|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-502 |
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: 1063.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 1 MSINAEEISTLIKKQIENFDSDIEVTDVGTVIEIGDGIARAHGLDNAMAGELLEFSNGVMGLAQNLEESNVGIVILGPYE 80
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 81 EIKEGDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIG 160
Cdd:COG0056 81 GIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 161 RGQRELIIGDRQTGKTTVAVDTILNQADQDMICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPY 240
Cdd:COG0056 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 241 AGVAMGEEFMYNGKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKLSDAKGGGSLTALPFVE 320
Cdd:COG0056 241 AGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 321 TQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFRELEAFSQFGS 400
Cdd:COG0056 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 401 DLDKATQAKLNRGQRTVEVLKQGLHKPMGVEKQVAIIYALTRGFLDDIPVEDIQRFEEEMNIWIEHNQNDIFTTIRETGA 480
Cdd:COG0056 401 DLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGK 480
|
490 500
....*....|....*....|....
gi 755605751 481 LPDD--KEFSGAIESFKNTFLPSN 502
Cdd:COG0056 481 LDDEieEKLKAAIEEFKKTFAASA 504
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-500 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 1062.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 1 MSINAEEISTLIKKQIENFDSDIEVTDVGTVIEIGDGIARAHGLDNAMAGELLEFSNGVMGLAQNLEESNVGIVILGPYE 80
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 81 EIKEGDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIG 160
Cdd:PRK09281 81 DIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 161 RGQRELIIGDRQTGKTTVAVDTILNQADQDMICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPY 240
Cdd:PRK09281 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 241 AGVAMGEEFMYNGKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKLSDAKGGGSLTALPFVE 320
Cdd:PRK09281 241 AGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 321 TQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFRELEAFSQFGS 400
Cdd:PRK09281 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 401 DLDKATQAKLNRGQRTVEVLKQGLHKPMGVEKQVAIIYALTRGFLDDIPVEDIQRFEEEMNIWIEHNQNDIFTTIRETGA 480
Cdd:PRK09281 401 DLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKD 480
|
490 500
....*....|....*....|..
gi 755605751 481 LPDD--KEFSGAIESFKNTFLP 500
Cdd:PRK09281 481 LSDEieAKLKAAIEEFKKTFAA 502
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
2-500 |
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: 895.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 2 SINAEEISTLIKKQIENFDSDIEVTDVGTVIEIGDGIARAHGLDNAMAGELLEFSNGVMGLAQNLEESNVGIVILGPYEE 81
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 82 IKEGDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGR 161
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 162 GQRELIIGDRQTGKTTVAVDTILNQADQDMICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPYA 241
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 242 GVAMGEEFMYNGKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKLSDAKGGGSLTALPFVET 321
Cdd:TIGR00962 241 GCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 322 QAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFRELEAFSQFGSD 401
Cdd:TIGR00962 321 QAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 402 LDKATQAKLNRGQRTVEVLKQGLHKPMGVEKQVAIIYALTRGFLDDIPVEDIQRFEEEMNIWIEHNQNDIFTTIRETGAL 481
Cdd:TIGR00962 401 LDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKL 480
|
490 500
....*....|....*....|.
gi 755605751 482 PDDKE--FSGAIESFKNTFLP 500
Cdd:TIGR00962 481 TEELEakLKEALKNFKKTFAW 501
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-498 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 795.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 1 MSINAEEISTLIKKQIENFDSDIEVTDVGTVIEIGDGIARAHGLDNAMAGELLEFSNGVMGLAQNLEESNVGIVILGPYE 80
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 81 EIKEGDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIG 160
Cdd:PRK13343 81 DILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 161 RGQRELIIGDRQTGKTTVAVDTILNQADQDMICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPY 240
Cdd:PRK13343 161 RGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 241 AGVAMGEEFMYNGKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKLSDAKGGGSLTALPFVE 320
Cdd:PRK13343 241 AGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 321 TQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFRELEAFSQFGS 400
Cdd:PRK13343 321 TLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 401 DLDKATQAKLNRGQRTVEVLKQGLHKPMGVEKQVAIIYALTRGFLDDIPVEDIQRFEEEMNIWIEHNQNDIFTTIRETGA 480
Cdd:PRK13343 401 LLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRE 480
|
490 500
....*....|....*....|
gi 755605751 481 LPDD--KEFSGAIESFKNTF 498
Cdd:PRK13343 481 LDEAwlAALEEILREAGERF 500
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
22-503 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 774.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 22 DIEVTDVGTVIEIGDGIARAHGLDNAMAGELLEFSNGVMGLAQNLEESNVGIVILGPYEEIKEGDEVRRTGRIMQVPAGE 101
Cdd:CHL00059 1 EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 102 ELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTVAVD 181
Cdd:CHL00059 81 AYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 182 TILNQADQDMICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPYAGVAMGEEFMYNGKHVLVVYD 261
Cdd:CHL00059 161 TILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 262 DLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKLSDAKGGGSLTALPFVETQAGDISAYIPTNVISITDGQ 341
Cdd:CHL00059 241 DLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 342 IFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFRELEAFSQFGSDLDKATQAKLNRGQRTVEVLK 421
Cdd:CHL00059 321 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 422 QGLHKPMGVEKQVAIIYALTRGFLDDIPVEDIQRFEEEMNIWIEHNQNDIFTTIRETGALPDDKE--FSGAIESFKNTFL 499
Cdd:CHL00059 401 QSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEalLKEAIQEQLELFL 480
|
....
