|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-497 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 1035.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 1 MAINAQEISALIKQQIENFQPNFDVTETGVVTYIGDGIARAHGLENAMSGELLIFENGSYGMAQNLETTDVGIIILGDFT 80
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 81 DIREGDSIRRTGKIMEVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIG 160
Cdd:PRK09281 81 DIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 161 RGQRELIIGDRQTGKTSIAIDTILNQKDQDMICIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPY 240
Cdd:PRK09281 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 241 AGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVSDELGGGSITALPIIE 320
Cdd:PRK09281 241 AGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 321 TQAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAFTKFGS 400
Cdd:PRK09281 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 401 DLDAATQAKLNRGRRTVEVLKQPVHEPLTVEKQVVILYALTHGFLDSVPVDDILRFEEELFAFVEVHHPEIFETIRTTKD 480
Cdd:PRK09281 401 DLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKD 480
|
490
....*....|....*....
gi 552782762 481 LPSE--ETMDAVITDFVNQ 497
Cdd:PRK09281 481 LSDEieAKLKAAIEEFKKT 499
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-497 |
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: 1028.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 1 MAINAQEISALIKQQIENFQPNFDVTETGVVTYIGDGIARAHGLENAMSGELLIFENGSYGMAQNLETTDVGIIILGDFT 80
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 81 DIREGDSIRRTGKIMEVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIG 160
Cdd:COG0056 81 GIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 161 RGQRELIIGDRQTGKTSIAIDTILNQKDQDMICIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPY 240
Cdd:COG0056 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 241 AGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVSDELGGGSITALPIIE 320
Cdd:COG0056 241 AGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 321 TQAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAFTKFGS 400
Cdd:COG0056 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 401 DLDAATQAKLNRGRRTVEVLKQPVHEPLTVEKQVVILYALTHGFLDSVPVDDILRFEEELFAFVEVHHPEIFETIRTTKD 480
Cdd:COG0056 401 DLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGK 480
|
490
....*....|....*....
gi 552782762 481 LPSE--ETMDAVITDFVNQ 497
Cdd:COG0056 481 LDDEieEKLKAAIEEFKKT 499
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
2-495 |
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: 864.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 2 AINAQEISALIKQQIENFQPNFDVTETGVVTYIGDGIARAHGLENAMSGELLIFENGSYGMAQNLETTDVGIIILGDFTD 81
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 82 IREGDSIRRTGKIMEVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGR 161
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 162 GQRELIIGDRQTGKTSIAIDTILNQKDQDMICIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPYA 241
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 242 GVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVSDELGGGSITALPIIET 321
Cdd:TIGR00962 241 GCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 322 QAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAFTKFGSD 401
Cdd:TIGR00962 321 QAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 402 LDAATQAKLNRGRRTVEVLKQPVHEPLTVEKQVVILYALTHGFLDSVPVDDILRFEEELFAFVEVHHPEIFETIRTTKDL 481
Cdd:TIGR00962 401 LDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKL 480
|
490
....*....|....*.
gi 552782762 482 PS--EETMDAVITDFV 495
Cdd:TIGR00962 481 TEelEAKLKEALKNFK 496
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-492 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 789.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 1 MAINAQEISALIKQQIENFQPNFDVTETGVVTYIGDGIARAHGLENAMSGELLIFENGSYGMAQNLETTDVGIIILGDFT 80
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 81 DIREGDSIRRTGKIMEVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIG 160
Cdd:PRK13343 81 DILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 161 RGQRELIIGDRQTGKTSIAIDTILNQKDQDMICIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPY 240
Cdd:PRK13343 161 RGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 241 AGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVSDELGGGSITALPIIE 320
Cdd:PRK13343 241 AGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 321 TQAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAFTKFGS 400
Cdd:PRK13343 321 TLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 401 DLDAATQAKLNRGRRTVEVLKQPVHEPLTVEKQVVILYALTHGFLDSVPVDDILRFEEELFAFVEVHHPEIFETIRTTKD 480
Cdd:PRK13343 401 LLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRE 480
|
490
....*....|..
