|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
36-545 |
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: 972.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 36 KVSPAEISKLLQTKIGGWDSQKDVRDVGHVINVGDGIARIYGLKEVKAGELVMFSSGVAGMALNLETDNIGVVIFGDDRN 115
Cdd:COG0056 2 QIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 116 ILEGDTVTRTNRILDVPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGR 195
Cdd:COG0056 82 IKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 196 GQRELIIGDRQTGKTALAIDTILNQRlvnegleeNKRLYCIYVAIGQKRSTVARILKILEDNDALKYTIVVAATASDPAP 275
Cdd:COG0056 162 GQRELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 276 LQFLAPFTGCSMGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAKMSDTKGSGSL 355
Cdd:COG0056 234 LQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 356 TALPVIETQAGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQSKAMKQVSGTMKLDLAQFREIQ 435
Cdd:COG0056 314 TALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 436 AFSQFGSDLDSSTQQLLTRGTLLTELLKQKQYAPLSIPLQICVIYGGVNGLLDKLDPKLVGKYEEQLLQHLTTQHSDLLS 515
Cdd:COG0056 394 AFAQFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLK 473
|
490 500 510
....*....|....*....|....*....|
gi 71027907 516 TLEREGVLSPETEAKLKSTLEQFVDNFNKS 545
Cdd:COG0056 474 EIRETGKLDDEIEEKLKAAIEEFKKTFAAS 503
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
36-544 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 968.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 36 KVSPAEISKLLQTKIGGWDSQKDVRDVGHVINVGDGIARIYGLKEVKAGELVMFSSGVAGMALNLETDNIGVVIFGDDRN 115
Cdd:PRK09281 2 QINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 116 ILEGDTVTRTNRILDVPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGR 195
Cdd:PRK09281 82 IKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 196 GQRELIIGDRQTGKTALAIDTILNQRlvnegleeNKRLYCIYVAIGQKRSTVARILKILEDNDALKYTIVVAATASDPAP 275
Cdd:PRK09281 162 GQRELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 276 LQFLAPFTGCSMGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAKMSDTKGSGSL 355
Cdd:PRK09281 234 LQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 356 TALPVIETQAGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQSKAMKQVSGTMKLDLAQFREIQ 435
Cdd:PRK09281 314 TALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 436 AFSQFGSDLDSSTQQLLTRGTLLTELLKQKQYAPLSIPLQICVIYGGVNGLLDKLDPKLVGKYEEQLLQHLTTQHSDLLS 515
Cdd:PRK09281 394 AFAQFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLE 473
|
490 500
....*....|....*....|....*....
gi 71027907 516 TLEREGVLSPETEAKLKSTLEQFVDNFNK 544
Cdd:PRK09281 474 EIRETKDLSDEIEAKLKAAIEEFKKTFAA 502
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
36-542 |
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: 809.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 36 KVSPAEISKLLQTKIGGWDSQKDVRDVGHVINVGDGIARIYGLKEVKAGELVMFSSGVAGMALNLETDNIGVVIFGDDRN 115
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 116 ILEGDTVTRTNRILDVPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGR 195
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 196 GQRELIIGDRQTGKTALAIDTILNQRlvnegleeNKRLYCIYVAIGQKRSTVARILKILEDNDALKYTIVVAATASDPAP 275
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQK--------DSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSAS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 276 LQFLAPFTGCSMGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAKMSDTKGSGSL 355
Cdd:TIGR00962 233 LQYLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 356 TALPVIETQAGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQSKAMKQVSGTMKLDLAQFREIQ 435
Cdd:TIGR00962 313 TALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 436 AFSQFGSDLDSSTQQLLTRGTLLTELLKQKQYAPLSIPLQICVIYGGVNGLLDKLDPKLVGKYEEQLLQHLTTQHSDLLS 515
Cdd:TIGR00962 393 AFSQFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILE 472
|
490 500
....*....|....*....|....*..
gi 71027907 516 TLEREGVLSPETEAKLKSTLEQFVDNF 542
Cdd:TIGR00962 473 EINTTKKLTEELEAKLKEALKNFKKTF 499
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
59-542 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 775.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 59 VRDVGHVINVGDGIARIYGLKEVKAGELVMFSSGVAGMALNLETDNIGVVIFGDDRNILEGDTVTRTNRILDVPVGPELL 138
Cdd:CHL00059 4 IVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 139 GRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGKTALAIDTIL 218
Cdd:CHL00059 84 GRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 219 NQRLVNegleenkrLYCIYVAIGQKRSTVARILKILEDNDALKYTIVVAATASDPAPLQFLAPFTGCSMGEWFRNNKKHC 298
Cdd:CHL00059 164 NQKGQN--------VICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 299 VIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAKMSDTKGSGSLTALPVIETQAGDVSAYIPTNVIS 378
Cdd:CHL00059 236 LIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVIS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 379 ITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQSKAMKQVSGTMKLDLAQFREIQAFSQFGSDLDSSTQQLLTRGTLL 458
Cdd:CHL00059 316 ITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 459 TELLKQKQYAPLSIPLQICVIYGGVNGLLDKLDPKLVGKYEEQLLQHLTTQHSDLLSTLEREGVLSPETEAKLKSTLEQF 538
Cdd:CHL00059 396 RELLKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQ 475
|
....
