK 488
Cdd:PRK13343 399 GGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESP 478
|
490 500
....*....|....*....|..
gi 300193115 489 GELSKELLASLKSATESFVATF 510
Cdd:PRK13343 479 RELDEAWLAALEEILREAGERF 500
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-377 |
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: 597.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 96 IVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQT 175
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 176 GKTAVALDTILNQKRwnngsdesKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASI 255
Cdd:cd01132 81 GKTAIAIDTIINQKG--------KKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 256 GEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTALPVIETQGGD 335
Cdd:cd01132 153 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 300193115 336 VSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVG 377
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
14-494 |
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: 550.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 14 LEERIKGVSDEANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKEGELVKRT 93
Cdd:TIGR03324 12 LDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 94 GNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDR 173
Cdd:TIGR03324 92 GRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 174 QTGKTAVALDTILNQKRWNngsdeskkLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAA 253
Cdd:TIGR03324 172 QTGKTAIAIDTILNQKGRN--------VLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 254 SIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTALPVIETQG 333
Cdd:TIGR03324 244 SIGEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 334 GDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFGSDLD 413
Cdd:TIGR03324 324 QNISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 414 ASTKQTLVRGERLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYLKSNHNELLTEIREKGELSK 493
Cdd:TIGR03324 404 ENTRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSD 483
|
.
gi 300193115 494 E 494
Cdd:TIGR03324 484 E 484
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
63-467 |
3.58e-124 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 374.76 E-value: 3.58e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 63 GMALNLEP-GQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGPGLLGRVVDALGNPIdgkgPIDAAGRSRAQVK------- 134
Cdd:PTZ00185 80 GLVFNLEKdGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEV----PVGLLTRSRALLEseqtlgk 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 135 ----APGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDTILNQKRWNNGSDESKKLYCVYVAVGQ 210
Cdd:PTZ00185 156 vdagAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVISIYVSIGQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 211 KRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRP 290
Cdd:PTZ00185 236 RCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 291 PGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVG 370
Cdd:PTZ00185 316 PGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 371 LSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFGSDLDAStkqTLVRGERLTQLLkqNQYSPLATEEQVPLIYAG 450
Cdd:PTZ00185 396 LSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTV---PMIRGARFVALF--NQKNPSFFMNALVSLYAC 470
|
410
....*....|....*..
gi 300193115 451 VNGHLDGIELSRIGEFE 467
Cdd:PTZ00185 471 LNGYLDDVKVNYAKLYE 487
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
98-376 |
7.64e-121 |
|
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: 355.22 E-value: 7.64e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 98 DVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGK 177
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 178 TAVALDTILNQKrwnngsdESKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIGE 257
Cdd:cd19476 81 TVLAMQLARNQA-------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 258 WFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLseKEGSGSLTALPVIETQGGDVS 337
Cdd:cd19476 154 YFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKV--KDGGGSITAIPAVSTPGDDLT 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 300193115 338 AYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRV 376
Cdd:cd19476 232 DPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
151-374 |
6.68e-116 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 340.49 E-value: 6.68e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 151 GLKAVDALVPIGRGQRELIIGDRQTGKTAVAlDTILNQkrwnngsdeSKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKY 230
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQ---------ASADVVVYALIGERGREVREFIEELLGSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 231 SIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLER 310
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300193115 311 AAKLSEKEgsGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVS 374
Cdd:pfam00006 151 AGRVKGKG--GSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
107-437 |
4.25e-100 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 310.75 E-value: 4.25e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 107 GRVVDALGNPIDGKGPIDA-----AGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVA 181
Cdd:PRK07165 81 GKIIDIDGNIIYPEAQNPLskkflPNTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 182 LDTILNQKRWNngsdeskkLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAAtASEAAPLQYLAPFTAASIGE---W 258
Cdd:PRK07165 161 LNTIINQKNTN--------VKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAEnisY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 259 FRDngkhALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEgsgSLTALPVIETQGGDVSA 338
Cdd:PRK07165 232 NDD----VLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNRK---TITALPILQTVDNDITS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 339 YIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSL-KLFLAqYREVAAFAQFGSDLDASTK 417
Cdd:PRK07165 305 LISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEIsKIYRA-YKRQLKLSMLDYDLNKETS 383
|
330 340
....*....|....*....|
gi 300193115 418 QTLVRGERLTQLLKQNQYSP 437
Cdd:PRK07165 384 DLLFKGKMIEKMFNQKGFSL 403
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
386-510 |
3.22e-65 |
|
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: 206.83 E-value: 3.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 386 KQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRGERLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGE 465
Cdd:cd18113 2 KKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIKE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 300193115 466 FESSFLSYLKSNHNELLTEIREKGELSKELLASLKSATESFVATF 510
Cdd:cd18113 82 FEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
381-506 |
2.11e-64 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 204.98 E-value: 2.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 381 QVKALKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRGERLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIEL 460
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 300193115 461 SRIGEFESSFLSYLKSNHNELLTEIREKGELSKELLASLKSATESF 506
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
99-376 |
1.73e-53 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 181.22 E-value: 1.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 99 VPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKT 178
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 179 avaldTILNQKRWNNGSDESkklycVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIGEW 258
Cdd:cd01136 82 -----TLLGMIARNTDADVN-----VIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 259 FRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEkegsGSLTALPVIETQGGDVSA 338
Cdd:cd01136 152 FRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----GSITAFYTVLVEGDDFND 227
|
250 260 270
....*....|....*....|....*....|....*...
