|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-515 |
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: 1063.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 1 MDIRAEEISRIIRSQIEGFDTQVDVSEVGTIISVGDGIARAHGLEKAMAGELLELPHGVMGLTFNLEEDNVGIILLGDVT 80
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 81 LIKEGDTVKRTGRIMNVPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVG 160
Cdd:COG0056 81 GIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 161 RGQRELIIGDRQTGKTAVAIDTIINQKDTGVICIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPAPLLYLAPM 240
Cdd:COG0056 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 241 TGAALGEYFMwhgtngqpagsDNpGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKLSDER 320
Cdd:COG0056 241 AGCAMGEYFM-----------DQ-GKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 321 GAGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQVKAMKQVSGSVKLELAQ 400
Cdd:COG0056 309 GGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 401 YRELAAFAQFGSDLDKATLAQLNRGQRLVEILKQAQYQPMPVEKQIVSIWAATNGYVDDLPVSEVRRFEKELHDYLDINA 480
Cdd:COG0056 389 YRELEAFAQFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKH 468
|
490 500 510
....*....|....*....|....*....|....*
gi 2624589777 481 PEVLRAVRETKTMSDESKAILKTQTTAFKESFTGS 515
Cdd:COG0056 469 PDLLKEIRETGKLDDEIEEKLKAAIEEFKKTFAAS 503
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-514 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 1058.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 1 MDIRAEEISRIIRSQIEGFDTQVDVSEVGTIISVGDGIARAHGLEKAMAGELLELPHGVMGLTFNLEEDNVGIILLGDVT 80
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 81 LIKEGDTVKRTGRIMNVPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVG 160
Cdd:PRK09281 81 DIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 161 RGQRELIIGDRQTGKTAVAIDTIINQKDTGVICIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPAPLLYLAPM 240
Cdd:PRK09281 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 241 TGAALGEYFMwhgtngqpagsDNpGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKLSDER 320
Cdd:PRK09281 241 AGCAMGEYFM-----------DN-GKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 321 GAGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQVKAMKQVSGSVKLELAQ 400
Cdd:PRK09281 309 GGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 401 YRELAAFAQFGSDLDKATLAQLNRGQRLVEILKQAQYQPMPVEKQIVSIWAATNGYVDDLPVSEVRRFEKELHDYLDINA 480
Cdd:PRK09281 389 YRELEAFAQFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNH 468
|
490 500 510
....*....|....*....|....*....|....
gi 2624589777 481 PEVLRAVRETKTMSDESKAILKTQTTAFKESFTG 514
Cdd:PRK09281 469 ADLLEEIRETKDLSDEIEAKLKAAIEEFKKTFAA 502
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
3-512 |
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: 884.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 3 IRAEEISRIIRSQIEGFDTQVDVSEVGTIISVGDGIARAHGLEKAMAGELLELPHGVMGLTFNLEEDNVGIILLGDVTLI 82
Cdd:TIGR00962 2 LKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 83 KEGDTVKRTGRIMNVPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRG 162
Cdd:TIGR00962 82 REGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 163 QRELIIGDRQTGKTAVAIDTIINQKDTGVICIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPAPLLYLAPMTG 242
Cdd:TIGR00962 162 QRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 243 AALGEYFMWHGtngqpagsdnpgQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKLSDERGA 322
Cdd:TIGR00962 242 CTMGEYFRDNG------------KHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 323 GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQVKAMKQVSGSVKLELAQYR 402
Cdd:TIGR00962 310 GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 403 ELAAFAQFGSDLDKATLAQLNRGQRLVEILKQAQYQPMPVEKQIVSIWAATNGYVDDLPVSEVRRFEKELHDYLDINAPE 482
Cdd:TIGR00962 390 ELEAFSQFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPD 469
|
490 500 510
....*....|....*....|....*....|
gi 2624589777 483 VLRAVRETKTMSDESKAILKTQTTAFKESF 512
Cdd:TIGR00962 470 ILEEINTTKKLTEELEAKLKEALKNFKKTF 499
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
22-517 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 813.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 22 QVDVSEVGTIISVGDGIARAHGLEKAMAGELLELPHGVMGLTFNLEEDNVGIILLGDVTLIKEGDTVKRTGRIMNVPVGP 101
Cdd:CHL00059 1 EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 102 AFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQTGKTAVAID 181
Cdd:CHL00059 81 AYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 182 TIINQKDTGVICIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPAPLLYLAPMTGAALGEYFMWHGtngqpags 261
Cdd:CHL00059 161 TILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRG-------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 262 dnpgQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKLSDERGAGSLTALPIIETQAGDVSAY 341
Cdd:CHL00059 233 ----RHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 342 IPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQVKAMKQVSGSVKLELAQYRELAAFAQFGSDLDKATLAQ 421
Cdd:CHL00059 309 IPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 422 LNRGQRLVEILKQAQYQPMPVEKQIVSIWAATNGYVDDLPVSEVRRFEKELHDYLDINAPEVLRAVRETKTMSDESKAIL 501
Cdd:CHL00059 389 LARGQRLRELLKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALL 468
|
490
....*....|....*.