gi 755605751 500 PSNQ 503
Cdd:CHL00059 481 LQEQ 484
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
6-451 |
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: 587.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 6 EEISTLIKKQIENFDSDIEVTDVGTVIEIGDGIARAHGLDNAMAGELLEFSNGVMGLAQNLEESNVGIVILGPYEEIKEG 85
Cdd:TIGR03324 6 DKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 86 DEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRE 165
Cdd:TIGR03324 86 DEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 166 LIIGDRQTGKTTVAVDTILNQADQDMICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPYAGVAM 245
Cdd:TIGR03324 166 LILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 246 GEEFMYNGKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKLSDAKGGGSLTALPFVETQAGD 325
Cdd:TIGR03324 246 GEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 326 ISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFRELEAFSQFGSDLDKA 405
Cdd:TIGR03324 326 ISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDEN 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 755605751 406 TQAKLNRGQRTVEVLKQGLHKPMGVEKQVAIIYALTRGFLDDIPVE 451
Cdd:TIGR03324 406 TRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLD 451
|
|
| 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: 576.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 94 IMQVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQT 173
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 174 GKTTVAVDTILNQADQDMICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPYAGVAMGEEFMYNG 253
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 254 KHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKLSDAKGGGSLTALPFVETQAGDISAYIPTN 333
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 755605751 334 VISITDGQIFLQSDLFFSGVRPAINPGLSVSRVG 367
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
61-457 |
2.01e-124 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 375.15 E-value: 2.01e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 61 GLAQNLE-ESNVGIVILGPYEEIKEGDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDgQGAIETSK--------MRPIEA 131
Cdd:PTZ00185 80 GLVFNLEkDGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVP-VGLLTRSRalleseqtLGKVDA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 132 QAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTVAVDTILNQ--------ADQDMICIYVAIGQKES 203
Cdd:PTZ00185 159 GAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 204 TVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPYAGVAMGEEFMYNGKHVLVVYDDLSKQAVAYRELSLLLRRPPGR 283
Cdd:PTZ00185 239 NVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 284 EAFPGDVFYLHSRLLERAAKLSDAKGGGSLTALPFVETQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSV 363
Cdd:PTZ00185 319 EAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSV 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 364 SRVGGSAQIKAMKKVAGTLRLDLASFRELEAFSQFGSdldKATQAKLNRGQRTVEVLKQglHKPMGVEKQVAIIYALTRG 443
Cdd:PTZ00185 399 SRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGS---QVQTVPMIRGARFVALFNQ--KNPSFFMNALVSLYACLNG 473
|
410
....*....|....
gi 755605751 444 FLDDIPVEDIQRFE 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 |
5.40e-116 |
|
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: 340.49 E-value: 5.40e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 149 GIKAIDALVPIGRGQRELIIGDRQTGKTTVAvDTILNQADQDmICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGA 228
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD-VVVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 229 SDPAPLLYLSPYAGVAMGEEFMYNGKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKLSDak 308
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKG-- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 755605751 309 GGGSLTALPFVETQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVS 364
Cdd:pfam00006 157 KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
80-496 |
3.55e-109 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 333.86 E-value: 3.55e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 80 EEIKEGDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAIETSK-----MRPIEAQAPGVMDRKSVDEPLQTGIKAID 154
Cdd:PRK07165 56 GKIKINDELIELNNTNKVKTSKEYFGKIIDIDGNIIYPEAQNPLSKkflpnTSSIFNLAHGLMTVKTLNEQLYTGIIAID 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 155 ALVPIGRGQRELIIGDRQTGKTTVAVDTILNQADQDMICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPl 234
Cdd:PRK07165 136 LLIPIGKGQRELIIGDRQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSPYE- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 235 LYLSPYAGVAMGEEFMYNgKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKLsdaKGGGSLT 314
Cdd:PRK07165 215 QYLAPYVAMAHAENISYN-DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKF---KNRKTIT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 315 ALPFVETQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFRELEA 394
Cdd:PRK07165 291 ALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLK 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 395 FSQFGSDLDKATQAKLNRGQRTVEVLKQGLHKPMGVEKQVAIIYALTRGFLDDipVEDIQRFEEEMNIWIEHNQN--DIF 472
Cdd:PRK07165 371 LSMLDYDLNKETSDLLFKGKMIEKMFNQKGFSLYSYRFVLLISKLISWGLLKD--VKDEQKALDFIDYLIENDPDakKIF 448
|
410 420
....*....|....*....|....*...
