|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 1083.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 1 MSIRAEEISALIKQQIENYQSEIEVSDVGTVIQVGDGIARAHGLDNVMAGELVEFSNGVMGLAQNLEENNVGIIILGPYT 80
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 81 EIREGDEVRRTGRIMQVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIG 160
Cdd:PRK09281 81 DIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 161 RGQRELIIGDRQTGKTAVALDTIINQKDEDMICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPY 240
Cdd:PRK09281 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 241 AGVTMGEEFMYNGKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDARGGGSLTALPFIE 320
Cdd:PRK09281 241 AGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 321 TQAGDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASYRELEAFAQFGS 400
Cdd:PRK09281 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 401 DLDKATQAKLNRGARTVEVLKQGLHKPLRVEKQVIILYALTRGFLDDIPVVDITRFEEEFHAWLDSNATDLLEEIRTTKK 480
Cdd:PRK09281 401 DLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKD 480
|
490 500
....*....|....*....|..
gi 228817196 481 LADD--DKFAAAINGFKKVFVA 500
Cdd:PRK09281 481 LSDEieAKLKAAIEEFKKTFAA 502
|
|
| 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: 1078.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 1 MSIRAEEISALIKQQIENYQSEIEVSDVGTVIQVGDGIARAHGLDNVMAGELVEFSNGVMGLAQNLEENNVGIIILGPYT 80
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 81 EIREGDEVRRTGRIMQVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIG 160
Cdd:COG0056 81 GIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 161 RGQRELIIGDRQTGKTAVALDTIINQKDEDMICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPY 240
Cdd:COG0056 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 241 AGVTMGEEFMYNGKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDARGGGSLTALPFIE 320
Cdd:COG0056 241 AGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 321 TQAGDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASYRELEAFAQFGS 400
Cdd:COG0056 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 401 DLDKATQAKLNRGARTVEVLKQGLHKPLRVEKQVIILYALTRGFLDDIPVVDITRFEEEFHAWLDSNATDLLEEIRTTKK 480
Cdd:COG0056 401 DLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGK 480
|
490 500
....*....|....*....|....
gi 228817196 481 LADD--DKFAAAINGFKKVFVASE 502
Cdd:COG0056 481 LDDEieEKLKAAIEEFKKTFAASA 504
|
|
| 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: 914.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 2 SIRAEEISALIKQQIENYQSEIEVSDVGTVIQVGDGIARAHGLDNVMAGELVEFSNGVMGLAQNLEENNVGIIILGPYTE 81
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 82 IREGDEVRRTGRIMQVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGR 161
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 162 GQRELIIGDRQTGKTAVALDTIINQKDEDMICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYA 241
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 242 GVTMGEEFMYNGKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDARGGGSLTALPFIET 321
Cdd:TIGR00962 241 GCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 322 QAGDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASYRELEAFAQFGSD 401
Cdd:TIGR00962 321 QAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 402 LDKATQAKLNRGARTVEVLKQGLHKPLRVEKQVIILYALTRGFLDDIPVVDITRFEEEFHAWLDSNATDLLEEIRTTKKL 481
Cdd:TIGR00962 401 LDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKL 480
|
490 500
....*....|....*....|.
gi 228817196 482 ADD--DKFAAAINGFKKVFVA 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: 804.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 1 MSIRAEEISALIKQQIENYQSEIEVSDVGTVIQVGDGIARAHGLDNVMAGELVEFSNGVMGLAQNLEENNVGIIILGPYT 80
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 81 EIREGDEVRRTGRIMQVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIG 160
Cdd:PRK13343 81 DILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 161 RGQRELIIGDRQTGKTAVALDTIINQKDEDMICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPY 240
Cdd:PRK13343 161 RGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 241 AGVTMGEEFMYNGKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDARGGGSLTALPFIE 320
Cdd:PRK13343 241 AGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 321 TQAGDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASYRELEAFAQFGS 400
Cdd:PRK13343 321 TLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 401 DLDKATQAKLNRGARTVEVLKQGLHKPLRVEKQVIILYALTRGFLDDIPVVDITRFEEEFHAWLDSNATDLLEEIRTTKK 480
Cdd:PRK13343 401 LLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRE 480
|
490 500
....*....|....*....|
gi 228817196 481 LADDDK--FAAAINGFKKVF 498
Cdd:PRK13343 481 LDEAWLaaLEEILREAGERF 500
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
22-502 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 785.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 22 EIEVSDVGTVIQVGDGIARAHGLDNVMAGELVEFSNGVMGLAQNLEENNVGIIILGPYTEIREGDEVRRTGRIMQVPVGK 101
Cdd:CHL00059 1 EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 102 ELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTAVALD 181
Cdd:CHL00059 81 AYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 182 TIINQKDEDMICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNGKHVLVVYD 261
Cdd:CHL00059 161 TILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 262 DLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDARGGGSLTALPFIETQAGDVSAYIPTNVISITDGQ 341
Cdd:CHL00059 241 DLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 342 IFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASYRELEAFAQFGSDLDKATQAKLNRGARTVEVLK 421
Cdd:CHL00059 321 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 422 QGLHKPLRVEKQVIILYALTRGFLDDIPVVDITRFEEEFHAWLDSNATDLLEEIRTTKKLADDDK--FAAAINGFKKVFV 499
Cdd:CHL00059 401 QSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEalLKEAIQEQLELFL 480
|
...