gi 300193115 339 YIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRV 376
Cdd:cd01136 228 PIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
90-452 |
9.96e-51 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 179.18 E-value: 9.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 90 VKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELI 169
Cdd:PRK06936 88 VSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 170 IGDRQTGKTavaldTILNQKRWNNGSDeskklYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAP 249
Cdd:PRK06936 168 FAAAGGGKS-----TLLASLIRSAEVD-----VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 250 FTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKlSEKegsGSLTALPVI 329
Cdd:PRK06936 238 FVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ-SDK---GSITALYTV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 330 ETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFG 409
Cdd:PRK06936 314 LVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIG 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 300193115 410 S---DLDASTKQTLVRGERLTQLLKQNQYSPLATEEQVPLIYAGVN 452
Cdd:PRK06936 394 EyqkGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETLTQ 439
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
31-443 |
1.58e-47 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 170.77 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 31 GRVLAVGDGIARVfGLNNIQAEELVEFS-SGVKGMALNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGPGLLGRV 109
Cdd:PRK06820 31 GPIVEIGPTLLRA-SLPGVAQGELCRIEpQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 110 VDALGNPIDGKGPIDAAGRSRaQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTavaldTILNQK 189
Cdd:PRK06820 110 LDGLGAPIDGGPPLTGQWREL-DCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKS-----TLLGML 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 190 rwnngSDESKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATaSEAAPLQYL-APFTAASIGEWFRDNGKHALI 268
Cdd:PRK06820 184 -----CADSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVAT-SDRPALERLkGLSTATTIAEYFRDRGKKVLL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 269 VYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKlSEKegsGSLTALPVIETQGGDVSAYIPTNVISIT 348
Cdd:PRK06820 258 MADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGN-SDR---GSITAFYTVLVEGDDMNEPVADEVRSLL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 349 DGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFG---SDLDASTKQTLVRGER 425
Cdd:PRK06820 334 DGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGeyqAGEDLQADEALQRYPA 413
|
410 420
....*....|....*....|
gi 300193115 426 LTQLLKQ--NQYSPLATEEQ 443
Cdd:PRK06820 414 ICAFLQQdhSETAHLETTLE 433
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
24-437 |
2.15e-47 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 170.33 E-value: 2.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 24 EANLNETGRVLAVGDGIARVFGLNN---------------IQAEELVEFSSGVkgmALnLEPgqvgivlFGSDRLVKEGE 88
Cdd:PRK09099 19 LPAVRRTGKVVEVIGTLLRVSGLDVtlgelcelrqrdgtlLQRAEVVGFSRDV---AL-LSP-------FGELGGLSRGT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 89 LVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQREL 168
Cdd:PRK09099 88 RVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 169 IIGDRQTGKTavaldTILNQKRWNNGSDESkklycVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLA 248
Cdd:PRK09099 168 IFAPAGVGKS-----TLMGMFARGTQCDVN-----VIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 249 PFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAkLSEkegSGSLTALPV 328
Cdd:PRK09099 238 AYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-MGE---TGSITALYT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 329 IETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQF 408
Cdd:PRK09099 314 VLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQV 393
|
410 420 430
....*....|....*....|....*....|....
