|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
30-536 |
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: 997.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 30 KAAPTEVPSILEERIRGAYNQAQMMESGRVLSIGDGIARISGLSNVQAEELVEFSSGIKGMALNLEADTVGCVLFGNDRL 109
Cdd:COG0056 2 QIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 110 VREGEVVKRTRHIVDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGR 189
Cdd:COG0056 82 IKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 190 GQRELIIGDRQTGKTAIALDTILNHKrwnnssdeSKKLYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAP 269
Cdd:COG0056 162 GQRELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 270 LQYLAPFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPKHGGGSL 349
Cdd:COG0056 234 LQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 350 TALPVIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVA 429
Cdd:COG0056 314 TALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 430 SFAQFGSDLDAGTRATLDRGLRLTELLKQPQYSPLAVEEQVPLIYCGVKGYLDKIPVDRVVEFEHKFIPYLRSSGAEIME 509
Cdd:COG0056 394 AFAQFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLK 473
|
490 500
....*....|....*....|....*..
gi 19115831 510 AIRKEGVLSKTTEDSLKAVIKEFLSSF 536
Cdd:COG0056 474 EIRETGKLDDEIEEKLKAAIEEFKKTF 500
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
33-536 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 993.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 33 PTEVPSILEERIRGAYNQAQMMESGRVLSIGDGIARISGLSNVQAEELVEFSSGIKGMALNLEADTVGCVLFGNDRLVRE 112
Cdd:PRK09281 5 PEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 113 GEVVKRTRHIVDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQR 192
Cdd:PRK09281 85 GDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 193 ELIIGDRQTGKTAIALDTILNHKrwnnssdeSKKLYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQY 272
Cdd:PRK09281 165 ELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 273 LAPFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPKHGGGSLTAL 352
Cdd:PRK09281 237 LAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 353 PVIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVASFA 432
Cdd:PRK09281 317 PIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 433 QFGSDLDAGTRATLDRGLRLTELLKQPQYSPLAVEEQVPLIYCGVKGYLDKIPVDRVVEFEHKFIPYLRSSGAEIMEAIR 512
Cdd:PRK09281 397 QFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIR 476
|
490 500
....*....|....*....|....
gi 19115831 513 KEGVLSKTTEDSLKAVIKEFLSSF 536
Cdd:PRK09281 477 ETKDLSDEIEAKLKAAIEEFKKTF 500
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
33-536 |
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: 831.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 33 PTEVPSILEERIRGAYNQAQMMESGRVLSIGDGIARISGLSNVQAEELVEFSSGIKGMALNLEADTVGCVLFGNDRLVRE 112
Cdd:TIGR00962 4 LEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 113 GEVVKRTRHIVDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQR 192
Cdd:TIGR00962 84 GSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 193 ELIIGDRQTGKTAIALDTILNHKrwnnssdeSKKLYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQY 272
Cdd:TIGR00962 164 ELIIGDRQTGKTAVAIDTIINQK--------DSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 273 LAPFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPKHGGGSLTAL 352
Cdd:TIGR00962 236 LAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 353 PVIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVASFA 432
Cdd:TIGR00962 316 PIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 433 QFGSDLDAGTRATLDRGLRLTELLKQPQYSPLAVEEQVPLIYCGVKGYLDKIPVDRVVEFEHKFIPYLRSSGAEIMEAIR 512
Cdd:TIGR00962 396 QFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEIN 475
|
490 500
....*....|....*....|....
gi 19115831 513 KEGVLSKTTEDSLKAVIKEFLSSF 536
Cdd:TIGR00962 476 TTKKLTEELEAKLKEALKNFKKTF 499
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
57-536 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 776.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 57 GRVLSIGDGIARISGLSNVQAEELVEFSSGIKGMALNLEADTVGCVLFGNDRLVREGEVVKRTRHIVDVPVGEALLGRVV 136
Cdd:CHL00059 8 GTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 137 DALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTGKTAIALDTILNHKr 216
Cdd:CHL00059 88 NALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQK- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 217 wnnssdeSKKLYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQYLAPFSGCAMGEWFRDNGKHGLVVY 296
Cdd:CHL00059 167 -------GQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 297 DDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPKHGGGSLTALPVIETQGGDVSAYIPTNVISITDG 376
Cdd:CHL00059 240 DDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 377 QIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVASFAQFGSDLDAGTRATLDRGLRLTELL 456
Cdd:CHL00059 320 QIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 457 KQPQYSPLAVEEQVPLIYCGVKGYLDKIPVDRVVEFEHKFIPYLRSSGAEIMEAIRKEGVLSKTTEDSLKAVIKEFLSSF 536
Cdd:CHL00059 400 KQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQLELF 479
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
35-536 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 745.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 35 EVPSILEERIRGAYNQAQMMESGRVLSIGDGIARISGLSNVQAEELVEFSSGIKGMALNLEADTVGCVLFGNDRLVREGE 114
Cdd:PRK13343 7 EWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILAGT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 115 VVKRTRHIVDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQREL 194
Cdd:PRK13343 87 EVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQREL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 195 IIGDRQTGKTAIALDTILNHKrwnnssdeSKKLYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQYLA 274
Cdd:PRK13343 167 IIGDRQTGKTAIAIDAIINQK--------DSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 275 PFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPKHGGGSLTALPV 354
Cdd:PRK13343 239 PFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 355 IETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVASFAQF 434
Cdd:PRK13343 319 IETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 435 GSDLDAGTRATLDRGLRLTELLKQPQYSPLAVEEQVPLIYCGVKGYLDKIPVDRVVEFEHKFIPYLRSSGAEIMEAIRKE 514
Cdd:PRK13343 399 GGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESP 478
|
490 500
....*....|....*....|..
