|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-510 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 1023.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 1 MQLNSTEISEIIRKRIEGFNVVSDARNEGTIVSVSDGIIRIHGLADVMQGEMIELPGGNFALALNLERDSVGAVVMGPYT 80
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 81 DLSEGMKVTSTGRILEVPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIG 160
Cdd:PRK09281 81 DIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 161 RGQRELIIGDRQTGKTALAIDAIINQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPY 240
Cdd:PRK09281 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 241 SGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVSEvyverftngevKGK 320
Cdd:PRK09281 241 AGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSD-----------ELG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 321 TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAAY 400
Cdd:PRK09281 310 GGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 401 RELAAFAQFASDLDEATKRQLNHGQKVTELMKQKQYAPMSVFDQALVIFAAERGYLSDVELNKVLDFESALLSYAHSQYA 480
Cdd:PRK09281 390 RELEAFAQFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHA 469
|
490 500 510
....*....|....*....|....*....|
gi 1119772071 481 DFKTEIDKTGAYNDEIEAKLKKLVEDFKAT 510
Cdd:PRK09281 470 DLLEEIRETKDLSDEIEAKLKAAIEEFKKT 499
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-513 |
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: 1001.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 1 MQLNSTEISEIIRKRIEGFNVVSDARNEGTIVSVSDGIIRIHGLADVMQGEMIELPGGNFALALNLERDSVGAVVMGPYT 80
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 81 DLSEGMKVTSTGRILEVPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIG 160
Cdd:COG0056 81 GIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 161 RGQRELIIGDRQTGKTALAIDAIINQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPY 240
Cdd:COG0056 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 241 SGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVSEVYverftngevkgK 320
Cdd:COG0056 241 AGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEL-----------G 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 321 TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAAY 400
Cdd:COG0056 310 GGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 401 RELAAFAQFASDLDEATKRQLNHGQKVTELMKQKQYAPMSVFDQALVIFAAERGYLSDVELNKVLDFESALLSYAHSQYA 480
Cdd:COG0056 390 RELEAFAQFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHP 469
|
490 500 510
....*....|....*....|....*....|...
gi 1119772071 481 DFKTEIDKTGAYNDEIEAKLKKLVEDFKATQTW 513
Cdd:COG0056 470 DLLKEIRETGKLDDEIEEKLKAAIEEFKKTFAA 502
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
2-513 |
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: 875.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 2 QLNSTEISEIIRKRIEGFNVVSDARNEGTIVSVSDGIIRIHGLADVMQGEMIELPGGNFALALNLERDSVGAVVMGPYTD 81
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 82 LSEGMKVTSTGRILEVPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGR 161
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 162 GQRELIIGDRQTGKTALAIDAIINQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPYS 241
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 242 GCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVSevyverftngEVKGKt 321
Cdd:TIGR00962 241 GCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLN----------DEKGG- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 322 GSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAAYR 401
Cdd:TIGR00962 310 GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 402 ELAAFAQFASDLDEATKRQLNHGQKVTELMKQKQYAPMSVFDQALVIFAAERGYLSDVELNKVLDFESALLSYAHSQYAD 481
Cdd:TIGR00962 390 ELEAFSQFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPD 469
|
490 500 510
....*....|....*....|....*....|..
gi 1119772071 482 FKTEIDKTGAYNDEIEAKLKKLVEDFKATQTW 513
Cdd:TIGR00962 470 ILEEINTTKKLTEELEAKLKEALKNFKKTFAW 501
|
|
| 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: 793.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 1 MQLNSTEISEIIRKRIEGFNVVSDARNEGTIVSVSDGIIRIHGLADVMQGEMIELPGGNFALALNLERDSVGAVVMGPYT 80
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 81 DLSEGMKVTSTGRILEVPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIG 160
Cdd:PRK13343 81 DILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 161 RGQRELIIGDRQTGKTALAIDAIINQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPY 240
Cdd:PRK13343 161 RGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 241 SGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVSEVYverftngevkgK 320
Cdd:PRK13343 241 AGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPEL-----------G 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 321 TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAAY 400
Cdd:PRK13343 310 GGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 401 RELAAFAQFASDLDEATKRQLNHGQKVTELMKQKQYAPMSVFDQALVIFAAERGYLSDVELNKVLDFESALLSYAHSQYA 480
Cdd:PRK13343 390 LELEAFTRFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFA 469
|
490 500 510
....*....|....*....|....*....|...