gi 2624589777 502 KTQTTAFKESFTGSLK 517
Cdd:CHL00059 469 KEAIQEQLELFLLQEQ 484
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-513 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 781.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 1 MDIRAEEISRIIRSQIEGFDTQVDVSEVGTIISVGDGIARAHGLEKAMAGELLELPHGVMGLTFNLEEDNVGIILLGDVT 80
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 81 LIKEGDTVKRTGRIMNVPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVG 160
Cdd:PRK13343 81 DILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 161 RGQRELIIGDRQTGKTAVAIDTIINQKDTGVICIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPAPLLYLAPM 240
Cdd:PRK13343 161 RGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 241 TGAALGEYFMWHGtngqpagsdnpgQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKLSDER 320
Cdd:PRK13343 241 AGCAIAEYFRDQG------------QDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPEL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 321 GAGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQVKAMKQVSGSVKLELAQ 400
Cdd:PRK13343 309 GGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 401 YRELAAFAQFGSDLDKATLAQLNRGQRLVEILKQAQYQPMPVEKQIVSIWAATNGYVDDLPVSEVRRFEKELHDYLDINA 480
Cdd:PRK13343 389 FLELEAFTRFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARF 468
|
490 500 510
....*....|....*....|....*....|...
gi 2624589777 481 PEVLRAVRETKTMSDESKAILKTQTTAFKESFT 513
Cdd:PRK13343 469 AALSLALESPRELDEAWLAALEEILREAGERFA 501
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
12-501 |
0e+00 |
|
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic species, including Methanosarcina barkeri, have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 alpha subunit of this apparent second ATP synthase.
Pssm-ID: 132367 [Multi-domain] Cd Length: 497 Bit Score: 581.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 12 IRSQIEGFDTQVDVSEVGTIISVGDGIARAHGLEKAMAGELLELPHGVMGLTFNLEEDNVGIILLGDVTLIKEGDTVKRT 91
Cdd:TIGR03324 12 LDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 92 GRIMNVPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDR 171
Cdd:TIGR03324 92 GRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 172 QTGKTAVAIDTIINQKDTGVICIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPAPLLYLAPMTGAALGEYFMW 251
Cdd:TIGR03324 172 QTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSIGEHFME 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 252 HGTNgqpagsdnpgqhVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKLSDERGAGSLTALPII 331
Cdd:TIGR03324 252 QGRD------------VLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPII 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 332 ETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQVKAMKQVSGSVKLELAQYRELAAFAQFG 411
Cdd:TIGR03324 320 ETEAQNISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 412 SDLDKATLAQLNRGQRLVEILKQAQYQPMPVEKQIVSIWAATNGYVDDLPVSEVRRFEKELHDYLDINAPEVLRAVRETK 491
Cdd:TIGR03324 400 ARLDENTRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGK 479
|
490
....*....|
gi 2624589777 492 TMSDESKAIL 501
Cdd:TIGR03324 480 KLSDEDREQI 489
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
94-379 |
0e+00 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 579.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 94 IMNVPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQT 173
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 174 GKTAVAIDTIINQKDTGVICIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPAPLLYLAPMTGAALGEYFMWHg 253
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDN- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 254 tngqpagsdnpGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKLSDERGAGSLTALPIIET 333
Cdd:cd01132 160 -----------GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIET 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2624589777 334 QAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVG 379
Cdd:cd01132 229 QAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
61-469 |
3.48e-128 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 385.55 E-value: 3.48e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 61 GLTFNLEEDN-VGIILLGDVTLIKEGDTVKRTGRIMNVPVGPAFVGRVVDALGNPID------GKGPIES-VSFNPIERI 132
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESeQTLGKVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 133 APGIVDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQTGKTAVAIDTIINQ--------KDTGVICIYVAIGQKRST 204
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 205 IAQVVKTLEEYDAMKHTIVVAASASEPAPLLYLAPMTGAALGEYFMwhgtngqpagsdNPGQHVLCIYDDLSKQAVAYRE 284
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFM------------NRGRHCLCVYDDLSKQAVAYRQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 285 ISLLVRRPPGREAYPGDVFYLHSRLLERACKLSDERGAGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAG 364
Cdd:PTZ00185 308 ISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 365 VRPAMNVGISVSRVGGAAQVKAMKQVSGSVKLELAQYRELAAFAQFGSDLDKATLAqlnRGQRLVEILKQAqyQPMPVEK 444
Cdd:PTZ00185 388 QRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVPMI---RGARFVALFNQK--NPSFFMN 462
|
410 420
....*....|....*....|....*
gi 2624589777 445 QIVSIWAATNGYVDDLPVSEVRRFE 469
Cdd:PTZ00185 463 ALVSLYACLNGYLDDVKVNYAKLYE 487
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
149-376 |
5.33e-109 |
|
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: 323.15 E-value: 5.33e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 149 GLKVIDALIPVGRGQRELIIGDRQTGKTAVAiDTIINQKDTGViCIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAASA 228
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 229 SEPAPLLYLAPMTGAALGEYFMWHGtngqpagsdnpgQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSR 308
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQG------------KDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2624589777 309 LLERACKLSDERgaGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVS 376
Cdd:pfam00006 147 LLERAGRVKGKG--GSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
103-439 |
5.01e-105 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 323.85 E-value: 5.01e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 103 FVGRVVDALGNPI---------DGKGPIESVSFNpierIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQT 173
Cdd:PRK07165 79 YFGKIIDIDGNIIypeaqnplsKKFLPNTSSIFN----LAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 174 GKTAVAIDTIINQKDTGVICIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPAPlLYLAPMTGaalgeyfMWHG 253
Cdd:PRK07165 155 GKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSPYE-QYLAPYVA-------MAHA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 254 TNgqPAGSDNpgqhVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKLSDERgagSLTALPIIET 333
Cdd:PRK07165 227 EN--ISYNDD----VLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNRK---TITALPILQT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 334 QAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQVKAMKQVSGSVKLELAQYRELAAFAQFGSD 413
Cdd:PRK07165 298 VDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYD 377
|
330 340
....*....|....*....|....*.