gi 552782762 481 LpSEETMDAVIT 492
Cdd:PRK13343 481 L-DEAWLAALEE 491
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
25-484 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 745.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 25 VTETGVVTYIGDGIARAHGLENAMSGELLIFENGSYGMAQNLETTDVGIIILGDFTDIREGDSIRRTGKIMEVPAGDALI 104
Cdd:CHL00059 4 IVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 105 GRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTSIAIDTIL 184
Cdd:CHL00059 84 GRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 185 NQKDQDMICIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPYAGVAMAEEFMYNGKHVLIVYDDLS 264
Cdd:CHL00059 164 NQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 265 KQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVSDELGGGSITALPIIETQAGDISAYIATNVISITDGQIFL 344
Cdd:CHL00059 244 KQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 345 QDSLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAFTKFGSDLDAATQAKLNRGRRTVEVLKQPV 424
Cdd:CHL00059 324 SADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQ 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 425 HEPLTVEKQVVILYALTHGFLDSVPVDDILRFEEELFAFVEVHHPEIFETIRTTKDLPSE 484
Cdd:CHL00059 404 SAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEE 463
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
6-492 |
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: 603.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 6 QEISALIKQQIENFQPNFDVTETGVVTYIGDGIARAHGLENAMSGELLIFENGSYGMAQNLETTDVGIIILGDFTDIREG 85
Cdd:TIGR03324 6 DKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 86 DSIRRTGKIMEVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRE 165
Cdd:TIGR03324 86 DEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 166 LIIGDRQTGKTSIAIDTILNQKDQDMICIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPYAGVAM 245
Cdd:TIGR03324 166 LILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 246 AEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVSDELGGGSITALPIIETQAGD 325
Cdd:TIGR03324 246 GEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 326 ISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAFTKFGSDLDAA 405
Cdd:TIGR03324 326 ISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDEN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 406 TQAKLNRGRRTVEVLKQPVHEPLTVEKQVVILYALTHGFLDSVPVDDILRFEEELFAFVEVHHPEIFETIRTTKDLpSEE 485
Cdd:TIGR03324 406 TRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKL-SDE 484
|
....*..
gi 552782762 486 TMDAVIT 492
Cdd:TIGR03324 485 DREQILD 491
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
94-367 |
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: 566.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 94 IMEVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQT 173
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 174 GKTSIAIDTILNQKDQDMICIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPYAGVAMAEEFMYNG 253
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 254 KHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVSDELGGGSITALPIIETQAGDISAYIATN 333
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 552782762 334 VISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVG 367
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
61-457 |
8.84e-121 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 365.90 E-value: 8.84e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 61 GMAQNLETTD-VGIIILGDFTDIREGDSIRRTGKIMEVPAGDALIGRVVNPLGQPVDgLGEIV--------TDTFRPVET 131
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVP-VGLLTrsrallesEQTLGKVDA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 132 PAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTSIAIDTILNQ--------KDQDMICIYVAIGQKES 203
Cdd:PTZ00185 159 GAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 204 TVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPYAGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGR 283
Cdd:PTZ00185 239 NVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 284 EAFPGDVFYLHSRLLERSAKVSDELGGGSITALPIIETQAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSV 363
Cdd:PTZ00185 319 EAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSV 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 364 SRVGGSAQIKAMKKVAGTLRIDLASYRELEAFTKFGSDLDAatqAKLNRGRRTVEVLKQpvHEPLTVEKQVVILYALTHG 443
Cdd:PTZ00185 399 SRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQT---VPMIRGARFVALFNQ--KNPSFFMNALVSLYACLNG 473
|
410
....*....|....
gi 552782762 444 FLDSVPVDDILRFE 457
Cdd:PTZ00185 474 YLDDVKVNYAKLYE 487
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
149-364 |
1.35e-111 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 328.93 E-value: 1.35e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 149 GLKAIDALVPIGRGQRELIIGDRQTGKTSIAiDTILNQKDQDmICIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASA 228
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD-VVVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 229 SQPSPLLFLAPYAGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVSDEl 308
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGK- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 552782762 309 gGGSITALPIIETQAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVS 364
Cdd:pfam00006 158 -GGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
133-413 |
8.98e-108 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 330.01 E-value: 8.98e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 133 APGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTSIAIDTILNQKDQDMICIYVAIGQKESTVRTQVETL 212
Cdd:PRK07165 114 AHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 213 RKYGAMDYTIVVTASASQPSPlLFLAPYAGVAMAEEFMYNgKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFY 292
Cdd:PRK07165 194 KEHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAENISYN-DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFF 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 293 LHSRLLERSAKVsdeLGGGSITALPIIETQAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQI 372
Cdd:PRK07165 272 AHSKLLERAGKF---KNRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQS 348
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 552782762 373 KAMKKVAGTLRIDLASYRELEAFTKFGSDLDAATQAKLNRG 413
Cdd:PRK07165 349 KTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKG 389
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
97-366 |
4.35e-105 |
|
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: 314.78 E-value: 4.35e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 97 VPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKT 176
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 177 SIAIDTILNQKDQD-MICIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPYAGVAMAEEFMYNGKH 255
Cdd:cd19476 82 VLAMQLARNQAKAHaGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 256 VLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVSDelGGGSITALPIIETQAGDISAYIATNVI 335
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNTF 239
|
250 260 270
....*....|....*....|....*....|.
