|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
3-496 |
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: 868.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 3 SDGIIEELRERIRSFDMKLDARETGQVVSLADGIATVYGLDRVTYGELVVFEDDSLGMAMNLESDRVGVVLFSDGGGLRE 82
Cdd:COG0056 5 PEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEGIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 83 GTLCRRGGQAASVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQR 162
Cdd:COG0056 85 GDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 163 ELIIGDRQTGKTTIAVDAILNQKDQNVICIYCAIGQKNSSIAQIHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATA 242
Cdd:COG0056 165 ELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 243 MGEYFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDHWGGGSMTALPIIETQAG 322
Cdd:COG0056 245 MGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 323 DVSAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRVGGAAQPAGIRALAGNLRVTLARFAELEVFTQFAGDLDD 402
Cdd:COG0056 325 DVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 403 ATREALDSGHRLTEVLKQTPGSSLSTAGQLVTLYYVTSGGFSDVPLAHVRDFARDVRKYLSQEDGPLMQELERGEKLTDG 482
Cdd:COG0056 405 ATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGKLDDE 484
|
490
....*....|....
gi 495796248 483 QKEALDKRLAAFKA 496
Cdd:COG0056 485 IEEKLKAAIEEFKK 498
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
6-496 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 838.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 6 IIEELRERIRSFDMKLDARETGQVVSLADGIATVYGLDRVTYGELVVFEDDSLGMAMNLESDRVGVVLFSDGGGLREGTL 85
Cdd:PRK09281 8 ISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIKEGDT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 86 CRRGGQAASVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELI 165
Cdd:PRK09281 88 VKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 166 IGDRQTGKTTIAVDAILNQKDQNVICIYCAIGQKNSSIAQIHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATAMGE 245
Cdd:PRK09281 168 IGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 246 YFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDHWGGGSMTALPIIETQAGDVS 325
Cdd:PRK09281 248 YFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 326 AYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRVGGAAQPAGIRALAGNLRVTLARFAELEVFTQFAGDLDDATR 405
Cdd:PRK09281 328 AYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 406 EALDSGHRLTEVLKQTPGSSLSTAGQLVTLYYVTSGGFSDVPLAHVRDFARDVRKYLSQEDGPLMQELERGEKLTDGQKE 485
Cdd:PRK09281 408 AQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKDLSDEIEA 487
|
490
....*....|.
gi 495796248 486 ALDKRLAAFKA 496
Cdd:PRK09281 488 KLKAAIEEFKK 498
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
3-500 |
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: 716.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 3 SDGIIEELRERIRSFDMKLDARETGQVVSLADGIATVYGLDRVTYGELVVFEDDSLGMAMNLESDRVGVVLFSDGGGLRE 82
Cdd:TIGR00962 4 LEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 83 GTLCRRGGQAASVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQR 162
Cdd:TIGR00962 84 GSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 163 ELIIGDRQTGKTTIAVDAILNQKDQNVICIYCAIGQKNSSIAQIHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATA 242
Cdd:TIGR00962 164 ELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 243 MGEYFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDHWGGGSMTALPIIETQAG 322
Cdd:TIGR00962 244 MGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIETQAG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 323 DVSAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRVGGAAQPAGIRALAGNLRVTLARFAELEVFTQFAGDLDD 402
Cdd:TIGR00962 324 DVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASDLDE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 403 ATREALDSGHRLTEVLKQTPGSSLSTAGQLVTLYYVTSGGFSDVPLAHVRDFARDVRKYLSQEDGPLMQELERGEKLTDG 482
Cdd:TIGR00962 404 ATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKLTEE 483
|
490
....*....|....*...
gi 495796248 483 QKEALDKRLAAFKAHEAP 500
Cdd:TIGR00962 484 LEAKLKEALKNFKKTFAW 501
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
3-500 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 700.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 3 SDGIIEELRERIRSFDMKLDARETGQVVSLADGIATVYGLDRVTYGELVVFEDDSLGMAMNLESDRVGVVLFSDGGGLRE 82
Cdd:PRK13343 5 ADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 83 GTLCRRGGQAASVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQR 162
Cdd:PRK13343 85 GTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 163 ELIIGDRQTGKTTIAVDAILNQKDQNVICIYCAIGQKNSSIAQIHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATA 242
Cdd:PRK13343 165 ELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 243 MGEYFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDHWGGGSMTALPIIETQAG 322
Cdd:PRK13343 245 IAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETLAG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 323 DVSAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRVGGAAQPAGIRALAGNLRVTLARFAELEVFTQFAGDLDD 402
Cdd:PRK13343 325 ELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLLDA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 403 ATREALDSGHRLTEVLKQTPGSSLSTAGQLVTLYYVTSGGFSDVPLAHVRDFARDVRKYLSQEDGPLMQELERGEKLTDG 482
Cdd:PRK13343 405 GTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRELDEA 484
|
490
....*....|....*...