gi 2624589777 414 LDKATLAQLNRGQRLVEILKQAQYQP 439
Cdd:PRK07165 378 LNKETSDLLFKGKMIEKMFNQKGFSL 403
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
97-378 |
3.31e-104 |
|
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: 313.24 E-value: 3.31e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 97 VPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQTGKT 176
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 177 AVAIDTIINQKDT-GVICIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPAPLLYLAPMTGAALGEYFmwhgtn 255
Cdd:cd19476 82 VLAMQLARNQAKAhAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYF------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 256 gqpagSDNpGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKLSDerGAGSLTALPIIETQA 335
Cdd:cd19476 156 -----RDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPG 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2624589777 336 GDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRV 378
Cdd:cd19476 228 DDLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
387-512 |
1.84e-71 |
|
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: 223.40 E-value: 1.84e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 387 MKQVSGSVKLELAQYRELAAFAQFGSDLDKATLAQLNRGQRLVEILKQAQYQPMPVEKQIVSIWAATNGYVDDLPVSEVR 466
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2624589777 467 RFEKELHDYLDINAPEVLRAVRETKTMSDESKAILKTQTTAFKESF 512
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
383-508 |
3.82e-69 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 217.69 E-value: 3.82e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 383 QVKAMKQVSGSVKLELAQYRELAAFAQFGSDLDKATLAQLNRGQRLVEILKQAQYQPMPVEKQIVSIWAATNGYVDDLPV 462
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2624589777 463 SEVRRFEKELHDYLDINAPEVLRAVRETKTMSDESKAILKTQTTAF 508
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
97-378 |
2.32e-46 |
|
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: 162.73 E-value: 2.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 97 VPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQTGKT 176
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 177 aVAIDTIINQKDTGVICIyVAIGQK-RSTIAQVVKTLEEyDAMKHTIVVAASASEPAPLLYLAPMTGAALGEYFMwhgtn 255
Cdd:cd01136 82 -TLLGMIARNTDADVNVI-ALIGERgREVREFIEKDLGE-EGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFR----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 256 gqpagsdNPGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKLSdergAGSLTALPIIETQA 335
Cdd:cd01136 154 -------DQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGE----KGSITAFYTVLVEG 222
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2624589777 336 GDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRV 378
Cdd:cd01136 223 DDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
28-443 |
3.82e-46 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 166.74 E-value: 3.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 28 VGTIISVGDGIARAHGLEKAMaGEL--LELPHG------VMGLtfnlEEDNVGIILLGDVTLIKEGDTVKRTGRIMNVPV 99
Cdd:COG1157 20 SGRVTRVVGLLIEAVGPDASI-GELceIETADGrpvlaeVVGF----RGDRVLLMPLGDLEGISPGARVVPTGRPLSVPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 100 GPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQReliIGdr---qtGKT 176
Cdd:COG1157 95 GDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR---IGifagsgvGKS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 177 avaidTIInqkdtGVICiyvaigqkRSTIAQVV-----------------KTLEEyDAMKHTIVVAASASEPAPLLYLAP 239
Cdd:COG1157 172 -----TLL-----GMIA--------RNTEADVNvialigergrevrefieDDLGE-EGLARSVVVVATSDEPPLMRLRAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 240 MTGAALGEYFmwhgtngqpagSDNpGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKlsde 319
Cdd:COG1157 233 YTATAIAEYF-----------RDQ-GKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN---- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 320 RGAGSLTAL------------PIIETqagdvsayiptnVISITDGQIFLESDLFNAGVRPAMNVGISVSRVggaaqvkaM 387
Cdd:COG1157 297 GGKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRV--------M 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2624589777 388 KQVSGSVKLELAQ-YREL-AAFA-----------QFGSD--LDKAtlaqLNRGQRLVEILKQAQYQPMPVE 443
Cdd:COG1157 357 PDIVSPEHRALARrLRRLlARYEenedlirigayQPGSDpeLDEA----IALIPAIEAFLRQGMDERVSFE 423
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
14-454 |
1.35e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 160.30 E-value: 1.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 14 SQIEGFDTQVdvseVGTII-SVGDGIArahglekamAGELLELPHGvmGLTFNLEEDNVG-------IILLGDVTLIKEG 85
Cdd:PRK06936 21 IQIRGRVTQV----TGTILkAVVPGVR---------IGELCYLRNP--DNSLSLQAEVIGfaqhqalLTPLGEMYGISSN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 86 DTVKRTGRIMNVPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQRE 165
Cdd:PRK06936 86 TEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 166 LIIGDRQTGKTAVaIDTIINQKDTGViCIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPAPLLYLAPMTGAAL 245
Cdd:PRK06936 166 GIFAAAGGGKSTL-LASLIRSAEVDV-TVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 246 GEYFMwhgtngqpagsdNPGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKlSDErgaGSL 325
Cdd:PRK06936 244 AEYFR------------DQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ-SDK---GSI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 326 TALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQVKAMKQVSGSVKLELAQYRELA 405
Cdd:PRK06936 308 TALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVE 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2624589777 406 AFAQFGS---DLDKATLAQLNRGQRLVEILKQAQYQPMPVEKQIVSIWAATN 454
Cdd:PRK06936 388 LLLQIGEyqkGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETLTQ 439
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
68-414 |
2.46e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 159.50 E-value: 2.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 68 EDNVGIILLGDVTLIKEGDTVKRTGRIMNVPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQ 147