gi 552782762 336 SITDGQIFLQDSLFNSGIRPAIDAGSSVSRV 366
Cdd:cd19476 240 AILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
371-494 |
2.86e-65 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 206.91 E-value: 2.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 371 QIKAMKKVAGTLRIDLASYRELEAFTKFGSDLDAATQAKLNRGRRTVEVLKQPVHEPLTVEKQVVILYALTHGFLDSVPV 450
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 552782762 451 DDILRFEEELFAFVEVHHPEIFETIRTTKDLPSE--ETMDAVITDF 494
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDEleEKLKEAIEEF 126
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
375-497 |
1.13e-63 |
|
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: 202.60 E-value: 1.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 375 MKKVAGTLRIDLASYRELEAFTKFGSDLDAATQAKLNRGRRTVEVLKQPVHEPLTVEKQVVILYALTHGFLDSVPVDDIL 454
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 552782762 455 RFEEELFAFVEVHHPEIFETIRTTKDL--PSEETMDAVITDFVNQ 497
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLsdELEEKLKEAIEEFKKS 125
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
96-366 |
1.03e-54 |
|
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: 184.30 E-value: 1.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 96 EVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 176 TSIaIDTILNQKDQDMICIyVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPYAGVAMAEEFMYNGKH 255
Cdd:cd01136 81 STL-LGMIARNTDADVNVI-ALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 256 VLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKvSDElggGSITALPIIETQAGDISAYIATNVI 335
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN-GEK---GSITAFYTVLVEGDDFNDPIADEVR 234
|
250 260 270
....*....|....*....|....*....|.
gi 552782762 336 SITDGQIFLQDSLFNSGIRPAIDAGSSVSRV 366
Cdd:cd01136 235 SILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
76-431 |
4.61e-51 |
|
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: 179.46 E-value: 4.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 76 LGDFTDIREGDSIRRTGKIMEVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDA 155
Cdd:COG1157 71 LGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 156 LVPIGRGQReliIGdr---qtGKTsiaidTILNqkdqdMIC-------IYVA-IGQKESTVRTQVETLRKYGAMDYTIVV 224
Cdd:COG1157 151 LLTVGRGQR---IGifagsgvGKS-----TLLG-----MIArnteadvNVIAlIGERGREVREFIEDDLGEEGLARSVVV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 225 TASASQPSPLLFLAPYAGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKV 304
Cdd:COG1157 218 VATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNG 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 305 sdelGGGSITALPIIETQAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRI 384
Cdd:COG1157 298 ----GKGSITAFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRR 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 552782762 385 DLASYRELE------AFTKfGSD--LDAATQA--KLNrgrrtvEVLKQPVHEPLTVE 431
Cdd:COG1157 374 LLARYEENEdlirigAYQP-GSDpeLDEAIALipAIE------AFLRQGMDERVSFE 423
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
76-441 |
2.55e-50 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 178.02 E-value: 2.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 76 LGDFTDIREGDSIRRTGKIMEVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDA 155
Cdd:PRK06936 76 LGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 156 LVPIGRGQRELIIGDRQTGKTSIaIDTILNQKDQDmICIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLL 235
Cdd:PRK06936 156 LLTCGEGQRMGIFAAAGGGKSTL-LASLIRSAEVD-VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMER 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 236 FLAPYAGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERsAKVSDElggGSITA 315
Cdd:PRK06936 234 AKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMER-AGQSDK---GSITA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 316 LPIIETQAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAF 395
Cdd:PRK06936 310 LYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELL 389
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 552782762 396 TKFGS---DLDAATQAKLNRGRRTVEVLKQPVHEPLTVEKQVVILYALT 441
Cdd:PRK06936 390 LQIGEyqkGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETLT 438
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
74-443 |
1.09e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 176.07 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 74 IILGDFTDIRE---GDSIRRTGKIMEVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGL 150
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 151 KAIDALVPIGRGQRELIIGDRQTGKTSIaIDTILNQKDQDMICIYVaIGQKESTVRTQVEtlRKYGA--MDYTIVVTASA 228
Cdd:PRK07721 147 RAIDSLLTVGKGQRVGIFAGSGVGKSTL-MGMIARNTSADLNVIAL-IGERGREVREFIE--RDLGPegLKRSIVVVATS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 229 SQPSPLLFLAPYAGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAkvSDEL 308
Cdd:PRK07721 223 DQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG--TNAS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 309 ggGSITALPIIETQAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLAS 388
Cdd:PRK07721 301 --GSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLST 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552782762 389 YRELEAFTKFGS-------DLDAATQAKlnrgRRTVEVLKQPVHEPLTVEKQVVILYALTHG 443
Cdd:PRK07721 379 YQNSEDLINIGAykrgssrEIDEAIQFY----PQIISFLKQGTDEKATFEESIQALLSLFGK 436
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
4-426 |
2.90e-49 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 175.00 E-value: 2.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 4 NAQEISALIKQQIE-NFQPNFDVTETGVVTYIGDGIARAhGLENAMSGELLIFENgsygmaQNLETTDVGI----IILGD 78
Cdd:PRK06820 5 DIARLTPRLQQQLTrPSAPPEGLRYRGPIVEIGPTLLRA-SLPGVAQGELCRIEP------QGMLAEVVSIeqemALLSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 79 FTD---IREGDSIRRTGKIMEVPAGDALIGRVVNPLGQPVDGlGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDA 155
Cdd:PRK06820 78 FASsdgLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 156 LVPIGRGQRELIIGDRQTGKTSIaIDTILNQKDQDMIcIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLL 235
Cdd:PRK06820 157 ILSCGEGQRIGIFAAAGVGKSTL-LGMLCADSAADVM-VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 236 FLAPYAGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKvSDElggGSITA 315
Cdd:PRK06820 235 LKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGN-SDR---GSITA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 316 LPIIETQAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAF 395
Cdd:PRK06820 311 FYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELL 390
|
410 420 430
....*....|....*....|....*....|....