gi 755605751 473 TTIrETGALPDDK----EFSGAIESFKN 496
Cdd:PRK07165 449 NKI-KNNEDVDDElmknYFAFLLNQYSD 475
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
96-366 |
3.00e-107 |
|
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: 320.56 E-value: 3.00e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 96 QVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 176 TTVAVDTILNQADQD-MICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPYAGVAMGEEFMYNGK 254
Cdd:cd19476 81 TVLAMQLARNQAKAHaGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 255 HVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKLSDakGGGSLTALPFVETQAGDISAYIPTNV 334
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 755605751 335 ISITDGQIFLQSDLFFSGVRPAINPGLSVSRV 366
Cdd:cd19476 239 FAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
371-494 |
5.89e-63 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 201.13 E-value: 5.89e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 371 QIKAMKKVAGTLRLDLASFRELEAFSQFGSDLDKATQAKLNRGQRTVEVLKQGLHKPMGVEKQVAIIYALTRGFLDDIPV 450
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 755605751 451 EDIQRFEEEMNIWIEHNQNDIFTTIRETGALPDD--KEFSGAIESF 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 ... |
375-498 |
1.04e-62 |
|
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349748 [Multi-domain] Cd Length: 126 Bit Score: 200.28 E-value: 1.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 375 MKKVAGTLRLDLASFRELEAFSQFGSDLDKATQAKLNRGQRTVEVLKQGLHKPMGVEKQVAIIYALTRGFLDDIPVEDIQ 454
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 755605751 455 RFEEEMNIWIEHNQNDIFTTIRETGALPDD--KEFSGAIESFKNTF 498
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDEleEKLKEAIEEFKKSF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
96-366 |
1.86e-51 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 175.83 E-value: 1.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 96 QVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 176 TTVaVDTILNQADQDMICIyVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPYAGVAMGEEFMYNGKH 255
Cdd:cd01136 81 STL-LGMIARNTDADVNVI-ALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 256 VLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKLSDakggGSLTALPFVETQAGDISAYIPTNVI 335
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----GSITAFYTVLVEGDDFNDPIADEVR 234
|
250 260 270
....*....|....*....|....*....|.
gi 755605751 336 SITDGQIFLQSDLFFSGVRPAINPGLSVSRV 366
Cdd:cd01136 235 SILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
76-442 |
4.02e-51 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 179.95 E-value: 4.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 76 LGPYEEIKEGDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDA 155
Cdd:PRK06936 76 LGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 156 LVPIGRGQRELIIGDRQTGKTTVaVDTILNQADQDmICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLL 235
Cdd:PRK06936 156 LLTCGEGQRMGIFAAAGGGKSTL-LASLIRSAEVD-VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMER 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 236 YLSPYAGVAMGEEFMYNGKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKlSDAkggGSLTA 315
Cdd:PRK06936 234 AKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ-SDK---GSITA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 316 LPFVETQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFRELEAF 395
Cdd:PRK06936 310 LYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELL 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 755605751 396 SQFGS---DLDKATQAKLNRGQRTVEVLKQGLHKPMGVEKQVAIIYALTR 442
Cdd:PRK06936 390 LQIGEyqkGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETLTQ 439
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-422 |
1.52e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 173.08 E-value: 1.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 29 GTVIEIGDGIARAhGLDNAMAGELLEFSNgvmglaQNLEESNVGI----VILGPYEE---IKEGDEVRRTGRIMQVPAGE 101
Cdd:PRK06820 31 GPIVEIGPTLLRA-SLPGVAQGELCRIEP------QGMLAEVVSIeqemALLSPFASsdgLRCGQWVTPLGHMHQVQVGA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 102 ELLGRVVNPLGQPIDGqGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTVaVD 181
Cdd:PRK06820 104 DLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTL-LG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 182 TILNQADQDMIcIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPYAGVAMGEEFMYNGKHVLVVYD 261
Cdd:PRK06820 182 MLCADSAADVM-VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMAD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 262 DLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKlSDAkggGSLTALPFVETQAGDISAYIPTNVISITDGQ 341
Cdd:PRK06820 261 SLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGN-SDR---GSITAFYTVLVEGDDMNEPVADEVRSLLDGH 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 342 IFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFRELEAFSQFG---SDLDKATQAKLNRGQRTVE 418
Cdd:PRK06820 337 IVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGeyqAGEDLQADEALQRYPAICA 416
|
....
gi 755605751 419 VLKQ 422
Cdd:PRK06820 417 FLQQ 420
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
28-431 |
1.46e-47 |
|
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: 170.21 E-value: 1.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 28 VGTVIEIGDGIARAHGLDNAMaGELLEFSNG--------VMGLAQnleesnvGIVILGPYEE---IKEGDEVRRTGRIMQ 96
Cdd:COG1157 20 SGRVTRVVGLLIEAVGPDASI-GELCEIETAdgrpvlaeVVGFRG-------DRVLLMPLGDlegISPGARVVPTGRPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 97 VPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQReliIGdr---qt 173
Cdd:COG1157 92 VPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR---IGifagsgv 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 174 GKTTVaVDTILNQADQDMICIyvA-IGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPYAGVAMGEEFMYN 252
Cdd:COG1157 169 GKSTL-LGMIARNTEADVNVI--AlIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 253 GKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKlsdaKGGGSLTALPFVETQAGDISAYIPT 332
Cdd:COG1157 246 GKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN----GGKGSITAFYTVLVEGDDMNDPIAD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 333 NVISITDGQIFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFRELE------AFsQFGSD--LDK 404
Cdd:COG1157 322 AVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEdlirigAY-QPGSDpeLDE 400
|
410 420
....*....|....*....|....*....