gi 300193115 409 G---SDLDASTKQTLVRGERLTQLLKQ--NQYSP 437
Cdd:PRK09099 394 GeyrAGSDPVADEAIAKIDAIRDFLSQrtDEYSD 427
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
16-446 |
6.53e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 166.01 E-value: 6.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 16 ERIKGVSDEANLNET-GRVLAVGDGIARVFGLN----NIQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKEGELV 90
Cdd:PRK08472 4 ESLKNKLQKFNLSPRfGSITKISPTIIEADGLNpsvgDIVKIESSDNGKECLGMVVVIEKEQFGISPFSFIEGFKIGDKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 91 KRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAgRSRAQVKAP-GILPRRSVHEPVQTGLKAVDALVPIGRGQRELI 169
Cdd:PRK08472 84 FISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYE-RYAPIMKAPiAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 170 IGDRQTGKTAVaLDTILNqkrwnnGSDESKKlycVYVAVGQKRSTVAQLVQTLEQHDaMKYSIIVAATASEAAPLQYLAP 249
Cdd:PRK08472 163 FAGSGVGKSTL-MGMIVK------GCLAPIK---VVALIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSPLMRKYGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 250 FTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKlseKEGSGSLTALPVI 329
Cdd:PRK08472 232 FCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 330 ETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYRE------VA 403
Cdd:PRK08472 309 LVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKEnevlirIG 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 300193115 404 AFaQFGSD--LDastkQTLVRGERLTQLLKQNqysplaTEEQVPL 446
Cdd:PRK08472 389 AY-QKGNDkeLD----EAISKKEFMEQFLKQN------PNELFPF 422
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
30-446 |
9.32e-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: 165.59 E-value: 9.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 30 TGRVLAVGDGIARVFGLnniQAE--ELVEFSSG----VKGMALNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGP 103
Cdd:COG1157 20 SGRVTRVVGLLIEAVGP---DASigELCEIETAdgrpVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 104 GLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQReliIGdr---qtGKTav 180
Cdd:COG1157 97 GLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR---IGifagsgvGKS-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 181 aldTILNQkrwnngsdeskklycvyVAvgqkRSTVAQLV-------------QTLEQH---DAMKYSIIVAATASEAAPL 244
Cdd:COG1157 172 ---TLLGM-----------------IA----RNTEADVNvialigergrevrEFIEDDlgeEGLARSVVVVATSDEPPLM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 245 QYLAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAklseKEGSGSLT 324
Cdd:COG1157 228 RLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAG----NGGKGSIT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 325 ALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVA- 403
Cdd:COG1157 304 AFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEd 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 300193115 404 -----AFAQfGSD--LDAStkqtLVRGERLTQLLKQNqysplaTEEQVPL 446
Cdd:COG1157 384 lirigAYQP-GSDpeLDEA----IALIPAIEAFLRQG------MDERVSF 422
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
87-444 |
3.08e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 161.43 E-value: 3.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 87 GELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKgpidAAGRSRAQVKA----PGILPRRSVHEPVQTGLKAVDALVPIG 162
Cdd:PRK07721 81 GCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGS----ALPKGLAPVSTdqdpPNPLKRPPIREPMEVGVRAIDSLLTVG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 163 RGQRELIIGDRQTGKTavaldTILNQKRWNNGSDESkklycVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAA 242
Cdd:PRK07721 157 KGQRVGIFAGSGVGKS-----TLMGMIARNTSADLN-----VIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 243 PLQYLAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAklseKEGSGS 322
Cdd:PRK07721 227 LMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG----TNASGS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 323 LTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREV 402
Cdd:PRK07721 303 ITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNS 382
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 300193115 403 AAFAQFGSDLDASTK---QTLVRGERLTQLLKQNQYSPLATEEQV 444
Cdd:PRK07721 383 EDLINIGAYKRGSSReidEAIQFYPQIISFLKQGTDEKATFEESI 427
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
99-411 |
6.95e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 155.24 E-value: 6.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 99 VPVGPGLLGRVVDALGNPIDGKGPIDAAGRsrAQVKAPGILP--RRSVHEPVQTGLKAVDALVPIGRGQR---------- 166
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIYTDQR--ASRHSPPINPlsRRPITEPLDVGVRAINAMLTVGKGQRmglfagsgvg 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 167 -ELIIGDRQTGKTAvalDTIlnqkrwnngsdeskklycVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATAsEAAPLQ 245
Cdd:PRK08972 175 kSVLLGMMTRGTTA---DVI------------------VVGLVGERGREVKEFIEEILGEEGRARSVVVAAPA-DTSPLM 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 246 YL-APFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSekEGSGSLT 324
Cdd:PRK08972 233 RLkGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGG--PGQGSIT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 325 ALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYRE--- 401
Cdd:PRK08972 311 AFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQnrd 390
|
330
....*....|...
