|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
83-573 |
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: 847.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 83 LSLLTDKLKEFRPRTKGEEIGRVLSIGDGIAKLTGLESASYGEIVVFETGVKGMVLDLKKDYLGCIIFGEDKDISEGSQV 162
Cdd:COG0056 9 SSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEGIKEGDTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 163 FRTKKTAGIPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQRELII 242
Cdd:COG0056 89 KRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQRELII 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 243 GDRQTGKTAIALDTILKQKDEDLICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEY 322
Cdd:COG0056 169 GDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 323 FMDQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQLSEKLGGGSITSLPIVETQAGDISA 402
Cdd:COG0056 249 FMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 403 YIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYREMEIFTQFASDLDENTKR 482
Cdd:COG0056 329 YIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRA 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 483 QLVYGSGLMEILKQNQFSPLKHYEEVIILVVALAKLLIDLDKKKIKETLKNIISHIESEDPALIEEIERTKDLTDASREK 562
Cdd:COG0056 409 QLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGKLDDEIEEK 488
|
490
....*....|.
gi 1778695090 563 IISLAQAYLDS 573
Cdd:COG0056 489 LKAAIEEFKKT 499
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
84-570 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 802.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 84 SLLTDKLKEFRPRTKGEEIGRVLSIGDGIAKLTGLESASYGEIVVFETGVKGMVLDLKKDYLGCIIFGEDKDISEGSQVF 163
Cdd:PRK09281 10 AIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIKEGDTVK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 164 RTKKTAGIPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQRELIIG 243
Cdd:PRK09281 90 RTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 244 DRQTGKTAIALDTILKQKDEDLICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYF 323
Cdd:PRK09281 170 DRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 324 MDQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQLSEKLGGGSITSLPIVETQAGDISAY 403
Cdd:PRK09281 250 MDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAY 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 404 IPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYREMEIFTQFASDLDENTKRQ 483
Cdd:PRK09281 330 IPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 484 LVYGSGLMEILKQNQFSPLKHYEEVIILVVALAKLLIDLDKKKIKETLKNIISHIESEDPALIEEIERTKDLTDASREKI 563
Cdd:PRK09281 410 LERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKDLSDEIEAKL 489
|
....*..
gi 1778695090 564 ISLAQAY 570
Cdd:PRK09281 490 KAAIEEF 496
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
76-572 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 690.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 76 DTDSSNYLSLLTDKLKEFRPRTKGEEIGRVLSIGDGIAKLTGLESASYGEIVVFETGVKGMVLDLKKDYLGCIIFGEDKD 155
Cdd:PRK13343 2 KSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 156 ISEGSQVFRTKKTAGIPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGK 235
Cdd:PRK13343 82 ILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 236 GQRELIIGDRQTGKTAIALDTILKQKDEDLICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYS 315
Cdd:PRK13343 162 GQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 316 ATAIGEYFMDQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQLSEKLGGGSITSLPIVET 395
Cdd:PRK13343 242 GCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIET 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 396 QAGDISAYIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYREMEIFTQFASD 475
Cdd:PRK13343 322 LAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 476 LDENTKRQLVYGSGLMEILKQNQFSPLKHYEEVIILVVALAKLLIDLDKKKIKETLKNIISHIESEDPALIEEIERTKDL 555
Cdd:PRK13343 402 LDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPREL 481
|
490
....*....|....*..
gi 1778695090 556 TDASREKIISLAQAYLD 572
Cdd:PRK13343 482 DEAWLAALEEILREAGE 498
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
82-563 |
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: 688.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 82 YLSLLTDKLKEFRPRTKGEEIGRVLSIGDGIAKLTGLESASYGEIVVFETGVKGMVLDLKKDYLGCIIFGEDKDISEGSQ 161
Cdd:TIGR00962 7 ISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIREGST 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 162 VFRTKKTAGIPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQRELI 241
Cdd:TIGR00962 87 VKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 242 IGDRQTGKTAIALDTILKQKDEDLICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGE 321
Cdd:TIGR00962 167 IGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 322 YFMDQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQLSEKLGGGSITSLPIVETQAGDIS 401
Cdd:TIGR00962 247 YFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIETQAGDVS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 402 AYIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYREMEIFTQFASDLDENTK 481
Cdd:TIGR00962 327 AYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASDLDEATK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 482 RQLVYGSGLMEILKQNQFSPLKHYEEVIILVVALAKLLIDLDKKKIKETLKNIISHIESEDPALIEEIERTKDLTDASRE 561
Cdd:TIGR00962 407 KQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKLTEELEA 486
|
..