gi 755605751 405 ATQA--KLNrgqrtvEVLKQGLHKPMGVE 431
Cdd:COG1157 401 AIALipAIE------AFLRQGMDERVSFE 423
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
29-399 |
4.97e-46 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 166.48 E-value: 4.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 29 GTVIEIGDGIARAHGLDNAMaGELLEFSNGVMGLAQNLEEsnVG----IVILGPY---EEIKEGDEVRRTGRIMQVPAGE 101
Cdd:PRK09099 26 GKVVEVIGTLLRVSGLDVTL-GELCELRQRDGTLLQRAEV--VGfsrdVALLSPFgelGGLSRGTRVIGLGRPLSVPVGP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 102 ELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTVAvd 181
Cdd:PRK09099 103 ALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLM-- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 182 TILNQADQDMICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPYAGVAMGEEFMYNGKHVLVVYD 261
Cdd:PRK09099 181 GMFARGTQCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 262 DLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAkLSDAkggGSLTALPFVETQAGDISAYIPTNVISITDGQ 341
Cdd:PRK09099 261 SLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-MGET---GSITALYTVLAEDESGSDPIAEEVRGILDGH 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 755605751 342 IFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFRELEAFSQFG 399
Cdd:PRK09099 337 MILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVG 394
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
29-423 |
3.12e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 164.09 E-value: 3.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 29 GTVIEIGDGIARAHGLDNAMAG----ELLEFSNGVMGLAQNLEESNVGIVILGPYEEIKEGDEVRRTGRIMQVPAGEELL 104
Cdd:PRK08472 20 GSITKISPTIIEADGLNPSVGDivkiESSDNGKECLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 105 GRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTVaVDTIL 184
Cdd:PRK08472 100 GRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTL-MGMIV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 185 NQADQDmICIYVAIGQKEstvRSTVETFRKH--GALDYTIVVSAgASDPAPLL--YlSPYAGVAMGEEFMYNGKHVLVVY 260
Cdd:PRK08472 179 KGCLAP-IKVVALIGERG---REIPEFIEKNlgGDLENTVIVVA-TSDDSPLMrkY-GAFCAMSVAEYFKNQGLDVLFIM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 261 DDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKlsdAKGGGSLTALPFVETQAGDISAYIPTNVISITDG 340
Cdd:PRK08472 253 DSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 341 QIFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFRELEAFSQFGS-------DLDKAtqakLNRG 413
Cdd:PRK08472 330 HIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAyqkgndkELDEA----ISKK 405
|
410
....*....|
gi 755605751 414 QRTVEVLKQG 423
Cdd:PRK08472 406 EFMEQFLKQN 415
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
74-443 |
4.57e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 161.04 E-value: 4.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 74 VILGPYEEIKE---GDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGI 150
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 151 KAIDALVPIGRGQRELIIGDRQTGKTTVaVDTILNQADQDMICIYVaIGQKESTVRSTVETFRKHGALDYTIVVSAGASD 230
Cdd:PRK07721 147 RAIDSLLTVGKGQRVGIFAGSGVGKSTL-MGMIARNTSADLNVIAL-IGERGREVREFIERDLGPEGLKRSIVVVATSDQ 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 231 PAPLLYLSPYAGVAMGEEFMYNGKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAklsdAKGG 310
Cdd:PRK07721 225 PALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG----TNAS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 311 GSLTALPFVETQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFR 390
Cdd:PRK07721 301 GSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQ 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 391 ELEAFSQFGS-------DLDKATQAKlnrgQRTVEVLKQGLHKPMGVEKQVAIIYALTRG 443
Cdd:PRK07721 381 NSEDLINIGAykrgssrEIDEAIQFY----PQIISFLKQGTDEKATFEESIQALLSLFGK 436
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
94-380 |
2.47e-42 |
|
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: 151.99 E-value: 2.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 94 IMQVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQT 173
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 174 GKTTVAVdTILNQA-----DQDMICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPYAGVAMGEE 248
Cdd:cd01135 81 PHNELAA-QIARQAgvvgsEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 249 FMY-NGKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGdvfYLHSRL---LERAAKLSDAKggGSLTALPFVETQAG 324
Cdd:cd01135 160 LAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGRK--GSITQIPILTMPND 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 755605751 325 DISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVSRVggsaqikaMKKVAG 380
Cdd:cd01135 235 DITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRL--------MKSGIG 282
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
29-452 |
4.93e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 147.45 E-value: 4.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 29 GTVIEIGDGIARAHGL-DNAMAGELLEF-SNGVMGLAQ--NLEESNVGIVILGPYEEIKEGDEVRRTGRiMQVPAGEELL 104
Cdd:PRK06002 28 GTVSEVTASHYRVRGLsRFVRLGDFVAIrADGGTHLGEvvRVDPDGVTVKPFEPRIEIGLGDAVFRKGP-LRIRPDPSWK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 105 GRVVNPLGQPIDGQGAIET-SKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTVAvdTI 183
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLL--AM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 184 LNQADQ-DMICIYVaIGQKESTVRSTVE-TFRKHgaLDYTIVVSAgASDPAPLLY-LSPYAGVAMGEEFMYNGKHVLVVY 260
Cdd:PRK06002 185 LARADAfDTVVIAL-VGERGREVREFLEdTLADN--LKKAVAVVA-TSDESPMMRrLAPLTATAIAEYFRDRGENVLLIV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 261 DDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAklSDAKGGGSLTALPFVETQAGDISAYIPTNVISITDG 340
Cdd:PRK06002 261 DSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAG--PGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 341 QIFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASF---RELEAFS--QFGSD--LDKATqaklnrg 413
Cdd:PRK06002 339 HIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFeetRDLRLIGgyRAGSDpdLDQAV------- 411
|
410 420 430
....*....|....*....|....*....|....*....