gi 300193115 402 ---VAAFAQfGSD 411
Cdd:PRK08972 391 lisIGAYKQ-GSD 402
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
99-441 |
1.28e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 146.25 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 99 VPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILpRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKT 178
Cdd:PRK07594 91 VPVGEALLGRVIDGFGRPLDGRELPDVCWKDYDAMPPPAMV-RQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 179 avaldTILNQKRWNNGSDESkklycVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIGEW 258
Cdd:PRK07594 170 -----TLLAMLCNAPDADSN-----VLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEF 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 259 FRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAkLSEKegsGSLTALPVIETQGGDVSA 338
Cdd:PRK07594 240 FRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-MGEK---GSITAFYTVLVEGDDMNE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 339 YIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFGS---DLDAS 415
Cdd:PRK07594 316 PLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEyqrGVDTD 395
|
330 340
....*....|....*....|....*.
gi 300193115 416 TKQTLVRGERLTQLLKQNQYSPLATE 441
Cdd:PRK07594 396 TDKAIDTYPDICTFLRQSKDEVCGPE 421
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
31-441 |
5.80e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 144.76 E-value: 5.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 31 GRVLAVGDGIARVFGLNN-IQAEELVEFSSG---VKGMALNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPvGPGLL 106
Cdd:PRK06002 28 GTVSEVTASHYRVRGLSRfVRLGDFVAIRADggtHLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGPLRIRP-DPSWK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 107 GRVVDALGNPIDGKGPIDAAGRSRA-QVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTavaldTI 185
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPMSiDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKS-----TL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 186 LNQKRWNNGSDEskklycVYVA-VGQKRSTVAQLVQ-TLEQHdaMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNG 263
Cdd:PRK06002 182 LAMLARADAFDT------VVIAlVGERGREVREFLEdTLADN--LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 264 KHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAklSEKEGSGSLTALPVIETQGGDVSAYIPTN 343
Cdd:PRK06002 254 ENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAG--PGAEGGGSITGIFSVLVDGDDHNDPVADS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 344 VISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYRE------VAAFaQFGSD--LDAS 415
Cdd:PRK06002 332 IRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdlrlIGGY-RAGSDpdLDQA 410
|
410 420
....*....|....*....|....*.
gi 300193115 416 TKQTlvrgERLTQLLKQNQYSPLATE 441
Cdd:PRK06002 411 VDLV----PRIYEALRQSPGDPPSDD 432
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
101-433 |
1.43e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 140.41 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 101 VGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTaV 180
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKS-V 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 181 ALDTIlnqkrwnngSDESKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFR 260
Cdd:PRK07196 171 LLGMI---------TRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 261 DNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKlseKEGSGSLTALPVIETQGGDVSAYI 340
Cdd:PRK07196 242 DKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGN---SSGNGTMTAIYTVLAEGDDQQDPI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 341 PTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFGSDL---DASTK 417
Cdd:PRK07196 319 VDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVagaDPMAD 398
|
330
....*....|....*.
gi 300193115 418 QTLVRGERLTQLLKQN 433
Cdd:PRK07196 399 QAVHYYPAITQFLRQE 414
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
99-439 |
1.50e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 140.64 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 99 VPVGPGLLGRVVDALGNPIDGKGPIdaAGRSRAQVKAPGILP--RRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTG 176
Cdd:PRK05688 103 LPMGMSMLGRVLDGAGRALDGKGPM--KAEDWVPMDGPTINPlnRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 177 KTaVALDTIlnqKRWNNGSdeskklYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIG 256
Cdd:PRK05688 181 KS-VLLGMM---TRFTEAD------IIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 257 EWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAklSEKEGSGSLTALPVIETQGGDV 336
Cdd:PRK05688 251 EYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEGDDQ 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 337 SAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYRE------VAAFAQFGs 410
Cdd:PRK05688 329 QDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQsrdlisVGAYVAGG- 407
|
330 340 350
....*....|....*....|....*....|.