gi 71027907 539 VDNF 542
Cdd:CHL00059 476 LELF 479
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
35-544 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 749.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 35 NKVSPAEISKLLQTKIGGWDSQKDVRDVGHVINVGDGIARIYGLKEVKAGELVMFSSGVAGMALNLETDNIGVVIFGDDR 114
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 115 NILEGDTVTRTNRILDVPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIG 194
Cdd:PRK13343 81 DILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 195 RGQRELIIGDRQTGKTALAIDTILNQRlvnegleeNKRLYCIYVAIGQKRSTVARILKILEDNDALKYTIVVAATASDPA 274
Cdd:PRK13343 161 RGQRELIIGDRQTGKTAIAIDAIINQK--------DSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 275 PLQFLAPFTGCSMGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAKMSDTKGSGS 354
Cdd:PRK13343 233 GLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 355 LTALPVIETQAGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQSKAMKQVSGTMKLDLAQFREI 434
Cdd:PRK13343 313 LTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLEL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 435 QAFSQFGSDLDSSTQQLLTRGTLLTELLKQKQYAPLSIPLQICVIYGGVNGLLDKLDPKLVGKYEEQLLQHLTTQHSDLL 514
Cdd:PRK13343 393 EAFTRFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALS 472
|
490 500 510
....*....|....*....|....*....|
gi 71027907 515 STLEREGVLSPETEAKLKSTLEQFVDNFNK 544
Cdd:PRK13343 473 LALESPRELDEAWLAALEEILREAGERFAA 502
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
128-409 |
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: 593.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 128 ILDVPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQT 207
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 208 GKTALAIDTILNQRlvnegleeNKRLYCIYVAIGQKRSTVARILKILEDNDALKYTIVVAATASDPAPLQFLAPFTGCSM 287
Cdd:cd01132 81 GKTAIAIDTIINQK--------GKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 288 GEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAKMSDTKGSGSLTALPVIETQAGD 367
Cdd:cd01132 153 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 71027907 368 VSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVG 409
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
59-537 |
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: 542.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 59 VRDVGHVINVGDGIARIYGLKEVKAGELVMFSSGVAGMALNLETDNIGVVIFGDDRNILEGDTVTRTNRILDVPVGPELL 138
Cdd:TIGR03324 25 VQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERTGRVMDVPVGDGLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 139 GRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGKTALAIDTIL 218
Cdd:TIGR03324 105 GRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDRQTGKTAIAIDTIL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 219 NQRlvnegleeNKRLYCIYVAIGQKRSTVARILKILEDNDALKYTIVVAATASDPAPLQFLAPFTGCSMGEWFRNNKKHC 298
Cdd:TIGR03324 185 NQK--------GRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSIGEHFMEQGRDV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 299 VIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAKMSDTKGSGSLTALPVIETQAGDVSAYIPTNVIS 378
Cdd:TIGR03324 257 LIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQNISAYIPTNLIS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 379 ITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQSKAMKQVSGTMKLDLAQFREIQAFSQFGSDLDSSTQQLLTRGTLL 458
Cdd:TIGR03324 337 ITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDENTRKTIEHGRRI 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71027907 459 TELLKQKQYAPLSIPLQICVIYGGVNGLLDKLDPKLVGKYEEQLLQHLTTQHSDLLSTLEREGVLSPETEAKLKSTLEQ 537
Cdd:TIGR03324 417 RACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSDEDREQILDIARG 495
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
94-504 |
2.38e-126 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 381.70 E-value: 2.38e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 94 AGMALNLETDN-IGVVIFGDDRNILEGDTVTRTNRILDVPVGPELLGRVVDALGRPID------GKGDLVTKET-SRVEV 165
Cdd:PTZ00185 79 AGLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQTlGKVDA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 166 PAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGKTALAIDTILNQRLVNEGLEENKRLYCIYVAIGQKRS 245
Cdd:PTZ00185 159 GAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVISIYVSIGQRCS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 246 TVARILKILEDNDALKYTIVVAATASDPAPLQFLAPFTGCSMGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGR 325
Cdd:PTZ00185 239 NVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 326 EAYPGDIFYLHSRLLERAAKMSDTKGSGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSV 405
Cdd:PTZ00185 319 EAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSV 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 406 SRVGSAAQSKAMKQVSGTMKLDLAQFREIQAFSQFGSDLDSSTqqlLTRGTLLTELLKQKQyaPLSIPLQICVIYGGVNG 485
Cdd:PTZ00185 399 SRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNALVSLYACLNG 473
|
410
....*....|....*....