gi 1778695090 562 KI 563
Cdd:TIGR00962 487 KL 488
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
102-575 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 640.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 102 IGRVLSIGDGIAKLTGLESASYGEIVVFETGVKGMVLDLKKDYLGCIIFGEDKDISEGSQVFRTKKTAGIPVGPDLLGRV 181
Cdd:CHL00059 7 TGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 182 VNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQRELIIGDRQTGKTAIALDTILKQK 261
Cdd:CHL00059 87 VNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 262 DEDLICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYFMDQGKDVLIIYDDLSKHA 341
Cdd:CHL00059 167 GQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 342 VAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQLSEKLGGGSITSLPIVETQAGDISAYIPTNIISITDGQIFLESD 421
Cdd:CHL00059 247 QAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSAD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 422 LFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYREMEIFTQFASDLDENTKRQLVYGSGLMEILKQNQFSP 501
Cdd:CHL00059 327 LFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQSAP 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1778695090 502 LKHYEEVIILVVALAKLLIDLDKKKIKETLKNIISHIESEDPALIEEIERTKDLTDAS----REKIISLAQAYLDSSK 575
Cdd:CHL00059 407 LTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAeallKEAIQEQLELFLLQEQ 484
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
90-571 |
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: 544.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 90 LKEFRPRTKGEEIGRVLSIGDGIAKLTGLESASYGEIVVFETGVKGMVLDLKKDYLGCIIFGEDKDISEGSQVFRTKKTA 169
Cdd:TIGR03324 16 RESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERTGRVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 170 GIPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQRELIIGDRQTGK 249
Cdd:TIGR03324 96 DVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDRQTGK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 250 TAIALDTILKQKDEDLICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYFMDQGKD 329
Cdd:TIGR03324 176 TAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSIGEHFMEQGRD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 330 VLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQLSEKLGGGSITSLPIVETQAGDISAYIPTNII 409
Cdd:TIGR03324 256 VLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQNISAYIPTNLI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 410 SITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYREMEIFTQFASDLDENTKRQLVYGSG 489
Cdd:TIGR03324 336 SITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDENTRKTIEHGRR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 490 LMEILKQNQFSPLKHYEEVIILVVALAKLLIDLDKKKIKETLKNIISHIESEDPALIEEIERTKDLTDASREKIISLAQA 569
Cdd:TIGR03324 416 IRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSDEDREQILDIARG 495
|
..
gi 1778695090 570 YL 571
Cdd:TIGR03324 496 AL 497
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
171-441 |
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: 512.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 171 IPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQRELIIGDRQTGKT 250
Cdd:cd01132 4 VPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 251 AIALDTILKQKDEDLICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYFMDQGKDV 330
Cdd:cd01132 84 AIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 331 LIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQLSEKLGGGSITSLPIVETQAGDISAYIPTNIIS 410
Cdd:cd01132 164 LIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTNVIS 243
|
250 260 270
....*....|....*....|....*....|.
gi 1778695090 411 ITDGQIFLESDLFFAGQRPAINVGLSVSRVG 441
Cdd:cd01132 244 ITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
223-438 |
2.30e-107 |
|
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: 320.84 E-value: 2.30e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 223 GILAIDSMFPIGKGQRELIIGDRQTGKTAIAlDTILKQKDEDlICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATA 302
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD-VVVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 303 ADSAAFQYIAPYSATAIGEYFMDQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQLSEKl 382
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGK- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1778695090 383 gGGSITSLPIVETQAGDISAYIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVS 438
Cdd:pfam00006 158 -GGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
100-466 |
6.94e-104 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 324.69 E-value: 6.94e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 100 EEIGRVLSIGDGIAKLT---GLESASYGEIVVFE----TGVKGMVLDLKKD-YLGCIIFGEDKDISEGSQVFRTKKTAGI 171
Cdd:PTZ00185 38 EMIGYVHSIDGTIATLIpapGNPGVAYNTIIMIQvsptTFAAGLVFNLEKDgRIGIILMDNITEVQSGQKVMATGKLLYI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 172 PVGPDLLGRVVNPLGEPIDgQGKI--------SPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQRELIIG 243
Cdd:PTZ00185 118 PVGAGVLGKVVNPLGHEVP-VGLLtrsralleSEQTLGKVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 244 DRQTGKTAIALDTILKQ--------KDEDLICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYS 315
Cdd:PTZ00185 197 DRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 316 ATAIGEYFMDQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQLSEKLGGGSITSLPIVET 395
Cdd:PTZ00185 277 GVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVET 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1778695090 396 QAGDISAYIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYREM 466
Cdd:PTZ00185 357 LSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRKL 427
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
171-440 |
4.70e-100 |
|
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: 304.38 E-value: 4.70e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 171 IPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQRELIIGDRQTGKT 250
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 251 AIALDTILKQKDED-LICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYFMDQGKD 329
Cdd:cd19476 82 VLAMQLARNQAKAHaGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 330 VLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQLseKLGGGSITSLPIVETQAGDISAYIPTNII 409
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKV--KDGGGSITAIPAVSTPGDDLTDPIPDNTF 239
|
250 260 270
....*....|....*....|....*....|.