gi 552782762 396 TKFG---SDLDAATQAKLNRGRRTVEVLKQPVHE 426
Cdd:PRK06820 391 VRVGeyqAGEDLQADEALQRYPAICAFLQQDHSE 424
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
77-441 |
1.31e-44 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 162.63 E-value: 1.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 77 GDFTDIREGDSIRRTGKIMEVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDAL 156
Cdd:PRK09099 78 GELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 157 VPIGRGQRELIIGDRQTGKTSIAidTILNQKDQDMICIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLF 236
Cdd:PRK09099 158 MTLGEGQRMGIFAPAGVGKSTLM--GMFARGTQCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 237 LAPYAGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVSDelggGSITAL 316
Cdd:PRK09099 236 KAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGET----GSITAL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 317 PIIETQAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAFT 396
Cdd:PRK09099 312 YTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLL 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 552782762 397 KFG---SDLDAATQAKLNRGRRTVEVLKQPVHEPLTVEKQVVILYALT 441
Cdd:PRK09099 392 QVGeyrAGSDPVADEAIAKIDAIRDFLSQRTDEYSDPDATLAALAELS 439
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
88-441 |
1.06e-42 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 157.08 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 88 IRRTGKIMEVPAGDALIGRVVNPLGQPVDGLGEIVTD----TFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQ 163
Cdd:PRK08149 73 LKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVgpisEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 164 RELIIGDRQTGKTSIaIDTILNQKDQDmicIYVA--IGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPYA 241
Cdd:PRK08149 153 RMGIFASAGCGKTSL-MNMLIEHSEAD---VFVIglIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 242 GVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKvsdeLGGGSITALPIIET 321
Cdd:PRK08149 229 ATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGA----TLAGSITAFYTVLL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 322 QAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAFTKFG-- 399
Cdd:PRK08149 305 ESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGey 384
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 552782762 400 -----SDLDAAtqakLNRGRRTVEVLKQPVHEPLTVEKQVVILYALT 441
Cdd:PRK08149 385 rrgenADNDRA----MDKRPALEAFLKQDVAEKSSFSDTLERLNEFA 427
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
28-431 |
1.98e-41 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 153.57 E-value: 1.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 28 TGVVTYIGDGIARAHgLENAMSGELL-IFENGSYGMAQNLETTDVGIIILGDFTDIREGDSIRRTGKIMEVPAGDALIGR 106
Cdd:PRK07594 22 WGRIQDVSATLLNAW-LPGVFMGELCcIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 107 VVNPLGQPVDGLgEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTSIaIDTILNQ 186
Cdd:PRK07594 101 VIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLCNA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 187 KDQDmICIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPYAGVAMAEEFMYNGKHVLIVYDDLSKQ 266
Cdd:PRK07594 179 PDAD-SNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 267 AVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVSDelggGSITALPIIETQAGDISAYIATNVISITDGQIFLQD 346
Cdd:PRK07594 258 ARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEK----GSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 347 SLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAFTKFGS---DLDAATQAKLNRGRRTVEVLKQP 423
Cdd:PRK07594 334 RLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEyqrGVDTDTDKAIDTYPDICTFLRQS 413
|
....*...