gi 495796248 483 QKEALDKRLAAFKAHEAP 500
Cdd:PRK13343 485 WLAALEEILREAGERFAA 502
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
26-498 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 650.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 26 TGQVVSLADGIATVYGLDRVTYGELVVFEDDSLGMAMNLESDRVGVVLFSDGGGLREGTLCRRGGQAASVSCGDGLIGRV 105
Cdd:CHL00059 7 TGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 106 VNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDRQTGKTTIAVDAILNQK 185
Cdd:CHL00059 87 VNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 186 DQNVICIYCAIGQKNSSIAQIHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATAMGEYFMDQGRDVLIIYDDLSKHA 265
Cdd:CHL00059 167 GQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 266 VAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDHWGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLESH 345
Cdd:CHL00059 247 QAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSAD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 346 LFRSGVRPAVNTGLSVSRVGGAAQPAGIRALAGNLRVTLARFAELEVFTQFAGDLDDATREALDSGHRLTEVLKQTPGSS 425
Cdd:CHL00059 327 LFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQSAP 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495796248 426 LSTAGQLVTLYYVTSGGFSDVPLAHVRDFARDVRKYLSQEDGPLMQELERGEKLTDGQ----KEALDKRLAAFKAHE 498
Cdd:CHL00059 407 LTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAeallKEAIQEQLELFLLQE 483
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
4-487 |
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: 585.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 4 DGIIEELRERIRSFDMKLDARETGQVVSLADGIATVYGLDRVTYGELVVFEDDSLGMAMNLESDRVGVVLFSDGGGLREG 83
Cdd:TIGR03324 6 DKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 84 TLCRRGGQAASVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRE 163
Cdd:TIGR03324 86 DEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 164 LIIGDRQTGKTTIAVDAILNQKDQNVICIYCAIGQKNSSIAQIHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATAM 243
Cdd:TIGR03324 166 LILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 244 GEYFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDHWGGGSMTALPIIETQAGD 323
Cdd:TIGR03324 246 GEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 324 VSAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRVGGAAQPAGIRALAGNLRVTLARFAELEVFTQFAGDLDDA 403
Cdd:TIGR03324 326 ISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDEN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 404 TREALDSGHRLTEVLKQTPGSSLSTAGQLVTLYYVTSGGFSDVPLAHVRDFARDVRKYLSQEDGPLMQELERGEKLTDGQ 483
Cdd:TIGR03324 406 TRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSDED 485
|
....
gi 495796248 484 KEAL 487
Cdd:TIGR03324 486 REQI 489
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
93-365 |
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: 525.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 93 ASVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDRQTG 172
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 173 KTTIAVDAILNQKDQNVICIYCAIGQKNSSIAQIHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATAMGEYFMDQGR 252
Cdd:cd01132 82 KTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 253 DVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDHWGGGSMTALPIIETQAGDVSAYIPTNV 332
Cdd:cd01132 162 HALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTNV 241
|
250 260 270
....*....|....*....|....*....|...
gi 495796248 333 ISITDGQIYLESHLFRSGVRPAVNTGLSVSRVG 365
Cdd:cd01132 242 ISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
59-452 |
9.21e-112 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 342.79 E-value: 9.21e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 59 GMAMNLESD-RVGVVLFSDGGGLREGTLCRRGGQAASVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDM-------PVERE 130
Cdd:PTZ00185 80 GLVFNLEKDgRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPVGLLTRSRALLeseqtlgKVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 131 ASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDRQTGKTTIAVDAILNQKDQN--------VICIYCAIGQKNSS 202
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINqqilsknaVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 203 IAQIHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATAMGEYFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGRE 282
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGRE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 283 AYPGDVFYLHSRLLERSCRLEDHWGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVS 362
Cdd:PTZ00185 320 AYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVS 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 363 RVGGAAQPAGIRALAGNLRVTLARFAELEVFTQFAGDLDDAtreALDSGHRLTEVLKQTPGSSLSTAgqLVTLYYVTSGG 442
Cdd:PTZ00185 400 RVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTV---PMIRGARFVALFNQKNPSFFMNA--LVSLYACLNGY 474
|
410
....*....|
gi 495796248 443 FSDVPLAHVR 452
Cdd:PTZ00185 475 LDDVKVNYAK 484
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
147-362 |
1.34e-106 |
|
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: 316.22 E-value: 1.34e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 147 GILAVDALVPVGRGQRELIIGDRQTGKTTIAvDAILNQKDQNViCIYCAIGQKNSSIAQIHASLRAAGALDYTFIVSSPA 226
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 227 SDSPSLQYLAPYAATAMGEYFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDhw 306
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKG-- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495796248 307 GGGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVS 362
Cdd:pfam00006 157 KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
131-446 |
3.04e-103 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 318.46 E-value: 3.04e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 131 ASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDRQTGKTTIAVDAILNQKDQNVICIYCAIGQKNSSIAQIHASL 210
Cdd:PRK07165 114 AHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 211 RAAGALDYTFIVSSPaSDSPSLQYLAPYAATAMGEYFMdQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFY 290
Cdd:PRK07165 194 KEHDALKNTIIIDAP-STSPYEQYLAPYVAMAHAENIS-YNDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFF 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 291 LHSRLLERSCRLEdhwGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRVGGAAQP 370
Cdd:PRK07165 272 AHSKLLERAGKFK---NRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQS 348
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495796248 371 AGIRALAGNLRVTLARFAELEVFTQFAGDLDDATREALDSGHRLTEVLKQTPGSSLSTAGQLVTLYYVTSGGFSDV 446
Cdd:PRK07165 349 KTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKGKMIEKMFNQKGFSLYSYRFVLLISKLISWGLLKDV 424
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
94-364 |
1.91e-93 |
|
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: 285.12 E-value: 1.91e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 94 SVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDRQTGK 173
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 174 TTIAVDAILNQKDQNV-ICIYCAIGQKNSSIAQIHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATAMGEYFMDQGR 252
Cdd:cd19476 81 TVLAMQLARNQAKAHAgVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 253 DVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDhwGGGSMTALPIIETQAGDVSAYIPTNV 332
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 495796248 333 ISITDGQIYLESHLFRSGVRPAVNTGLSVSRV 364
Cdd:cd19476 239 FAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
94-364 |
1.36e-45 |
|
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: 160.42 E-value: 1.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 94 SVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDRQTGK 173
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 174 TTIAVDAILNQK-DQNVICIycaIGQKNSSIAQIHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATAMGEYFMDQGR 252
Cdd:cd01136 81 STLLGMIARNTDaDVNVIAL---IGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 253 DVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDhwggGSMTALPIIETQAGDVSAYIPTNV 332
Cdd:cd01136 158 KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----GSITAFYTVLVEGDDFNDPIADEV 233
|
250 260 270
....*....|....*....|....*....|..