gi 19115831 515 GVLSKTTEDSLKAVIKEFLSSF 536
Cdd:PRK13343 479 RELDEAWLAALEEILREAGERF 500
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
122-403 |
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: 608.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 122 IVDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQT 201
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 202 GKTAIALDTILNHKRwnnssdesKKLYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQYLAPFSGCAM 281
Cdd:cd01132 81 GKTAIAIDTIINQKG--------KKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 282 GEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPKHGGGSLTALPVIETQGGD 361
Cdd:cd01132 153 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 19115831 362 VSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVG 403
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
40-519 |
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: 533.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 40 LEERIRGAYNQAQMMESGRVLSIGDGIARISGLSNVQAEELVEFSSGIKGMALNLEADTVGCVLFGNDRLVREGEVVKRT 119
Cdd:TIGR03324 12 LDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 120 RHIVDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDR 199
Cdd:TIGR03324 92 GRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 200 QTGKTAIALDTILNHKRWNnssdeskkLYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQYLAPFSGC 279
Cdd:TIGR03324 172 QTGKTAIAIDTILNQKGRN--------VLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 280 AMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPKHGGGSLTALPVIETQG 359
Cdd:TIGR03324 244 SIGEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 360 GDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVASFAQFGSDLD 439
Cdd:TIGR03324 324 QNISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 440 AGTRATLDRGLRLTELLKQPQYSPLAVEEQVPLIYCGVKGYLDKIPVDRVVEFEHKFIPYLRSSGAEIMEAIRKEGVLSK 519
Cdd:TIGR03324 404 ENTRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSD 483
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
124-402 |
3.19e-124 |
|
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: 364.85 E-value: 3.19e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 124 DVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTGK 203
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 204 TAIALDTILNhkrwnnsSDESKKLYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQYLAPFSGCAMGE 283
Cdd:cd19476 81 TVLAMQLARN-------QAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 284 WFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMspKHGGGSLTALPVIETQGGDVS 363
Cdd:cd19476 154 YFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKV--KDGGGSITAIPAVSTPGDDLT 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 19115831 364 AYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRV 402
Cdd:cd19476 232 DPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
89-497 |
1.43e-123 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 374.38 E-value: 1.43e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 89 GMALNLEAD-TVGCVLFGNDRLVREGEVVKRTRHIVDVPVGEALLGRVVDALGNPIdgkgPIKTTERRRVQLK------- 160
Cdd:PTZ00185 80 GLVFNLEKDgRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEV----PVGLLTRSRALLEseqtlgk 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 161 ----APGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTGKTAIALDTILNHKRWNNSSDESKKLYCVYVAVGQ 236
Cdd:PTZ00185 156 vdagAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVISIYVSIGQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 237 KRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQYLAPFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRP 316
Cdd:PTZ00185 236 RCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 317 PGREAYPGDVFYLHSRLLERAAKMSPKHGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVG 396
Cdd:PTZ00185 316 PGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 397 LSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVASFAQFGSDLDAgtrATLDRGLRLTELLKQPQysPLAVEEQVPLIYCG 476
Cdd:PTZ00185 396 LSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQT---VPMIRGARFVALFNQKN--PSFFMNALVSLYAC 470
|
410 420
....*....|....*....|.
gi 19115831 477 VKGYLDKIPVDRVVEFEHKFI 497
Cdd:PTZ00185 471 LNGYLDDVKVNYAKLYEYLLV 491
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
177-400 |
1.96e-114 |
|
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: 337.41 E-value: 1.96e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 177 GLKAIDSMVPIGRGQRELIIGDRQTGKTAIAlDTILNHkrwnnssdeSKKLYCVYVAVGQKRSTVAQLVQKLEENDSLKY 256
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQ---------ASADVVVYALIGERGREVREFIEELLGSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 257 SIIVAATASESAPLQYLAPFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLER 336
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115831 337 AAKMSPKhgGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVS 400
Cdd:pfam00006 151 AGRVKGK--GGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
58-463 |
6.98e-98 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 305.74 E-value: 6.98e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 58 RVLSIGDGIARISGLSNVQAEELVEFSS--GIKGMALNLEADTVGCVLFGNDRLVREGEVVKRTRHIVDVPVGEALLGRV 135
Cdd:PRK07165 4 KIKSIFDYIVEVKGEYDYQQNQFFTLKNnpNVKAFVISATEDKAYLLINNEKGKIKINDELIELNNTNKVKTSKEYFGKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 136 VDALGNPIDGKGPIKTTERRRVQL-----KAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTGKTAIALDT 210
Cdd:PRK07165 84 IDIDGNIIYPEAQNPLSKKFLPNTssifnLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 211 ILNHKRWNnssdeskkLYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAAtASESAPLQYLAPFSGCAMGEwfrdNGK 290
Cdd:PRK07165 164 IINQKNTN--------VKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAE----NIS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 291 HG---LVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPKHgggSLTALPVIETQGGDVSAYIP 367
Cdd:PRK07165 231 YNddvLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNRK---TITALPILQTVDNDITSLIS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 368 TNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQI-KLFLAqYREVASFAQFGSDLDAGTRATL 446
Cdd:PRK07165 308 SNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEIsKIYRA-YKRQLKLSMLDYDLNKETSDLL 386
|
410
....*....|....*..