gi 1778695090 410 SITDGQIFLESDLFFAGQRPAINVGLSVSRV 440
Cdd:cd19476 240 AILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
133-539 |
7.44e-94 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 296.50 E-value: 7.44e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 133 VKGMVLDLKKDYLGCIIFGEDKDISEGSQVFRTKKTAGIPVGPDLLGRVVNPLGEPIDGQGKIS-PIAYY----KIEKEA 207
Cdd:PRK07165 35 VKAFVISATEDKAYLLINNEKGKIKINDELIELNNTNKVKTSKEYFGKIIDIDGNIIYPEAQNPlSKKFLpntsSIFNLA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 208 PEIIDRQSVYRPLETGILAIDSMFPIGKGQRELIIGDRQTGKTAIALDTILKQKDEDLICIYAAIGQKASSLALLVENLK 287
Cdd:PRK07165 115 HGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 288 KKNAFDNCIVVAATAADSAAfQYIAPYSATAIGEYFMdQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYL 367
Cdd:PRK07165 195 EHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAENIS-YNDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 368 HSRLLERSAQLsekLGGGSITSLPIVETQAGDISAYIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTK 447
Cdd:PRK07165 273 HSKLLERAGKF---KNRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 448 AIKKAAASLRLSLAQYREMEIFTQFASDLDENTKRQLVYGSGLMEILKQNQFSplkHYEEVIILVValAKLL---IDLDK 524
Cdd:PRK07165 350 TITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKGKMIEKMFNQKGFS---LYSYRFVLLI--SKLIswgLLKDV 424
|
410
....*....|....*
gi 1778695090 525 KKIKETLKNIISHIE 539
Cdd:PRK07165 425 KDEQKALDFIDYLIE 439
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
171-440 |
8.85e-55 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 186.23 E-value: 8.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 171 IPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQRELIIGDRQTGKT 250
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 251 AIaLDTILKQKDEDLICIyAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYFMDQGKDV 330
Cdd:cd01136 82 TL-LGMIARNTDADVNVI-ALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 331 LIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAqlseKLGGGSITSLPIVETQAGDISAYIPTNIIS 410
Cdd:cd01136 160 LLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAG----NGEKGSITAFYTVLVEGDDFNDPIADEVRS 235
|
250 260 270
....*....|....*....|....*....|
gi 1778695090 411 ITDGQIFLESDLFFAGQRPAINVGLSVSRV 440
Cdd:cd01136 236 ILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
151-471 |
9.69e-53 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 186.11 E-value: 9.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 151 GEDKDISEGSQVFRTKKTAGIPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSM 230
Cdd:PRK06936 77 GEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 231 FPIGKGQRELIIGDRQTGKTAIaLDTILKQKDEDlICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQY 310
Cdd:PRK06936 157 LTCGEGQRMGIFAAAGGGKSTL-LASLIRSAEVD-VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 311 IAPYSATAIGEYFMDQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQlSEKlggGSITSL 390
Cdd:PRK06936 235 KAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ-SDK---GSITAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 391 PIVETQAGDISAYIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYREMEIFT 470
Cdd:PRK06936 311 YTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLL 390
|
.
gi 1778695090 471 Q 471
Cdd:PRK06936 391 Q 391
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
81-467 |
1.02e-51 |
|
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: 182.92 E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 81 NYLSLLTDKLKEFRPRTKgeeIGRVLSIGDGIAKLTGLEsASYGEIVVFETG----VKGMVLDLKKDYLGCIIFGEDKDI 156
Cdd:COG1157 2 DRLARLLARLEELPPVRV---SGRVTRVVGLLIEAVGPD-ASIGELCEIETAdgrpVLAEVVGFRGDRVLLMPLGDLEGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 157 SEGSQVFRTKKTAGIPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKG 236
Cdd:COG1157 78 SPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 237 QReliIGdr---qtGKTAIaLDTILKQKDEDLICIyAAIGQKASSLALLVENLKKKNAFDNCIVVaataadsaafqyIAP 313
Cdd:COG1157 158 QR---IGifagsgvGKSTL-LGMIARNTEADVNVI-ALIGERGREVREFIEDDLGEEGLARSVVV------------VAT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 314 ------------YSATAIGEYFMDQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAqlseK 381
Cdd:COG1157 221 sdepplmrlraaYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAG----N 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 382 LGGGSITSL------------PIVETqagdisayiptnIISITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTKAI 449
Cdd:COG1157 297 GGKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEH 364
|
410
....*....|....*...
gi 1778695090 450 KKAAASLRLSLAQYREME 467
Cdd:COG1157 365 RALARRLRRLLARYEENE 382
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
103-513 |
3.28e-49 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 176.54 E-value: 3.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 103 GRVLSIGDGIAKLTgLESASYGEIVVFE-TGVKGMVLDLKKDYLGCIIFGEDKDISEGSQVFRTKKTAGIPVGPDLLGRV 181
Cdd:PRK06820 31 GPIVEIGPTLLRAS-LPGVAQGELCRIEpQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 182 VNPLGEPIDGQGkisPIAYY--KIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQRELIIGDRQTGKTAIaLDTILK 259
Cdd:PRK06820 110 LDGLGAPIDGGP---PLTGQwrELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTL-LGMLCA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 260 QKDEDLIcIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYFMDQGKDVLIIYDDLSK 339
Cdd:PRK06820 186 DSAADVM-VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 340 HAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQlSEKlggGSITSLPIVETQAGDISAYIPTNIISITDGQIFLE 419
Cdd:PRK06820 265 YARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGN-SDR---GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 420 SDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYREMEIFTQ---FASDLDENTKRQLVYGSGLMEILKQ 496
Cdd:PRK06820 341 RRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRvgeYQAGEDLQADEALQRYPAICAFLQQ 420
|
410
....*....|....*....