gi 495796248 333 ISITDGQIYLESHLFRSGVRPAVNTGLSVSRV 364
Cdd:cd01136 234 RSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
6-391 |
4.64e-45 |
|
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: 163.66 E-value: 4.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 6 IIEELRERIRSFDMkldARETGQVVSLADGIATVYGLDrVTYGELVVFEDDS----LGMAMNLESDRVGVVLFSDGGGLR 81
Cdd:COG1157 3 RLARLLARLEELPP---VRVSGRVTRVVGLLIEAVGPD-ASIGELCEIETADgrpvLAEVVGFRGDRVLLMPLGDLEGIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 82 EGTLCRRGGQAASVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQ 161
Cdd:COG1157 79 PGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 162 ReliIGdr---qtGKTT----IA--VDAilnqkDQNVICIycaIGQKNSSIAQ-IHASLRAAGaLDYTFIVSSPASDSPS 231
Cdd:COG1157 159 R---IGifagsgvGKSTllgmIArnTEA-----DVNVIAL---IGERGREVREfIEDDLGEEG-LARSVVVVATSDEPPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 232 LQYLAPYAATAMGEYFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERScrledhwG---G 308
Cdd:COG1157 227 MRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERA-------GnggK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 309 GSMTAL------------PIIETqagdvsayiptnVISITDGQIYLESHLFRSGVRPAVNTGLSVSRVGGAAQPAGIRAL 376
Cdd:COG1157 300 GSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRAL 367
|
410
....*....|....*
gi 495796248 377 AGNLRVTLARFAELE 391
Cdd:COG1157 368 ARRLRRLLARYEENE 382
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
7-366 |
4.18e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 158.31 E-value: 4.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 7 IEELRERIRSFDMkldARETGQVVSLADGIATVYGLdRVTYGELV--VFEDDS---LGMAMNLESDRVGVVLFSDGGGLR 81
Cdd:PRK08472 3 LESLKNKLQKFNL---SPRFGSITKISPTIIEADGL-NPSVGDIVkiESSDNGkecLGMVVVIEKEQFGISPFSFIEGFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 82 EGTLCRRGGQAASVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQ 161
Cdd:PRK08472 79 IGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 162 RELIIGDRQTGKTTIAVDAILNQKDQnvICIYCAIGQKNSSIAQ-IHASLraAGALDYTFIVSSPASDSPSLQYLAPYAA 240
Cdd:PRK08472 159 KLGIFAGSGVGKSTLMGMIVKGCLAP--IKVVALIGERGREIPEfIEKNL--GGDLENTVIVVATSDDSPLMRKYGAFCA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 241 TAMGEYFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDHwggGSMTALPIIETQ 320
Cdd:PRK08472 235 MSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGK---GSITAFFTVLVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 495796248 321 AGDVSAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRVGG 366
Cdd:PRK08472 312 GDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN 357
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
42-421 |
1.07e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 157.28 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 42 LDRVTYGELVVFEDDSL-GMAMNLESDRVGVVLFSDGGGLREGTLCRRGGQAASVSCGDGLIGRVVNPLGEAIDGGAPIV 120
Cdd:PRK06820 45 LPGVAQGELCRIEPQGMlAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 121 GQKdMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDRQTGKTTIaVDAILNQKDQNVIcIYCAIGQKN 200
Cdd:PRK06820 125 GQW-RELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTL-LGMLCADSAADVM-VLALIGERG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 201 SSIAQIHASLRAAGALDYTFIVSSpASDSPSLQYL-APYAATAMGEYFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSP 279
Cdd:PRK06820 202 REVREFLEQVLTPEARARTVVVVA-TSDRPALERLkGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 280 GREAYPGDVFYLHSRLLERSCRLEDhwggGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGL 359
Cdd:PRK06820 281 AAGSFPPSVFANLPRLLERTGNSDR----GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAA 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495796248 360 SVSRVGGAAQPAGIRALAGNLRVTLARFAELEVFTQ---FAGDLDDATREALDSGHRLTEVLKQT 421
Cdd:PRK06820 357 SVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRvgeYQAGEDLQADEALQRYPAICAFLQQD 421
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
90-439 |
2.18e-41 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 153.75 E-value: 2.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 90 GQAASVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDR 169
Cdd:PRK06936 92 GTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 170 QTGKTTIaVDAILNQKDQNViCIYCAIGQKNSSIAQ-IHASLRAAGALDYTFIVSSpaSDSPSLQYL-APYAATAMGEYF 247
Cdd:PRK06936 172 GGGKSTL-LASLIRSAEVDV-TVLALIGERGREVREfIESDLGEEGLRKAVLVVAT--SDRPSMERAkAGFVATSIAEYF 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 248 MDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDhwggGSMTALPIIETQAGDVSAY 327
Cdd:PRK06936 248 RDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDK----GSITALYTVLVEGDDMTEP 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 328 IPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRVGGAAQPAGIRALAGNLRVTLARFAELEVFTQ---FAGDLDDAT 404
Cdd:PRK06936 324 VADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQigeYQKGQDKEA 403
|
330 340 350
....*....|....*....|....*....|....*
gi 495796248 405 REALDSGHRLTEVLKQTPGSSLSTAGQLVTLYYVT 439
Cdd:PRK06936 404 DQAIERIGAIRGFLRQGTHELSHFNETLNLLETLT 438
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
78-391 |