gi 1119772071 481 DFKTEIDKTGAYNDEIEAKLKKLVEDFKATQTW 513
Cdd:PRK13343 470 ALSLALESPRELDEAWLAALEEILREAGERFAA 502
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
27-511 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 681.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 27 NEGTIVSVSDGIIRIHGLADVMQGEMIELPGGNFALALNLERDSVGAVVMGPYTDLSEGMKVTSTGRILEVPVGPELLGR 106
Cdd:CHL00059 6 NTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 107 VVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALAIDAIINQ 186
Cdd:CHL00059 86 VVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 187 KDSGIYSIYVAIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPYSGCAMGEYFRDRGEDALIVYDDLSKQ 266
Cdd:CHL00059 166 KGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 267 AVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVSEVYverftnGEvkgktGSLTALPIIETQAGDVSAFVPTNVI 346
Cdd:CHL00059 246 AQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQL------GE-----GSMTALPIVETQAGDVSAYIPTNVI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 347 SITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAAYRELAAFAQFASDLDEATKRQLNHGQK 426
Cdd:CHL00059 315 SITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 427 VTELMKQKQYAPMSVFDQALVIFAAERGYLSDVELNKVLDFESALLSYAHSQYADFKTEIDKTGAYNDEIEAKLKKLVED 506
Cdd:CHL00059 395 LRELLKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQE 474
|
....*
gi 1119772071 507 FKATQ 511
Cdd:CHL00059 475 QLELF 479
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
94-378 |
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: 557.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 94 ILEVPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQT 173
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 174 GKTALAIDAIINQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPYSGCAMGEYFRDRG 253
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 254 EDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVSEvyverftngevKGKTGSLTALPIIETQ 333
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSD-----------ELGGGSLTALPIIETQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1119772071 334 AGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVG 378
Cdd:cd01132 230 AGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
12-495 |
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: 525.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 12 IRKRIEGFNVVSDARNEGTIVSVSDGIIRIHGLADVMQGEMIELPGGNFALALNLERDSVGAVVMGPYTDLSEGMKVTST 91
Cdd:TIGR03324 12 LDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 92 GRILEVPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIGDR 171
Cdd:TIGR03324 92 GRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 172 QTGKTALAIDAIINQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPYSGCAMGEYFRD 251
Cdd:TIGR03324 172 QTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSIGEHFME 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 252 RGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVSEvyverftngEVKGktGSLTALPIIE 331
Cdd:TIGR03324 252 QGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNE---------ELGG--GSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 332 TQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAAYRELAAFAQFAS 411
Cdd:TIGR03324 321 TEAQNISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 412 DLDEATKRQLNHGQKVTELMKQKQYAPMSVFDQALVIFAAERGYLSDVELNKVLDFESALLSYAHSQYADFKTEIDKTGA 491
Cdd:TIGR03324 401 RLDENTRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKK 480
|
....
gi 1119772071 492 YNDE 495
Cdd:TIGR03324 481 LSDE 484
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
52-472 |
7.13e-118 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 358.58 E-value: 7.13e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 52 MIELPGGNFA--LALNLERDS-VGAVVMGPYTDLSEGMKVTSTGRILEVPVGPELLGRVVNTLG--VPID----GKGPIE 122
Cdd:PTZ00185 69 MIQVSPTTFAagLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGheVPVGlltrSRALLE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 123 AKLT-SPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALAIDAIINQ--------KDSGIYS 193
Cdd:PTZ00185 149 SEQTlGKVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVIS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 194 IYVAIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPYSGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQI 273
Cdd:PTZ00185 229 IYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 274 SLLLRRPPGREAFPGDVFYLHSRLLERAARVSevyverftngevKGK-TGSLTALPIIETQAGDVSAFVPTNVISITDGQ 352
Cdd:PTZ00185 309 SLLLRRPPGREAYPGDVFYLHSRLLERAAMLS------------PGKgGGSVTALPIVETLSNDVTAYIVTNVISITDGQ 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 353 IFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAAYRELAAFAQFASDLDEATkrqLNHGQKVTELMK 432
Cdd:PTZ00185 377 IYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFN 453
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1119772071 433 QKQyapMSVFDQALV-IFAAERGYLSDVELNKVLDFESALL 472
Cdd:PTZ00185 454 QKN---PSFFMNALVsLYACLNGYLDDVKVNYAKLYEYLLV 491
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
149-375 |
1.47e-111 |
|
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: 329.32 E-value: 1.47e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 149 GYKSVDAMIPIGRGQRELIIGDRQTGKTALAiDAIINQKDSGIySIYVAIGQKASTIANVVRKLEEHGALKNTIVVVASA 228
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 229 SESAALQYLAPYSGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARvsevy 308
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGR----- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119772071 309 verftngeVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVS 375
Cdd:pfam00006 154 --------VKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
30-496 |
1.07e-106 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 327.70 E-value: 1.07e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 30 TIVSVSDGIIRIHGLADVMQGEMIELPGG-NF-ALALNLERDSVGAVVMGPYTDLSEGMKVTSTGRILEVPVGPELLGRV 107
Cdd:PRK07165 4 KIKSIFDYIVEVKGEYDYQQNQFFTLKNNpNVkAFVISATEDKAYLLINNEKGKIKINDELIELNNTNKVKTSKEYFGKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 108 VNtlgvpIDGK--GPIEAK--------LTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTA 177
Cdd:PRK07165 84 ID-----IDGNiiYPEAQNplskkflpNTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 178 LAIDAIINQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALKNTIVVVASaSESAALQYLAPYSGCAMGE---YFrdrgE 254
Cdd:PRK07165 159 IALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAP-STSPYEQYLAPYVAMAHAEnisYN----D 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 255 DALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvsevyverftnGEVKGKTgSLTALPIIETQA 334
Cdd:PRK07165 234 DVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERA-------------GKFKNRK-TITALPILQTVD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 335 GDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAAYRELAAFAQFASDLD 414
Cdd:PRK07165 300 NDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 415 EATKRQLNHGQKVTELMKQKQYAPMSVFDQALVIFAAERGYLSDV-ELNKVLDFESALL---SYAHSQYADFKTEIDktg 490
Cdd:PRK07165 380 KETSDLLFKGKMIEKMFNQKGFSLYSYRFVLLISKLISWGLLKDVkDEQKALDFIDYLIendPDAKKIFNKIKNNED--- 456
|
....*.