gi 19115831 447 DRGLRLTELLKQPQYSP 463
Cdd:PRK07165 387 FKGKMIEKMFNQKGFSL 403
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
411-536 |
5.60e-67 |
|
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: 212.23 E-value: 5.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 411 MKQVAGQIKLFLAQYREVASFAQFGSDLDAGTRATLDRGLRLTELLKQPQYSPLAVEEQVPLIYCGVKGYLDKIPVDRVV 490
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 19115831 491 EFEHKFIPYLRSSGAEIMEAIRKEGVLSKTTEDSLKAVIKEFLSSF 536
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
407-532 |
5.43e-66 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 209.61 E-value: 5.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 407 QVKAMKQVAGQIKLFLAQYREVASFAQFGSDLDAGTRATLDRGLRLTELLKQPQYSPLAVEEQVPLIYCGVKGYLDKIPV 486
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 19115831 487 DRVVEFEHKFIPYLRSSGAEIMEAIRKEGVLSKTTEDSLKAVIKEF 532
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
125-402 |
1.17e-51 |
|
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: 176.98 E-value: 1.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 125 VPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTGKT 204
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 205 aialdTILNHKRWNNSSDESkklycVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQYLAPFSGCAMGEW 284
Cdd:cd01136 82 -----TLLGMIARNTDADVN-----VIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 285 FRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMSPKhggGSLTALPVIETQGGDVSA 364
Cdd:cd01136 152 FRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAG-NGEK---GSITAFYTVLVEGDDFND 227
|
250 260 270
....*....|....*....|....*....|....*...
gi 19115831 365 YIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRV 402
Cdd:cd01136 228 PIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
56-468 |
1.97e-49 |
|
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: 175.99 E-value: 1.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 56 SGRVLSIGDGIARISGLsNVQAEELVEFSSG----IKGMALNLEADTVGCVLFGNDRLVREGEVVKRTRHIVDVPVGEAL 131
Cdd:COG1157 20 SGRVTRVVGLLIEAVGP-DASIGELCEIETAdgrpVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 132 LGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQReliIGdr---qtGKT---- 204
Cdd:COG1157 99 LGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR---IGifagsgvGKStllg 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 205 AIAldtilnhkRwNNSSDeskklycvyVAVgqkrstVAqLV------------QKLEEnDSLKYSIIVAATASESAPLQY 272
Cdd:COG1157 176 MIA--------R-NTEAD---------VNV------IA-LIgergrevrefieDDLGE-EGLARSVVVVATSDEPPLMRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 273 LAPFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMspkhGGGSLTAL 352
Cdd:COG1157 230 RAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNG----GKGSITAF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 353 PVIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVAsfa 432
Cdd:COG1157 306 YTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENE--- 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 19115831 433 qfgsDL------DAGTRATLDRGLR----LTELLKQPQYSPLAVEE 468
Cdd:COG1157 383 ----DLirigayQPGSDPELDEAIAlipaIEAFLRQGMDERVSFEE 424
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
40-463 |
2.83e-46 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 167.64 E-value: 2.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 40 LEERIRGAynqAQMMESGRVLSIGDGIARISGLsNVQAEELVEFSSGiKGmALNLEADTVGcvlFGNDRLV-----REGE 114
Cdd:PRK09099 12 LERELAAL---PAVRRTGKVVEVIGTLLRVSGL-DVTLGELCELRQR-DG-TLLQRAEVVG---FSRDVALlspfgELGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 115 VVKRTRHI-----VDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGR 189
Cdd:PRK09099 83 LSRGTRVIglgrpLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 190 GQRELIIGDRQTGKTaialdTILNHKRWNNSSDESkklycVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAP 269
Cdd:PRK09099 163 GQRMGIFAPAGVGKS-----TLMGMFARGTQCDVN-----VIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 270 LQYLAPFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMSPKhggGSL 349
Cdd:PRK09099 233 ERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-MGET---GSI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 350 TALPVIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVA 429
Cdd:PRK09099 309 TALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVE 388
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 19115831 430 SFAQFGsDLDAGTRATLDRGLR----LTELLKQP--QYSP 463
Cdd:PRK09099 389 TLLQVG-EYRAGSDPVADEAIAkidaIRDFLSQRtdEYSD 427
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
57-435 |
1.34e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 163.06 E-value: 1.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 57 GRVLSIGDGIARISgLSNVQAEELVEFS-SGIKGMALNLEADTVGCVLFGNDRLVREGEVVKRTRHIVDVPVGEALLGRV 135
Cdd:PRK06820 31 GPIVEIGPTLLRAS-LPGVAQGELCRIEpQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 136 VDALGNPIDGkGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTGKTAIaLDTILNHk 215
Cdd:PRK06820 110 LDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTL-LGMLCAD- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 216 rwnnssdeSKKLYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATaSESAPLQYL-APFSGCAMGEWFRDNGKHGLV 294
Cdd:PRK06820 187 --------SAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVAT-SDRPALERLkGLSTATTIAEYFRDRGKKVLL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 295 VYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPkhggGSLTALPVIETQGGDVSAYIPTNVISIT 374