5.88e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 147.18 E-value: 5.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 78 GGLREGTlcrrgGQAASVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPV 157
Cdd:PRK07721 81 GCLVEAT-----GKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 158 GRGQRELIIGDRQTGKTTI-AVDAILNQKDQNVICIycaIGQKNSSIAQ-IHASLRAAGaLDYTFIVSSpASDSPSLQYL 235
Cdd:PRK07721 156 GKGQRVGIFAGSGVGKSTLmGMIARNTSADLNVIAL---IGERGREVREfIERDLGPEG-LKRSIVVVA-TSDQPALMRI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 236 -APYAATAMGEYFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDhwggGSMTAL 314
Cdd:PRK07721 231 kGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS----GSITAF 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495796248 315 PIIETQAGDVSAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRV-GGAAQPAGIRAlAGNLRVTLARFAELE 391
Cdd:PRK07721 307 YTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVmNHIVSPEHKEA-ANRFRELLSTYQNSE 383
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
373-496 |
1.11e-38 |
|
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: 137.11 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 373 IRALAGNLRVTLARFAELEVFTQFAGDLDDATREALDSGHRLTEVLKQTPGSSLSTAGQLVTLYYVTSGGFSDVPLAHVR 452
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 495796248 453 DFARDVRKYLSQEDGPLMQELERGEKLTDGQKEALDKRLAAFKA 496
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKK 124
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
24-427 |
1.39e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 146.30 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 24 RETGQVVSLADGIATVYGLDR-VTYGELVVFEDD---SLGMAMNLESDRVGVVLFSDGGGLREGTLCRRGGqAASVSCGD 99
Cdd:PRK06002 25 RIGGTVSEVTASHYRVRGLSRfVRLGDFVAIRADggtHLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKG-PLRIRPDP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 100 GLIGRVVNPLGEAIDGGAPIV-GQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDRQTGKTTIAv 178
Cdd:PRK06002 104 SWKGRVINALGEPIDGLGPLApGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLL- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 179 dAILNQKDQNVICIYCAIGQKNSSIAQ-IHASLraAGALDYTFIVSSPASDSPSLQYLAPYAATAMGEYFMDQGRDVLII 257
Cdd:PRK06002 183 -AMLARADAFDTVVIALVGERGREVREfLEDTL--ADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 258 YDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDhwGGGSMTALPIIETQAGDVSAYIPTNVISITD 337
Cdd:PRK06002 260 VDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLVDGDDHNDPVADSIRGTLD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 338 GQIYLESHLFRSGVRPAVNTGLSVSRVGGAAQPAGIRALAGNLRVTLARFAELEVFTQFAG-------DLDDATREAlds 410
Cdd:PRK06002 338 GHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGGyragsdpDLDQAVDLV--- 414
|
410
....*....|....*..
gi 495796248 411 gHRLTEVLKQTPGSSLS 427
Cdd:PRK06002 415 -PRIYEALRQSPGDPPS 430
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
24-395 |
2.25e-38 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 145.30 E-value: 2.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 24 RETGQVVSLADGIATVYGLDrVTYGELVVFEDDSlGMAMNlesdRVGVVLFSDG----------GGLREGTLCRRGGQAA 93
Cdd:PRK09099 23 RRTGKVVEVIGTLLRVSGLD-VTLGELCELRQRD-GTLLQ----RAEVVGFSRDvallspfgelGGLSRGTRVIGLGRPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 94 SVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDRQTGK 173
Cdd:PRK09099 97 SVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 174 TT-IAVDAILNQKDQNVICIycaIGQKNSSIAQIHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATAMGEYFMDQGR 252
Cdd:PRK09099 177 STlMGMFARGTQCDVNVIAL---IGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 253 DVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDhwggGSMTALPIIETQAGDVSAYIPTNV 332
Cdd:PRK09099 254 RVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGET----GSITALYTVLAEDESGSDPIAEEV 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495796248 333 ISITDGQIYLESHLFRSGVRPAVNTGLSVSRVGGAAQPAGIRALAGNLRVTLARFAELEVFTQ 395
Cdd:PRK09099 330 RGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQ 392
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
73-420 |
8.39e-38 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 143.60 E-value: 8.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 73 LFSDGGGLREGTLCRRGGQAASVSCGDGLIGRVVNPLGEAID----GGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGI 148
Cdd:PRK08149 60 LIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVErfdaPPTVGPISEERVIDVAPPSYAERRPIREPLITGV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 149 LAVDALVPVGRGQRELIIGDRQTGKTTIaVDAILNQKDQNVICIyCAIGQKNSSIAQIHASLRAAGALDYTFIVSSpASD 228
Cdd:PRK08149 140 RAIDGLLTCGVGQRMGIFASAGCGKTSL-MNMLIEHSEADVFVI-GLIGERGREVTEFVESLRASSRREKCVLVYA-TSD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 229 SPSLQYL-APYAATAMGEYFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLedhwG 307
Cdd:PRK08149 217 FSSVDRCnAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT----L 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 308 GGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRVGGAAQPAGIRALAGNLRVTLARF 387
Cdd:PRK08149 293 AGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRL 372
|
330 340 350
....*....|....*....|....*....|....*..