gi 228817196 500 ASE 502
Cdd:CHL00059 481 LQE 483
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
6-486 |
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: 611.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 6 EEISALIKQQIENYQSEIEVSDVGTVIQVGDGIARAHGLDNVMAGELVEFSNGVMGLAQNLEENNVGIIILGPYTEIREG 85
Cdd:TIGR03324 6 DKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 86 DEVRRTGRIMQVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRE 165
Cdd:TIGR03324 86 DEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 166 LIIGDRQTGKTAVALDTIINQKDEDMICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTM 245
Cdd:TIGR03324 166 LILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 246 GEEFMYNGKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDARGGGSLTALPFIETQAGD 325
Cdd:TIGR03324 246 GEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 326 VSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASYRELEAFAQFGSDLDKA 405
Cdd:TIGR03324 326 ISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDEN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 406 TQAKLNRGARTVEVLKQGLHKPLRVEKQVIILYALTRGFLDDIPVVDITRFEEEFHAWLDSNATDLLEEIRTTKKLADDD 485
Cdd:TIGR03324 406 TRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSDED 485
|
.
gi 228817196 486 K 486
Cdd:TIGR03324 486 R 486
|
|
| 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: 582.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 94 IMQVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQT 173
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 174 GKTAVALDTIINQKDEDMICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNG 253
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 254 KHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDARGGGSLTALPFIETQAGDVSAYIPTN 333
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 228817196 334 VISITDGQIFLQSDLFFSGVRPAIDAGTSVSRVG 367
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
61-457 |
1.78e-124 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 375.53 E-value: 1.78e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 61 GLAQNLEENN-VGIIILGPYTEIREGDEVRRTGRIMQVPVGKELIGRVVNPLGQPVdglgPIN--TTNTRPIESP----- 132
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEV----PVGllTRSRALLESEqtlgk 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 133 ----APGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTAVALDTIINQ--------KDEDMICIYVAIGQ 200
Cdd:PTZ00185 156 vdagAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 201 KESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNGKHVLVVYDDLSKQAAAYRELSLLLRRP 280
Cdd:PTZ00185 236 RCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 281 PGREAYPGDVFYLHSRLLERAAKLSDARGGGSLTALPFIETQAGDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAG 360
Cdd:PTZ00185 316 PGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 361 TSVSRVGGSAQIKAMSKVSGTLRLDLASYRELEAFAQFGSdldKATQAKLNRGARTVEVLKQglHKPLRVEKQVIILYAL 440
Cdd:PTZ00185 396 LSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGS---QVQTVPMIRGARFVALFNQ--KNPSFFMNALVSLYAC 470
|
410
....*....|....*..
gi 228817196 441 TRGFLDDIPVVDITRFE 457
Cdd:PTZ00185 471 LNGYLDDVKVNYAKLYE 487
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
149-364 |
7.04e-114 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 335.10 E-value: 7.04e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 149 GIKAIDALVPIGRGQRELIIGDRQTGKTAVAlDTIINQKDEDmICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASA 228
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD-VVVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 229 SQPAPLLYLAPYAGVTMGEEFMYNGKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDar 308
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKG-- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 228817196 309 GGGSLTALPFIETQAGDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGTSVS 364
Cdd:pfam00006 157 KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
85-413 |
2.96e-109 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 333.86 E-value: 2.96e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 85 GDEVRRTGRIMQVPVGKELIGRVVNPLGQPVDglgPINTTNTR----PIESP----APGVMDRKSVHEPLQTGIKAIDAL 156
Cdd:PRK07165 61 NDELIELNNTNKVKTSKEYFGKIIDIDGNIIY---PEAQNPLSkkflPNTSSifnlAHGLMTVKTLNEQLYTGIIAIDLL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 157 VPIGRGQRELIIGDRQTGKTAVALDTIINQKDEDMICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPlLY 236
Cdd:PRK07165 138 IPIGKGQRELIIGDRQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSPYE-QY 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 237 LAPYAGVTMGEEFMYNgKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLsdaRGGGSLTAL 316
Cdd:PRK07165 217 LAPYVAMAHAENISYN-DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKF---KNRKTITAL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 317 PFIETQAGDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASYRELEAFA 396
Cdd:PRK07165 293 PILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLS 372
|
330
....*....|....*..