gi 1119772071 491 aYNDEI 496
Cdd:PRK07165 457 -VDDEL 461
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
97-377 |
3.38e-106 |
|
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: 317.86 E-value: 3.38e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 97 VPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKT 176
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 177 ALAIDAIINQ-KDSGIYSIYVAIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPYSGCAMGEYFRDRGED 255
Cdd:cd19476 82 VLAMQLARNQaKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 256 ALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARvsevyverftngeVKGKTGSLTALPIIETQAG 335
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGK-------------VKDGGGSITAIPAVSTPGD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1119772071 336 DVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 377
Cdd:cd19476 229 DLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
382-507 |
5.15e-62 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 198.82 E-value: 5.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 382 QTKIIKKLSGGIRTALAAYRELAAFAQFASDLDEATKRQLNHGQKVTELMKQKQYAPMSVFDQALVIFAAERGYLSDVEL 461
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1119772071 462 NKVLDFESALLSYAHSQYADFKTEIDKTGAYNDEIEAKLKKLVEDF 507
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 ... |
386-510 |
5.61e-62 |
|
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: 198.74 E-value: 5.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 386 IKKLSGGIRTALAAYRELAAFAQFASDLDEATKRQLNHGQKVTELMKQKQYAPMSVFDQALVIFAAERGYLSDVELNKVL 465
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1119772071 466 DFESALLSYAHSQYADFKTEIDKTGAYNDEIEAKLKKLVEDFKAT 510
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKS 125
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
96-377 |
7.28e-50 |
|
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: 171.97 E-value: 7.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 96 EVPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGK 175
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 176 TALaIDAIINQKDSGIYSIyVAIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPYSGCAMGEYFRDRGED 255
Cdd:cd01136 81 STL-LGMIARNTDADVNVI-ALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 256 ALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvsevyverftngevKGKTGSLTALPIIETQAG 335
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAG---------------NGEKGSITAFYTVLVEGD 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1119772071 336 DVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 377
Cdd:cd01136 224 DFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
26-408 |
3.77e-49 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 174.96 E-value: 3.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 26 RNEGTIVSVSDGIIRIHGLaDVMQGEMIELPGGNFALALNLE-----RDSVGAVVMGPYTDLSEGMKVTSTGRILEVPVG 100
Cdd:PRK09099 23 RRTGKVVEVIGTLLRVSGL-DVTLGELCELRQRDGTLLQRAEvvgfsRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 101 PELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGK-TALA 179
Cdd:PRK09099 102 PALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKsTLMG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 180 IDAIINQKDsgiYSIYVAIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPYSGCAMGEYFRDRGEDALIV 259
Cdd:PRK09099 182 MFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 260 YDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARvsevyverftngevkGKTGSLTALPIIETQAGDVSA 339
Cdd:PRK09099 259 MDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM---------------GETGSITALYTVLAEDESGSD 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1119772071 340 FVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAAYRELAAFAQ 408
Cdd:PRK09099 324 PIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQ 392
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
12-402 |
3.22e-48 |
|
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: 172.14 E-value: 3.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 12 IRKRIEGFNVVsdaRNEGTIVSVSDGIIRIHGLaDVMQGE--MIELPGGNFALA--LNLERDSVgaVVMgPYTD---LSE 84
Cdd:COG1157 7 LLARLEELPPV---RVSGRVTRVVGLLIEAVGP-DASIGElcEIETADGRPVLAevVGFRGDRV--LLM-PLGDlegISP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 85 GMKVTSTGRILEVPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQR 164
Cdd:COG1157 80 GARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 165 eliIGdr---qtGKTALaIDAIINQKDSGIysiyvaigqkastiaNVV---------------RKLEEHGaLKNTIVVVA 226
Cdd:COG1157 160 ---IGifagsgvGKSTL-LGMIARNTEADV---------------NVIaligergrevrefieDDLGEEG-LARSVVVVA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 227 SASESAALQYLAPYSGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvse 306
Cdd:COG1157 220 TSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERA----- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 307 vyverftnGevKGKTGSLTAL------------PIIETqagdvsafvptnVISITDGQIFLQTELFNAGVRPAVDPGISV 374
Cdd:COG1157 295 --------G--NGGKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASI 352
|
410 420
....*....|....*....|....*...