gi 495796248 388 AELEVFTQF----AGDLDDATReALDSGHRLTEVLKQ 420
Cdd:PRK08149 373 EELQLFIDLgeyrRGENADNDR-AMDKRPALEAFLKQ 408
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
369-494 |
1.30e-35 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 128.71 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 369 QPAGIRALAGNLRVTLARFAELEVFTQFAGDLDDATREALDSGHRLTEVLKQTPGSSLSTAGQLVTLYYVTSGGFSDVPL 448
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 495796248 449 AHVRDFARDVRKYLSQEDGPLMQELERGEKLTDGQKEALDKRLAAF 494
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
74-423 |
5.30e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 135.79 E-value: 5.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 74 FSDGGGLREGTLCRRGGQAASVSCGDGLIGRVVNPLGEAIDGGAPIVGqkDMPVEREASGV--MSRKPVNVPLKTGILAV 151
Cdd:PRK07196 69 FKHPGGVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGG--STPLQQQLPQIhpLQRRAVDTPLDVGVNAI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 152 DALVPVGRGQRELIIGDRQTGKTTIAvdAILNQKDQNVICIYCAIGQKNSSIAQ-IHASLRAAGaLDYTFIVSSPASDSP 230
Cdd:PRK07196 147 NGLLTIGKGQRVGLMAGSGVGKSVLL--GMITRYTQADVVVVGLIGERGREVKEfIEHSLQAAG-MAKSVVVAAPADESP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 231 SLQYLAPYAATAMGEYFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEdhwGGGS 310
Cdd:PRK07196 224 LMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSS---GNGT 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 311 MTALPIIETQAGDVSAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRVGGAAQPAGIRALAGNLRVTLARFAEL 390
Cdd:PRK07196 301 MTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAI 380
|
330 340 350
....*....|....*....|....*....|....*.
gi 495796248 391 EVFTQFAGDL---DDATREALDSGHRLTEVLKQTPG 423
Cdd:PRK07196 381 KPLIPLGGYVagaDPMADQAVHYYPAITQFLRQEVG 416
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
93-363 |
5.95e-33 |
|
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: 126.57 E-value: 5.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 93 ASVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDrqTG 172
Cdd:cd01135 2 LKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSG--SG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 173 ------KTTIAVDAILNQKDQNVICIYCAIGQKNSSIAQIHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATAMGEY 246
Cdd:cd01135 80 lphnelAAQIARQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 247 F-MDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGdvfYLHSRL---LERSCRLEDHwgGGSMTALPIIETQAG 322
Cdd:cd01135 160 LaYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTMPND 234
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 495796248 323 DVSAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSR 363
Cdd:cd01135 235 DITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
98-364 |
4.80e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 124.84 E-value: 4.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 98 GDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDRQTGKTTIA 177
Cdd:PRK05688 106 GMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 178 vdAILNQKDQNVICIYCAIGQKNSSIAQIHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATAMGEYFMDQGRDVLII 257
Cdd:PRK05688 186 --GMMTRFTEADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 258 YDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDhwGGGSMTALPIIETQAGDVSAYIPTNVISITD 337
Cdd:PRK05688 264 MDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEP--GGGSITAFYTVLSEGDDQQDPIADSARGVLD 341
|
250 260
....*....|....*....|....*..
gi 495796248 338 GQIYLESHLFRSGVRPAVNTGLSVSRV 364
Cdd:PRK05688 342 GHIVLSRRLAEEGHYPAIDIEASISRV 368
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
9-421 |
1.79e-30 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 123.14 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 9 ELRERIRSFDMKLDA-RETGQVVSLADGIATVYgLDRVTYGELV-VFEDDSLGMAMNLESDRVGVVLFSDGGGLREGTLC 86
Cdd:PRK07594 4 ELMQRLRLKYPPPDGyCRWGRIQDVSATLLNAW-LPGVFMGELCcIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 87 RRGGQAASVSCGDGLIGRVVNPLGEAIDGGA-PIVGQKDMpvEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELI 165
Cdd:PRK07594 83 MALRRRHQVPVGEALLGRVIDGFGRPLDGRElPDVCWKDY--DAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 166 IGDRQTGKTTI-AVDAILNQKDQNVICIycaIGQKNSSIAQ-IHASLRAAGALDYTFIVSSpaSDSPSLQYL-APYAATA 242
Cdd:PRK07594 161 FSAPGVGKSTLlAMLCNAPDADSNVLVL---IGERGREVREfIDFTLSEETRKRCVIVVAT--SDRPALERVrALFVATT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 243 MGEYFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDhwggGSMTALPIIETQAG 322
Cdd:PRK07594 236 IAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEK----GSITAFYTVLVEGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 323 DVSAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRVGGAAQPAGIRALAGNLRVTLARFAELEVFT---QFAGD 399
Cdd:PRK07594 312 DMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIrigEYQRG 391
|
410 420
....*....|....*....|..