gi 755605751 414 qrtvevlkqglhkpmgveKQVAIIYALTRGFLDDIPVED 452
Cdd:PRK06002 412 ------------------DLVPRIYEALRQSPGDPPSDD 432
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-429 |
2.29e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 145.10 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 29 GTVIEIGDGIARAHgLDNAMAGELLEFSNGvMGLAQ--NLEESNVGIVILGPYEEIKEGDEVRRTGRIMQVPAGEELLGR 106
Cdd:PRK07594 23 GRIQDVSATLLNAW-LPGVFMGELCCIKPG-EELAEvvGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 107 VVNPLGQPIDGQGAIETSkMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTVaVDTILNQ 186
Cdd:PRK07594 101 VIDGFGRPLDGRELPDVC-WKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLCNA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 187 ADQDmICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPYAGVAMGEEFMYNGKHVLVVYDDLSKQ 266
Cdd:PRK07594 179 PDAD-SNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 267 AVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKLSDakggGSLTALPFVETQAGDISAYIPTNVISITDGQIFLQS 346
Cdd:PRK07594 258 ARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEK----GSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 347 DLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFRELEAFSQFG-------SDLDKATQAK------LNRG 413
Cdd:PRK07594 334 RLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGeyqrgvdTDTDKAIDTYpdictfLRQS 413
|
410
....*....|....*....
gi 755605751 414 QRTV---EVLKQGLHKPMG 429
Cdd:PRK07594 414 KDEVcgpELLIEKLHQILT 432
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
59-440 |
7.66e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 138.71 E-value: 7.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 59 VMGLaqnlEESNVGIVILGPYEEIKEGDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMD 138
Cdd:PRK05688 69 VMGF----SGDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLN 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 139 RKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTT-VAVDTILNQADqdmICIYVAIGQKESTVRSTVETFRKHGA 217
Cdd:PRK05688 145 RHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVlLGMMTRFTEAD---IIVVGLIGERGREVKEFIEHILGEEG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 218 LDYTIVVSAGASDpAPLLYL--SPYAgVAMGEEFMYNGKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHS 295
Cdd:PRK05688 222 LKRSVVVASPADD-APLMRLraAMYC-TRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLP 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 296 RLLERAAklSDAKGGGSLTALPFVETQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVSRVggsaqikaM 375
Cdd:PRK05688 300 KLVERAG--NAEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV--------M 369
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755605751 376 KKVAGTLRLDLAS-FRELEAFSQFGSDL----------DKATQAKLNRGQRTVEVLKQGLHKPMGVEKQVAIIYAL 440
Cdd:PRK05688 370 PQVVDPEHLRRAQrFKQLWSRYQQSRDLisvgayvaggDPETDLAIARFPHLVQFLRQGLRENVSLAQSREQLAAI 445
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
91-399 |
1.28e-35 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 137.43 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 91 TGRIMQVPAGEELLGRVVNPLGQPIDGQGAIET----SKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQREL 166
Cdd:PRK08149 76 TGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTvgpiSEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 167 IIGDRQTGKTTVaVDTILNQADQDmicIYVA--IGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPYAGVA 244
Cdd:PRK08149 156 IFASAGCGKTSL-MNMLIEHSEAD---VFVIglIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 245 MGEEFMYNGKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKLSDakggGSLTALPFVETQAG 324
Cdd:PRK08149 232 VAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA----GSITAFYTVLLESE 307
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755605751 325 DISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFRELEAFSQFG 399
Cdd:PRK08149 308 EEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLG 382
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
47-409 |
1.47e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 137.52 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 47 AMAGELLEfsnGVMGLAQNleesnvgIVILGPYEEIK---EGDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAIET 123
Cdd:PRK08972 54 TMAGELEA---EVVGFDGD-------LLYLMPIEELRgvlPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 124 SKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKT-TVAVDTILNQADqdmICIYVAIGQKE 202
Cdd:PRK08972 124 DQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSvLLGMMTRGTTAD---VIVVGLVGERG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 203 STVRSTVETFRKHGALDYTIVVSAGAsDPAPLLYLSP-YAGVAMGEEFMYNGKHVLVVYDDLSKQAVAYRELSLLLRRPP 281
Cdd:PRK08972 201 REVKEFIEEILGEEGRARSVVVAAPA-DTSPLMRLKGcETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 282 GREAFPGDVFYLHSRLLERAAKLSDakGGGSLTALPFVETQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGL 361