gi 1119772071 375 SRVGGAAQTKIIKKLSGGIRTALAAYRE 402
Cdd:COG1157 353 SRVMPDIVSPEHRALARRLRRLLARYEE 380
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
12-446 |
3.68e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 166.85 E-value: 3.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 12 IRKRIEgfNVVsdarneGTIVSVSDGIIRIhgladvmqGEMIEL--PGGNFAL---ALNLERDSVGAVVMGPYTDLSEGM 86
Cdd:PRK06936 23 IRGRVT--QVT------GTILKAVVPGVRI--------GELCYLrnPDNSLSLqaeVIGFAQHQALLTPLGEMYGISSNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 87 KVTSTGRILEVPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQREL 166
Cdd:PRK06936 87 EVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 167 IIGDRQTGKTALaIDAIINQKDSGIySIYVAIGQKASTianvVRKLEEHG----ALKNTIVVVASASESAALQYLAPYSG 242
Cdd:PRK06936 167 IFAAAGGGKSTL-LASLIRSAEVDV-TVLALIGERGRE----VREFIESDlgeeGLRKAVLVVATSDRPSMERAKAGFVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 243 CAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvsevyverftngevKGKTG 322
Cdd:PRK06936 241 TSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG---------------QSDKG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 323 SLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAAYRE 402
Cdd:PRK06936 306 SITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEE 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1119772071 403 ---LAAFAQFASDLDEATKRQLNHGQKVTELMKQKQYAPmSVFDQAL 446
Cdd:PRK06936 386 velLLQIGEYQKGQDKEADQAIERIGAIRGFLRQGTHEL-SHFNETL 431
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
1-434 |
1.85e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 162.29 E-value: 1.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 1 MQLNSTE-ISEIIRKRIEGFN-VVSDARNEGTIVSVSDGIIRIhGLADVMQGEMIEL-PGGNFALALNLERDSVgavVMG 77
Cdd:PRK06820 1 MKLPDIArLTPRLQQQLTRPSaPPEGLRYRGPIVEIGPTLLRA-SLPGVAQGELCRIePQGMLAEVVSIEQEMA---LLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 78 PYTD---LSEGMKVTSTGRILEVPVGPELLGRVVNTLGVPIDGKGPIEAKLtSPVEVIAPGVIDRKSVDQPVQTGYKSVD 154
Cdd:PRK06820 77 PFASsdgLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQW-RELDCPPPSPLTRQPIEQMLTTGIRAID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 155 AMIPIGRGQRELIIGDRQTGK-TALAIDAIINQKDSGIYSIyvaIGQKASTianvVRKLEEHG----ALKNTIVVVASaS 229
Cdd:PRK06820 156 GILSCGEGQRIGIFAAAGVGKsTLLGMLCADSAADVMVLAL---IGERGRE----VREFLEQVltpeARARTVVVVAT-S 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 230 ESAALQYL-APYSGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvsevy 308
Cdd:PRK06820 228 DRPALERLkGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG------ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 309 verftngevKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKK 388
Cdd:PRK06820 302 ---------NSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLA 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1119772071 389 LSGGIRTALAAYRELAAFAQF-----ASDL--DEATKRQlnhgQKVTELMKQK 434
Cdd:PRK06820 373 MAQKLRRMLACYQEIELLVRVgeyqaGEDLqaDEALQRY----PAICAFLQQD 421
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
74-434 |
3.41e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 156.04 E-value: 3.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 74 VVMGPYTDLSE---GMKVTSTGRILEVPVGPELLGRVVNTLGVPIDGKgPIEAKLTS-PVEVIAPGVIDRKSVDQPVQTG 149
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGS-ALPKGLAPvSTDQDPPNPLKRPPIREPMEVG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 150 YKSVDAMIPIGRGQRELIIGDRQTGKTALAidAIINQKDSGIYSIYVAIGQKASTIANVV-RKLEEHGaLKNTIVVVASA 228
Cdd:PRK07721 146 VRAIDSLLTVGKGQRVGIFAGSGVGKSTLM--GMIARNTSADLNVIALIGERGREVREFIeRDLGPEG-LKRSIVVVATS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 229 SESAALQYLAPYSGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvsevy 308
Cdd:PRK07721 223 DQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG------ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 309 verfTNGEvkgktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKK 388
Cdd:PRK07721 297 ----TNAS-----GSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKE 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1119772071 389 LSGGIRTALAAYRE------LAAFAQFAS-DLDEATKRQlnhgQKVTELMKQK 434
Cdd:PRK07721 368 AANRFRELLSTYQNsedlinIGAYKRGSSrEIDEAIQFY----PQIISFLKQG 416
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
10-384 |
2.01e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 150.99 E-value: 2.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 10 EIIRKRIEGFNVVSDArneGTIVSVSDGIIRIHGL----ADVMQGEMIELPGGNFALALNLERDSVGAVVMGPYTDLSEG 85
Cdd:PRK08472 4 ESLKNKLQKFNLSPRF---GSITKISPTIIEADGLnpsvGDIVKIESSDNGKECLGMVVVIEKEQFGISPFSFIEGFKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 86 MKVTSTGRILEVPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRE 165
Cdd:PRK08472 81 DKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 166 LIIGDRQTGKTALaIDAIINQKDSGIYSIYVaIGQKASTIANVVRKlEEHGALKNTIVVVASASESAALQYLAPYSGCAM 245
Cdd:PRK08472 161 GIFAGSGVGKSTL-MGMIVKGCLAPIKVVAL-IGERGREIPEFIEK-NLGGDLENTVIVVATSDDSPLMRKYGAFCAMSV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 246 GEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvsevyverftnGEVKGKtGSLT 325
Cdd:PRK08472 238 AEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERA-------------GKEEGK-GSIT 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1119772071 326 ALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTK 384
Cdd:PRK08472 304 AFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
26-438 |
3.20e-37 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 142.40 E-value: 3.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 26 RNEGTIVSVSDGIIRIHgLADVMQGEMIEL-PGGNFALALNLERDSVGAVVMGPYTDLSEGMKVTSTGRILEVPVGPELL 104
Cdd:PRK07594 20 CRWGRIQDVSATLLNAW-LPGVFMGELCCIkPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 105 GRVVNTLGVPIDGKgPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALaIDAII 184
Cdd:PRK07594 99 GRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 185 NQKDSGIySIYVAIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPYSGCAMGEYFRDRGEDALIVYDDLS 264
Cdd:PRK07594 177 NAPDADS-NVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 265 KQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvsevyverftngevKGKTGSLTALPIIETQAGDVSAFVPTN 344
Cdd:PRK07594 256 RYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG---------------MGEKGSITAFYTVLVEGDDMNEPLADE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 345 VISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAAYRE---LAAFAQFASDLDEATKRQL 421
Cdd:PRK07594 321 VRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEvelLIRIGEYQRGVDTDTDKAI 400
|
410
....*....|....*..