gi 495796248 400 LDDATREALDSGHRLTEVLKQT 421
Cdd:PRK07594 392 VDTDTDKAIDTYPDICTFLRQS 413
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
39-363 |
8.66e-29 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 118.78 E-value: 8.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 39 VYGLDRVTYGELVVFEDDS----LGMAMNLESDRVGVVLFSDGGGL-REGTLCRRGGQAASVSCGDGLIGRVVNPLGEAI 113
Cdd:PRK04196 17 VEGVEGVAYGEIVEIELPNgekrRGQVLEVSEDKAVVQVFEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 114 DGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQR------------ELIIgdrQtgkttIAVDAI 181
Cdd:PRK04196 97 DGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnELAA---Q-----IARQAK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 182 LNQKDQNVICIYCAIGQKNSSIAQIHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATAMGEYF-MDQGRDVLIIYDD 260
Cdd:PRK04196 169 VLGEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLaFEKGMHVLVILTD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 261 LSKHAVAYRALSLLLRRSPGREAYPGdvfYLHSRL---LERSCRLEDHwgGGSMTALPIIETQAGDVSAYIPTNVISITD 337
Cdd:PRK04196 249 MTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHPIPDLTGYITE 323
|
330 340
....*....|....*....|....*.
gi 495796248 338 GQIYLESHLFRSGVRPAVNTGLSVSR 363
Cdd:PRK04196 324 GQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
90-364 |
1.94e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 117.49 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 90 GQAASVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDR 169
Cdd:PRK08972 92 GEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 170 QTGKTTIAvdAILNQKDQNVICIYCAIGQKNSSIAQ-IHASLRAAGaLDYTFIVSSPASDSPSLQYLAPYAATAMGEYFM 248
Cdd:PRK08972 172 GVGKSVLL--GMMTRGTTADVIVVGLVGERGREVKEfIEEILGEEG-RARSVVVAAPADTSPLMRLKGCETATTIAEYFR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 249 DQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDhwGGGSMTALPIIETQAGDVSAYI 328
Cdd:PRK08972 249 DQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVLTEGDDLQDPI 326
|
250 260 270
....*....|....*....|....*....|....*.
gi 495796248 329 PTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRV 364
Cdd:PRK08972 327 ADASRAILDGHIVLSRELADSGHYPAIDIEASISRV 362
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
31-391 |
1.31e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 108.91 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 31 SLADGIATVYGLDRVTYGELVVFEDD-SLGMAmnlesdrvgvvlFSDGGGLREGTLCRRGGQAASVSCGDGLIGRVVNPL 109
Cdd:PRK08927 39 SVGARIVVETRGGRPVPCEVVGFRGDrALLMP------------FGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 110 GEAIDGGAPIV-GQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDRQTGKTTI------AVDAil 182
Cdd:PRK08927 107 GEPIDGKGPLPqGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLlsmlarNADA-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 183 nqkDQNVICIycaIGQKNSSIAQ-IHASLRAAGALDYTFIVSSpaSDSPSL-QYLAPYAATAMGEYFMDQGRDVLIIYDD 260
Cdd:PRK08927 185 ---DVSVIGL---IGERGREVQEfLQDDLGPEGLARSVVVVAT--SDEPALmRRQAAYLTLAIAEYFRDQGKDVLCLMDS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 261 LSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCrlEDHWGGGSMTALPIIETQAGDVSAYIPTNVISITDGQI 340
Cdd:PRK08927 257 VTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHI 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 495796248 341 YLESHLFRSGVRPAVNTGLSVSR-VGGAAQPAgIRALAGNLRVTLARFAELE 391
Cdd:PRK08927 335 VMERAIAERGRYPAINVLKSVSRtMPGCNDPE-ENPLVRRARQLMATYADME 385
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
93-405 |
2.52e-25 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 108.07 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 93 ASVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDRQTG 172
Cdd:PRK05922 90 PSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 173 KTTI-AVDAILNQKDQNVICIYCAIGQKNSSIAQIHASLRAAgalDYTFIVSSPASDSPSLQYLAPYAATAMGEYFMDQG 251
Cdd:PRK05922 170 KSSLlSTIAKGSKSTINVIALIGERGREVREYIEQHKEGLAA---QRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 252 RDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDhwggGSMTALPIIETQAGDVSAYIPTn 331
Cdd:PRK05922 247 HRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDK----GSITALYAILHYPNHPDIFTDY- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 332 VISITDGQIYLeSHLFRSGVRPAVNTGLSVSRVGGAAQPAGIRALAGNLRVTLARFAELEVFTQFAG-------DLDDAT 404
Cdd:PRK05922 322 LKSLLDGHFFL-TPQGKALASPPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAyvpgqdaHLDRAV 400
|
.