gi 71027907 486 LLDKLDPKLVGKYEEQLLQ 504
Cdd:PTZ00185 474 YLDDVKVNYAKLYEYLLVN 492
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
130-408 |
6.90e-120 |
|
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: 354.07 E-value: 6.90e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 130 DVPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGK 209
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 210 TALAIDTILNQRlvnegleENKRLYCIYVAIGQKRSTVARILKILEDNDALKYTIVVAATASDPAPLQFLAPFTGCSMGE 289
Cdd:cd19476 81 TVLAMQLARNQA-------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 290 WFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAKMSDtkGSGSLTALPVIETQAGDVS 369
Cdd:cd19476 154 YFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLT 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 71027907 370 AYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRV 408
Cdd:cd19476 232 DPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
183-406 |
7.03e-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: 328.93 E-value: 7.03e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 183 GMKCVDSLVPIGRGQRELIIGDRQTGKTALAiDTILNQRLVNegleenkrlYCIYVAIGQKRSTVARILKILEDNDALKY 262
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD---------VVVYALIGERGREVREFIEELLGSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 263 TIVVAATASDPAPLQFLAPFTGCSMGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLER 342
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71027907 343 AAKMSDTKgsGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVS 406
Cdd:pfam00006 151 AGRVKGKG--GSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
93-471 |
2.39e-99 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 309.98 E-value: 2.39e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 93 VAGMALNLETDNIGVVIFGDDRNILEGDTVTRTNRILDVPVGPELLGRVVDALGRPIDGKGDLVTKE-----TSRVEVPA 167
Cdd:PRK07165 35 VKAFVISATEDKAYLLINNEKGKIKINDELIELNNTNKVKTSKEYFGKIIDIDGNIIYPEAQNPLSKkflpnTSSIFNLA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 168 PGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGKTALAIDTILNQRlvnegleeNKRLYCIYVAIGQKRSTV 247
Cdd:PRK07165 115 HGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQK--------NTNVKCIYVAIGQKRENL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 248 ARILKILEDNDALKYTIVVAATASDPAPlQFLAPFTGCSMGEWFRNNKKhCVIIYDDLSKQATAYRQMSLLLRRPPGREA 327
Cdd:PRK07165 187 SRIYETLKEHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAENISYNDD-VLIVFDDLTKHANIYREIALLTNKPVGKEA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 328 YPGDIFYLHSRLLERAAKMsdtKGSGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSR 407
Cdd:PRK07165 265 FPGDMFFAHSKLLERAGKF---KNRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSR 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71027907 408 VGSAAQSKAMKQVSGTM-KLDLAQFREIQaFSQFGSDLDSSTQQLLTRGTLLTELLKQKQYAPLS 471
Cdd:PRK07165 342 TGSSVQSKTITKVAGEIsKIYRAYKRQLK-LSMLDYDLNKETSDLLFKGKMIEKMFNQKGFSLYS 405
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
417-542 |
1.47e-60 |
|
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: 195.66 E-value: 1.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 417 MKQVSGTMKLDLAQFREIQAFSQFGSDLDSSTQQLLTRGTLLTELLKQKQYAPLSIPLQICVIYGGVNGLLDKLDPKLVG 496
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 71027907 497 KYEEQLLQHLTTQHSDLLSTLEREGVLSPETEAKLKSTLEQFVDNF 542
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
413-538 |
1.58e-60 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 195.74 E-value: 1.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 413 QSKAMKQVSGTMKLDLAQFREIQAFSQFGSDLDSSTQQLLTRGTLLTELLKQKQYAPLSIPLQICVIYGGVNGLLDKLDP 492
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 71027907 493 KLVGKYEEQLLQHLTTQHSDLLSTLEREGVLSPETEAKLKSTLEQF 538
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
131-408 |
1.04e-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: 164.27 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 131 VPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGKT 210
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 211 ALAIDTILNQRL-VNegleenkrlycIYVAIGQK-RSTVARILKILEDnDALKYTIVVAATASDPAPLQFLAPFTGCSMG 288
Cdd:cd01136 82 TLLGMIARNTDAdVN-----------VIALIGERgREVREFIEKDLGE-EGLKRSVLVVATSDESPLLRVRAAYTATAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 289 EWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAkMSDTkgsGSLTALPVIETQAGDV 368
Cdd:cd01136 150 EYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAG-NGEK---GSITAFYTVLVEGDDF 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 71027907 369 SAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRV 408
Cdd:cd01136 226 NDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
59-441 |
1.46e-42 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 157.62 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 59 VRDVGHVINVGDGIARIYGLkEVKAGEL----------------VMFSSGVAGMAlnletdnigvvIFGDDRNILEGDTV 122
Cdd:PRK09099 22 VRRTGKVVEVIGTLLRVSGL-DVTLGELcelrqrdgtllqraevVGFSRDVALLS-----------PFGELGGLSRGTRV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 123 TRTNRILDVPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELII 202
Cdd:PRK09099 90 IGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 203 GDRQTGKTAL----AIDTilnQRLVNegleenkrlycIYVAIGQKRSTVARILKILEDNDALKYTIVVAATASDPAPLQF 278
Cdd:PRK09099 170 APAGVGKSTLmgmfARGT---QCDVN-----------VIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 279 LAPFTGCSMGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAkMSDTkgsGSLTAL 358
Cdd:PRK09099 236 KAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-MGET---GSITAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 359 PVIETQAGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQSKAMKQVSGTMKLDLAQFREIQAFS 438
Cdd:PRK09099 312 YTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLL 391
|
...
gi 71027907 439 QFG 441
Cdd:PRK09099 392 QVG 394
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
59-435 |
1.99e-42 |
|
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: 157.11 E-value: 1.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 59 VRDVGHVINVGDGIARIYGLKeVKAGELVMFSSGVAGMALnLEtdnigVVIFGDDRNIL----------EGDTVTRTNRI 128
Cdd:COG1157 17 VRVSGRVTRVVGLLIEAVGPD-ASIGELCEIETADGRPVL-AE-----VVGFRGDRVLLmplgdlegisPGARVVPTGRP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 129 LDVPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQReliIGdr--- 205
Cdd:COG1157 90 LSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR---IGifags 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 206 qtGKTalaidTILNQ-------------------RLVNEGLEenkrlyciyvaigqkrstvaRILkileDNDALKYTIVV 266
Cdd:COG1157 167 gvGKS-----TLLGMiarnteadvnvialigergREVREFIE--------------------DDL----GEEGLARSVVV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 267 AATASDPAPLQFLAPFTGCSMGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAkm 346
Cdd:COG1157 218 VATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAG-- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 347 sdTKGSGSLTAL------------PVIETqagdvsayiptnVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQS 414
Cdd:COG1157 296 --NGGKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVS 361
|
410 420
....*....|....*....|.