gi 1119772071 422 NHGQKVTELMKQKQYAP 438
Cdd:PRK07594 401 DTYPDICTFLRQSKDEV 417
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
29-402 |
3.29e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 142.44 E-value: 3.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 29 GTIVSVSDGIIRIHGLA-DVMQGEMIELPGGN---FALALNLERDSVGAVVMGPYTDLSEGMKVTSTGRiLEVPVGPELL 104
Cdd:PRK06002 28 GTVSEVTASHYRVRGLSrFVRLGDFVAIRADGgthLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGP-LRIRPDPSWK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 105 GRVVNTLGVPIDGKGPIEAKLTS-PVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGK-TALAIDA 182
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPmSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKsTLLAMLA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 183 iinqKDSGIYSIYVA-IGQKASTianvVRK-LEEH--GALKNTIVVVASASESAALQYLAPYSGCAMGEYFRDRGEDALI 258
Cdd:PRK06002 187 ----RADAFDTVVIAlVGERGRE----VREfLEDTlaDNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 259 VYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvsevyverftnGEVKGKTGSLTALPIIETQAGDVS 338
Cdd:PRK06002 259 IVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERA-------------GPGAEGGGSITGIFSVLVDGDDHN 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119772071 339 AFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAAYRE 402
Cdd:PRK06002 326 DPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEE 389
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
63-377 |
7.85e-37 |
|
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: 141.78 E-value: 7.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 63 ALNLERDSVGAVVMGPYTDLSEGMKVTSTGRILEVPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSV 142
Cdd:TIGR01039 44 AQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 143 DQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALAIDAIIN-QKDSGIYSIYVAIGQKASTIANVVRKLEEHGALKNT 221
Cdd:TIGR01039 124 VEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 222 IVVVASASESAALQYLAPYSGCAMGEYFRD-RGEDALIVYDDLSKQAVAYRQISLLLRRppgreaFPGDVFYLHSrlleR 300
Cdd:TIGR01039 204 ALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGR------MPSAVGYQPT----L 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119772071 301 AARVSEVYvERFTNgevkGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 377
Cdd:TIGR01039 274 ATEMGELQ-ERITS----TKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRL 345
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
82-433 |
7.29e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 135.79 E-value: 7.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 82 LSEGMKVTSTGRILEVPVGPELLGRVVNTLGVPIDGKGPI--EAKLTSPVEVIAPgvIDRKSVDQPVQTGYKSVDAMIPI 159
Cdd:PRK07196 75 VLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLggSTPLQQQLPQIHP--LQRRAVDTPLDVGVNAINGLLTI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 160 GRGQRELIIGDRQTGKTALAidAIINQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAP 239
Cdd:PRK07196 153 GKGQRVGLMAGSGVGKSVLL--GMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKAT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 240 YSGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvsevyverftNGEvkg 319
Cdd:PRK07196 231 ELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG-----------NSS--- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 320 KTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSR----VGGAAQTKIIKKLSGGIrT 395
Cdd:PRK07196 297 GNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCY-A 375
|
330 340 350
....*....|....*....|....*....|....*...
gi 1119772071 396 ALAAYRELAAFAQFASDLDEATKRQLNHGQKVTELMKQ 433
Cdd:PRK07196 376 DYMAIKPLIPLGGYVAGADPMADQAVHYYPAITQFLRQ 413
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
85-377 |
2.37e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 134.44 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 85 GMKVTSTGRILEVPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQR 164
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 165 ELIIGDRQTGKTAL--------AIDAIInqkdSGIysiyvaIGQKASTIANVVRK-LEEHGaLKNTIVVVASASESAALQ 235
Cdd:PRK08972 165 MGLFAGSGVGKSVLlgmmtrgtTADVIV----VGL------VGERGREVKEFIEEiLGEEG-RARSVVVAAPADTSPLMR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 236 YLAPYSGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvsevyverftNG 315
Cdd:PRK08972 234 LKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAG-----------NG 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119772071 316 evKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 377
Cdd:PRK08972 303 --GPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRV 362
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
94-376 |
4.93e-34 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 129.65 E-value: 4.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 94 ILEVPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQT 173
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 174 GKTALAI----DAIINQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPYSGCAMGEYF 249
Cdd:cd01135 81 PHNELAAqiarQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 250 R-DRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRLleraarvSEVYvERftNGEVKGKTGSLTALP 328
Cdd:cd01135 161 AyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDL-------ATIY-ER--AGRVEGRKGSITQIP 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1119772071 329 IIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSR 376
Cdd:cd01135 228 ILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
30-376 |
3.21e-31 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 125.71 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 30 TIVSVSDGIIRIHGLADVMQGEM--IELPGGNFALA--LNLERDSVGAVVMGPYTDLS-EGMKVTSTGRILEVPVGPELL 104
Cdd:PRK04196 6 TVSEIKGPLLFVEGVEGVAYGEIveIELPNGEKRRGqvLEVSEDKAVVQVFEGTTGLDlKDTKVRFTGEPLKLPVSEDML 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 105 GRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQR------------ELiigdrq 172
Cdd:PRK04196 86 GRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnEL------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 173 tgktALAI--DAIINQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPYSGCAMGEYFR 250
Cdd:PRK04196 160 ----AAQIarQAKVLGEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 251 -DRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAarvsevyverftnGEVKGKTGSLTA 326
Cdd:PRK04196 236 fEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERA-------------GRIKGKKGSITQ 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1119772071 327 LPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSR 376
Cdd:PRK04196 300 IPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
91-406 |
3.21e-31 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 125.11 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 91 TGRILEVPVGPELLGRVVNTLGVpIDGK--GPIEAK---LTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRE 165
Cdd:PRK08149 76 TGKPLSVWVGEALLGAVLDPTGK-IVERfdAPPTVGpisEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 166 LIIGDRQTGKTALaIDAIINQKDSGIYSIYVaIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPYSGCAM 245
Cdd:PRK08149 155 GIFASAGCGKTSL-MNMLIEHSEADVFVIGL-IGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTV 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 246 GEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVsevyverftngevkgKTGSLT 325
Cdd:PRK08149 233 AEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT---------------LAGSIT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 326 ALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAAYRELAA 405
Cdd:PRK08149 298 AFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQL 377
|
.