Cdd:PRK06820 258 MADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDR----GSITAFYTVLVEGDDMNEPVADEVRSLL 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115831 375 DGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVASFAQFG 435
Cdd:PRK06820 334 DGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVG 394
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
61-427 |
2.83e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 159.47 E-value: 2.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 61 SIGDgIARIsglsnvqaeELVEFSSGIKGMALNLEADTVGCVLFGNDRLVREGEVVKRTRHIVDVPVGEALLGRVVDALG 140
Cdd:PRK08472 38 SVGD-IVKI---------ESSDNGKECLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 141 NPIDGKGPIKTTERRRVqLKAP-GILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTGKTAIaLDTILNhkrwnN 219
Cdd:PRK08472 108 RPIDGKGAIDYERYAPI-MKAPiAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTL-MGMIVK-----G 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 220 SSDESKklycVYVAVGQKRSTVAQLVQKlEENDSLKYSIIVAATASESAPLQYLAPFSGCAMGEWFRDNGKHGLVVYDDL 299
Cdd:PRK08472 181 CLAPIK----VVALIGERGREIPEFIEK-NLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 300 SKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmspKHGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIF 379
Cdd:PRK08472 256 TRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIV 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 19115831 380 LESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYRE 427
Cdd:PRK08472 333 LSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKE 380
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
42-474 |
3.53e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 159.15 E-value: 3.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 42 ERIRGAYNQAQMME-SGRVLSIGDGIARISgLSNVQAEELVEFSSgiKGMALNLEADTVGCVL-------FGNDRLVREG 113
Cdd:PRK06936 9 HHLRHAIVGSRLIQiRGRVTQVTGTILKAV-VPGVRIGELCYLRN--PDNSLSLQAEVIGFAQhqalltpLGEMYGISSN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 114 EVVKRTRHIVDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQRE 193
Cdd:PRK06936 86 TEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 194 LIIGDRQTGKTaialdTILNHKRWNNSSDeskklYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQYL 273
Cdd:PRK06936 166 GIFAAAGGGKS-----TLLASLIRSAEVD-----VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 274 APFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMSPKhggGSLTALP 353
Cdd:PRK06936 236 AGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG-QSDK---GSITALY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 354 VIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVASFAQ 433
Cdd:PRK06936 312 TVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQ 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 19115831 434 FGS---DLDAGTRATLDRGLRLTELLKQPQYSPLAVEEQVPLIY 474
Cdd:PRK06936 392 IGEyqkGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLE 435
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
113-470 |
2.21e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 157.19 E-value: 2.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 113 GEVVKRTRHIVDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQR 192
Cdd:PRK07721 81 GCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 193 ELIIGDRQTGKTaialdTILNHKRWNNSSDESkklycVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQY 272
Cdd:PRK07721 161 VGIFAGSGVGKS-----TLMGMIARNTSADLN-----VIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 273 LAPFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmspKHGGGSLTAL 352
Cdd:PRK07721 231 KGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG----TNASGSITAF 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 353 PVIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVASFA 432
Cdd:PRK07721 307 YTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLI 386
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 19115831 433 QFGSdLDAGTRATLDRGLR----LTELLKQPQYSPLAVEEQV 470
Cdd:PRK07721 387 NIGA-YKRGSSREIDEAIQfypqIISFLKQGTDEKATFEESI 427
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
87-452 |
8.44e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 152.93 E-value: 8.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 87 IKGMALNLEADTVGcvlFGNDRL----------VREGEVVKRTRHIVDVPVGEALLGRVVDALGNPIDGKGPIKTTERrr 156
Cdd:PRK08972 52 IETMAGELEAEVVG---FDGDLLylmpieelrgVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQR-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 157 VQLKAPGILP--RTSVCEPMQTGLKAIDSMVPIGRGQR-----------ELIIGDRQTGKTAialDTIlnhkrwnnssde 223
Cdd:PRK08972 127 ASRHSPPINPlsRRPITEPLDVGVRAINAMLTVGKGQRmglfagsgvgkSVLLGMMTRGTTA---DVI------------ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 224 skklycVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESaPLQYLapfSGC----AMGEWFRDNGKHGLVVYDDL 299
Cdd:PRK08972 192 ------VVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTS-PLMRL---KGCetatTIAEYFRDQGLNVLLLMDSL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 300 SKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPkhGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIF 379
Cdd:PRK08972 262 TRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVLTEGDDLQDPIADASRAILDGHIV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 380 LESELFFKGIRPAINVGLSVSRVG----SAAQVKAMKQVagqiklflaqyREVASFAQFGSDL------DAGTRATLDRG 449
Cdd:PRK08972 340 LSRELADSGHYPAIDIEASISRVMpmviSEEHLEAMRRV-----------KQVYSLYQQNRDLisigayKQGSDPRIDNA 408
|
...