gi 495796248 405 R 405
Cdd:PRK05922 401 K 401
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
26-342 |
3.22e-25 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 107.81 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 26 TGQVVSL-ADGiatvygldrVTYGELVVFED---DSLGMAMNLESDRVGVVLFSDGGGLREGTLCRRGGQAASVSCGDGL 101
Cdd:PRK02118 12 TGNVITVeAEG---------VGYGELATVERkdgSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 102 IGRVVNPLGEAIDGGaPIVGQKDMPVereasGVMSRKPVN--VP---LKTGILAVDALVPVGRGQRELIIGDrqTGKTTI 176
Cdd:PRK02118 83 LGRRFNGSGKPIDGG-PELEGEPIEI-----GGPSVNPVKriVPremIRTGIPMIDVFNTLVESQKIPIFSV--SGEPYN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 177 AVDA-ILNQKDQNVIcIYCAIGQKNSSIAQIHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATAMGEYF-MDQGRDV 254
Cdd:PRK02118 155 ALLArIALQAEADII-ILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFaLEGKKKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 255 LIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDvfyLHSRLLERSCRLEDHWGGGSMTALPIIETQAGDVSAYIPTNVIS 334
Cdd:PRK02118 234 LVLLTDMTNFADALKEISITMDQIPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGY 310
|
....*...
gi 495796248 335 ITDGQIYL 342
Cdd:PRK02118 311 ITEGQFYL 318
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
98-364 |
2.02e-24 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 105.64 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 98 GDGLIGRVVNPLGEAIDG-GAPIVGQKdMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDRQTGKTTI 176
Cdd:PRK07960 113 GPALLGRVLDGSGKPLDGlPAPDTGET-GALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 177 -AVDAILNQKDQNVICIycaIGQKNSSIAQIHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATAMGEYFMDQGRDVL 255
Cdd:PRK07960 192 lGMMARYTQADVIVVGL---IGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 256 IIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCRLEDhwGGGSMTALPIIETQAGDVSAYIPTNVISI 335
Cdd:PRK07960 269 LIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGDDQQDPIADSARAI 346
|
250 260
....*....|....*....|....*....
gi 495796248 336 TDGQIYLESHLFRSGVRPAVNTGLSVSRV 364
Cdd:PRK07960 347 LDGHIVLSRRLAEAGHYPAIDIEASISRA 375
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
25-91 |
7.05e-24 |
|
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: 94.44 E-value: 7.05e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495796248 25 ETGQVVSLADGIATVYGLDRVTYGELVVFEDDSLGMAMNLESDRVGVVLFSDGGGLREGTLCRRGGQ 91
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
94-393 |
1.98e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 102.75 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 94 SVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDRQTGK 173
Cdd:PRK06793 90 VIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 174 TTIAVDAILNQK-DQNVICIycaIGQKNSSIAQ-IHASLRAAGaLDYTFIVSSPASDSPSLQYLAPYAATAMGEYFMDQG 251
Cdd:PRK06793 170 STLLGMIAKNAKaDINVISL---VGERGREVKDfIRKELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 252 RDVLIIYDDLSKHAVAYRALSLLLRRSPgreaYPGDVFYLHS---RLLERSCRLEDhwggGSMTALPIIETQAGDVSAYI 328
Cdd:PRK06793 246 NNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK----GSITGIYTVLVDGDDLNGPV 317
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495796248 329 PTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRVGGAAQPAGIRALAGNLRVTLARFAELEVF 393
Cdd:PRK06793 318 PDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELY 382
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
84-364 |
1.37e-20 |
|
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: 94.40 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 84 TLCRRGGQAASVSCGDGLIGRVVNPLGEAIDGGAPIV--------GQKDMPVEREASGVMsrkpvnvpLKTGILAVDALV 155
Cdd:TIGR01040 65 TTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLaedyldinGQPINPYARIYPEEM--------IQTGISAIDVMN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 156 PVGRGQRELIIGD-------------RQTGKTTIAVDAILNQKDQNVICIYCAIGQKNSSIAQIHASLRAAGALDYTFIV 222
Cdd:TIGR01040 137 SIARGQKIPIFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLF 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 223 SSPASDSPSLQYLAPYAATAMGEYFMDQ-GRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLERSCR 301
Cdd:TIGR01040 217 LNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGR 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495796248 302 LEDHwgGGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRV 364
Cdd:TIGR01040 297 VEGR--NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 357
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
58-391 |
2.97e-20 |
|
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: 93.24 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 58 LGMAMNLESDRVGVVLFSDGGGLREGTLCRRGGQAASVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSR 137
Cdd:TIGR01039 41 LEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 138 KPVNVPLKTGILAVDALVPVGRGQRELIIGDRQTGKTTIAVDAILN-QKDQNVICIYCAIGQKNSSIAQIHASLRAAGAL 216
Cdd:TIGR01039 121 STKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKESGVI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 217 DYTFIVSSPASDSPSLQYLAPYAATAMGEYFMD-QGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAY----PGDVFYL 291
Cdd:TIGR01039 201 DKTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYqptlATEMGEL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 292 HSRLLERScrledhwgGGSMTALPIIETQAGDVSAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRVgGAAQPA 371
Cdd:TIGR01039 281 QERITSTK--------TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRL-LDPSVV 351
|
330 340
....*....|....*....|..