gi 552782762 424 VHEPLTVE 431
Cdd:PRK07594 414 KDEVCGPE 421
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
94-370 |
1.50e-40 |
|
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: 147.37 E-value: 1.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 94 IMEVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGD--- 170
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGsgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 171 ----------RQTGktsiaidtiLNQKDQDMICIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPY 240
Cdd:cd01135 81 phnelaaqiaRQAG---------VVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 241 AGVAMAEEFMY-NGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGdvfYLHSRL---LERSAKVSDElgGGSITAL 316
Cdd:cd01135 152 MALTTAEYLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQI 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 552782762 317 PIIETQAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSA 370
Cdd:cd01135 227 PILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSG 280
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
12-409 |
3.97e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 147.14 E-value: 3.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 12 IKQQIENFQ--PNFdvtetGVVTYIGDGIARAHGLENAMSGELLIFENGS----YGMAQNLETTDVGIIILGDFTDIREG 85
Cdd:PRK08472 6 LKNKLQKFNlsPRF-----GSITKISPTIIEADGLNPSVGDIVKIESSDNgkecLGMVVVIEKEQFGISPFSFIEGFKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 86 DSIRRTGKIMEVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRE 165
Cdd:PRK08472 81 DKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 166 LIIGDRQTGKTSIAIDTILNQKDQdmICIYVAIGQKEstvRTQVETLRKY--GAMDYTIVVTASaSQPSPLLF-LAPYAG 242
Cdd:PRK08472 161 GIFAGSGVGKSTLMGMIVKGCLAP--IKVVALIGERG---REIPEFIEKNlgGDLENTVIVVAT-SDDSPLMRkYGAFCA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 243 VAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKvsdELGGGSITALPIIETQ 322
Cdd:PRK08472 235 MSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTVLVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 323 AGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAFTKFGS-- 400
Cdd:PRK08472 312 GDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAyq 391
|
410
....*....|....
gi 552782762 401 -----DLDAATQAK 409
Cdd:PRK08472 392 kgndkELDEAISKK 405
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
96-395 |
1.11e-37 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 143.77 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 96 EVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 176 tSIAIDTILNQKDQDMICIYVaIGQKESTVRTQVETLRKYGAMDYTIVVTASASQpSPLLFL--APYAgVAMAEEFMYNG 253
Cdd:PRK07960 189 -SVLLGMMARYTQADVIVVGL-IGERGREVKDFIENILGAEGRARSVVIAAPADV-SPLLRMqgAAYA-TRIAEDFRDRG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 254 KHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVSDelGGGSITALPIIETQAGDISAYIATN 333
Cdd:PRK07960 265 QHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGDDQQDPIADS 342
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552782762 334 VISITDGQIFLQDSLFNSGIRPAIDAGSSVSRvggsaqikAMkkvagTLRIDLASYRELEAF 395
Cdd:PRK07960 343 ARAILDGHIVLSRRLAEAGHYPAIDIEASISR--------AM-----TALIDEQHYARVRQF 391
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
97-440 |
1.27e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 143.30 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 97 VPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKt 176
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGK- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 177 SIAIDTILNQKDQDMICIYVaIGQKESTVRTQVETLRKYGAMDYTIVVTASASQpSPLLFL-APYAGVAMAEEFMYNGKH 255
Cdd:PRK08972 176 SVLLGMMTRGTTADVIVVGL-VGERGREVKEFIEEILGEEGRARSVVVAAPADT-SPLMRLkGCETATTIAEYFRDQGLN 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 256 VLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVSDelGGGSITALPIIETQAGDISAYIATNVI 335
Cdd:PRK08972 254 VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVLTEGDDLQDPIADASR 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 336 SITDGQIFLQDSLFNSGIRPAIDAGSSVSRVG----GSAQIKAMKKVAGTLRI-----DLASyreLEAFTKfGSD--LDA 404
Cdd:PRK08972 332 AILDGHIVLSRELADSGHYPAIDIEASISRVMpmviSEEHLEAMRRVKQVYSLyqqnrDLIS---IGAYKQ-GSDprIDN 407
|
330 340 350
....*....|....*....|....*....|....*...
gi 552782762 405 A--TQAKLNrgrrtvEVLKQPVHEPLTVEKQVVILYAL 440
Cdd:PRK08972 408 AirLQPAMN------AFLQQTMKEAVPYDMSVNMLKQL 439
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
95-366 |
1.65e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 134.86 E-value: 1.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 95 MEVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTG 174
Cdd:PRK05688 101 GRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 175 KtSIAIDTILNQKDQDMICIYVaIGQKESTVRTQVETLRKYGAMDYTIVVtASASQPSPLLFL--APYAgVAMAEEFMYN 252
Cdd:PRK05688 181 K-SVLLGMMTRFTEADIIVVGL-IGERGREVKEFIEHILGEEGLKRSVVV-ASPADDAPLMRLraAMYC-TRIAEYFRDK 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 253 GKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAkvSDELGGGSITALPIIETQAGDISAYIAT 332
Cdd:PRK05688 257 GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEGDDQQDPIAD 334
|
250 260 270
....*....|....*....|....*....|....