gi 1778695090 497 --NQFSPLKHYEEVIILVV 513
Cdd:PRK06820 421 dhSETAHLETTLEHLAQVV 439
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
83-471 |
9.22e-48 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 172.65 E-value: 9.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 83 LSLLTDKL-KEFRPRTKGEEIGRVLSIGDGIAKLTGLEsASYGEIVVFETG-----VKGMVLDLKKDYLGCIIFGEDKDI 156
Cdd:PRK09099 5 LSRLADALeRELAALPAVRRTGKVVEVIGTLLRVSGLD-VTLGELCELRQRdgtllQRAEVVGFSRDVALLSPFGELGGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 157 SEGSQVFRTKKTAGIPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKG 236
Cdd:PRK09099 84 SRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 237 QRELIIGDRQTGK-TAIALDTILKQKDEDLIciyAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYS 315
Cdd:PRK09099 164 QRMGIFAPAGVGKsTLMGMFARGTQCDVNVI---ALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 316 ATAIGEYFMDQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERsAQLSEKlggGSITSLPIV-- 393
Cdd:PRK09099 241 ATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLER-AGMGET---GSITALYTVla 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1778695090 394 ETQAGdiSAYIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYREMEIFTQ 471
Cdd:PRK09099 317 EDESG--SDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQ 392
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
121-497 |
2.34e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 171.44 E-value: 2.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 121 ASYGEIVVFETG------VKGMVLDLKKDYLGCIIFGEDKDISEGSQVFRTKKTAGIPVGPDLLGRVVNPLGEPIDGQGK 194
Cdd:PRK07721 37 SSIGDVCYIHTKgggdkaIKAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 195 ISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQRELIIGDRQTGKTAIaLDTILKQKDEDLICIyAAIGQ 274
Cdd:PRK07721 117 PKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTL-MGMIARNTSADLNVI-ALIGE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 275 KASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYFMDQGKDVLIIYDDLSKHAVAYRSISLLLERS 354
Cdd:PRK07721 195 RGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 355 PGREAYPGDVFYLHSRLLERSAQlSEKlggGSITSLPIVETQAGDISAYIPTNIISITDGQIFLESDLFFAGQRPAINVG 434
Cdd:PRK07721 275 PTTKGYTPSVFAILPKLLERTGT-NAS---GSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVL 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 435 LSVSRVGGAAQTKAIKKAAASLRLSLAQYREMEIFTQFAS-------DLDENTKRQLVygsgLMEILKQN 497
Cdd:PRK07721 351 KSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAykrgssrEIDEAIQFYPQ----IISFLKQG 416
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
83-497 |
1.79e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 166.01 E-value: 1.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 83 LSLLTDKLKEFRPRTKgeeIGRVLSIGDGIAKLTGLEsASYGEIVVFETGVK-----GMVLDLKKDYLGCIIFGEDKDIS 157
Cdd:PRK08472 3 LESLKNKLQKFNLSPR---FGSITKISPTIIEADGLN-PSVGDIVKIESSDNgkeclGMVVVIEKEQFGISPFSFIEGFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 158 EGSQVFRTKKTAGIPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQ 237
Cdd:PRK08472 79 IGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 238 RELIIGDRQTGKTAIaLDTILKQKDEDlICIYAAIGQKASSLALLVE-NLkkKNAFDNCIVVAATAADSAAFQYIAPYSA 316
Cdd:PRK08472 159 KLGIFAGSGVGKSTL-MGMIVKGCLAP-IKVVALIGERGREIPEFIEkNL--GGDLENTVIVVATSDDSPLMRKYGAFCA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 317 TAIGEYFMDQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQlsEKlGGGSITSLPIVETQ 396
Cdd:PRK08472 235 MSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK--EE-GKGSITAFFTVLVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 397 AGDISAYIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYREMEIFTQFAS-- 474
Cdd:PRK08472 312 GDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAyq 391
|
410 420
....*....|....*....|....*....
gi 1778695090 475 -----DLDENTKRQlvygsGLME-ILKQN 497
Cdd:PRK08472 392 kgndkELDEAISKK-----EFMEqFLKQN 415
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
445-570 |
6.32e-45 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 154.91 E-value: 6.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 445 QTKAIKKAAASLRLSLAQYREMEIFTQFASDLDENTKRQLVYGSGLMEILKQNQFSPLKHYEEVIILVVALAKLLIDLDK 524
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1778695090 525 KKIKETLKNIISHIESEDPALIEEIERTKDLTDASREKIISLAQAY 570
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
449-573 |
6.07e-43 |
|
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: 149.82 E-value: 6.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 449 IKKAAASLRLSLAQYREMEIFTQFASDLDENTKRQLVYGSGLMEILKQNQFSPLKHYEEVIILVVALAKLLIDLDKKKIK 528
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1778695090 529 ETLKNIISHIESEDPALIEEIERTKDLTDASREKIISLAQAYLDS 573
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKS 125
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
165-469 |
4.29e-41 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 154.00 E-value: 4.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 165 TKKTAGIPVGPDLLGRVVNPLGEpIDGQGKISPIAYYK-----IEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQRE 239
Cdd:PRK08149 76 TGKPLSVWVGEALLGAVLDPTGK-IVERFDAPPTVGPIseervIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 240 LIIGDRQTGKTAIaLDTILKQKDEDlICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAI 319
Cdd:PRK08149 155 GIFASAGCGKTSL-MNMLIEHSEAD-VFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTV 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 320 GEYFMDQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQLSEklggGSITSLPIVETQAGD 399
Cdd:PRK08149 233 AEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA----GSITAFYTVLLESEE 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 400 ISAYIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYREMEIF 469
Cdd:PRK08149 309 EPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLF 378
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
150-471 |
3.09e-40 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 151.64 E-value: 3.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 150 FGEDKDISEGSQVFRTKKTAGIPVGPDLLGRVVNPLGEPIDGQgKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDS 229
Cdd:PRK07594 70 FTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 230 MFPIGKGQRELIIGDRQTGKTAIaLDTILKQKDEDlICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQ 309
Cdd:PRK07594 149 VATCGEGQRVGIFSAPGVGKSTL-LAMLCNAPDAD-SNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALER 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 310 YIAPYSATAIGEYFMDQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAqLSEKlggGSITS 389
Cdd:PRK07594 227 VRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-MGEK---GSITA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 390 LPIVETQAGDISAYIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYREMEIF 469
Cdd:PRK07594 303 FYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELL 382
|
..