gi 1119772071 406 F 406
Cdd:PRK08149 378 F 378
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
88-377 |
2.00e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 123.30 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 88 VTSTGRIlevPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVE--VIAPgvIDRKSVDQPVQTGYKSVDAMIPIGRGQRE 165
Cdd:PRK05688 97 LADTGRL---PMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDgpTINP--LNRHPISEPLDVGIRSINGLLTVGRGQRL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 166 LIIGDRQTGKTALaIDAIINQKDSGIysIYVA-IGQKASTIANVVRKLEEHGALKNTiVVVASASESAALQYLAPYSGCA 244
Cdd:PRK05688 172 GLFAGTGVGKSVL-LGMMTRFTEADI--IVVGlIGERGREVKEFIEHILGEEGLKRS-VVVASPADDAPLMRLRAAMYCT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 245 -MGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvsevyverftNGEVKGktGS 323
Cdd:PRK05688 248 rIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG-----------NAEPGG--GS 314
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1119772071 324 LTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 377
Cdd:PRK05688 315 ITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV 368
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
26-418 |
3.87e-28 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 116.54 E-value: 3.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 26 RNEGTIVSVSDGIIRIHGLADVMqGEM--IELPGGNFALA--LNLERDSVGAVVMGPYTDLSEGMKVTSTGRILEVPVGP 101
Cdd:PRK05922 18 RECGLLSRVSGNLLEAQGLSACL-GELcqISLSKSPPILAevIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 102 ELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALaID 181
Cdd:PRK05922 97 HLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSL-LS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 182 AIINQKDSGIYSIYVaIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPYSGCAMGEYFRDRGEDALIVYD 261
Cdd:PRK05922 176 TIAKGSKSTINVIAL-IGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 262 DLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvsevyverftNGEvkgkTGSLTALPIIETQAGDVSAFV 341
Cdd:PRK05922 255 SLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG-----------NND----KGSITALYAILHYPNHPDIFT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 342 PTnVISITDGQIFLqTELFNAGVRPAVDPGISVSRvgGAAQTKIIKKLSGG--IRTALAAYRELAAFAQFAS-------D 412
Cdd:PRK05922 320 DY-LKSLLDGHFFL-TPQGKALASPPIDILTSLSR--SARQLALPHHYAAAeeLRSLLKAYHEALDIIQLGAyvpgqdaH 395
|
....*.
gi 1119772071 413 LDEATK 418
Cdd:PRK05922 396 LDRAVK 401
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
90-411 |
2.20e-26 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 111.80 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 90 STGRILevPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIG 169
Cdd:PRK07960 105 QSGKQL--PLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 170 DRQTGKTAL-AIDAIINQKDSgiysIYVA-IGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQYLAPYSGCAMGE 247
Cdd:PRK07960 183 GSGVGKSVLlGMMARYTQADV----IVVGlIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 248 YFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvsevyverftNGEVKGktGSLTAL 327
Cdd:PRK07960 259 DFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG-----------NGISGG--GSITAF 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 328 PIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRvggaAQTKIIKKlsggirtalAAYRELAAFA 407
Cdd:PRK07960 326 YTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISR----AMTALIDE---------QHYARVRQFK 392
|
....