gi 552782762 333 NVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRV 366
Cdd:PRK05688 335 SARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV 368
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
100-427 |
9.62e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 132.32 E-value: 9.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 100 GDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKtSIA 179
Cdd:PRK07196 93 GDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGK-SVL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 180 IDTILNQKDQDMICIYVaIGQKESTVRTQVETLRKYGAMDYTIVVTASASQpSPLLFL-APYAGVAMAEEFMYNGKHVLI 258
Cdd:PRK07196 172 LGMITRYTQADVVVVGL-IGERGREVKEFIEHSLQAAGMAKSVVVAAPADE-SPLMRIkATELCHAIATYYRDKGHDVLL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 259 VYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAkvsDELGGGSITALPIIETQAGDISAYIATNVISIT 338
Cdd:PRK07196 250 LVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQDPIVDCARAVL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 339 DGQIFLQDSLFNSGIRPAIDAGSSVSR----VGGSAQIKAMKKVAGTLRiDLASYRELEAFTKFGSDLDAATQAKLNRGR 414
Cdd:PRK07196 327 DGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCYA-DYMAIKPLIPLGGYVAGADPMADQAVHYYP 405
|
330
....*....|...
gi 552782762 415 RTVEVLKQPVHEP 427
Cdd:PRK07196 406 AITQFLRQEVGHP 418
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
20-391 |
1.59e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 132.04 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 20 QPNFDVTETGVVTYIGDGIARAHGL-ENAMSGELLIFENG---SYGMAQNLETTDVGIIILGDFTDIREGDSIRRTGKIM 95
Cdd:PRK06002 19 APEPLVRIGGTVSEVTASHYRVRGLsRFVRLGDFVAIRADggtHLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGPLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 96 EVPAgDALIGRVVNPLGQPVDGLGEIVT-DTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTG 174
Cdd:PRK06002 99 IRPD-PSWKGRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 175 KTSI--------AIDTILnqkdqdmiciyVA-IGQKESTVRTQVE-TLRkyGAMDYTIVVTASaSQPSPLLF-LAPYAGV 243
Cdd:PRK06002 178 KSTLlamlaradAFDTVV-----------IAlVGERGREVREFLEdTLA--DNLKKAVAVVAT-SDESPMMRrLAPLTAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 244 AMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVSDelGGGSITALPIIETQA 323
Cdd:PRK06002 244 AIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLVDG 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552782762 324 GDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRE 391
Cdd:PRK06002 322 DDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEE 389
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
43-365 |
2.48e-32 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 128.79 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 43 GLENAMSGEL--LIFENGSYGMAQNLETTD--VGIIILGDFTDI-REGDSIRRTGKIMEVPAGDALIGRVVNPLGQPVDG 117
Cdd:PRK04196 19 GVEGVAYGEIveIELPNGEKRRGQVLEVSEdkAVVQVFEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 118 LGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQR------------EL---IIgdRQTgktsiaidT 182
Cdd:PRK04196 99 GPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnELaaqIA--RQA--------K 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 183 ILNQKDQDMIcIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPYAGVAMAEEFMYN-GKHVLIVYD 261
Cdd:PRK04196 169 VLGEEENFAV-VFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFEkGMHVLVILT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 262 DLSKQAVAYRELSLLLRRPPGREAFPGdvfYLHSRL---LERSAKVSDElgGGSITALPIIETQAGDISAYIATNVISIT 338
Cdd:PRK04196 248 DMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHPIPDLTGYIT 322
|
330 340
....*....|....*....|....*..
gi 552782762 339 DGQIFLQDSLFNSGIRPAIDAGSSVSR 365
Cdd:PRK04196 323 EGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
86-399 |
7.94e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 127.02 E-value: 7.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 86 DSIRRTGKIMEVPAGDAL------IGRVVNPLGQPVDGLGEIVT-DTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVP 158
Cdd:PRK08927 75 EGVRRGCRAVIANAAAAVrpsrawLGRVVNALGEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 159 IGRGQRELIIGDRQTGKtSIAIDTILNQKDQDMICIYVaIGQKESTVRTQVE-TLRKYGaMDYTIVVTASASQPSPLLFL 237
Cdd:PRK08927 155 CCRGQRMGIFAGSGVGK-SVLLSMLARNADADVSVIGL-IGERGREVQEFLQdDLGPEG-LARSVVVVATSDEPALMRRQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 238 APYAGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAkvSDELGGGSITALP 317
Cdd:PRK08927 232 AAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLF 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 318 IIETQAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAFTK 397
Cdd:PRK08927 310 TVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIR 389
|
..