Cdd:PRK07721 64 DEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPME 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 148 TGLKVIDALIPVGRGQRELIIGDRQTGK-TAVAIDTIINQKDTGVICIyvaIGQKRSTIAQVV-KTLEEyDAMKHTIVVA 225
Cdd:PRK07721 144 VGVRAIDSLLTVGKGQRVGIFAGSGVGKsTLMGMIARNTSADLNVIAL---IGERGREVREFIeRDLGP-EGLKRSIVVV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 226 ASASEPAPLLYLAPMTGAALGEYFMwhgtngqpagsdNPGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYL 305
Cdd:PRK07721 220 ATSDQPALMRIKGAYTATAIAEYFR------------DQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAI 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 306 HSRLLERacklSDERGAGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVggaaqvk 385
Cdd:PRK07721 288 LPKLLER----TGTNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRV------- 356
|
330 340 350
....*....|....*....|....*....|
gi 2624589777 386 aMKQVSGSVKLELAQ-YRELAAFAQFGSDL 414
Cdd:PRK07721 357 -MNHIVSPEHKEAANrFRELLSTYQNSEDL 385
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
4-411 |
7.17e-40 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 149.92 E-value: 7.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 4 RAEEISRIIRSQIEGFDTQVDVSEVGTIISVGDGIARAHGLEKAMaGELLEL--PHG-------VMGLTfnleEDNVGII 74
Cdd:PRK09099 1 ALAELSRLADALERELAALPAVRRTGKVVEVIGTLLRVSGLDVTL-GELCELrqRDGtllqraeVVGFS----RDVALLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 75 LLGDVTLIKEGDTVKRTGRIMNVPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVID 154
Cdd:PRK09099 76 PFGELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 155 ALIPVGRGQRELIIGDRQTGKTavaidTIINQKDTGVIC---IYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAA----S 227
Cdd:PRK09099 156 GLMTLGEGQRMGIFAPAGVGKS-----TLMGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCAtsdrS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 228 ASEPAPLLYlapmTGAALGEYFMwhgtngqpagsdNPGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHS 307
Cdd:PRK09099 231 SIERAKAAY----VATAIAEYFR------------DRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 308 RLLERAcklsdERGA-GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQVKA 386
Cdd:PRK09099 295 RLLERA-----GMGEtGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPRE 369
|
410 420
....*....|....*....|....*
gi 2624589777 387 MKQVSGSVKLELAQYRELAAFAQFG 411
Cdd:PRK09099 370 HVQAAGRLRQLLAKHREVETLLQVG 394
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
28-446 |
1.82e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 145.98 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 28 VGTIISVGDgIARAHGLEKAmagellelpHGVMGLTFNLEEDNVGIILLGDVTLIKEGDTVKRTGRIMNVPVGPAFVGRV 107
Cdd:PRK08472 33 DGLNPSVGD-IVKIESSDNG---------KECLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLLGRV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 108 VDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQTGKTAVAidTIINQK 187
Cdd:PRK08472 103 VDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLM--GMIVKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 188 DTGVICIYVAIGQKRSTIAQVV-KTLEeyDAMKHTIVVAASaSEPAPLL--YLApMTGAALGEYFmwhgtngqpagsDNP 264
Cdd:PRK08472 181 CLAPIKVVALIGERGREIPEFIeKNLG--GDLENTVIVVAT-SDDSPLMrkYGA-FCAMSVAEYF------------KNQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 265 GQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKlsdERGAGSLTALPIIETQAGDVSAYIPT 344
Cdd:PRK08472 245 GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTVLVEGDDMSDPIAD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 345 NVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQVKAMKQVSGSVKLELAQYRE------LAAFaQFGSD--LDK 416
Cdd:PRK08472 322 QSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKEnevlirIGAY-QKGNDkeLDE 400
|
410 420 430
....*....|....*....|....*....|
gi 2624589777 417 AtlaqLNRGQRLVEILKQAQYQPMPVEKQI 446
Cdd:PRK08472 401 A----ISKKEFMEQFLKQNPNELFPFEQTF 426
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-451 |
3.46e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 145.34 E-value: 3.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 29 GTIISVGDGIARAhGLEKAMAGELLEL-PHGVMGLTFNLEEDNVgiiLLG--DVTL-IKEGDTVKRTGRIMNVPVGPAFV 104
Cdd:PRK06820 31 GPIVEIGPTLLRA-SLPGVAQGELCRIePQGMLAEVVSIEQEMA---LLSpfASSDgLRCGQWVTPLGHMHQVQVGADLA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 105 GRVVDALGNPIDGkGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQTGKTAVaIDTII 184
Cdd:PRK06820 107 GRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTL-LGMLC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 185 NQKDTGVIcIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPAPLLYLAPMTGAALGEYFMWHGTNgqpagsdnp 264
Cdd:PRK06820 185 ADSAADVM-VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKK--------- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 265 gqhVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKlSDErgaGSLTALPIIETQAGDVSAYIPT 344
Cdd:PRK06820 255 ---VLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGN-SDR---GSITAFYTVLVEGDDMNEPVAD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 345 NVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQVKAMKQVSGSVKLELAQYRELAAFAQFG---SDLDKATLAQ 421
Cdd:PRK06820 328 EVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGeyqAGEDLQADEA 407
|
410 420 430
....*....|....*....|....*....|
gi 2624589777 422 LNRGQRLVEILKQAQYQPMPVEKQIVSIWA 451
Cdd:PRK06820 408 LQRYPAICAFLQQDHSETAHLETTLEHLAQ 437
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
85-441 |
9.13e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 138.68 E-value: 9.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 85 GDTVKRTGRIMNVPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQR 164
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 165 ELIIGDRQTGKTavaidtiinqkdtgviciyVAIGQ-KRSTIAQVV---------KTLEEY-------DAMKHTIVVAAS 227
Cdd:PRK08972 165 MGLFAGSGVGKS-------------------VLLGMmTRGTTADVIvvglvgergREVKEFieeilgeEGRARSVVVAAP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 228 AsEPAPLLYL-APMTGAALGEYFMWHGTNgqpagsdnpgqhVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLH 306