gi 300193115 411 dlDASTKQTLVRGERLTQLLKQ--NQYSPLA 439
Cdd:PRK05688 408 --DPETDLAIARFPHLVQFLRQglRENVSLA 436
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
99-375 |
2.73e-34 |
|
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: 130.42 E-value: 2.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 99 VPVGPGLLGRVVDALGNPIDGKGPIDAagRSRAQVKAPGILP--RRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTG 176
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDGGPPILP--EDYLDINGPPINPvaRIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 177 KTAVALdTILNQKRWNnGSDESKKLycVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIG 256
Cdd:cd01135 82 HNELAA-QIARQAGVV-GSEENFAI--VFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 257 EWFR-DNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSEKEGSgsLTALPVIETQ 332
Cdd:cd01135 158 EYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGRKGS--ITQIPILTMP 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 300193115 333 GGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSR 375
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
89-409 |
2.36e-33 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 131.27 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 89 LVKRTGNIVDVPVGPGLLGRVVDALGN---PIDGKGPIDAAGRSRA-QVKAPGILPRRSVHEPVQTGLKAVDALVPIGRG 164
Cdd:PRK08149 72 VLKPTGKPLSVWVGEALLGAVLDPTGKiveRFDAPPTVGPISEERViDVAPPSYAERRPIREPLITGVRAIDGLLTCGVG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 165 QRELIIGDRQTGKTAVaLDTILNQkrwnngSDESkklycVYVA--VGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAA 242
Cdd:PRK08149 152 QRMGIFASAGCGKTSL-MNMLIEH------SEAD-----VFVIglIGERGREVTEFVESLRASSRREKCVLVYATSDFSS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 243 PLQYLAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSekegSGS 322
Cdd:PRK08149 220 VDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATL----AGS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 323 LTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREV 402
Cdd:PRK08149 296 ITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEEL 375
|
....*..
gi 300193115 403 AAFAQFG 409
Cdd:PRK08149 376 QLFIDLG 382
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
99-375 |
5.61e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 130.48 E-value: 5.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 99 VPVGPGLLGRVVDALGNPIDGKGPIdAAGRSRAQVKA--PGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTG 176
Cdd:PRK08927 92 VRPSRAWLGRVVNALGEPIDGKGPL-PQGPVPYPLRAppPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 177 KTavaldTILNQKRWNNGSDESkklycVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIG 256
Cdd:PRK08927 171 KS-----VLLSMLARNADADVS-----VIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 257 EWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAklSEKEGSGSLTALPVIETQGGDV 336
Cdd:PRK08927 241 EYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVDGDDH 318
|
250 260 270
....*....|....*....|....*....|....*....
gi 300193115 337 SAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSR 375
Cdd:PRK08927 319 NEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSR 357
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
29-95 |
6.79e-32 |
|
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, in mitochondrial inner membranes, and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349740 [Multi-domain] Cd Length: 67 Bit Score: 116.78 E-value: 6.79e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300193115 29 ETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKEGELVKRTGN 95
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
99-411 |
3.28e-31 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 125.67 E-value: 3.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 99 VPVGPGLLGRVVDALGNPIDGKGPIDAAgrSRAQVKAPGILP--RRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTG 176
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTG--ETGALITPPFNPlqRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 177 KTaVALDTIlnqKRWNNGSdeskklYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIG 256
Cdd:PRK07960 188 KS-VLLGMM---ARYTQAD------VIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 257 EWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAklSEKEGSGSLTALPVIETQGGDV 336
Cdd:PRK07960 258 EDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG--NGISGGGSITAFYTVLTEGDDQ 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 337 SAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSA-------AQVKALKQVagslklfLAQYRE------VA 403
Cdd:PRK07960 336 QDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAlideqhyARVRQFKQL-------LSSFQRnrdlvsVG 408
|
....*...