gi 495796248 372 GIR--ALAGNLRVTLARFAELE 391
Cdd:TIGR01039 352 GEEhyDVARGVQQILQRYKELQ 373
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
94-364 |
1.85e-15 |
|
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: 76.49 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 94 SVSCGDGLIGRVVNPLGEAIDGGAPIVGQKDMPVEREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELIIGDRQTGK 173
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 174 TTIAVDAILN-QKDQNVICIYCAIGQK----NSSIAQ-IHASLRAAGALDYTFIVSSPASDSPSLQYLAPYAATAMGEYF 247
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGERtregNDLYHEmKESGVINLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 248 MDQ-GRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGDVFYLHSRLLER--SCRledhwgGGSMTALPIIETQAGDV 324
Cdd:cd01133 161 RDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERitSTK------KGSITSVQAVYVPADDL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 495796248 325 SAYIPTNVISITDGQIYLESHLFRSGVRPAVNTGLSVSRV 364
Cdd:cd01133 235 TDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
94-363 |
6.36e-12 |
|
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: 66.06 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 94 SVSCGDGLIGRVV----NPLGEAIDGGAPIVGQKDM----PVeREASGVMSRKPVNVPLKTGILAVDALVPVGRGQRELI 165
Cdd:cd01134 3 SVELGPGLLGSIFdgiqRPLEVIAETGSIFIPRGVNvqrwPV-RQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 166 IGDRQTGKTTIAvDAILNQKDQNVIcIYCAIGQKNSSIAQIHASL-------RAAGALDYTFIVSSpASDSP------SL 232
Cdd:cd01134 82 PGPFGCGKTVIS-QSLSKWSNSDVV-IYVGCGERGNEMAEVLEEFpelkdpiTGESLMERTVLIAN-TSNMPvaareaSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 233 qylapYAATAMGEYFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGdvfYLHSRL---LERSCR---LEDHW 306
Cdd:cd01134 159 -----YTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYERAGRvrcLGSPG 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 495796248 307 GGGSMTALPIIETQAGDVSAYIPTNVISITdgQIY--LESHLFRSGVRPAVNTGLSVSR 363
Cdd:cd01134 231 REGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
24-90 |
4.30e-10 |
|
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: 55.63 E-value: 4.30e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495796248 24 RETGQVVSLADGIATVYGLDRVTYGELVVFEDDSLGMAMNLESDRVGVVLFSDGGGLREGTLCRRGG 90
Cdd:pfam02874 3 QVIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
47-279 |
1.39e-08 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 56.97 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 47 YGELVVFEDDSLGMAMN--------LESDRVGVVLFSDGGGLREGTLCRRGGQAASVSCGDGLIGRVVNPLGEAIDGGAP 118
Cdd:CHL00060 40 YNALVVKGRDTAGQEINvtcevqqlLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 119 IVGQKDMPVEREAsgvmsrkPVNVPL-------KTGILAVDALVPVGRGQRELIIGDRQTGKTTIAVDAILN-QKDQNVI 190
Cdd:CHL00060 120 VDTRTTSPIHRSA-------PAFIQLdtklsifETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 191 CIYCAIGQKNSSIAQIHASLRAAGALDYTFIVSSPAS-------DSPSLQYLAPYAATAMGEYFMDQGR-DVLIIYDDLS 262
Cdd:CHL00060 193 SVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVAlvygqmnEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIF 272
|
250
....*....|....*..
gi 495796248 263 KHAVAYRALSLLLRRSP 279
Cdd:CHL00060 273 RFVQAGSEVSALLGRMP 289
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
238-356 |
1.65e-08 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 57.34 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 238 YAATAMGEYFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGdvfYLHSRLLE------RSCRLEDHWGGGSM 311
Cdd:PRK14698 739 YTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSV 815
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 495796248 312 TALPIIETQAGDVSAYIPTNVISITDGQIYLESHLFRSGVRPAVN 356
Cdd:PRK14698 816 SVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAIN 860
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
238-313 |
1.23e-06 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 50.94 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 238 YAATAMGEYFMDQGRDVLIIYDDLSKHAVAYRALSLLLRRSPGREAYPGdvfYLHSRL---LERSCRLEDHWGG-GSMTA 313
Cdd:PRK04192 310 YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASRLaefYERAGRVKTLGGEeGSVTI 386
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
375-436 |
3.74e-05 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 41.66 E-value: 3.74e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495796248 375 ALAGNLRVTLARFAELEVFTQFAGD--LDDATREALDSGHRLTEVLKQTPGSSLSTAGQLVTLY 436
Cdd:cd01429 3 AVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLY 66
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| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
151-272 |
1.73e-03 |
|
transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]
Pssm-ID: 162030 [Multi-domain] Cd Length: 415 Bit Score: 40.83 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495796248 151 VDALVPVGRGQRELIIGDRQTGKTT----IAVDAILNQKDqnVICIYCAIGQKNSSIAQIHASLRAAgaldytfIVSS-- 224
Cdd:TIGR00767 159 LDLFAPIGKGQRGLIVAPPKAGKTVllqkIAQAITRNHPE--VELIVLLIDERPEEVTDMQRSVKGE-------VVAStf 229
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 495796248 225 --PASDSPSLQYLAPYAATAMGEyfmdQGRDVLIIYDDLSKHAVAYRALS 272
Cdd:TIGR00767 230 dePASRHVQVAEMVIEKAKRLVE----HKKDVVILLDSITRLARAYNTVT 275
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