gi 1119772071 408 QFAS 411
Cdd:PRK07960 393 QLLS 396
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
85-402 |
7.76e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 109.68 E-value: 7.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 85 GMKVTSTGRILEVPVGPELLGRVVNTLGVPIDGkgPIEAKLTSPVEVIAPGV--IDRKSVDQPVQTGYKSVDAMIPIGRG 162
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 163 QRELIIGDRQTGK-TALAIDAIINQKDSGIYSIyvaIGQKASTIANVVRK-LEEHGaLKNTIVVVASASESAALQYLAPY 240
Cdd:PRK06793 157 QKIGIFAGSGVGKsTLLGMIAKNAKADINVISL---VGERGREVKDFIRKeLGEEG-MRKSVVVVATSDESHLMQLRAAK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 241 SGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPgreaFPGDVFYLHS---RLLERAArvsevyverftngev 317
Cdd:PRK06793 233 LATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSG--------------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 318 KGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTAL 397
Cdd:PRK06793 294 KTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKIL 373
|
....*
gi 1119772071 398 AAYRE 402
Cdd:PRK06793 374 SIYKE 378
|
|
| 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 |
1.80e-25 |
|
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: 99.06 E-value: 1.80e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1119772071 27 NEGTIVSVSDGIIRIHGLADVMQGEMIELPGGNFALALNLERDSVGAVVMGPYTDLSEGMKVTSTGR 93
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 ... |
91-377 |
2.83e-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: 108.66 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 91 TGRILEVPVGPELLGRVVNTLGVPIDGKGPI--EAKLTSPVEVIAPgvIDRKSVDQPVQTGYKSVDAMIPIGRGQRELII 168
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVlaEDYLDINGQPINP--YARIYPEEMIQTGISAIDVMNSIARGQKIPIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 169 GD-------------RQTGKTALAIDAIINQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALKNTIVVVASASESAALQ 235
Cdd:TIGR01040 148 SAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIER 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 236 YLAPYSGCAMGEYFR-DRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVsevyverftn 314
Cdd:TIGR01040 228 IITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV---------- 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1119772071 315 gevKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 377
Cdd:TIGR01040 298 ---EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 357
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
40-404 |
5.40e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 107.37 E-value: 5.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 40 RIHGLADVM--------QGEMIELPGGNFALAL----NLER--------DSVG-----AVVMgPYTDLsEGMKVTSTGRI 94
Cdd:PRK08927 8 AIGDIDTLViygrvvavRGLLVEVAGPIHALSVgariVVETrggrpvpcEVVGfrgdrALLM-PFGPL-EGVRRGCRAVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 95 LE----VPVGPELLGRVVNTLGVPIDGKGPIEAKLTS-PVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIG 169
Cdd:PRK08927 86 ANaaaaVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPyPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 170 DRQTGKTALaIDAIINQKDSGIYSIYVaIGQKASTIANVVRK-LEEHGaLKNTIVVVASASESAALQYLAPYSGCAMGEY 248
Cdd:PRK08927 166 GSGVGKSVL-LSMLARNADADVSVIGL-IGERGREVQEFLQDdLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAIAEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 249 FRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvsevyverftnGEVKGKTGSLTALP 328
Cdd:PRK08927 243 FRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERA-------------GPGPIGEGTITGLF 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119772071 329 IIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAAYRELA 404
Cdd:PRK08927 310 TVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADME 385
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-377 |
3.17e-24 |
|
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: 102.30 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 96 EVPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGK 175
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 176 TALAIDAIIN-QKDSGIYSIYVAIGQKASTIANVVRKLEEHG-----ALKNTIVVVASASESAALQYLAPYSGCAMGEYF 249
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGERTREGNDLYHEMKESGvinldGLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 250 RD-RGEDALIVYDDLSKQAVAYRQISLLLRRPPGReafpgdVFYlHSRLlerAARVSEVYvERFTNgevkGKTGSLTALP 328
Cdd:cd01133 161 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSA------VGY-QPTL---ATEMGSLQ-ERITS----TKKGSITSVQ 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1119772071 329 IIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 377
Cdd:cd01133 226 AVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
69-403 |
4.62e-23 |
|
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: 101.70 E-value: 4.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 69 DSVGAVVMGPyTD-LSEGMKVTSTGRILEVPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQ 147
Cdd:COG0055 53 NTVRCIAMDS-TDgLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 148 TGYKSVDAMIPIGRGQRELIIGDRQTGKTALaIDAIIN---QKDSGiYSIYVAIGQKASTIANVVRKLEEHGALKNTIVV 224
Cdd:COG0055 132 TGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL-IMELIHniaKEHGG-VSVFAGVGERTREGNDLYREMKESGVLDKTALV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 225 VASASESAALQYLAPYSGCAMGEYFRD-RGEDALIVYDDLSK--QAVAyrQISLLLRRPPGReafpgdVFY---LHSRL- 297
Cdd:COG0055 210 FGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRftQAGS--EVSALLGRMPSA------VGYqptLATEMg 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 298 -LEraarvsevyvERFTNgevkGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSR 376
Cdd:COG0055 282 aLQ----------ERITS----TKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSR 347
|
330 340 350
....*....|....*....|....*....|....*..