gi 19115831 450 LRL 452
Cdd:PRK08972 409 IRL 411
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
113-467 |
2.52e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 145.87 E-value: 2.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 113 GEVVKRTRHIVDVPVGEALLGRVVDALGNPIDGKgPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQR 192
Cdd:PRK07594 79 GQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 193 ELIIGDRQTGKTaialdTILNHKRWNNSSDESkklycVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQY 272
Cdd:PRK07594 158 VGIFSAPGVGKS-----TLLAMLCNAPDADSN-----VLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 273 LAPFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMSPKhggGSLTAL 352
Cdd:PRK07594 228 RALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-MGEK---GSITAF 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 353 PVIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVASFA 432
Cdd:PRK07594 304 YTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLI 383
|
330 340 350
....*....|....*....|....*....|....*...
gi 19115831 433 QFGS---DLDAGTRATLDRGLRLTELLKQPQYSPLAVE 467
Cdd:PRK07594 384 RIGEyqrGVDTDTDKAIDTYPDICTFLRQSKDEVCGPE 421
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
56-467 |
4.20e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 139.75 E-value: 4.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 56 SGRVLSIGDGIARISGLSN-VQAEELVEFSSGikgmalnlEADTVGCVLfgndRLVREGEVVKRTRHIVDVPVGEALL-- 132
Cdd:PRK06002 27 GGTVSEVTASHYRVRGLSRfVRLGDFVAIRAD--------GGTHLGEVV----RVDPDGVTVKPFEPRIEIGLGDAVFrk 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 133 ------------GRVVDALGNPIDGKGPIKTTERRR-VQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDR 199
Cdd:PRK06002 95 gplrirpdpswkGRVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 200 QTGKT--------AIALDTilnhkrwnnssdeskklycVYVA-VGQKRSTVAQLvqkLEEN--DSLKYSIIVAATASESA 268
Cdd:PRK06002 175 GVGKStllamlarADAFDT-------------------VVIAlVGERGREVREF---LEDTlaDNLKKAVAVVATSDESP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 269 PLQYLAPFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmsP-KHGGG 347
Cdd:PRK06002 233 MMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAG---PgAEGGG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 348 SLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYRE 427
Cdd:PRK06002 310 SITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEE 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 19115831 428 VASFAQFGSdLDAGTRATLDRGLRLT----ELLKQPQYSPLAVE 467
Cdd:PRK06002 390 TRDLRLIGG-YRAGSDPDLDQAVDLVpriyEALRQSPGDPPSDD 432
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
125-427 |
7.68e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 139.10 E-value: 7.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 125 VPVGEALLGRVVDALGNPIDGKGPIKTTERrrVQLKAPGILP--RTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTG 202
Cdd:PRK05688 103 LPMGMSMLGRVLDGAGRALDGKGPMKAEDW--VPMDGPTINPlnRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 203 KTaialdTILNHKRWNNSSDeskklYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASEsAPLQYLAPFSGCA-M 281
Cdd:PRK05688 181 KS-----VLLGMMTRFTEAD-----IIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADD-APLMRLRAAMYCTrI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 282 GEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPkhGGGSLTALPVIETQGGD 361
Cdd:PRK05688 250 AEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEP--GGGSITAFYTVLSEGDD 327
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115831 362 VSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYRE 427
Cdd:PRK05688 328 QQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQ 393
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
125-416 |
1.34e-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: 131.58 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 125 VPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQlkAPGILP--RTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTG 202
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDIN--GPPINPvaRIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 203 KTAIALdTILNHKRWNNSSDESKklyCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQYLAPFSGCAMG 282
Cdd:cd01135 82 HNELAA-QIARQAGVVGSEENFA---IVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 283 EWFR-DNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMSPKhgGGSLTALPVIETQ 358
Cdd:cd01135 158 EYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTMP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115831 359 GGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVgsaaqvkaMKQVAG 416
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRL--------MKSGIG 282
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
127-458 |
3.92e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 131.17 E-value: 3.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 127 VGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTGKTAI 206
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 207 aLDTILNHkrwnnssdeSKKLYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESaPLQYLAPFSGC-AMGEWF 285
Cdd:PRK07196 172 -LGMITRY---------TQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADES-PLMRIKATELChAIATYY 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 286 RDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmspKHGGGSLTALPVIETQGGDVSAY 365
Cdd:PRK07196 241 RDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGN---SSGNGTMTAIYTVLAEGDDQQDP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 366 IPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVASFAQFGSDLdAGTRAT 445
Cdd:PRK07196 318 IVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYV-AGADPM 396
|
330
....*....|....*..