gi 552782762 398 FG 399
Cdd:PRK08927 390 LG 391
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
91-375 |
1.79e-29 |
|
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: 120.60 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 91 TGKIMEVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGD 170
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 171 -------------RQTGKTSIAIDTILNQKDQDMICIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFL 237
Cdd:TIGR01040 150 aglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERII 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 238 APYAGVAMAEEFMYN-GKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVsdELGGGSITAL 316
Cdd:TIGR01040 230 TPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV--EGRNGSITQI 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 552782762 317 PIIETQAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQIKAM 375
Cdd:TIGR01040 308 PILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
97-429 |
4.40e-29 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 119.24 E-value: 4.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 97 VPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKT 176
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 177 SIaIDTILnQKDQDMICIYVAIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPYAGVAMAEEFMYNGKHV 256
Cdd:PRK05922 172 SL-LSTIA-KGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 257 LIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKvSDElggGSITALPIIETQAG--DIsayIATNV 334
Cdd:PRK05922 250 LFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-NDK---GSITALYAILHYPNhpDI---FTDYL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 335 ISITDGQIFL--QDSLFNSgirPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAFTKFGSdLDAATQAKLNR 412
Cdd:PRK05922 323 KSLLDGHFFLtpQGKALAS---PPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGA-YVPGQDAHLDR 398
|
330
....*....|....*..
gi 552782762 413 GRRTVEVLKQPVHEPLT 429
Cdd:PRK05922 399 AVKLLPSIKQFLSQPLS 415
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
27-93 |
1.72e-28 |
|
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: 107.54 E-value: 1.72e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552782762 27 ETGVVTYIGDGIARAHGLENAMSGELLIFENGSYGMAQNLETTDVGIIILGDFTDIREGDSIRRTGK 93
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
85-460 |
1.61e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 108.53 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 85 GDSIRRTGKIMEVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQR 164
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 165 ELIIGDRQTGKTSIaIDTILNQKDQDMICIYVaIGQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPYAGVA 244
Cdd:PRK06793 159 IGIFAGSGVGKSTL-LGMIAKNAKADINVISL-VGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATS 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 245 MAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLLRRPPgreaFPGDVFYLHS---RLLERSAKVSDelggGSITALPIIET 321
Cdd:PRK06793 237 IAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK----GSITGIYTVLV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 322 QAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAFTKFGSD 401
Cdd:PRK06793 309 DGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTI 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 552782762 402 LDAATQAKLNRGRRTVEVLKQpvhepltvekqvvilyALTHGFLDSVPVDDILRFEEEL 460
Cdd:PRK06793 389 QENAENAYIFECKNKVEGINT----------------FLKQGRSDSFQFDDIVEAMHHI 431
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
45-365 |
2.63e-24 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 105.12 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 45 ENAMSGELLIFEN---GSYGMAQNLETTDVGIIILGDFTDIREGDSIRRTGKIMEVPAGDALIGRVVNPLGQPVDGLGEI 121
Cdd:PRK02118 21 EGVGYGELATVERkdgSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 122 VTDtfrPVETPAPGV--MQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDrqTGKTSIAI-DTILNQKDQDMIcIYVAI 198
Cdd:PRK02118 101 EGE---PIEIGGPSVnpVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSV--SGEPYNALlARIALQAEADII-ILGGM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 199 GQKESTVRTQVETLRKYGAMDYTIVVTASASQPSPLLFLAPYAGVAMAEEFMYNG-KHVLIVYDDLSKQAVAYRELSLLL 277
Cdd:PRK02118 175 GLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLTDMTNFADALKEISITM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 278 RRPPGREAFPGDvfyLHSRLLERSAKVSDELGGGSITALPIIETQAGDISAYIATNVISITDGQIFLQdslfnsgiRPAI 357
Cdd:PRK02118 255 DQIPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLR--------RGRI 323
|
....*...
gi 552782762 358 DAGSSVSR 365
Cdd:PRK02118 324 DPFGSLSR 331
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-366 |
4.25e-21 |
|
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: 93.05 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 96 EVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 176 TSIAIDTILN-QKDQDMICIYVAIGQ------------KESTVrtqvetlRKYGAMDYTIVVTASASQPSPLLFLAPYAG 242
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGErtregndlyhemKESGV-------INLDGLSKVALVYGQMNEPPGARARVALTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 243 VAMAEEFM-YNGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVSDelggGSITALPIIET 321
Cdd:cd01133 154 LTMAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKK----GSITSVQAVYV 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 552782762 322 QAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVSRV 366
Cdd:cd01133 230 PADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
128-365 |
1.25e-15 |
|
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: 77.23 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 128 PVETPAPgVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTSIaIDTILNQKDQDMIcIYVAIGQKESTVrt 207
Cdd:cd01134 43 PVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVI-SQSLSKWSNSDVV-IYVGCGERGNEM-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 208 qVETLRKY----------GAMDYTIVVTASASQPSPLLFLAPYAGVAMAEEFMYNGKHVLIVYDDLSKQAVAYRELSLLL 277
Cdd:cd01134 118 -AEVLEEFpelkdpitgeSLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 278 RRPPGREAFPGdvfYLHSRL---LERSAKVSdELGG----GSITALPIIETQAGDISAYIATNVISITdgQIF--LQDSL 348
Cdd:cd01134 197 EEMPAEEGYPA---YLGARLaefYERAGRVR-CLGSpgreGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKL 270
|
250
....*....|....*..