gi 1778695090 470 TQ 471
Cdd:PRK07594 383 IR 384
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
171-439 |
1.41e-37 |
|
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: 140.44 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 171 IPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQRELIIGDrqTGKT 250
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSG--SGLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 251 A------IALDTILKQKDEDLICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYF- 323
Cdd:cd01135 82 HnelaaqIARQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 324 MDQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGdvfYLHSRLlersAQLSEKLG-----GGSITSLPIVETQAG 398
Cdd:cd01135 162 YEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDL----ATIYERAGrvegrKGSITQIPILTMPND 234
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1778695090 399 DISAYIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSR 439
Cdd:cd01135 235 DITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
159-465 |
1.18e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 141.76 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 159 GSQVFRTKKTAGIPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQR 238
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 239 ELIIGDRQTGKTaIALDTILKQKDEDLICIyAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATA 318
Cdd:PRK08972 165 MGLFAGSGVGKS-VLLGMMTRGTTADVIVV-GLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 319 IGEYFMDQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQLSEklGGGSITSLPIVETQAG 398
Cdd:PRK08972 243 IAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVLTEGD 320
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1778695090 399 DISAYIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYRE 465
Cdd:PRK08972 321 DLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQ 387
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
117-439 |
1.02e-35 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 139.58 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 117 GLESASYGEIVVFETG----VKGMVLDLKKDYLGCIIFGEDKDIS-EGSQVFRTKKTAGIPVGPDLLGRVVNPLGEPIDG 191
Cdd:PRK04196 19 GVEGVAYGEIVEIELPngekRRGQVLEVSEDKAVVQVFEGTTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 192 QGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQR------------ELIIgdrqtgktAIALDTILK 259
Cdd:PRK04196 99 GPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnELAA--------QIARQAKVL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 260 QKDEDLICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYF-MDQGKDVLIIYDDLS 338
Cdd:PRK04196 171 GEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLaFEKGMHVLVILTDMT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 339 KHAVAYRSISLLLERSPGREAYPGdvfYLHSRLlersAQLSEKLG-----GGSITSLPIVETQAGDISAYIPTNIISITD 413
Cdd:PRK04196 251 NYCEALREISAAREEVPGRRGYPG---YMYTDL----ATIYERAGrikgkKGSITQIPILTMPDDDITHPIPDLTGYITE 323
|
330 340
....*....|....*....|....*.
gi 1778695090 414 GQIFLESDLFFAGQRPAINVGLSVSR 439
Cdd:PRK04196 324 GQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
103-465 |
5.56e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 137.05 E-value: 5.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 103 GRVLSIGDGIAKLTGLES-ASYGEIVVFETG---VKGMVLdlKKDYLGCII--FGEDKDISEGSQVFRtKKTAGIPVGPD 176
Cdd:PRK06002 28 GTVSEVTASHYRVRGLSRfVRLGDFVAIRADggtHLGEVV--RVDPDGVTVkpFEPRIEIGLGDAVFR-KGPLRIRPDPS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 177 LLGRVVNPLGEPIDGQGKISP-IAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQRELIIGDRQTGKTAIaLD 255
Cdd:PRK06002 105 WKGRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTL-LA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 256 TILKQKDEDLICIyAAIGQKASSL-----ALLVENLKKKnafdncIVVAATAADSAAFQYIAPYSATAIGEYFMDQGKDV 330
Cdd:PRK06002 184 MLARADAFDTVVI-ALVGERGREVrefleDTLADNLKKA------VAVVATSDESPMMRRLAPLTATAIAEYFRDRGENV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 331 LIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQLSEklGGGSITSLPIVETQAGDISAYIPTNIIS 410
Cdd:PRK06002 257 LLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLVDGDDHNDPVADSIRG 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1778695090 411 ITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYRE 465
Cdd:PRK06002 335 TLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEE 389
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
112-508 |
2.68e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 135.02 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 112 IAKLTGLESASYGeiVVFETGVKGMVLDLKKDYLGCIIFGEDKDIS------------EGSQVFRTKKTAGIPVGPDLLG 179
Cdd:PRK07196 21 LVRVTGLLLESVG--CRLAIGQRCRIESVDETFIEAQVVGFDRDITylmpfkhpggvlGGARVFPSEQDGELLIGDSWLG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 180 RVVNPLGEPIDGQGKISPIAyyKIEKEAPEI--IDRQSVYRPLETGILAIDSMFPIGKGQRELIIGDRQTGKTAIaLDTI 257
Cdd:PRK07196 99 RVINGLGEPLDGKGQLGGST--PLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVL-LGMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 258 LKQKDEDLICIyAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYFMDQGKDVLIIYDDL 337
Cdd:PRK07196 176 TRYTQADVVVV-GLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 338 SKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLErSAQLSEklGGGSITSLPIVETQAGDISAYIPTNIISITDGQIF 417
Cdd:PRK07196 255 TRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAE-SAGNSS--GNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 418 LESDLFFAGQRPAINVGLSVSR----VGGAAQTkaikKAAASLRLSLAQYREMEIFTQ---FASDLDENTKRQLVYGSGL 490
Cdd:PRK07196 332 LSRKLAEAGHYPAIDISQSISRcmsqVIGSQQA----KAASLLKQCYADYMAIKPLIPlggYVAGADPMADQAVHYYPAI 407
|
410
....*....|....*...