gi 19115831 446 LDRGL----RLTELLKQ 458
Cdd:PRK07196 397 ADQAVhyypAITQFLRQ 413
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
113-470 |
7.31e-33 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 130.41 E-value: 7.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 113 GEVVKRTRHIVDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQR 192
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 193 ELIIGDRQTGKTAIaLDTIlnhkrwnnsSDESKKLYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQY 272
Cdd:PRK05922 160 IGVFSEPGSGKSSL-LSTI---------AKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKV 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 273 LAPFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmspKHGGGSLTAL 352
Cdd:PRK05922 230 IAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG----NNDKGSITAL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 353 PVIetqggdvsAYIPTN-------VISITDGQIFLESE--LFFKgirPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLA 423
Cdd:PRK05922 306 YAI--------LHYPNHpdiftdyLKSLLDGHFFLTPQgkALAS---PPIDILTSLSRSARQLALPHHYAAAEELRSLLK 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 19115831 424 QYREVASFAQFGSdLDAGTRATLDRGLRL----TELLKQPQYSPLAVEEQV 470
Cdd:PRK05922 375 AYHEALDIIQLGA-YVPGQDAHLDRAVKLlpsiKQFLSQPLSSYCALHNTL 424
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
125-456 |
7.32e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 130.48 E-value: 7.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 125 VPVGEALLGRVVDALGNPIDGKGPIKTTERRRvQLKA--PGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTG 202
Cdd:PRK08927 92 VRPSRAWLGRVVNALGEPIDGKGPLPQGPVPY-PLRAppPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 203 KTaialdTILNHKRWNNSSDESkklycVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQYLAPFSGCAMG 282
Cdd:PRK08927 171 KS-----VLLSMLARNADADVS-----VIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 283 EWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPkhGGGSLTALPVIETQGGDV 362
Cdd:PRK08927 241 EYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPI--GEGTITGLFTVLVDGDDH 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 363 SAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVASFAQFGSdLDAGT 442
Cdd:PRK08927 319 NEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGA-YRAGS 397
|
330
....*....|....
gi 19115831 443 RATLDRGLRLTELL 456
Cdd:PRK08927 398 DPEVDEAIRLNPAL 411
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
125-452 |
8.90e-33 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 130.67 E-value: 8.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 125 VPVGEALLGRVVDALGNPIDGKGPIKTTERrrVQLKAPGILP--RTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTG 202
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGET--GALITPPFNPlqRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 203 KTAIaLDTILNHKRWNnssdeskklYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQYLAPFSGCAMG 282
Cdd:PRK07960 188 KSVL-LGMMARYTQAD---------VIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 283 EWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmSPKHGGGSLTALPVIETQGGDV 362
Cdd:PRK07960 258 EDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG--NGISGGGSITAFYTVLTEGDDQ 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 363 SAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQY---REVASFAQFGsdld 439
Cdd:PRK07960 336 QDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFqrnRDLVSVGAYA---- 411
|
330
....*....|...
gi 19115831 440 AGTRATLDRGLRL 452
Cdd:PRK07960 412 KGSDPMLDKAIAL 424
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
55-121 |
1.45e-32 |
|
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, in mitochondrial inner membranes, and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349740 [Multi-domain] Cd Length: 67 Bit Score: 118.71 E-value: 1.45e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115831 55 ESGRVLSIGDGIARISGLSNVQAEELVEFSSGIKGMALNLEADTVGCVLFGNDRLVREGEVVKRTRH 121
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
91-459 |
2.19e-32 |
|
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: 129.45 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 91 ALNLEADTVGCVLFG-NDRLVReGEVVKRTRHIVDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTS 169
Cdd:TIGR01039 44 AQHLGDDTVRTIAMGsTDGLVR-GLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQST 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 170 VCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTGKTAIALDTILNHKRWNNSsdeskklYCVYVAVGQKRSTVAQLVQKLE 249
Cdd:TIGR01039 123 KVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGG-------YSVFAGVGERTREGNDLYHEMK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 250 ENDSLKYSIIVAATASESAPLQYLAPFSGCAMGEWFRD-NGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFY 328
Cdd:TIGR01039 196 ESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 329 LHSRLLERAAkmSPKHggGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQV 408
Cdd:TIGR01039 276 EMGELQERIT--STKT--GSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVV 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 19115831 409 -KAMKQVAGQIKLFLAQYREVAS-FAQFGSD-LDAGTRATLDRGLRLTELLKQP 459
Cdd:TIGR01039 352 gEEHYDVARGVQQILQRYKELQDiIAILGMDeLSEEDKLTVERARRIQRFLSQP 405
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
68-474 |
5.57e-32 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 127.80 E-value: 5.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 68 RISG------LSNVQAEELVEFSSGIKGMALNLEADTVGcvlFGNDRLVRE--GEVVKRTRHIVDVP--------VGEAL 131
Cdd:PRK08149 12 RIQGpiieaeLPDVAIGEICEIRAGWHSNEVIARAQVVG---FQRERTILSliGNAQGLSRQVVLKPtgkplsvwVGEAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 132 LGRVVDALGN---PIDGKGPIKT-TERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTGKTAIa 207
Cdd:PRK08149 89 LGAVLDPTGKiveRFDAPPTVGPiSEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSL- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 208 LDTILNHkrwnNSSDeskklycVYVA--VGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQYLAPFSGCAMGEWF 285
Cdd:PRK08149 168 MNMLIEH----SEAD-------VFVIglIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 286 RDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSpkhgGGSLTALPVIETQGGDVSAY 365
Cdd:PRK08149 237 RDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATL----AGSITAFYTVLLESEEEPDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 366 IPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYREVASFAQFGsDLDAGTRAT 445
Cdd:PRK08149 313 IGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLG-EYRRGENAD 391
|
410 420 430
....*....|....*....|....*....|...