gi 552782762 349 FNSGIRPAIDAGSSVSR 365
Cdd:cd01134 271 AQRRHFPSINWLISYSK 287
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
80-393 |
1.59e-13 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 72.77 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 80 TD-IREGDSIRRTGKIMEVPAGDALIGRVVNPLGQPVDGLGEIVTDTFRPVETPAPGVMQRKSVSEPLQTGLKAIDALVP 158
Cdd:CHL00060 78 TDgLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 159 IGRGQRELIIGDRQTGKTSIAIDTILN-QKDQDMICIYVAIGQ------------KESTV-RTQVETLRK----YGAMDY 220
Cdd:CHL00060 158 YRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGErtregndlymemKESGViNEQNIAESKvalvYGQMNE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 221 TivvtasasqPSPLLFLAPYAgVAMAEEFM-YNGKHVLIVYDDLSKQAVAYRELSLLLRRppgreaFPGDVFY---LHSR 296
Cdd:CHL00060 238 P---------PGARMRVGLTA-LTMAEYFRdVNKQDVLLFIDNIFRFVQAGSEVSALLGR------MPSAVGYqptLSTE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 297 ---LLERSAKVSDelggGSITALPIIETQAGDISAYIATNVISITDGQIFLQDSLFNSGIRPAIDAGSSVS-----RVGG 368
Cdd:CHL00060 302 mgsLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTStmlqpRIVG 377
|
330 340
....*....|....*....|....*
gi 552782762 369 SAQIKAMKKVAGTLRidlaSYRELE 393
Cdd:CHL00060 378 EEHYETAQRVKQTLQ----RYKELQ 398
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
27-92 |
1.67e-13 |
|
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: 65.26 E-value: 1.67e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552782762 27 ETGVVTYIGDGIARAHGLENAMSGELLIFENGSYGMAQNLETTDVGIIILGDFTDIREGDSIRRTG 92
Cdd:pfam02874 4 VIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
375-441 |
2.56e-13 |
|
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: 64.77 E-value: 2.56e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552782762 375 MKKVAGTLRIDLASYRELEAFTKFGSD--LDAATQAKLNRGRRTVEVLKQPVHEPLTVEKQVVILYALT 441
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIK 69
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
116-315 |
4.09e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 62.11 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 116 DGLGEIVTDTFR-PVETPAPgVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTsIAIDTILNQKDQDmICI 194
Cdd:PRK04192 181 DGEGVELTMMQKwPVRRPRP-YKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT-VTQHQLAKWADAD-IVI 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 195 YVAIGQKESTVrtqVETLR--------KYGA--MDYTIVVTASASQPspllfLAP-----YAGVAMAEEFMYNGKHVLIV 259
Cdd:PRK04192 258 YVGCGERGNEM---TEVLEefpelidpKTGRplMERTVLIANTSNMP-----VAAreasiYTGITIAEYYRDMGYDVLLM 329
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552782762 260 YDDLSKQAVAYRELSLLLRRPPGREAFPGdvfYLHSRL---LERSAKVSdELGG--GSITA 315
Cdd:PRK04192 330 ADSTSRWAEALREISGRLEEMPGEEGYPA---YLASRLaefYERAGRVK-TLGGeeGSVTI 386
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
192-337 |
2.46e-07 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 53.49 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552782762 192 ICIYVAIGQKESTVRTQVETLRKYG-------AMDYTIVVTASASQPSPLLFLAPYAGVAMAEEFMYNGKHVLIVYDDLS 264
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPKLKdpktgkpLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTS 763
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552782762 265 KQAVAYRELSLLLRRPPGREAFPGdvfYLHSRLLE------RSAKVSDELGGGSITALPIIETQAGDISAYIATNVISI 337
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRV 839
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
151-192 |
9.94e-03 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 37.96 E-value: 9.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 552782762 151 KAIDALVPIGRGQRELIIGDRQTGKT----SIAIDTILNQKDQDMI 192
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTtllqNIANAIAKNHPEVELI 50
|
|
| |