Cdd:PRK08972 226 A-DTSPLMRLkGCETATTIAEYFRDQGLN------------VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 307 SRLLERACKLSDerGAGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQVKA 386
Cdd:PRK08972 293 PALVERAGNGGP--GQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEE 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2624589777 387 MKQVSGSVKLELAQYRE------LAAFAQfGSD--LDKATLAQlnrgQRLVEILKQAQYQPMP 441
Cdd:PRK08972 371 HLEAMRRVKQVYSLYQQnrdlisIGAYKQ-GSDprIDNAIRLQ----PAMNAFLQQTMKEAVP 428
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
59-441 |
2.28e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 137.55 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 59 VMGLtfnlEEDNVGIILLGDVTLIKEGDTVKRTGRIMNVPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVD 138
Cdd:PRK05688 69 VMGF----SGDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLN 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 139 RKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQTGKTA-VAIDTIINQKDTGVICIyvaIGQKRSTIAQVVKTLEEYDA 217
Cdd:PRK05688 145 RHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVlLGMMTRFTEADIIVVGL---IGERGREVKEFIEHILGEEG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 218 MKHTIVVAASASEpAPLLYL-APMTGAALGEYFMwhgtngqpagsdNPGQHVLCIYDDLSKQAVAYREISLLVRRPPGRE 296
Cdd:PRK05688 222 LKRSVVVASPADD-APLMRLrAAMYCTRIAEYFR------------DKGKNVLLLMDSLTRFAQAQREIALAIGEPPATK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 297 AYPGDVFYLHSRLLERACklSDERGAGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVS 376
Cdd:PRK05688 289 GYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASIS 366
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2624589777 377 RVggaaqvkaMKQVSGSVKLELAQY-----------RELAAFAQFGSDLDKATLAQLNRGQRLVEILKQAQYQPMP 441
Cdd:PRK05688 367 RV--------MPQVVDPEHLRRAQRfkqlwsryqqsRDLISVGAYVAGGDPETDLAIARFPHLVQFLRQGLRENVS 434
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
29-439 |
4.85e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 130.89 E-value: 4.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 29 GTIISVGDGIARAHGLEK-AMAGELLELPHG---VMGLTFNLEEDNVGIILLGDVTLIKEGDTVKRTGRIMNVPvGPAFV 104
Cdd:PRK06002 28 GTVSEVTASHYRVRGLSRfVRLGDFVAIRADggtHLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGPLRIRP-DPSWK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 105 GRVVDALGNPIDGKGPI-ESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQTGKT------- 176
Cdd:PRK06002 107 GRVINALGEPIDGLGPLaPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKStllamla 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 177 -AVAIDTIInqkdtgviciyVAIGQKRSTiaQVVKTLEEY--DAMKHTIVVAASASEPAPLLYLAPMTGAALGEYFmwhg 253
Cdd:PRK06002 187 rADAFDTVV-----------IALVGERGR--EVREFLEDTlaDNLKKAVAVVATSDESPMMRRLAPLTATAIAEYF---- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 254 tngqpagSDNpGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACklSDERGAGSLTALPIIET 333
Cdd:PRK06002 250 -------RDR-GENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAG--PGAEGGGSITGIFSVLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 334 QAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQVKAMKQVSGSVKLELAQY---RELAAFA-- 408
Cdd:PRK06002 320 DGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFeetRDLRLIGgy 399
|
410 420 430
....*....|....*....|....*....|...
gi 2624589777 409 QFGSD--LDKAtLAQLnrgQRLVEILKQAQYQP 439
Cdd:PRK06002 400 RAGSDpdLDQA-VDLV---PRIYEALRQSPGDP 428
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
94-377 |
1.30e-32 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 125.80 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 94 IMNVPVGPAFVGRVVDALGNPIDGKGP--------IESVSFNPIERIAPgivdrksvHEPMQTGLKVIDALIPVGRGQRE 165
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPilpedyldINGPPINPVARIYP--------EEMIQTGISAIDVMNTLVRGQKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 166 LIIGD-------------RQTGktavaidtiINQKDTGVICIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPA 232
Cdd:cd01135 73 PIFSGsglphnelaaqiaRQAG---------VVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 233 PLLYLAPMTGAALGEYFMWhgtngqpagsdNPGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGdvfYLHSRL--- 309
Cdd:cd01135 144 IERIITPRMALTTAEYLAY-----------EKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLati 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2624589777 310 LERACKLSDERGagSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSR 377
Cdd:cd01135 210 YERAGRVEGRKG--SITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
27-93 |
3.83e-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: 117.55 E-value: 3.83e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2624589777 27 EVGTIISVGDGIARAHGLEKAMAGELLELPHGVMGLTFNLEEDNVGIILLGDVTLIKEGDTVKRTGR 93
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-417 |
8.94e-31 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 124.29 E-value: 8.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 29 GTIISVGDGIARAHgLEKAMAGELLEL-PHGVMGLTFNLEEDNVGIILLGDVTLIKEGDTVKRTGRIMNVPVGPAFVGRV 107
Cdd:PRK07594 23 GRIQDVSATLLNAW-LPGVFMGELCCIkPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 108 VDALGNPIDGKgPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQTGKTAVaIDTIINQK 187
Cdd:PRK07594 102 IDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLCNAP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 188 DTGViCIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPAPLLYLAPMTGAALGEYFMWHGtngqpagsdnpgQH 267
Cdd:PRK07594 180 DADS-NVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNG------------KR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 268 VLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKLSdergAGSLTALPIIETQAGDVSAYIPTNVI 347
Cdd:PRK07594 247 VVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGE----KGSITAFYTVLVEGDDMNEPLADEVR 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2624589777 348 SITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQVKAMKQVSGSVKLELAQYRELAAFAQFG-------SDLDKA 417
Cdd:PRK07594 323 SLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGeyqrgvdTDTDKA 399
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
97-417 |
1.67e-30 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 123.74 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 97 VPVGPAFVGRVVDALGNPIDG--------KGPIESVSFNPIERIApgivdrksVHEPMQTGLKVIDALIPVGRGQRELII 168
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGlpapdtgeTGALITPPFNPLQRTP--------IEHVLDTGVRAINALLTVGRGQRMGLF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 169 GDRQTGKTaVAIDTIINQKDTGVICIYVaIGQKRSTIAQVVKTLEEYDAMKHTIVVAASAsEPAPLLYlapMTGAA---- 244
Cdd:PRK07960 182 AGSGVGKS-VLLGMMARYTQADVIVVGL-IGERGREVKDFIENILGAEGRARSVVIAAPA-DVSPLLR---MQGAAyatr 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 245 LGEYFMwhgtngqpagsdNPGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKLSDerGAGS 324
Cdd:PRK07960 256 IAEDFR------------DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGS 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 325 LTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGA-------AQVKAMKQVSGSVKle 397
Cdd:PRK07960 322 ITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAlideqhyARVRQFKQLLSSFQ-- 399
|
330 340
....*....|....*....|....*
gi 2624589777 398 laQYREL---AAFAQfGSD--LDKA 417
Cdd:PRK07960 400 --RNRDLvsvGAYAK-GSDpmLDKA 421
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
88-443 |
8.16e-29 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 118.56 E-value: 8.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 88 VKRTGRIMNVPVGPAFVGRVVDALGNpIDGK--GPIESVSFN---PIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRG 162
Cdd:PRK08149 73 LKPTGKPLSVWVGEALLGAVLDPTGK-IVERfdAPPTVGPISeerVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 163 QRELIIGDRQTGKTAVaIDTIINQKDTGVICIYVaIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPAPLLYLAPMTG 242
Cdd:PRK08149 152 QRMGIFASAGCGKTSL-MNMLIEHSEADVFVIGL-IGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 243 AALGEYFMWHGTNgqpagsdnpgqhVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKLSdergA 322
Cdd:PRK08149 230 TTVAEYFRDQGKR------------VVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATL----A 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 323 GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQVKAMKQVSGSVKLELAQYR 402
Cdd:PRK08149 294 GSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLE 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2624589777 403 ELAAFAQFG-------SDLDKAtlaqLNRGQRLVEILKQAQYQPMPVE 443
Cdd:PRK08149 374 ELQLFIDLGeyrrgenADNDRA----MDKRPALEAFLKQDVAEKSSFS 417
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
43-377 |
2.24e-28 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 117.62 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 43 GLEKAMAGEL--LELPHG--VMGLTFNLEEDNVGIILLGDVTLIKEGDT-VKRTGRIMNVPVGPAFVGRVVDALGNPIDG 117
Cdd:PRK04196 19 GVEGVAYGEIveIELPNGekRRGQVLEVSEDKAVVQVFEGTTGLDLKDTkVRFTGEPLKLPVSEDMLGRIFDGLGRPIDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 118 KGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQR------------EL---IIgdRQTgktavaidT 182
Cdd:PRK04196 99 GPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnELaaqIA--RQA--------K 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 183 IINQKDTGVIcIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPAPLLYLAPMTGAALGEYFMWhgtngqpagsd 262
Cdd:PRK04196 169 VLGEEENFAV-VFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAF----------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 263 NPGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGdvfYLHSRL---LERACKLsdeRG-AGSLTALPIIETQAGDV 338
Cdd:PRK04196 237 EKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRI---KGkKGSITQIPILTMPDDDI 310
|
330 340 350
....*....|....*....|....*....|....*....
gi 2624589777 339 SAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSR 377
Cdd:PRK04196 311 THPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
97-377 |
9.12e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 115.46 E-value: 9.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 97 VPVGPAFVGRVVDALGNPIDGKGPI-ESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQTGK 175
Cdd:PRK08927 92 VRPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 176 TaVAIDTIINQKDTGVICIYVaIGQKRSTIAQVVK-TLEEyDAMKHTIVVAASASEPAPLLYLAPMTGAALGEYFMwhgt 254
Cdd:PRK08927 172 S-VLLSMLARNADADVSVIGL-IGERGREVQEFLQdDLGP-EGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFR---- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 255 ngqpagsdNPGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACklSDERGAGSLTALPIIETQ 334
Cdd:PRK08927 245 --------DQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVD 314
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2624589777 335 AGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSR 377
Cdd:PRK08927 315 GDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSR 357
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
99-441 |
9.71e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 115.37 E-value: 9.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 99 VGPAFVGRVVDALGNPIDGKGPIESVSfnPIERIAPGI--VDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQTGKT 176
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGST--PLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 177 AV-AIDTIINQKDTGVICIyvaIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEpAPLLYL-APMTGAALGEYFMwhgt 254
Cdd:PRK07196 170 VLlGMITRYTQADVVVVGL---IGERGREVKEFIEHSLQAAGMAKSVVVAAPADE-SPLMRIkATELCHAIATYYR---- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 255 ngqpagsdNPGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERAcklSDERGAGSLTALPIIETQ 334
Cdd:PRK07196 242 --------DKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESA---GNSSGNGTMTAIYTVLAE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 335 AGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSR----VGGAAQVKAMKQVSGSVKlELAQYRELAAFAQF 410
Cdd:PRK07196 311 GDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCYA-DYMAIKPLIPLGGY 389
|
330 340 350
....*....|....*....|....*....|.