gi 71027907 415 KAMKQVSGTMKLDLAQFREIQ 435
Cdd:COG1157 362 PEHRALARRLRRLLARYEENE 382
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
59-475 |
4.37e-41 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 153.82 E-value: 4.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 59 VRDVGHVINVGDGIARIyGLKEVKAGELVMFS-SGVAGMALNLETDNIGVVIFGDDRNILEGDTVTRTNRILDVPVGPEL 137
Cdd:PRK06820 27 LRYRGPIVEIGPTLLRA-SLPGVAQGELCRIEpQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 138 LGRVVDALGRPIDGkGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGKTalaidTI 217
Cdd:PRK06820 106 AGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKS-----TL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 218 LNqrLVNEGLEENkrlyCIYVA-IGQKRSTVARILKILEDNDALKYTIVVAATASDPAPLQFLAPFTGCSMGEWFRNNKK 296
Cdd:PRK06820 180 LG--MLCADSAAD----VMVLAlIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 297 HCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAKmSDTkgsGSLTALPVIETQAGDVSAYIPTNV 376
Cdd:PRK06820 254 KVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGN-SDR---GSITAFYTVLVEGDDMNEPVADEV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 377 ISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQSKAMKQVSGTMKLDLAQFREIQAFSQFG---SDLDSSTQQLLT 453
Cdd:PRK06820 330 RSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGeyqAGEDLQADEALQ 409
|
410 420
....*....|....*....|....
gi 71027907 454 RGTLLTELLKQK--QYAPLSIPLQ 475
Cdd:PRK06820 410 RYPAICAFLQQDhsETAHLETTLE 433
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
63-464 |
6.02e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 153.30 E-value: 6.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 63 GHVINVGDGIARIYGLKeVKAGELVMFSSG-----VAGMALNLETDNIGVVIFGDDRNILEGDTVTRTNRILDVPVGPEL 137
Cdd:PRK08472 20 GSITKISPTIIEADGLN-PSVGDIVKIESSdngkeCLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 138 LGRVVDALGRPIDGKGDLVTKETS---RVEVPA--PGIIDrrsvhEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGKTAL 212
Cdd:PRK08472 99 LGRVVDPLGRPIDGKGAIDYERYApimKAPIAAmkRGLID-----EVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 213 aidtilnQRLVNEGLEENKRLyciyVA-IGQK-RSTVARILKILEDNdaLKYTIVVAATASDPAPLQFLAPFTGCSMGEW 290
Cdd:PRK08472 174 -------MGMIVKGCLAPIKV----VAlIGERgREIPEFIEKNLGGD--LENTVIVVATSDDSPLMRKYGAFCAMSVAEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 291 FRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAKmsdTKGSGSLTALPVIETQAGDVSA 370
Cdd:PRK08472 241 FKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTVLVEGDDMSD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 371 YIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQSKAMKQVSGTMKLDLAQFRE------IQAFsQFGSD- 443
Cdd:PRK08472 318 PIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKEnevlirIGAY-QKGNDk 396
|
410 420
....*....|....*....|..
gi 71027907 444 -LDSStqqlLTRGTLLTELLKQ 464
Cdd:PRK08472 397 eLDEA----ISKKEFMEQFLKQ 414
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
81-473 |
9.88e-41 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 152.60 E-value: 9.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 81 VKAGELVMFSSgvAGMALNLETDNIGVV-------IFGDDRNILEGDTVTRTNRILDVPVGPELLGRVVDALGRPIDGKG 153
Cdd:PRK06936 42 VRIGELCYLRN--PDNSLSLQAEVIGFAqhqalltPLGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 154 DLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGKTALaIDTILNQRLVNegleenkrl 233
Cdd:PRK06936 120 PPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTL-LASLIRSAEVD--------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 234 YCIYVAIGQKRSTVARILKILEDNDALKYTIVVAATASDPAPLQFLAPFTGCSMGEWFRNNKKHCVIIYDDLSKQATAYR 313
Cdd:PRK06936 190 VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 314 QMSLLLRRPPGREAYPGDIFYLHSRLLERAAkMSDTkgsGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESELFYK 393
Cdd:PRK06936 270 EIGLAAGEPPTRRGYPPSVFAALPRLMERAG-QSDK---GSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 394 GIRPAINVGLSVSRVGSAAQSKAMKQVSGTMKLDLAQFREIQAFSQFGS---DLDSSTQQLLTRGTLLTELLKQKQYAPL 470
Cdd:PRK06936 346 NHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEyqkGQDKEADQAIERIGAIRGFLRQGTHELS 425
|
...
gi 71027907 471 SIP 473
Cdd:PRK06936 426 HFN 428
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
110-465 |
5.58e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 150.64 E-value: 5.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 110 FGDDRNILEGDTVTRTNRILDVPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDS 189
Cdd:PRK07721 72 YTEVAEIAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 190 LVPIGRGQRELIIGDRQTGKTalaidTILNQRLVNEGLEENkrlycIYVAIGQKRSTVARILKILEDNDALKYTIVVAAT 269
Cdd:PRK07721 152 LLTVGKGQRVGIFAGSGVGKS-----TLMGMIARNTSADLN-----VIALIGERGREVREFIERDLGPEGLKRSIVVVAT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 270 ASDPAPLQFLAPFTGCSMGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAkmsdT 349
Cdd:PRK07721 222 SDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG----T 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 350 KGSGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQSKAMKQVSGTMKLDLA 429
Cdd:PRK07721 298 NASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLS 377
|
330 340 350
....*....|....*....|....*....|....*....