gi 1119772071 377 ------VG----GAAQtkiikklsgGIRTALAAYREL 403
Cdd:COG0055 348 ildpliVGeehyRVAR---------EVQRILQRYKEL 375
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
57-471 |
5.58e-20 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 92.40 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 57 GGNFALALNLERDSVGAVVMGPYTDLSEGMKVTSTGRILEVPVGPELLGRVVNTLGVPIDGKGPIEAKltsPVEVIAPGV 136
Cdd:PRK02118 36 GSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGE---PIEIGGPSV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 137 --IDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALAIdAIINQKDSGIYsIYVAIGQKASTIANVVRKLEE 214
Cdd:PRK02118 113 npVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA-RIALQAEADII-ILGGMGLTFDDYLFFKDTFEN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 215 HGALKNTIVVVASASESAALQYLAPYSGCAMGEYFR-DRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGDvfyL 293
Cdd:PRK02118 191 AGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGS---L 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 294 HSRLleraARVSEVYVErFTNGevkgktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQtelfnagvRPAVDPGIS 373
Cdd:PRK02118 268 YSDL----ASRYEKAVD-FEDG------GSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLR--------RGRIDPFGS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 374 VSRvggaaqtkiIKKLSGGIRTAlAAYRELA-AFAQFASDLDEATKRQLNhGQKVTElmkqkqyapmsvFDQALVIFAAE 452
Cdd:PRK02118 329 LSR---------LKQLVIGKKTR-EDHGDLMnAMIRLYADSREAKEKMAM-GFKLSN------------WDEKLLKFSEL 385
|
410 420
....*....|....*....|
gi 1119772071 453 -RGYLSDVELNkvLDFESAL 471
Cdd:PRK02118 386 fESRLMDLEVN--IPLEEAL 403
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
71-375 |
9.42e-20 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 92.03 E-value: 9.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 71 VGAVVMGPYTDLSEGMKVTSTGRILEVPVGPELLGRVVNTLGVPIDGKGPIEAKLTSPVEVIAPGVIDRKSVDQPVQTGY 150
Cdd:CHL00060 70 VRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 151 KSVDAMIPIGRGQRELIIGDRQTGKTALAIDAIIN-QKDSGIYSIYVAIGQ------------KASTIANVVRKLEEHGA 217
Cdd:CHL00060 150 KVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGErtregndlymemKESGVINEQNIAESKVA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 218 LkntivVVASASESAALQYLAPYSGCAMGEYFRD-RGEDALIVYDDLSKQAVAYRQISLLLRRppgreaFPGDVFYLHSR 296
Cdd:CHL00060 230 L-----VYGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGR------MPSAVGYQPTL 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1119772071 297 LLERAArvsevYVERFTNgevkGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVS 375
Cdd:CHL00060 299 STEMGS-----LQERITS----TKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 368
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
95-376 |
3.70e-19 |
|
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: 87.63 E-value: 3.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 95 LEVPVGPELLGRVVNTLGVPIDgkgpIEAKLTS------------PVEVIAPgVIDRKSVDQPVQTGYKSVDAMIPIGRG 162
Cdd:cd01134 2 LSVELGPGLLGSIFDGIQRPLE----VIAETGSifiprgvnvqrwPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 163 QRELIIGDRQTGKTALaIDAIINQKDSGIYsIYVAIGQKASTIANVVR-----KLEEHGA--LKNTIVVVASASESAALQ 235
Cdd:cd01134 77 GTAAIPGPFGCGKTVI-SQSLSKWSNSDVV-IYVGCGERGNEMAEVLEefpelKDPITGEslMERTVLIANTSNMPVAAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 236 YLAPYSGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAARVSevyverf 312
Cdd:cd01134 155 EASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYERAGRVR------- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119772071 313 TNGEvKGKTGSLTALPIIETQAGDVSAFVPTNVISITdgQIF--LQTELFNAGVRPAVDPGISVSR 376
Cdd:cd01134 225 CLGS-PGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
29-92 |
9.13e-12 |
|
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: 60.25 E-value: 9.13e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119772071 29 GTIVSVSDGIIRIHGLADVMQGEMIELPGGNFALALNLERDSVGAVVMGPYTDLSEGMKVTSTG 92
Cdd:pfam02874 6 GPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
136-326 |
1.49e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 63.65 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 136 VIDRKSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALaIDAIINQKDSGIySIYVAIGQKASTIANVvrkLEEH 215
Cdd:PRK04192 201 YKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVT-QHQLAKWADADI-VIYVGCGERGNEMTEV---LEEF 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 216 GALKN----------TIVV-------VAsASESAAlqylapYSGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLR 278
Cdd:PRK04192 276 PELIDpktgrplmerTVLIantsnmpVA-AREASI------YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLE 348
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1119772071 279 RPPGREAFPGdvfYLHSRL---LERAARVSevyverfTNGevkGKTGSLTA 326
Cdd:PRK04192 349 EMPGEEGYPA---YLASRLaefYERAGRVK-------TLG---GEEGSVTI 386
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
194-348 |
1.59e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 63.89 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 194 IYVAIGQKASTIANVvrkLEEHGALKN----------TIVVVASASESAALQYLAPYSGCAMGEYFRDRGEDALIVYDDL 263
Cdd:PRK14698 686 IYIGCGERGNEMTDV---LEEFPKLKDpktgkplmerTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADST 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119772071 264 SKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAARVSEVYVERftngevkgKTGSLTALPIIETQAGDVSAF 340
Cdd:PRK14698 763 SRWAEALREISGRLEEMPGEEGYPA---YLASKLaefYERAGRVVTLGSDY--------RVGSVSVIGAVSPPGGDFSEP 831
|
....*...
gi 1119772071 341 VPTNVISI 348
Cdd:PRK14698 832 VVQNTLRV 839
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
387-450 |
3.97e-09 |
|
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: 52.83 E-value: 3.97e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119772071 387 KKLSGGIRTALAAYRELAAFAQFASD--LDEATKRQLNHGQKVTELMKQKQYAPMSVFDQALVIFA 450
Cdd:cd01429 2 KAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYP 67
|
|
| 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 |
5.18e-04 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 38.45 E-value: 5.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1119772071 29 GTIVSVSDGIIRIHGLADVMQGEM--IELPGGNF-----ALALNLERDSVGAVVMGPYTDLSEGMKVTSTGR 93
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIGEVceIERGDGNNetvlkAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| |