gi 2624589777 411 GSDLDKATLAQLNRGQRLVEILKQAQYQPMP 441
Cdd:PRK07196 390 VAGADPMADQAVHYYPAITQFLRQEVGHPAL 420
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
87-387 |
8.16e-26 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 110.20 E-value: 8.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 87 TVKRTGRIMNVPVGPAFVGRVVDALGNPIDgKGP---------IESVSFNPIERIAPgivdrksvHEPMQTGLKVIDALI 157
Cdd:TIGR01040 66 TCEFTGDILRTPVSEDMLGRVFNGSGKPID-KGPpvlaedyldINGQPINPYARIYP--------EEMIQTGISAIDVMN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 158 PVGRGQRELIIGD-------------RQTGKTAVAIDTIINQKDTGVICIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVV 224
Cdd:TIGR01040 137 SIARGQKIPIFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLF 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 225 AASASEPAPLLYLAPMTGAALGEYFMWHgtngqpagsdnPGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFY 304
Cdd:TIGR01040 217 LNLANDPTIERIITPRLALTTAEYLAYQ-----------CEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 305 LHSRLLERACKLsdERGAGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQV 384
Cdd:TIGR01040 286 DLATIYERAGRV--EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIG 363
|
...
gi 2624589777 385 KAM 387
Cdd:TIGR01040 364 EGM 366
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
93-440 |
3.22e-25 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 108.07 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 93 RIMNVPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQ 172
Cdd:PRK05922 88 RPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 173 TGKTAVAIDTIINQKDTgvICIYVAIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPAPLLYLAPMTGAALGEYFMwh 252
Cdd:PRK05922 168 SGKSSLLSTIAKGSKST--INVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFR-- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 253 gtngqpagsdNPGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACklSDERgaGSLTALPIIE 332
Cdd:PRK05922 244 ----------DQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG--NNDK--GSITALYAIL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 333 TQAGDVSAYIPTnVISITDGQIFLeSDLFNAGVRPAMNVGISVSRvgGAAQVKAMKQVSGSVKLE--LAQYRELAAFAQF 410
Cdd:PRK05922 310 HYPNHPDIFTDY-LKSLLDGHFFL-TPQGKALASPPIDILTSLSR--SARQLALPHHYAAAEELRslLKAYHEALDIIQL 385
|
330 340 350
....*....|....*....|....*....|
gi 2624589777 411 GSdLDKATLAQLNRGQRLVEILKQAQYQPM 440
Cdd:PRK05922 386 GA-YVPGQDAHLDRAVKLLPSIKQFLSQPL 414
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
66-445 |
5.30e-25 |
|
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 211621 [Multi-domain] Cd Length: 461 Bit Score: 107.88 E-value: 5.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 66 LEEDNVGIILLGDVTLIKEGDTVKRTGRIMNVPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEP 145
Cdd:TIGR01039 47 LGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 146 MQTGLKVIDALIPVGRGQRELIIGDRQTGKTaVAIDTIINQ--KDTGVICIYVAIGQKRSTIAQVVKTLEEYDAMKHTIV 223
Cdd:TIGR01039 127 LETGIKVIDLLAPYAKGGKIGLFGGAGVGKT-VLIQELINNiaKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTAL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 224 VAASASEPAPLLYLAPMTGAALGEYFmwhgtngqpagSDNPGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAY----P 299
Cdd:TIGR01039 206 VYGQMNEPPGARMRVALTGLTMAEYF-----------RDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYqptlA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 300 GDVFYLHSRLLERAcklsdergAGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVG 379
Cdd:TIGR01039 275 TEMGELQERITSTK--------TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLL 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2624589777 380 GAAQV-KAMKQVSGSVKLELAQYRELA-AFAQFG----SDLDKATLAQLNRGQRLVEilkqaqyQPMPVEKQ 445
Cdd:TIGR01039 347 DPSVVgEEHYDVARGVQQILQRYKELQdIIAILGmdelSEEDKLTVERARRIQRFLS-------QPFFVAEV 411
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
65-359 |
2.39e-22 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 99.34 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 65 NLEEDNVGIILLGDVTLIKEGDTVKRTGRIMNVPVGPAFVGRVVDALGNPIDGKG-------PIESVSFNPIERIAPgiv 137
Cdd:PRK02118 44 RLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPelegepiEIGGPSVNPVKRIVP--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 138 drksvHEPMQTGLKVIDALIPVGRGQRELIIGDRQTGKTAVAIdTIINQKDTGVIcIYVAIGQKRSTIAQVVKTLEEYDA 217
Cdd:PRK02118 121 -----REMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA-RIALQAEADII-ILGGMGLTFDDYLFFKDTFENAGA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 218 MKHTIVVAASASEPAPLLYLAPMTGAALGEYFMWHGtngqpagsdnpGQHVLCIYDDLSKQAVAYREISLLVRRPPGREA 297
Cdd:PRK02118 194 LDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEG-----------KKKVLVLLTDMTNFADALKEISITMDQIPSNRG 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2624589777 298 YPGDvfyLHSRLLERACKLSDERGAGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESD 359
Cdd:PRK02118 263 YPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLRRG 321
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
27-443 |
3.99e-20 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 92.73 E-value: 3.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 27 EVGTIISVGDGIARAHGLEKAMAGELLELPHGVMGLTFNLEEDNVGIILLGDVTLIKEGDTVKRTGRIMNVPVGPAFVGR 106
Cdd:PRK06793 21 KVGKVHSVQEQFFVAKGPKAKIGDVCFVGEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 107 VVDALGNPIDGkgPIESVSFNPIERIAPGI--VDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQTGKTAVAIDTII 184
Cdd:PRK06793 101 VLSANGEVLNE--EAENIPLQKIKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 185 NQK-DTGVICIyvaIGQKRSTIAQVVKTLEEYDAMKHTIVVAASASEPAPLLYLAPMTGAALGEYFMWHGTNgqpagsdn 263
Cdd:PRK06793 179 NAKaDINVISL---VGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNN-------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 264 pgqhVLCIYDDLSKQAVAYREISLLVRRPPgreaYPGDVFYLHS---RLLERACKLSDergaGSLTALPIIETQAGDVSA 340
Cdd:PRK06793 248 ----VLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK----GSITGIYTVLVDGDDLNG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 341 YIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRVGGAAQVKAMKQVSGSVKLELAQYRELAAFAQFGSDLDKATLA 420
Cdd:PRK06793 316 PVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTIQENAENA 395
|
410 420
....*....|....*....|....*..