Cdd:PRK08972 280 ATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEA 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 755605751 362 SVSRVG----GSAQIKAMKKVAGTLRL-----DLASfreLEAFSQfGSD--LDKATQAK 409
Cdd:PRK08972 358 SISRVMpmviSEEHLEAMRRVKQVYSLyqqnrDLIS---IGAYKQ-GSDprIDNAIRLQ 412
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
88-365 |
8.73e-35 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 135.72 E-value: 8.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 88 VRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELI 167
Cdd:PRK04196 69 VRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 168 IGDRQTGKTTVAVDtILNQA-----DQDMICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYLSPYAG 242
Cdd:PRK04196 149 FSGSGLPHNELAAQ-IARQAkvlgeEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 243 VAMGEEFMYN-GKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGdvfYLHSRL---LERAAKLSDAKggGSLTALPF 318
Cdd:PRK04196 228 LTAAEYLAFEkGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGKK--GSITQIPI 302
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 755605751 319 VETQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVSR 365
Cdd:PRK04196 303 LTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
96-407 |
3.03e-34 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 134.14 E-value: 3.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 96 QVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 176 tTVAVDTILNQADQDMICIYVaIGQKESTVRSTVETFRKHGALDYTIVVSAGAsDPAPLLYL--SPYAgVAMGEEFMYNG 253
Cdd:PRK07960 189 -SVLLGMMARYTQADVIVVGL-IGERGREVKDFIENILGAEGRARSVVIAAPA-DVSPLLRMqgAAYA-TRIAEDFRDRG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 254 KHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAklSDAKGGGSLTALPFVETQAGDISAYIPTN 333
Cdd:PRK07960 265 QHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG--NGISGGGSITAFYTVLTEGDDQQDPIADS 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 334 VISITDGQIFLQSDLFFSGVRPAINPGLSVSRVGGS-------AQIKAMKKVagtlrldLASF---RELEAFSQF--GSD 401
Cdd:PRK07960 343 ARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAlideqhyARVRQFKQL-------LSSFqrnRDLVSVGAYakGSD 415
|
....*...
gi 755605751 402 --LDKATQ 407
Cdd:PRK07960 416 pmLDKAIA 423
|
|
| 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 |
2.88e-33 |
|
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: 120.64 E-value: 2.88e-33
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755605751 27 DVGTVIEIGDGIARAHGLDNAMAGELLEFSNGVMGLAQNLEESNVGIVILGPYEEIKEGDEVRRTGR 93
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
100-427 |
3.50e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 128.08 E-value: 3.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 100 GEELLGRVVNPLGQPIDGQGAIETSKmrPIEAQAPGV--MDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTt 177
Cdd:PRK07196 93 GDSWLGRVINGLGEPLDGKGQLGGST--PLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKS- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 178 VAVDTILNQADQDMICIYVaIGQKESTVRSTVETFRKHGALDYTIVVSAGAsDPAPLLYLSPYAGV-AMGEEFMYNGKHV 256
Cdd:PRK07196 170 VLLGMITRYTQADVVVVGL-IGERGREVKEFIEHSLQAAGMAKSVVVAAPA-DESPLMRIKATELChAIATYYRDKGHDV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 257 LVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAklsDAKGGGSLTALPFVETQAGDISAYIPTNVIS 336
Cdd:PRK07196 248 LLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQDPIVDCARA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 337 ITDGQIFLQSDLFFSGVRPAINPGLSVSR----VGGSAQIKAMKKVAGTLRlDLASFRELEAFSQFGSDLDKATQAKLNR 412
Cdd:PRK07196 325 VLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCYA-DYMAIKPLIPLGGYVAGADPMADQAVHY 403
|
330
....*....|....*
gi 755605751 413 GQRTVEVLKQGLHKP 427
Cdd:PRK07196 404 YPAITQFLRQEVGHP 418
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
76-428 |
1.15e-30 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 123.48 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 76 LGPYEEIKEGDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDA 155
Cdd:PRK05922 71 LSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 156 LVPIGRGQRELIIGDRQTGKTTVAvdTILNQADQDMICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLL 235
Cdd:PRK05922 151 FLTLGKGQRIGVFSEPGSGKSSLL--STIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 236 YLSPYAGVAMGEEFMYNGKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKlsdaKGGGSLTA 315
Cdd:PRK05922 229 VIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN----NDKGSITA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 316 LPFVETQAG--DI-SAYIPtnviSITDGQIFL--QSDLFFSgvrPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFR 390
Cdd:PRK05922 305 LYAILHYPNhpDIfTDYLK----SLLDGHFFLtpQGKALAS---PPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYH 377
|
330 340 350
....*....|....*....|....*....|....*...