gi 300193115 404 AFAQfGSD 411
Cdd:PRK07960 409 AYAK-GSD 415
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
99-444 |
2.07e-29 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 120.01 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 99 VPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKT 178
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 179 AVaLDTIlnqkrwnngSDESKKLYCVYVAVGQKRSTVAQLVqtlEQHD---AMKYSIIVAATASEAAPLQYLAPFTAASI 255
Cdd:PRK05922 172 SL-LSTI---------AKGSKSTINVIALIGERGREVREYI---EQHKeglAAQRTIIIASPAHETAPTKVIAGRAAMTI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 256 GEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKlSEKegsGSLTALPVIetqggd 335
Cdd:PRK05922 239 AEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-NDK---GSITALYAI------ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 336 vsAYIPTN-------VISITDGQIFL---EAELFykgiRPAINVGLSVSRvgSAAQVKALKQVAGSLKL--FLAQYREVA 403
Cdd:PRK05922 309 --LHYPNHpdiftdyLKSLLDGHFFLtpqGKALA----SPPIDILTSLSR--SARQLALPHHYAAAEELrsLLKAYHEAL 380
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 300193115 404 AFAQFGSDLDASTKQtLVRGERLTQLLKQNQYSPLATEEQV 444
Cdd:PRK05922 381 DIIQLGAYVPGQDAH-LDRAVKLLPSIKQFLSQPLSSYCAL 420
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
87-448 |
6.70e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 118.54 E-value: 6.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 87 GELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGkgPIDAAGRSRAQVKAPGI--LPRRSVHEPVQTGLKAVDALVPIGRG 164
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 165 QRELIIGDRQTGKTavaldTILNQKRWNNGSDESkklycVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPL 244
Cdd:PRK06793 157 QKIGIFAGSGVGKS-----TLLGMIAKNAKADIN-----VISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 245 QYLAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPgreaYPGDVFYLHS---RLLERAAKLSEkegsG 321
Cdd:PRK06793 227 QLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK----G 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 322 SLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYRE 401
Cdd:PRK06793 299 SITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKE 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 300193115 402 VAAFAQFGS----DLDASTKQTLVRGERLTQLLKQNQYSPLATEEQVPLIY 448
Cdd:PRK06793 379 NELYFKLGTiqenAENAYIFECKNKVEGINTFLKQGRSDSFQFDDIVEAMH 429
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
45-375 |
1.62e-28 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 118.00 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 45 GLNNIQAEELVEFSSG----VKGMALNLEPGQVGIVLF-GSDRLVKEGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDG 119
Cdd:PRK04196 19 GVEGVAYGEIVEIELPngekRRGQVLEVSEDKAVVQVFeGTTGLDLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 120 KGPIDAAGRsRAQVKAPgILP--RRSVHEPVQTGLKAVDALVPIGRGQR------------EL---IIgdRQTgktaval 182
Cdd:PRK04196 99 GPEIIPEKR-LDINGAP-INPvaREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnELaaqIA--RQA------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 183 dTILnqkrwnnGSDEskKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFR-D 261
Cdd:PRK04196 168 -KVL-------GEEE--NFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 262 NGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSEKEGSgsLTALPVIETQGGDVSA 338
Cdd:PRK04196 238 KGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGKKGS--ITQIPILTMPDDDITH 312
|
330 340 350
....*....|....*....|....*....|....*..