gi 71027907 430 QFREIQAFSQFGSDLDSSTQQL---LTRGTLLTELLKQK 465
Cdd:PRK07721 378 TYQNSEDLINIGAYKRGSSREIdeaIQFYPQIISFLKQG 416
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
60-441 |
1.58e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 140.86 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 60 RDVGHVINVGDGIARIYgLKEVKAGELVMFSSGvAGMA--LNLETDNIGVVIFGDDRNILEGDTVTRTNRILDVPVGPEL 137
Cdd:PRK07594 20 CRWGRIQDVSATLLNAW-LPGVFMGELCCIKPG-EELAevVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 138 LGRVVDALGRPIDGKGD--LVTKEtsrVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGKTalaid 215
Cdd:PRK07594 98 LGRVIDGFGRPLDGRELpdVCWKD---YDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKS----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 216 TILNQRLVNEGLEENkrlycIYVAIGQKRSTVARILKILEDNDALKYTIVVAATASDPAPLQFLAPFTGCSMGEWFRNNK 295
Cdd:PRK07594 170 TLLAMLCNAPDADSN-----VLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 296 KHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAkMSDTkgsGSLTALPVIETQAGDVSAYIPTN 375
Cdd:PRK07594 245 KRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-MGEK---GSITAFYTVLVEGDDMNEPLADE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71027907 376 VISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQSKAMKQVSGTMKLDLAQFREIQAFSQFG 441
Cdd:PRK07594 321 VRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIG 386
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
107-443 |
5.10e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 139.45 E-value: 5.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 107 VVIFGDD----------RNILEGDTVTRTNRILDVPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSV 176
Cdd:PRK08972 63 VVGFDGDllylmpieelRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 177 HEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGKTAL--------AIDTIL------NQRLVNEGLEEnkrlycIYVAIGQ 242
Cdd:PRK08972 143 TEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLlgmmtrgtTADVIVvglvgeRGREVKEFIEE------ILGEEGR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 243 KRStvarilkiledndalkytIVVAATAsDPAPLQFL-APFTGCSMGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRR 321
Cdd:PRK08972 217 ARS------------------VVVAAPA-DTSPLMRLkGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 322 PPGREAYPGDIFYLHSRLLERAAKMSDtkGSGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINV 401
Cdd:PRK08972 278 PPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDI 355
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 71027907 402 GLSVSRVGSAAQSKAMKQVSGTMKLDLAQFRE------IQAFSQfGSD 443
Cdd:PRK08972 356 EASISRVMPMVISEEHLEAMRRVKQVYSLYQQnrdlisIGAYKQ-GSD 402
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
131-446 |
2.53e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 132.16 E-value: 2.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 131 VPVGPELLGRVVDALGRPIDGKGDLvtKETSRVEVPAPGI--IDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTG 208
Cdd:PRK05688 103 LPMGMSMLGRVLDGAGRALDGKGPM--KAEDWVPMDGPTInpLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 209 KTAL--AIDTILNQRLVNEGLeenkrlyciyvaIGQKRSTVARILKILEDNDALKYTIVVAATASDpAPLQFLAPFTGCS 286
Cdd:PRK05688 181 KSVLlgMMTRFTEADIIVVGL------------IGERGREVKEFIEHILGEEGLKRSVVVASPADD-APLMRLRAAMYCT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 287 -MGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAkmSDTKGSGSLTALPVIETQA 365
Cdd:PRK05688 248 rIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 366 GDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVgsaaqskaMKQVSGTMKLDLAQ-FREIQAFSQFGSDL 444
Cdd:PRK05688 326 DDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV--------MPQVVDPEHLRRAQrFKQLWSRYQQSRDL 397
|
..
gi 71027907 445 DS 446
Cdd:PRK05688 398 IS 399
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
54-471 |
3.10e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 131.66 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 54 DSQKDVRDVGHVINVGDGIARIYGL-KEVKAGELVMFSSG---VAGMALNLETDNIGVVIFGDDRNILEGDTVTRTNRiL 129
Cdd:PRK06002 19 APEPLVRIGGTVSEVTASHYRVRGLsRFVRLGDFVAIRADggtHLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGP-L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 130 DVPVGPELLGRVVDALGRPIDGKGDLVTKETSR-VEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTG 208
Cdd:PRK06002 98 RIRPDPSWKGRVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 209 KTAL--------AIDTIL------NQRLVNEGLEEnkrlyciyvaigqkrsTVArilkilednDALKYTIVVAATaSDPA 274
Cdd:PRK06002 178 KSTLlamlaradAFDTVVialvgeRGREVREFLED----------------TLA---------DNLKKAVAVVAT-SDES 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 275 P-LQFLAPFTGCSMGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAkmSDTKGSG 353
Cdd:PRK06002 232 PmMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAG--PGAEGGG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 354 SLTALPVIETQAGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQSKAMKQVSGTMKLDLAQFRE 433
Cdd:PRK06002 310 SITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEE 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 71027907 434 ------IQAFsQFGSD--LDSSTQQLltrgTLLTELLKQKQYAPLS 471
Cdd:PRK06002 390 trdlrlIGGY-RAGSDpdLDQAVDLV----PRIYEALRQSPGDPPS 430
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
74-441 |
5.64e-31 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 125.11 E-value: 5.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 74 RIYG------LKEVKAGELV-----MFSSGVAGMALnletdnigVVIFGDDRNILE--GDTV--TR------TNRILDVP 132
Cdd:PRK08149 12 RIQGpiieaeLPDVAIGEICeiragWHSNEVIARAQ--------VVGFQRERTILSliGNAQglSRqvvlkpTGKPLSVW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 133 VGPELLGRVVDALGRPIDGKGDLVTKETSR----VEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTG 208