gi 1778695090 491 MEILKQNQFSPLKHYEEV 508
Cdd:PRK07196 408 TQFLRQEVGHPALFSASV 425
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
156-465 |
4.56e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 134.47 E-value: 4.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 156 ISEGSQVFRTKKTAGIPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGK 235
Cdd:PRK05688 88 IAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 236 GQRELIIGDRQTGKTAIaLDTILKQKDEDLICIyAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYS 315
Cdd:PRK05688 168 GQRLGLFAGTGVGKSVL-LGMMTRFTEADIIVV-GLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 316 ATAIGEYFMDQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQLSEklGGGSITSLPIVET 395
Cdd:PRK05688 246 CTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEP--GGGSITAFYTVLS 323
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 396 QAGDISAYIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYRE 465
Cdd:PRK05688 324 EGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQ 393
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
87-509 |
5.63e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 128.17 E-value: 5.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 87 TDKLKEFRPRTKGEEIGRVLSIGDGIAKLTGLESASYGEIVVFETGVKGMVLDLKKDYLGCIIFGEDKDISEGSQVFRTK 166
Cdd:PRK06793 7 NQKWNTFIETPFYTKVGKVHSVQEQFFVAKGPKAKIGDVCFVGEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLIA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 167 KTAGIPVGPDLLGRVVNPLGEPIDGQGKISPIAyyKIEKEAPEI--IDRQSVYRPLETGILAIDSMFPIGKGQRELIIGD 244
Cdd:PRK06793 87 EDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQ--KIKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 245 RQTGKTAIaLDTILKQKDEDlICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYFM 324
Cdd:PRK06793 165 SGVGKSTL-LGMIAKNAKAD-INVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 325 DQGKDVLIIYDDLSKHAVAYRSISLLLERSPgreaYPGDVFYLHS---RLLERSAqlseKLGGGSITSLPIVETQAGDIS 401
Cdd:PRK06793 243 DQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSG----KTQKGSITGIYTVLVDGDDLN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 402 AYIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYREMEIFTQFASdLDENTK 481
Cdd:PRK06793 315 GPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGT-IQENAE 393
|
410 420 430
....*....|....*....|....*....|...
gi 1778695090 482 RQLVYGS-----GLMEILKQNQfSPLKHYEEVI 509
Cdd:PRK06793 394 NAYIFECknkveGINTFLKQGR-SDSFQFDDIV 425
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
103-467 |
5.04e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 122.78 E-value: 5.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 103 GRVLSIGDGIAKLTGLESA-SYGEIVVFETG----VKGMVLDLKKDYLGCIIFGEDKDISEGSQVFRTKKTAGIPVGPDL 177
Cdd:PRK08927 19 GRVVAVRGLLVEVAGPIHAlSVGARIVVETRggrpVPCEVVGFRGDRALLMPFGPLEGVRRGCRAVIANAAAAVRPSRAW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 178 LGRVVNPLGEPIDGQGKISP-IAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQRELIIGDRQTGKTAIaLDT 256
Cdd:PRK08927 99 LGRVVNALGEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVL-LSM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 257 ILKQKDEDLICIyAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYFMDQGKDVLIIYDD 336
Cdd:PRK08927 178 LARNADADVSVI-GLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 337 LSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAqlSEKLGGGSITSLPIVETQAGDISAYIPTNIISITDGQI 416
Cdd:PRK08927 257 VTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHI 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1778695090 417 FLESDLFFAGQRPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYREME 467
Cdd:PRK08927 335 VMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADME 385
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
171-489 |
3.46e-29 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 120.66 E-value: 3.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 171 IPVGPDLLGRVVNPLGEPIDGQGkiSPIAYYKIEKEAPEI--IDRQSVYRPLETGILAIDSMFPIGKGQRELIIGDRQTG 248
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLP--APDTGETGALITPPFnpLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 249 KTAIaLDTILKQKDEDLICIyAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYFMDQGK 328
Cdd:PRK07960 188 KSVL-LGMMARYTQADVIVV-GLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQ 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 329 DVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQLSEklGGGSITSLPIVETQAGDISAYIPTNI 408
Cdd:PRK07960 266 HVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGDDQQDPIADSA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 409 ISITDGQIFLESDLFFAGQRPAINVGLSVSRvggaAQTKAIKKaaaslrlslAQYREMEIFTQFASDLDENtkRQLV--- 485
Cdd:PRK07960 344 RAILDGHIVLSRRLAEAGHYPAIDIEASISR----AMTALIDE---------QHYARVRQFKQLLSSFQRN--RDLVsvg 408
|
....*
gi 1778695090 486 -YGSG 489
Cdd:PRK07960 409 aYAKG 413
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
156-518 |
5.77e-27 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 113.85 E-value: 5.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 156 ISEGSQVFRTKKTAGIPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGK 235
Cdd:PRK05922 77 VALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 236 GQRELIIGDRQTGKTAIaLDTILKqKDEDLICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYS 315
Cdd:PRK05922 157 GQRIGVFSEPGSGKSSL-LSTIAK-GSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 316 ATAIGEYFMDQGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQlSEKlggGSITSLPIVET 395
Cdd:PRK05922 235 AMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-NDK---GSITALYAILH 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 396 QAG--DI-SAYIPtniiSITDGQIFLES--DLFFAgqrPAINVGLSVSRVGGAAQTKAIKKAAASLRLSLAQYRE-MEI- 468