gi 300193115 339 YIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSR 375
Cdd:PRK04196 313 PIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
75-433 |
4.69e-28 |
|
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 211621 [Multi-domain] Cd Length: 461 Bit Score: 116.74 E-value: 4.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 75 IVLFGSDRLVKeGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKA 154
Cdd:TIGR01039 55 IAMGSTDGLVR-GLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 155 VDALVPIGRGQRELIIGDRQTGKTAVALDTILNQKRWNNGsdeskklYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIV 234
Cdd:TIGR01039 134 IDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGG-------YSVFAGVGERTREGNDLYHEMKESGVIDKTALV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 235 AATASEAAPLQYLAPFTAASIGEWFRD-NGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYpgdvfylHSRLLERAAK 313
Cdd:TIGR01039 207 YGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGY-------QPTLATEMGE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 314 LSEKEGS---GSLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQV-KALKQVA 389
Cdd:TIGR01039 280 LQERITStktGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVgEEHYDVA 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 300193115 390 GSLKLFLAQYREVA-AFAQFGSD-LDASTKQTLVRGERLTQLLKQN 433
Cdd:TIGR01039 360 RGVQQILQRYKELQdIIAILGMDeLSEEDKLTVERARRIQRFLSQP 405
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
93-380 |
7.89e-24 |
|
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: 104.03 E-value: 7.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 93 TGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAagRSRAQVKAPGILPRRSVH--EPVQTGLKAVDALVPIGRGQRELII 170
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLA--EDYLDINGQPINPYARIYpeEMIQTGISAIDVMNSIARGQKIPIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 171 GD-------------RQTGKTAVALDTILNqkrwnngsDESKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAAT 237
Cdd:TIGR01040 148 SAaglphneiaaqicRQAGLVKLPTKDVHD--------GHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 238 ASEAAPLQYLAPFTAASIGEWFR-DNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSE 316
Cdd:TIGR01040 220 ANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEG 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300193115 317 KEGSgsLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAA 380
Cdd:TIGR01040 300 RNGS--ITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 361
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
99-375 |
4.25e-20 |
|
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: 90.33 E-value: 4.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 99 VPVGPGLLGRVVDALGNPI----DGKGPIDAAGRS--RAQVKAPGILPRR-SVHEPVQTGLKAVDALVPIGRGQRELIIG 171
Cdd:cd01134 4 VELGPGLLGSIFDGIQRPLeviaETGSIFIPRGVNvqRWPVRQPRPVKEKlPPNVPLLTGQRVLDTLFPVAKGGTAAIPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 172 DRQTGKTavaldtILNQK--RWNNgSDeskklYCVYVAVGQKRSTVA-------QLVQTLEQHDAMKYSIIVAAT----- 237
Cdd:cd01134 84 PFGCGKT------VISQSlsKWSN-SD-----VVIYVGCGERGNEMAevleefpELKDPITGESLMERTVLIANTsnmpv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 238 -ASEAAPlqylapFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL---LERAAK 313
Cdd:cd01134 152 aAREASI------YTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYERAGR 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300193115 314 ---LSEKEGSGSLTALPVIETQGGDVSAYIPTNVISITdgQIF--LEAELFYKGIRPAINVGLSVSR 375
Cdd:cd01134 223 vrcLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
99-376 |
8.67e-19 |
|
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: 86.50 E-value: 8.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 99 VPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKT 178
Cdd:cd01133 2 VPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 179 AVALDTILNQKRWNNGsdeskklYCVYVAVGQKrstvaqlvqTLEQHD---AMKYSIIVAATASEAAPLQY--------- 246
Cdd:cd01133 82 VLIMELINNIAKAHGG-------YSVFAGVGER---------TREGNDlyhEMKESGVINLDGLSKVALVYgqmneppga 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 247 --LAPFTAASIGEWFRD-NGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAklSEKEgsGSL 323
Cdd:cd01133 146 raRVALTGLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERIT--STKK--GSI 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 300193115 324 TALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRV 376
Cdd:cd01133 222 TSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
66-354 |
7.41e-18 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 85.86 E-value: 7.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 66 LNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKG-----PIDAAGRSRAQVKApgILP 140
Cdd:PRK02118 43 IRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPelegePIEIGGPSVNPVKR--IVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 141 RrsvhEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVaLDTILNQKrwnngsdESKKLycVYVAVGQKRSTVAQLVQ 220
Cdd:PRK02118 121 R----EMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNAL-LARIALQA-------EADII--ILGGMGLTFDDYLFFKD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 221 TLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFR-DNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGD 299
Cdd:PRK02118 187 TFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGS 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 300193115 300 vfyLHSRLLERAAKLSEKEGSGSLTALPVIETQGGDVSAYIPTNVISITDGQIFL 354
Cdd:PRK02118 267 ---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
29-94 |
7.14e-16 |
|
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: 72.19 E-value: 7.14e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300193115 29 ETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKEGELVKRTG 94
Cdd:pfam02874 4 VIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
386-452 |
1.44e-15 |
|
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: 71.32 E-value: 1.44e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300193115 386 KQVAGSLKLFLAQYREVAAFAQFGSD--LDASTKQTLVRGERLTQLLKQNQYSPLATEEQVPLIYAGVN 452
Cdd:cd01429 2 KAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
74-164 |
5.26e-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: 77.05 E-value: 5.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 74 GIVLFGSDRLVKeGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLK 153
Cdd:COG0055 57 CIAMDSTDGLVR-GMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIK 135
|
90
....*....|.