Cdd:PRK08149 84 VGEALLGAVLDPTGKIVERFDAPPTVGPISeervIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 209 KTALaidtiLNQrLVNEGLEEnkrlycIYVA--IGQKRSTVARILKILEDNDALKYTIVVAATASDPAPLQFLAPFTGCS 286
Cdd:PRK08149 164 KTSL-----MNM-LIEHSEAD------VFVIglIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 287 MGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAKMSdtkgSGSLTALPVIETQAG 366
Cdd:PRK08149 232 VAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATL----AGSITAFYTVLLESE 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71027907 367 DVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQSKAMKQVSGTMKLDLAQFREIQAFSQFG 441
Cdd:PRK08149 308 EEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLG 382
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
128-407 |
6.83e-31 |
|
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: 121.56 E-value: 6.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 128 ILDVPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQT 207
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 208 GKTALAIDTILNQRLVNEglEENKRLycIYVAIGQKRSTVARILKILEDNDALKYTIVVAATASDPAPLQFLAPFTGCSM 287
Cdd:cd01135 81 PHNELAAQIARQAGVVGS--EENFAI--VFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 288 GEWFRNNK-KHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGdifYLHSRL---LERAAKMSDTKGSgsLTALPVIET 363
Cdd:cd01135 157 AEYLAYEKgKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGRKGS--ITQIPILTM 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 71027907 364 QAGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSR 407
Cdd:cd01135 232 PNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
61-127 |
2.45e-29 |
|
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: 110.24 E-value: 2.45e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71027907 61 DVGHVINVGDGIARIYGLKEVKAGELVMFSSGVAGMALNLETDNIGVVIFGDDRNILEGDTVTRTNR 127
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
133-464 |
8.92e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 115.76 E-value: 8.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 133 VGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGKTAL 212
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 213 --AIDTILNQRLVNEGLeenkrlyciyvaIGQKRSTVARILKILEDNDALKYTIVVAATAsDPAPLQFLAPFTGC-SMGE 289
Cdd:PRK07196 172 lgMITRYTQADVVVVGL------------IGERGREVKEFIEHSLQAAGMAKSVVVAAPA-DESPLMRIKATELChAIAT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 290 WFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAkmsDTKGSGSLTALPVIETQAGDVS 369
Cdd:PRK07196 239 YYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQ 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 370 AYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSR----VGSAAQSKAMKQVSGtMKLDLAQFREIQAFSQFGSDLD 445
Cdd:PRK07196 316 DPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQ-CYADYMAIKPLIPLGGYVAGAD 394
|
330
....*....|....*....
gi 71027907 446 SSTQQLLTRGTLLTELLKQ 464
Cdd:PRK07196 395 PMADQAVHYYPAITQFLRQ 413
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
57-408 |
2.00e-27 |
|
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: 115.20 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 57 KDVRDVGHVINV---GDGIARIYGLKEVK---AGELVMfssgvaGMALNLETDNIGVVIFGDDRNILEGDTVTRTNRILD 130
Cdd:TIGR01039 4 KVVQVIGPVVDVefeQGELPRIYNALKVQnraESELTL------EVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 131 VPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGKT 210
Cdd:TIGR01039 78 VPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 211 ALAIDTILNQRLVNEGleenkrlYCIYVAIGQKRSTVARILKILEDNDALKYTIVVAATASDPAPLQFLAPFTGCSMGEW 290
Cdd:TIGR01039 158 VLIQELINNIAKEHGG-------YSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 291 FRNNKKHCVIIY-DDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERaakMSDTKGsGSLTALPVIETQAGDVS 369
Cdd:TIGR01039 231 FRDEQGQDVLLFiDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQER---ITSTKT-GSITSVQAVYVPADDLT 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 71027907 370 AYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRV 408
Cdd:TIGR01039 307 DPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRL 345
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
131-439 |
2.91e-26 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 111.80 E-value: 2.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 131 VPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGKT 210
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKS 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 211 AL--------AIDTILnqrlvnEGLeenkrlyciyvaIGQKRSTVARILKILEDNDALKYTIVVAATAsDPAPL---QFL 279
Cdd:PRK07960 190 VLlgmmarytQADVIV------VGL------------IGERGREVKDFIENILGAEGRARSVVIAAPA-DVSPLlrmQGA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 280 APFTgcSMGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAKMSDtkGSGSLTALP 359
Cdd:PRK07960 251 AYAT--RIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFY 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 360 VIETQAGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRvgsaaqskAMkqvsgTMKLDLAQFREIQAFSQ 439
Cdd:PRK07960 327 TVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISR--------AM-----TALIDEQHYARVRQFKQ 393
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
80-442 |
4.39e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 110.84 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 80 EVKAGELVMF-SSGVAGMALNLETDNIGVVIFGDDRNILEGDTVTRTNRILDVPVGPELLGRVVDALGRPIDGKGDLVTK 158
Cdd:PRK06793 39 KAKIGDVCFVgEHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 159 ETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGKTalaidTILNQRLVNEGLEENkrlycIYV 238
Cdd:PRK06793 119 QKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKS-----TLLGMIAKNAKADIN-----VIS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 239 AIGQKRSTVARILKILEDNDALKYTIVVAATASDPAPLQFLAPFTGCSMGEWFRNNKKHCVIIYDDLSKQATAYRQMSLL 318