Cdd:PRK05922 311 YPNhpDIfTDYLK----SLLDGHFFLTPqgKALAS---PPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEaLDIi 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1778695090 469 -FTQFASDLDENTKRQLVYGSGLMEILKQnqfsPLKHY---EEVIILVVALAKL 518
Cdd:PRK05922 384 qLGAYVPGQDAHLDRAVKLLPSIKQFLSQ----PLSSYcalHNTLKQLEALLKH 433
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
101-167 |
1.60e-26 |
|
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, in mitochondrial inner membranes, and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349740 [Multi-domain] Cd Length: 67 Bit Score: 102.53 E-value: 1.60e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1778695090 101 EIGRVLSIGDGIAKLTGLESASYGEIVVFETGVKGMVLDLKKDYLGCIIFGEDKDISEGSQVFRTKK 167
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
123-440 |
1.44e-25 |
|
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: 109.81 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 123 YGEIVVFE----TGVKGMVLDLKKDYLGCIIFgedkdisEGSQVFRTKKTA--------GIPVGPDLLGRVVNPLGEPID 190
Cdd:TIGR01040 23 FAEIVNLTlpdgTVRSGQVLEVSGNKAVVQVF-------EGTSGIDAKKTTceftgdilRTPVSEDMLGRVFNGSGKPID 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 191 GQGKISPIAYYKIEKEApeiIDRQSVYRPLE---TGILAIDSMFPIGKGQRELIIGD-------------RQTGKTAIAL 254
Cdd:TIGR01040 96 KGPPVLAEDYLDINGQP---INPYARIYPEEmiqTGISAIDVMNSIARGQKIPIFSAaglphneiaaqicRQAGLVKLPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 255 DTILKQKDEDLICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYFMDQ-GKDVLII 333
Cdd:TIGR01040 173 KDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 334 YDDLSKHAVAYRSISLLLERSPGREAYPGDVFYLHSRLLERSAQLSEKlgGGSITSLPIVETQAGDISAYIPTNIISITD 413
Cdd:TIGR01040 253 LTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR--NGSITQIPILTMPNDDITHPIPDLTGYITE 330
|
330 340
....*....|....*....|....*..
gi 1778695090 414 GQIFLESDLFFAGQRPAINVGLSVSRV 440
Cdd:TIGR01040 331 GQIYVDRQLHNRQIYPPINVLPSLSRL 357
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
147-440 |
7.02e-23 |
|
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: 101.72 E-value: 7.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 147 CIIFGEDKDISEGSQVFRTKKTAGIPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILA 226
Cdd:TIGR01039 54 TIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 227 IDSMFPIGKGQRELIIGDRQTGKTAIALDTILK-QKDEDLICIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADS 305
Cdd:TIGR01039 134 IDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 306 AAFQYIAPYSATAIGEYFMD-QGKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYpgdvfylHSRLLERSAQLSEKLG- 383
Cdd:TIGR01039 214 PGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGY-------QPTLATEMGELQERITs 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1778695090 384 --GGSITSLPIVETQAGDISAYIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSRV 440
Cdd:TIGR01039 287 tkTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRL 345
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
119-421 |
2.26e-21 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 97.03 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 119 ESASYGEIVVFET---GVKGMVLDLKKDYLGCIIFGEDKDISEGSQVFRTKKTAGIPVGPDLLGRVVNPLGEPIDGQGKI 195
Cdd:PRK02118 21 EGVGYGELATVERkdgSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 196 spiayykIEKEAP----------EIIDRQSVyrplETGILAIDSMFPIGKGQRELIIGDRQTGKTAIaLDTILKQKDEDL 265
Cdd:PRK02118 101 -------EGEPIEiggpsvnpvkRIVPREMI----RTGIPMIDVFNTLVESQKIPIFSVSGEPYNAL-LARIALQAEADI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 266 IcIYAAIGQKASSLALLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYF-MDQGKDVLIIYDDLSKHAVAY 344
Cdd:PRK02118 169 I-ILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFaLEGKKKVLVLLTDMTNFADAL 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1778695090 345 RSISLLLERSPGREAYPGDvfyLHSRLLERSAQLSEKLGGGSITSLPIVETQAGDISAYIPTNIISITDGQIFLESD 421
Cdd:PRK02118 248 KEISITMDQIPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLRRG 321
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
171-440 |
1.85e-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: 88.82 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 171 IPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQRELIIGDRQTGKT 250
Cdd:cd01133 2 VPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 251 AIALDTILK-QKDEDLICIYAAIGQK---ASSLAL-LVE-NLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYFM 324
Cdd:cd01133 82 VLIMELINNiAKAHGGYSVFAGVGERtreGNDLYHeMKEsGVINLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYFR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 325 DQ-GKDVLIIYDDLSKHAVAYRSISLLLERSPGREAYpgdvfylHSRLLERSAQLSEKL---GGGSITSLPIVETQAGDI 400
Cdd:cd01133 162 DEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGY-------QPTLATEMGSLQERItstKKGSITSVQAVYVPADDL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1778695090 401 SAYIPTNIISITDGQIFLESDLFFAGQRPAINVGLSVSRV 440
Cdd:cd01133 235 TDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
204-439 |
5.08e-18 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 84.55 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 204 EKEAPEIidrqsvyrPLETGILAIDSMFPIGKGQRELIIGDRQTGKTAIaLDTILKQKDEDLIcIYAAIGQKASSLA--- 280
Cdd:cd01134 52 EKLPPNV--------PLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVI-SQSLSKWSNSDVV-IYVGCGERGNEMAevl 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 281 ----LLVENLKKKNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYFMDQGKDVLIIYDDLSKHAVAYRSISLLLERSPG 356
Cdd:cd01134 122 eefpELKDPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 357 REAYPGdvfYLHSRL---LERSAQLsEKLGG----GSITSLPIVETQAGDISAYIPTNIISITdgQIF--LESDLFFAGQ 427
Cdd:cd01134 202 EEGYPA---YLGARLaefYERAGRV-RCLGSpgreGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRH 275
|
250
....*....|..