gi 300193115 154 AVDALVPIGRG 164
Cdd:COG0055 136 VIDLLAPYAKG 146
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
204-368 |
1.31e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 64.27 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 204 VYVAVGQKRSTVAQLVQTLEQ-------HDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKHALIVYDDLSKQ 276
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 277 AVAYRQLSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKLSEKEGSGSLTALPVIETQGGDVSAYIPTNVISITDG 350
Cdd:PRK14698 766 AEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKV 842
|
170
....*....|....*...
gi 300193115 351 QIFLEAELFYKGIRPAIN 368
Cdd:PRK14698 843 FWALDADLARRRHFPAIN 860
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
79-368 |
6.34e-10 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 61.21 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 79 GSDRLvKEGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGIL---PRRSVHEpvqTGLKAV 155
Cdd:CHL00060 77 ATDGL-MRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTKLSIFE---TGIKVV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 156 DALVPIGRGQRELIIGDRQTGKTAVALDTILNQKRWNNGSDeskklycVYVAVGQKrstvaqlvqTLEQHD---AMKYS- 231
Cdd:CHL00060 153 DLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVS-------VFGGVGER---------TREGNDlymEMKESg 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 232 IIVAATASEA-APLQY-----------LAPFTAASIGEWFRD-NGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPG 298
Cdd:CHL00060 217 VINEQNIAESkVALVYgqmneppgarmRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQP 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 299 DVFYLHSRLLERAAklSEKEgsGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAIN 368
Cdd:CHL00060 297 TLSTEMGSLQERIT--STKE--GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 362
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
145-368 |
2.65e-08 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 56.33 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 145 HEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTavaldtILNQK--RWNNgSDeskklYCVYVAVGQKRSTVaqlVQTL 222
Cdd:PRK04192 208 VEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT------VTQHQlaKWAD-AD-----IVIYVGCGERGNEM---TEVL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 223 EQ----------HDAMKYSIIVAAT------ASEAAPlqylapFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLL 286
Cdd:PRK04192 273 EEfpelidpktgRPLMERTVLIANTsnmpvaAREASI------YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGR 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 287 LRRPPGREAYPGdvfYLHSRL---LERAAKLSEKEGS-GSLTALPVIETQGGDVSAYIPTNVISITdgQIF--LEAELFY 360
Cdd:PRK04192 347 LEEMPGEEGYPA---YLASRLaefYERAGRVKTLGGEeGSVTIIGAVSPPGGDFSEPVTQNTLRIV--KVFwaLDAELAD 421
|
....*...
gi 300193115 361 KGIRPAIN 368
Cdd:PRK04192 422 RRHFPAIN 429
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
92-393 |
2.46e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 40.07 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 92 RTGNIVDVPVGPGLLGRVVDALgNPIDGKGPIDAAGRSRAQVKAPgILPR---RSVHEPVQTGLKAVDALVPIGRGQREL 168
Cdd:PRK12608 60 RTGDVVEGVARPRERYRVLVRV-DSVNGTDPEKLARRPHFDDLTP-LHPRerlRLETGSDDLSMRVVDLVAPIGKGQRGL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 169 IIGDRQTGKTavaldTILNQkrwnngsdeskklycVYVAVGQKRSTVAQLVQTL----EQHDAMKYSI--IVAATASEAA 242
Cdd:PRK12608 138 IVAPPRAGKT-----VLLQQ---------------IAAAVAANHPEVHLMVLLIderpEEVTDMRRSVkgEVYASTFDRP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 243 PLQYLAPFTAA-SIGEWFRDNGKHALIVYDDLSKQAVAYRQLSlllrRPPGREAYPGdvfyLHSRLLER------AAKLS 315
Cdd:PRK12608 198 PDEHIRVAELVlERAKRLVEQGKDVVILLDSLTRLARAYNNEV----ESSGRTLSGG----VDARALQRpkrlfgAARNI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300193115 316 EKEGSGSLTALPVIETqGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSR-----VGSA--AQVKALKQV 388
Cdd:PRK12608 270 EEGGSLTIIATALVDT-GSRMDEVIFEEFKGTGNMEIVLDRELADKRVFPAIDIAKSGTRreellLDSKelEKVRRLRRA 348
|
....*
gi 300193115 389 AGSLK 393
Cdd:PRK12608 349 LASRK 353
|
|
| |