Cdd:PRK06793 189 LVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 319 LRRPPgreaYPGDIFYLHS---RLLERAAKMSdtkgSGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESELFYKGI 395
Cdd:PRK06793 269 VKELP----IGGKTLLMESymkKLLERSGKTQ----KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSH 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 71027907 396 RPAINVGLSVSRVGSAAQSKAMKQVSGTMKLDLAQFREIQAFSQFGS 442
Cdd:PRK06793 341 YPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGT 387
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
64-407 |
1.25e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 109.68 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 64 HVINVGDGIARIYGLKEVKAGELVMFSSGVAgmalnletdnigVVI-FGDdrniLEGdtVTRTNRILDVPVGPEL----- 137
Cdd:PRK08927 36 HALSVGARIVVETRGGRPVPCEVVGFRGDRA------------LLMpFGP----LEG--VRRGCRAVIANAAAAVrpsra 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 138 -LGRVVDALGRPIDGKGDLVTKETSR-VEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGKTAL--- 212
Cdd:PRK08927 98 wLGRVVNALGEPIDGKGPLPQGPVPYpLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLlsm 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 213 -----AIDTILnqrlvnEGLeenkrlyciyvaIGQKRSTVArilKILEDN---DALKYTIVVAATASDPAPLQFLAPFTG 284
Cdd:PRK08927 178 larnaDADVSV------IGL------------IGERGREVQ---EFLQDDlgpEGLARSVVVVATSDEPALMRRQAAYLT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 285 CSMGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAkmSDTKGSGSLTALPVIETQ 364
Cdd:PRK08927 237 LAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVD 314
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 71027907 365 AGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSR 407
Cdd:PRK08927 315 GDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSR 357
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
77-407 |
2.02e-25 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 109.15 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 77 GLKEVKAGELVMFSSG----VAGMALNLETDNIGVVIFGDDRNI-LEGDTVTRTNRILDVPVGPELLGRVVDALGRPIDG 151
Cdd:PRK04196 19 GVEGVAYGEIVEIELPngekRRGQVLEVSEDKAVVQVFEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 152 KGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQReLII--GdrqTGKTA--LAIDtILNQRLVnegL 227
Cdd:PRK04196 99 GPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQK-LPIfsG---SGLPHneLAAQ-IARQAKV---L 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 228 EENKRLYCIYVAIGQKRSTVARILKILEDNDALKYTIVVAATASDPAPLQFLAPFTGCSMGEWFRNNK-KHCVIIYDDLS 306
Cdd:PRK04196 171 GEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFEKgMHVLVILTDMT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 307 KQATAYRQMSLLLRRPPGREAYPGdifYLHSRL---LERAAKMSDTKGSgsLTALPVIETQAGDVSAYIPTNVISITDGQ 383
Cdd:PRK04196 251 NYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGKKGS--ITQIPILTMPDDDITHPIPDLTGYITEGQ 325
|
330 340
....*....|....*....|....
gi 71027907 384 IFLESELFYKGIRPAINVGLSVSR 407
Cdd:PRK04196 326 IVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
121-436 |
1.17e-22 |
|
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: 100.95 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 121 TVTRTNRILDVPVGPELLGRVVDALGRPIDgKGDLVTKETSRVEVPAPGIIDRRSVHEPM-TTGMKCVDSLVPIGRGQRE 199
Cdd:TIGR01040 66 TCEFTGDILRTPVSEDMLGRVFNGSGKPID-KGPPVLAEDYLDINGQPINPYARIYPEEMiQTGISAIDVMNSIARGQKI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 200 LIIGD-------------RQTGKTALAidtilnQRLVNEGLEENkrlYCI-YVAIGQKRSTvARILKI-LEDNDALKYTI 264
Cdd:TIGR01040 145 PIFSAaglphneiaaqicRQAGLVKLP------TKDVHDGHEDN---FAIvFAAMGVNMET-ARFFKQdFEENGSMERVC 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 265 VVAATASDPAPLQFLAPFTGCSMGEWFRNNK-KHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERA 343
Cdd:TIGR01040 215 LFLNLANDPTIERIITPRLALTTAEYLAYQCeKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 344 AKMSDTKGSgsLTALPVIETQAGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRVGSAAQSKAMKQ---- 419
Cdd:TIGR01040 295 GRVEGRNGS--ITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRkdhs 372
|
330
....*....|....*...
gi 71027907 420 -VSGTMKLDLAQFREIQA 436
Cdd:TIGR01040 373 dVSNQLYACYAIGKDVQA 390
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
119-407 |
1.69e-22 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 99.98 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 119 GDTVTRTNRILDVPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQR 198
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 199 ELIIGDRQTGKTALaIDTIL--NQRLVNegleenkrlycIYVAIGQKRSTVARILKILEDNDALKYTIVVAATASDPAPL 276
Cdd:PRK05922 160 IGVFSEPGSGKSSL-LSTIAkgSKSTIN-----------VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 277 QFLAPFTGCSMGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERAAkmsdTKGSGSLT 356
Cdd:PRK05922 228 KVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG----NNDKGSIT 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 71027907 357 ALPVIETQAGDVSAYIPTnVISITDGQIFLESElfYKGI-RPAINVGLSVSR 407
Cdd:PRK05922 304 ALYAILHYPNHPDIFTDY-LKSLLDGHFFLTPQ--GKALaSPPIDILTSLSR 352
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
131-408 |
2.96e-19 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 88.05 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 131 VPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGQRELIIGDRQTGKT 210
Cdd:cd01133 2 VPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 211 ALAIDTILNQRLVNEGleenkrlYCIYVAIGQ------------KRSTVArilkileDNDALKYTIVVAATASDPAPLQF 278
Cdd:cd01133 82 VLIMELINNIAKAHGG-------YSVFAGVGErtregndlyhemKESGVI-------NLDGLSKVALVYGQMNEPPGARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 279 LAPFTGCSMGEWFRNNKKHCVIIY-DDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLERaakMSDTKGsGSLTA 357
Cdd:cd01133 148 RVALTGLTMAEYFRDEEGQDVLLFiDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQER---ITSTKK-GSITS 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 71027907 358 LPVIETQAGDVSAYIPTNVISITDGQIFLESELFYKGIRPAINVGLSVSRV 408
Cdd:cd01133 224 VQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
129-407 |
3.87e-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: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 129 LDVPVGPELLGRVVDALGRPID----------GKGdlVTKETSRVEVPAPgIIDRRSVHEPMTTGMKCVDSLVPIGRGQR 198
Cdd:cd01134 2 LSVELGPGLLGSIFDGIQRPLEviaetgsifiPRG--VNVQRWPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 199 ELIIGDRQTGKTAL--AIDTILNQRLVnegleenkrlycIYVAIGQKRSTVARILK---ILED----NDALKYTIVVAAT 269
Cdd:cd01134 79 AAIPGPFGCGKTVIsqSLSKWSNSDVV------------IYVGCGERGNEMAEVLEefpELKDpitgESLMERTVLIANT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 270 ASDPAPLQFLAPFTGCSMGEWFRNNKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGdifYLHSRL---LERAAKM 346
Cdd:cd01134 147 SNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYERAGRV 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71027907 347 SdTKGS----GSLTALPVIETQAGDVSAYIPTNVISITdgQIF--LESELFYKGIRPAINVGLSVSR 407
Cdd:cd01134 224 R-CLGSpgreGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
81-386 |
4.15e-19 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 89.71 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 81 VKAGELVMFSS---GVAGMALNLETDNIGVVIFGDDRNILEGDTVTRTNRILDVPVGPELLGRVVDALGRPIDG----KG 153
Cdd:PRK02118 23 VGYGELATVERkdgSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGgpelEG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 154 DLVTKETSRVEvPAPGIIDRRSVHepmtTGMKCVD---SLVpigRGQRELIIGDRqtgktalaiDTILNQRLVNEGLEEN 230
Cdd:PRK02118 103 EPIEIGGPSVN-PVKRIVPREMIR----TGIPMIDvfnTLV---ESQKIPIFSVS---------GEPYNALLARIALQAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 231 KRLyCIYVAIGQKRSTVARILKILEDNDALKYTIVVAATASDPAPLQFLAPFTGCSMGEWFR-NNKKHCVIIYDDLSKQA 309
Cdd:PRK02118 166 ADI-IILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFA 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71027907 310 TAYRQMSLLLRRPPGREAYPGDifyLHSRLLERAAKMSDTKGSGSLTALPVIETQAGDVSAYIPTNVISITDGQIFL 386
Cdd:PRK02118 245 DALKEISITMDQIPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
119-212 |
6.07e-16 |
|
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: 80.13 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 119 GDTVTRTNRILDVPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIIDRRSVHEPMTTGMKCVDSLVPIGRGqr 198
Cdd:COG0055 69 GMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKG-- 146
|
90
....*....|....
gi 71027907 199 eliigdrqtGKTAL 212
Cdd:COG0055 147 ---------GKIGL 151
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
417-484 |
1.27e-14 |
|
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: 68.62 E-value: 1.27e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 417 MKQVSGTMKLDLAQFREIQAFSQFGSDLDSS--TQQLLTRGTLLTELLKQKQYAPLSIPLQICVIYGGVN 484
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSeaDKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
59-126 |
5.04e-14 |
|
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: 66.80 E-value: 5.04e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71027907 59 VRDVGHVINVGDGIARIYGLKEVKAGELVMFSSGVAGMALNLETDNIGVVIFGDDRNILEGDTVTRTN 126
Cdd:pfam02874 2 VQVIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
116-400 |
8.37e-13 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 70.45 E-value: 8.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 116 ILEGDTVTRTNRILDVPVGPELLGRVVDALGRPIDGKGDLVTKETSRVEVPAPGIID---RRSVHEpmtTGMKCVDSLVP 192
Cdd:CHL00060 81 LMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQldtKLSIFE---TGIKVVDLLAP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 193 IGRGQRELIIGDRQTGKTALAIDTILNQRL----------VNEGLEENKRLYciyvaIGQKRSTVARILKILEDNDALKY 262
Cdd:CHL00060 158 YRRGGKIGLFGGAGVGKTVLIMELINNIAKahggvsvfggVGERTREGNDLY-----MEMKESGVINEQNIAESKVALVY 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 263 tivvaATASDPAPLQFLAPFTGCSMGEWFRN-NKKHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDIFYLHSRLLE 341
Cdd:CHL00060 233 -----GQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQE 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 71027907 342 RAAKMSDtkgsGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESELFYKGIRPAIN 400
Cdd:CHL00060 308 RITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 362
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
236-420 |
6.95e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 61.96 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 236 IYVAIGQKRSTVARILK---ILEDNDA----LKYTIVVAATASDPAPLQFLAPFTGCSMGEWFRNNKKHCVIIYDDLSKQ 308
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEefpKLKDPKTgkplMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71027907 309 ATAYRQMSLLLRRPPGREAYPGdifYLHSRL---LERAAKMSdTKGS----GSLTALPVIETQAGDVSAYIPTNVISITD 381
Cdd:PRK14698 766 AEALREISGRLEEMPGEEGYPA---YLASKLaefYERAGRVV-TLGSdyrvGSVSVIGAVSPPGGDFSEPVVQNTLRVVK 841
|
170 180 190
....*....|....*....|....*....|....*....
gi 71027907 382 GQIFLESELFYKGIRPAINVGLSVSRVGSAAQSKAMKQV 420
Cdd:PRK14698 842 VFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNV 880
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
63-127 |
3.88e-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: 39.22 E-value: 3.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71027907 63 GHVINVGDGIARIYGLKEVKAGELVMF-----SSGVAGMA--LNLETDNIGVVIFGDDRNILEGDTVTRTNR 127
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIGEVCEIergdgNNETVLKAevIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
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