gi 2624589777 421 QL----NRGQRLVEILKQAQYQPMPVE 443
Cdd:PRK06793 396 YIfeckNKVEGINTFLKQGRSDSFQFD 422
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-378 |
6.22e-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: 86.89 E-value: 6.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 96 NVPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQTGK 175
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 176 TaVAIDTIINQ--KDTGVICIYVAIGQkRSTIAQvvktlEEYDAMKHTIVVAASASEPAPLLY-----------LAPMTG 242
Cdd:cd01133 81 T-VLIMELINNiaKAHGGYSVFAGVGE-RTREGN-----DLYHEMKESGVINLDGLSKVALVYgqmneppgaraRVALTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 243 AALGEYFmwhgtngqpagSDNPGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGDVFYLHSRLLERACKLSDerga 322
Cdd:cd01133 154 LTMAEYF-----------RDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKK---- 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2624589777 323 GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMNVGISVSRV 378
Cdd:cd01133 219 GSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
85-162 |
1.41e-18 |
|
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439825 [Multi-domain] Cd Length: 468 Bit Score: 88.22 E-value: 1.41e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2624589777 85 GDTVKRTGRIMNVPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVDRKSVHEPMQTGLKVIDALIPVGRG 162
Cdd:COG0055 69 GMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKG 146
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
387-454 |
1.88e-16 |
|
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: 74.02 E-value: 1.88e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 387 MKQVSGSVKLELAQYRELAAFAQFGSD--LDKATLAQLNRGQRLVEILKQAQYQPMPVEKQIVSIWAATN 454
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
25-92 |
3.39e-15 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 70.27 E-value: 3.39e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2624589777 25 VSEVGTIISVGDGIARAHGLEKAMAGELLELPHGVMGLTFNLEEDNVGIILLGDVTLIKEGDTVKRTG 92
Cdd:pfam02874 2 VQVIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
82-185 |
5.79e-13 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 70.84 E-value: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 82 IKEGDTVKRTGRIMNVPVGPAFVGRVVDALGNPIDGKGPIESVSFNPIERIAPGIVD---RKSVHEpmqTGLKVIDALIP 158
Cdd:CHL00060 81 LMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQldtKLSIFE---TGIKVVDLLAP 157
|
90 100
....*....|....*....|....*..
gi 2624589777 159 VGRGQRELIIGDRQTGKTaVAIDTIIN 185
Cdd:CHL00060 158 YRRGGKIGLFGGAGVGKT-VLIMELIN 183
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
81-327 |
4.55e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 62.11 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 81 LIKEGDTVKRTGRIMNVPVGPAFV----------GRVVDALGN-------PI----DGKGPIESVSFN---PIeRIAPGI 136
Cdd:PRK04192 123 TVKVGDKVEAGDILGTVQETPSIEhkimvppgvsGTVKEIVSEgdytvddTIavleDEDGEGVELTMMqkwPV-RRPRPY 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 137 VDRKSVHEPMQTGLKVIDALIPVGRGQRELIIGDRQTGKTaVAIDTIINQKDTGVIcIYVAIGQKRStiaQVVKTLEEY- 215
Cdd:PRK04192 202 KEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT-VTQHQLAKWADADIV-IYVGCGERGN---EMTEVLEEFp 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 216 ---DA------MKHTI---------VVAASASepaplLYlapmTGAALGEYF--MwhgtngqpagsdnpGQHVLCIYDDL 275
Cdd:PRK04192 277 eliDPktgrplMERTVliantsnmpVAAREAS-----IY----TGITIAEYYrdM--------------GYDVLLMADST 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2624589777 276 SKQAVAYREISLLVRRPPGREAYPGdvfYLHSRL---LERA----CKLSDErgaGSLTA 327
Cdd:PRK04192 334 SRWAEALREISGRLEEMPGEEGYPA---YLASRLaefYERAgrvkTLGGEE---GSVTI 386
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
192-370 |
1.09e-07 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 54.64 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 192 ICIYVAIGQKRSTIAQVvktLEEYDAMK----------HTIVVAASASEPAPLLYLAPMTGAALGEYFMwhgtngqpags 261
Cdd:PRK14698 684 VVIYIGCGERGNEMTDV---LEEFPKLKdpktgkplmeRTVLIANTSNMPVAAREASIYTGITIAEYFR----------- 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589777 262 dNPGQHVLCIYDDLSKQAVAYREISLLVRRPPGREAYPGdvfYLHSRLLE------RACKLSDERGAGSLTALPIIETQA 335
Cdd:PRK14698 750 -DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPG 825
|
170 180 190
....*....|....*....|....*....|....*
gi 2624589777 336 GDVSAYIPTNVISITDGQIFLESDLFNAGVRPAMN 370
Cdd:PRK14698 826 GDFSEPVVQNTLRVVKVFWALDADLARRRHFPAIN 860
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
29-93 |
8.67e-05 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 40.76 E-value: 8.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2624589777 29 GTIISVGDGIARAHGLEKAMAGELLELPH-------GVMGLTFNLEEDNVGIILLGDVTLIKEGDTVKRTGR 93
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIGEVCEIERgdgnnetVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| |