gi 755605751 391 ELEAFSQFGSdLDKATQAKLNRGQRTVEVLKQGLHKPM 428
Cdd:PRK05922 378 EALDIIQLGA-YVPGQDAHLDRAVKLLPSIKQFLSQPL 414
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
91-375 |
1.18e-30 |
|
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: 124.06 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 91 TGRIMQVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGD 170
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 171 -------------RQTGKTTVAVDTILNQADQDMICIYVAIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLLYL 237
Cdd:TIGR01040 150 aglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERII 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 238 SPYAGVAMGEEFMYN-GKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKLSDAKggGSLTAL 316
Cdd:TIGR01040 230 TPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRN--GSITQI 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 755605751 317 PFVETQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAM 375
Cdd:TIGR01040 308 PILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
62-365 |
4.52e-30 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 122.06 E-value: 4.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 62 LAQ--NLEESNVGIVILGPYEEIKEGDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAIETskmRPIEAQAPGV--M 137
Cdd:PRK02118 39 LAQviRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEG---EPIEIGGPSVnpV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 138 DRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDrqTGKTTVAV-DTILNQADQDMIcIYVAIGQKESTVRSTVETFRKHG 216
Cdd:PRK02118 116 KRIVPREMIRTGIPMIDVFNTLVESQKIPIFSV--SGEPYNALlARIALQAEADII-ILGGMGLTFDDYLFFKDTFENAG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 217 ALDYTIVVSAGASDPAPLLYLSPYAGVAMGEEFMYNG-KHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDvfyLHS 295
Cdd:PRK02118 193 ALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGS---LYS 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 296 RLLERAAKLSDAKGGGSLTALPFVETQAGDISAYIPTNVISITDGQIFLQSDlffsgvrpAINPGLSVSR 365
Cdd:PRK02118 270 DLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLRRG--------RIDPFGSLSR 331
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
77-393 |
8.68e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 118.16 E-value: 8.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 77 GPYEEIKEGDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAI-ETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDA 155
Cdd:PRK08927 72 GPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 156 LVPIGRGQRELIIGDRQTGKTTVaVDTILNQADQDMICIYVaIGQKESTVRSTVETFRKHGALDYTIVVSAGASDPAPLL 235
Cdd:PRK08927 152 FLTCCRGQRMGIFAGSGVGKSVL-LSMLARNADADVSVIGL-IGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 236 YLSPYAGVAMGEEFMYNGKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAklSDAKGGGSLTA 315
Cdd:PRK08927 230 RQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITG 307
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755605751 316 LPFVETQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVSRVGGSAQIKAMKKVAGTLRLDLASFRELE 393
Cdd:PRK08927 308 LFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADME 385
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
59-449 |
3.91e-28 |
|
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: 116.74 E-value: 3.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 59 VMGLAQNLEESNVGIVILGPYEEIKEGDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMD 138
Cdd:TIGR01039 40 TLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 139 RKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTVAVDTILNQADQ-DMICIYVAIGQKESTVRSTVETFRKHGA 217
Cdd:TIGR01039 120 QSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEhGGYSVFAGVGERTREGNDLYHEMKESGV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 218 LDYTIVVSAGASDPAPLLYLSPYAGVAMGEEFM-YNGKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSR 296
Cdd:TIGR01039 200 IDKTALVYGQMNEPPGARMRVALTGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 297 LLERAAklsdAKGGGSLTALPFVETQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVSR-----VGGSAQ 371
Cdd:TIGR01039 280 LQERIT----STKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRlldpsVVGEEH 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 372 IKAMKKVAGTLRldlaSFREL-EAFSQFG----SDLDKATqakLNRGQRTVEVLKQGLH----------KPMGVEKQVAI 436
Cdd:TIGR01039 356 YDVARGVQQILQ----RYKELqDIIAILGmdelSEEDKLT---VERARRIQRFLSQPFFvaevftgqpgKYVPLKDTIRG 428
|
410
....*....|...