gi 19115831 446 LDRGLR----LTELLKQPQYSPLAVEEQVPLIY 474
Cdd:PRK08149 392 NDRAMDkrpaLEAFLKQDVAEKSSFSDTLERLN 424
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
113-436 |
4.85e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 125.09 E-value: 4.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 113 GEVVKRTRHIVDVPVGEALLGRVVDALGNPIDGkgPIKTTERRRVQLKAPGI--LPRTSVCEPMQTGLKAIDSMVPIGRG 190
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 191 QRELIIGDRQTGKTaialdTILNHKRWNNSSDESkklycVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPL 270
Cdd:PRK06793 157 QKIGIFAGSGVGKS-----TLLGMIAKNAKADIN-----VISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 271 QYLAPFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPgreaYPGDVFYLHS---RLLERAAKMSpkhgGG 347
Cdd:PRK06793 227 QLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQ----KG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 348 SLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAMKQVAGQIKLFLAQYRE 427
Cdd:PRK06793 299 SITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKE 378
|
....*....
gi 19115831 428 VASFAQFGS 436
Cdd:PRK06793 379 NELYFKLGT 387
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
65-401 |
5.02e-27 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 113.77 E-value: 5.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 65 GIARISG-------LSNVQAEELVEF--SSGIK--GMALNLEADTVGCVLFGNDR-LVREGEVVKRTRHIVDVPVGEALL 132
Cdd:PRK04196 6 TVSEIKGpllfvegVEGVAYGEIVEIelPNGEKrrGQVLEVSEDKAVVQVFEGTTgLDLKDTKVRFTGEPLKLPVSEDML 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 133 GRVVDALGNPIDGKGPIKTTERRRVQLKApgILP--RTSVCEPMQTGLKAIDSMVPIGRGQreliigdrqtgKTAIALDT 210
Cdd:PRK04196 86 GRIFDGLGRPIDGGPEIIPEKRLDINGAP--INPvaREYPEEFIQTGISAIDGLNTLVRGQ-----------KLPIFSGS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 211 ILNHK-------RWNNSSDESKKLYCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATASESAPLQYLAPFSGCAMGE 283
Cdd:PRK04196 153 GLPHNelaaqiaRQAKVLGEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 284 WFR-DNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMSPKHGggSLTALPVIETQG 359
Cdd:PRK04196 233 YLAfEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGKKG--SITQIPILTMPD 307
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 19115831 360 GDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSR 401
Cdd:PRK04196 308 DDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
119-411 |
7.83e-26 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 110.58 E-value: 7.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 119 TRHIVDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGD 198
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 199 -------------RQTGKTAIALDTILNHKRWNNSsdeskklyCVYVAVGQKRSTVAQLVQKLEENDSLKYSIIVAATAS 265
Cdd:TIGR01040 150 aglphneiaaqicRQAGLVKLPTKDVHDGHEDNFA--------IVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLAN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 266 ESAPLQYLAPFSGCAMGEWFR-DNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPKh 344
Cdd:TIGR01040 222 DPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR- 300
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115831 345 gGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRVGSAAQVKAM 411
Cdd:TIGR01040 301 -NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
125-402 |
5.12e-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: 87.28 E-value: 5.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 125 VPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTGKT 204
Cdd:cd01133 2 VPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 205 AIALDTIlnhkrwNNSSdESKKLYCVYVAVGQKRSTVAQLVQKLEE-----NDSLKYSIIVAATASESAPLQYLAPFSGC 279
Cdd:cd01133 82 VLIMELI------NNIA-KAHGGYSVFAGVGERTREGNDLYHEMKEsgvinLDGLSKVALVYGQMNEPPGARARVALTGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 280 AMGEWFRD-NGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmSPKHggGSLTALPVIETQ 358
Cdd:cd01133 155 TMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERIT--STKK--GSITSVQAVYVP 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 19115831 359 GGDVSAYIPTNVISITDGQIFLESELFFKGIRPAINVGLSVSRV 402
Cdd:cd01133 231 ADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
94-190 |
7.42e-19 |
|
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: 89.38 E-value: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 94 LEADTVGCVLFGN-DRLVReGEVVKRTRHIVDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGILPRTSVCE 172
Cdd:COG0055 50 LGDNTVRCIAMDStDGLVR-GMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTE 128
|
90
....*....|....*...