gi 1778695090 428 RPAINVGLSVSR 439
Cdd:cd01134 276 FPSINWLISYSK 287
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
159-236 |
3.99e-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: 77.82 E-value: 3.99e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1778695090 159 GSQVFRTKKTAGIPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKG 236
Cdd:COG0055 69 GMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKG 146
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
204-401 |
2.73e-12 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 69.43 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 204 EKEAPEIidrqsvyrPLETGILAIDSMFPIGKGQRELIIGDRQTGKTaIALDTILKQKDEDlICIYAAIGQKASSLA-LL 282
Cdd:PRK04192 203 EKLPPVE--------PLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT-VTQHQLAKWADAD-IVIYVGCGERGNEMTeVL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 283 VE--NLKkknafD----------NCIvvaataadsaafqyIA-----P--------YSATAIGEYFMDQGKDVLIIYDDL 337
Cdd:PRK04192 273 EEfpELI-----DpktgrplmerTVL--------------IAntsnmPvaareasiYTGITIAEYYRDMGYDVLLMADST 333
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1778695090 338 SKHAVAYRSISLLLERSPGREAYPGdvfYLHSRL---LERsAQLSEKLGG--GSITSLPIVETQAGDIS 401
Cdd:PRK04192 334 SRWAEALREISGRLEEMPGEEGYPA---YLASRLaefYER-AGRVKTLGGeeGSVTIIGAVSPPGGDFS 398
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
100-165 |
4.45e-11 |
|
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: 58.71 E-value: 4.45e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778695090 100 EEIGRVLSIGDGIAKLTGLESASYGEIVVFETGVKGMVLDLKKDYLGCIIFGEDKDISEGSQVFRT 165
Cdd:pfam02874 3 QVIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRT 68
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
266-432 |
1.23e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 64.66 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 266 ICIYAAIGQKASSLALLVENLKK-------KNAFDNCIVVAATAADSAAFQYIAPYSATAIGEYFMDQGKDVLIIYDDLS 338
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 339 KHAVAYRSISLLLERSPGREAYPGdvfYLHSRLLE------RSAQLSEKLGGGSITSLPIVETQAGDISAYIPTNIISIT 412
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVV 840
|
170 180
....*....|....*....|
gi 1778695090 413 DGQIFLESDLFFAGQRPAIN 432
Cdd:PRK14698 841 KVFWALDADLARRRHFPAIN 860
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
159-257 |
1.21e-07 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 54.28 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 159 GSQVFRTKKTAGIPVGPDLLGRVVNPLGEPIDGQGKISPIAYYKIEKEAPEIIDRQSVYRPLETGILAIDSMFPIGKGQR 238
Cdd:CHL00060 84 GMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGK 163
|
90
....*....|....*....
gi 1778695090 239 ELIIGDRQTGKTAIALDTI 257
Cdd:CHL00060 164 IGLFGGAGVGKTVLIMELI 182
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
450-512 |
3.02e-05 |
|
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: 42.05 E-value: 3.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1778695090 450 KKAAASLRLSLAQYREMEIFTQFASD--LDENTKRQLVYGSGLMEILKQNQFSPLKHYEEVIILV 512
Cdd:cd01429 2 KAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLY 66
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
226-395 |
1.40e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 41.22 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 226 AIDSMFPIGKGQRELIIGDRQTGKTaialdTILKQkdedlicIYAAIGQ---KASSLALLV-ENLKKKNAFDNCI--VVA 299
Cdd:PRK12608 123 VVDLVAPIGKGQRGLIVAPPRAGKT-----VLLQQ-------IAAAVAAnhpEVHLMVLLIdERPEEVTDMRRSVkgEVY 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778695090 300 ATAADSAAFQYIAPYS-ATAIGEYFMDQGKDVLIIYDDLSKHAVAYRSISllleRSPGREAYPGdvfyLHSRLLER---- 374
Cdd:PRK12608 191 ASTFDRPPDEHIRVAElVLERAKRLVEQGKDVVILLDSLTRLARAYNNEV----ESSGRTLSGG----VDARALQRpkrl 262
|
170 180
....*....|....*....|....*
gi 1778695090 375 --SAQLSEklGGGSITSLP--IVET 395
Cdd:PRK12608 263 fgAARNIE--EGGSLTIIAtaLVDT 285
|
|
| |