gi 755605751 437 IYALTRGFLDDIP 449
Cdd:TIGR01039 429 FKEILEGKYDHLP 441
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
45-423 |
3.03e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 105.06 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 45 DNAMAGEllefsNGVMGLAQNLEESNVGIVILGPYEEIKEGDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGaiETS 124
Cdd:PRK06793 44 DVCFVGE-----HNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEA--ENI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 125 KMRPIEAQAPGV--MDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTVaVDTILNQADQDMICIYVaIGQKE 202
Cdd:PRK06793 117 PLQKIKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTL-LGMIAKNAKADINVISL-VGERG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 203 STVRSTVETFRKHGALDYTIVVSAgASDPAPLLYL-SPYAGVAMGEEFMYNGKHVLVVYDDLSKQAVAYRELSLLLRRPP 281
Cdd:PRK06793 195 REVKDFIRKELGEEGMRKSVVVVA-TSDESHLMQLrAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 282 greaFPGDVFYLHS---RLLERAAKLSDakggGSLTALPFVETQAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAIN 358
Cdd:PRK06793 274 ----IGGKTLLMESymkKLLERSGKTQK----GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAIS 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755605751 359 PGLSVSRVGGSAQIKAMKKVAGTLRLDLASFRELEAFSQFGSDLDKATQAKLNRGQRTVE----VLKQG 423
Cdd:PRK06793 346 VLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTIQENAENAYIFECKNKVEgintFLKQG 414
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
63-162 |
9.25e-23 |
|
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439825 [Multi-domain] Cd Length: 468 Bit Score: 100.93 E-value: 9.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 63 AQNLEESNVGIVILGPYEEIKEGDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSV 142
Cdd:COG0055 47 AQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTK 126
|
90 100
....*....|....*....|
gi 755605751 143 DEPLQTGIKAIDALVPIGRG 162
Cdd:COG0055 127 TEILETGIKVIDLLAPYAKG 146
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-366 |
8.39e-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: 92.28 E-value: 8.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 96 QVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 176 TTVAVDTILNQADQ-DMICIYVAIGQ------------KESTVRSTvetfrkhGALDYTIVVSAGASDPAPLLYLSPYAG 242
Cdd:cd01133 81 TVLIMELINNIAKAhGGYSVFAGVGErtregndlyhemKESGVINL-------DGLSKVALVYGQMNEPPGARARVALTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 243 VAMGEEFM-YNGKHVLVVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERAAKLSDakggGSLTALPFVET 321
Cdd:cd01133 154 LTMAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKK----GSITSVQAVYV 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 755605751 322 QAGDISAYIPTNVISITDGQIFLQSDLFFSGVRPAINPGLSVSRV 366
Cdd:cd01133 230 PADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
28-92 |
4.37e-18 |
|
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: 78.36 E-value: 4.37e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755605751 28 VGTVIEIGDGIARAHGLDNAMAGELLEFSNGVMGLAQNLEESNVGIVILGPYEEIKEGDEVRRTG 92
Cdd:pfam02874 5 IGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
125-365 |
1.04e-16 |
|
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: 80.31 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 125 KMRPIEAQAPGvmdrksvDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKtTVAVDTILNQADQDMIcIYVAIGQKEST 204
Cdd:cd01134 46 QPRPVKEKLPP-------NVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGK-TVISQSLSKWSNSDVV-IYVGCGERGNE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 205 VRSTVETF-------RKHGALDYTIVVSAGASDPAPLLYLSPYAGVAMGEEFMYNGKHVLVVYDDLSKQAVAYRELSLLL 277
Cdd:cd01134 117 MAEVLEEFpelkdpiTGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 278 RRPPGREAFPGdvfYLHSRL---LERAAK---LSDAKGGGSLTALPFVETQAGDISAYIPTNVISITdgQIF--LQSDLF 349
Cdd:cd01134 197 EEMPAEEGYPA---YLGARLaefYERAGRvrcLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLA 271
|
250
....*....|....*.
gi 755605751 350 FSGVRPAINPGLSVSR 365
Cdd:cd01134 272 QRRHFPSINWLISYSK 287
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
64-187 |
5.79e-15 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 77.00 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 64 QNLEESNVGIVILGPYEEIKEGDEVRRTGRIMQVPAGEELLGRVVNPLGQPIDGQGAIETSKMRPIEAQAPGVMDRKSVD 143
Cdd:CHL00060 63 QLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKL 142
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 755605751 144 EPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTTVAVDTILNQA 187
Cdd:CHL00060 143 SIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIA 186
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
375-442 |
8.20e-14 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 66.31 E-value: 8.20e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 375 MKKVAGTLRLDLASFRELEAFSQFGSD--LDKATQAKLNRGQRTVEVLKQGLHKPMGVEKQVAIIYALTR 442
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
138-327 |
2.63e-08 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 56.33 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 138 DRKSVDEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTtVAVDTILNQADQDmICIYVAIGQKESTVRSTVETFRK--- 214
Cdd:PRK04192 203 EKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT-VTQHQLAKWADAD-IVIYVGCGERGNEMTEVLEEFPElid 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 215 ----HGALDYTIVVSAGASDP-----ApllylSPYAGVAMGEEFMYNGKHVLVVYDDLSKQAVAYRELSLLLRRPPGREA 285
Cdd:PRK04192 281 pktgRPLMERTVLIANTSNMPvaareA-----SIYTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEG 355
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 755605751 286 FPGdvfYLHSRL---LERAAKLSdAKGG--GSLTALPFVETQAGDIS 327
Cdd:PRK04192 356 YPA---YLASRLaefYERAGRVK-TLGGeeGSVTIIGAVSPPGGDFS 398
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
192-358 |
2.76e-08 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 56.57 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 192 ICIYVAIGQKESTVRSTVETFRK-------HGALDYTIVVSAGASDPAPLLYLSPYAGVAMGEEFMYNGKHVLVVYDDLS 264
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605751 265 KQAVAYRELSLLLRRPPGREAFPGdvfYLHSRLLE------RAAKLSDAKGGGSLTALPFVETQAGDISAYIPTNVISIT 338
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVV 840
|
170 180
....*....|....*....|
gi 755605751 339 DGQIFLQSDLFFSGVRPAIN 358
Cdd:PRK14698 841 KVFWALDADLARRRHFPAIN 860
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
29-93 |
1.15e-03 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 37.68 E-value: 1.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755605751 29 GTVIEIGDGIARAHGLDNAMAGELLEF-----SNGVMGLAQ--NLEESNVGIVILGPYEEIKEGDEVRRTGR 93
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIGEVCEIergdgNNETVLKAEviGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| |