gi 19115831 173 PMQTGLKAIDSMVPIGRG 190
Cdd:COG0055 129 ILETGIKVIDLLAPYAKG 146
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
92-380 |
2.19e-17 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 84.70 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 92 LNLEADTVGCVLFGNDRLVREGEVVKRTRHIVDVPVGEALLGRVVDALGNPIDGkGPIktTERRRVQLKAPGILP--RTS 169
Cdd:PRK02118 43 IRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GPE--LEGEPIEIGGPSVNPvkRIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 170 VCEPMQTGLKAIDSMVPIGRGQRELIIGDRQTGKTA----IALDTilnhkrwnnssdESKKLycVYVAVGQKRSTVAQLV 245
Cdd:PRK02118 120 PREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNAllarIALQA------------EADII--ILGGMGLTFDDYLFFK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 246 QKLEENDSLKYSIIVAATASESAPLQYLAPFSGCAMGEWFR-DNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPG 324
Cdd:PRK02118 186 DTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPG 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 19115831 325 DvfyLHSRLLERAAKMSPKHGGGSLTALPVIETQGGDVSAYIPTNVISITDGQIFL 380
Cdd:PRK02118 266 S---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
411-478 |
1.22e-16 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 74.40 E-value: 1.22e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 411 MKQVAGQIKLFLAQYREVASFAQFGSD--LDAGTRATLDRGLRLTELLKQPQYSPLAVEEQVPLIYCGVK 478
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
53-119 |
7.84e-16 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 72.19 E-value: 7.84e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115831 53 MMESGRVLSIGDGIARISGLSNVQAEELVEFSSGIKGMALNLEADTVGCVLFGNDRLVREGEVVKRT 119
Cdd:pfam02874 2 VQVIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRT 68
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
125-401 |
5.62e-14 |
|
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: 72.61 E-value: 5.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 125 VPVGEALLGRVVDALGNPID----------GKG------PIKTTerRRVQLKAPGilprtsvCEPMQTGLKAIDSMVPIG 188
Cdd:cd01134 4 VELGPGLLGSIFDGIQRPLEviaetgsifiPRGvnvqrwPVRQP--RPVKEKLPP-------NVPLLTGQRVLDTLFPVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 189 RGQRELIIGDRQTGKTaialdtILNHK--RWNNSSdeskklYCVYVAVGQKRSTVA-------QLVQKLEENDSLKYSII 259
Cdd:cd01134 75 KGGTAAIPGPFGCGKT------VISQSlsKWSNSD------VVIYVGCGERGNEMAevleefpELKDPITGESLMERTVL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 260 VAATASESAPLQYLAPFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LER 336
Cdd:cd01134 143 IANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYER 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 337 AAKMS---PKHGGGSLTALPVIETQGGDVSAYIPTNVISITdgQIF--LESELFFKGIRPAINVGLSVSR 401
Cdd:cd01134 220 AGRVRclgSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
105-213 |
2.26e-09 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 59.67 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 105 GNDRLVREGEVVKrTRHIVDVPVGEALLGRVVDALGNPIDGKGPIKTTERRRVQLKAPGIL---PRTSVCEpmqTGLKAI 181
Cdd:CHL00060 77 ATDGLMRGMEVID-TGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTKLSIFE---TGIKVV 152
|
90 100 110
....*....|....*....|....*....|..
gi 19115831 182 DSMVPIGRGQRELIIGDRQTGKTAIALDTILN 213
Cdd:CHL00060 153 DLLAPYRRGGKIGLFGGAGVGKTVLIMELINN 184
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
209-394 |
2.35e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 60.04 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 209 DTILNHK--RWNNSSdeskklYCVYVAVGQKRSTVAQLVQ---KLEENDS----LKYSIIVAATASESAPLQYLAPFSGC 279
Cdd:PRK14698 669 NTVTQHQlaKWSDAQ------VVIYIGCGERGNEMTDVLEefpKLKDPKTgkplMERTVLIANTSNMPVAAREASIYTGI 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 280 AMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKMSPKHGGGSLTALP 353
Cdd:PRK14698 743 TIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIG 819
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19115831 354 VIETQGGDVSAYIPTNVISITDGQIFLESELFFKGIRPAIN 394
Cdd:PRK14698 820 AVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAIN 860
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
172-363 |
8.72e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 57.87 E-value: 8.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 172 EPMQTGLKAIDSMVPIGRGQRELIIGDRQTGKTaialdtILNHK--RWNNSSdeskklYCVYVAVGQKRSTVAQLVQ--- 246
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT------VTQHQlaKWADAD------IVIYVGCGERGNEMTEVLEefp 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 247 KLEE----NDSLKYSIIVAAT------ASESAPlqylapFSGCAMGEWFRDNGKHGLVVYDDLSKQAVAYRQMSLLLRRP 316
Cdd:PRK04192 277 ELIDpktgRPLMERTVLIANTsnmpvaAREASI------YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEM 350
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19115831 317 PGREAYPGdvfYLHSRL---LERAAKMSPKHGG-GSLTALPVIETQGGDVS 363
Cdd:PRK04192 351 PGEEGYPA---YLASRLaefYERAGRVKTLGGEeGSVTIIGAVSPPGGDFS 398
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
57-119 |
5.79e-03 |
|
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: 35.75 E-value: 5.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115831 57 GRVLSIGDGIARISGLSNVQAEELVEFSSGI-------KGMALNLEADTVGCVLFGNDRLVREGEVVKRT 119
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIGEVCEIERGDgnnetvlKAEVIGFRGDRAILQLFESTRGLSRGALVEPT 71
|
|
| |