gi 228817196 397 QFGSDLDKATQAKLNRG 413
Cdd:PRK07165 373 MLDYDLNKETSDLLFKG 389
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
96-366 |
8.75e-109 |
|
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: 324.41 E-value: 8.75e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 96 QVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 176 TAVALDTIINQKDED-MICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNGK 254
Cdd:cd19476 81 TVLAMQLARNQAKAHaGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 255 HVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDarGGGSLTALPFIETQAGDVSAYIPTNV 334
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 228817196 335 ISITDGQIFLQSDLFFSGVRPAIDAGTSVSRV 366
Cdd:cd19476 239 FAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| 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 |
3.48e-65 |
|
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: 206.83 E-value: 3.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 375 MSKVSGTLRLDLASYRELEAFAQFGSDLDKATQAKLNRGARTVEVLKQGLHKPLRVEKQVIILYALTRGFLDDIPVVDIT 454
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 228817196 455 RFEEEFHAWLDSNATDLLEEIRTTKKLADDD--KFAAAINGFKKVF 498
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELeeKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
371-494 |
2.31e-64 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 204.60 E-value: 2.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 371 QIKAMSKVSGTLRLDLASYRELEAFAQFGSDLDKATQAKLNRGARTVEVLKQGLHKPLRVEKQVIILYALTRGFLDDIPV 450
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 228817196 451 VDITRFEEEFHAWLDSNATDLLEEIRTTKKLADD--DKFAAAINGF 494
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDEleEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
96-366 |
4.91e-52 |
|
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: 177.37 E-value: 4.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 96 QVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 176 TaVALDTIINQKDEDMICIyVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNGKH 255
Cdd:cd01136 81 S-TLLGMIARNTDADVNVI-ALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 256 VLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDarggGSLTALPFIETQAGDVSAYIPTNVI 335
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----GSITAFYTVLVEGDDFNDPIADEVR 234
|
250 260 270
....*....|....*....|....*....|.
gi 228817196 336 SITDGQIFLQSDLFFSGVRPAIDAGTSVSRV 366
Cdd:cd01136 235 SILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
16-405 |
7.73e-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: 179.07 E-value: 7.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 16 IENYQSEIEVSD----VGTVIQVGDGIARAHGLDnVMAGELVEF--SNGVMGLAQ--NLEENNVGIIILGPYTEIREGDE 87
Cdd:COG1157 4 LARLLARLEELPpvrvSGRVTRVVGLLIEAVGPD-ASIGELCEIetADGRPVLAEvvGFRGDRVLLMPLGDLEGISPGAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 88 VRRTGRIMQVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQReli 167
Cdd:COG1157 83 VVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 168 IGdr---qtGKTaVALDTIINQKDEDMICIyvA-IGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGV 243
Cdd:COG1157 160 IGifagsgvGKS-TLLGMIARNTEADVNVI--AlIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 244 TMGEEFMYNGKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKlsdaRGGGSLTALPFIETQA 323
Cdd:COG1157 237 AIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN----GGKGSITAFYTVLVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 324 GDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGTSVSRVggsaqikaMSKV--------SGTLRLDLASYRELE-- 393
Cdd:COG1157 313 DDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRV--------MPDIvspehralARRLRRLLARYEENEdl 384
|
410
....*....|....*...
gi 228817196 394 ----AFAQfGSD--LDKA 405
Cdd:COG1157 385 irigAYQP-GSDpeLDEA 401
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-422 |
2.18e-50 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 178.08 E-value: 2.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 29 GTVIQVGDGIARAhGLDNVMAGELVEFS-NGVMGLAQNLEENNVgiiILGPYTE---IREGDEVRRTGRIMQVPVGKELI 104
Cdd:PRK06820 31 GPIVEIGPTLLRA-SLPGVAQGELCRIEpQGMLAEVVSIEQEMA---LLSPFASsdgLRCGQWVTPLGHMHQVQVGADLA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 105 GRVVNPLGQPVDGlGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTAVaLDTII 184
Cdd:PRK06820 107 GRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTL-LGMLC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 185 NQKDEDMIcIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNGKHVLVVYDDLS 264
Cdd:PRK06820 185 ADSAADVM-VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 265 KQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKlSDArggGSLTALPFIETQAGDVSAYIPTNVISITDGQIFL 344
Cdd:PRK06820 264 RYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGN-SDR---GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 345 QSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASYRELEAFAQFG---SDLDKATQAKLNRGARTVEVLK 421
Cdd:PRK06820 340 SRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGeyqAGEDLQADEALQRYPAICAFLQ 419
|
.
gi 228817196 422 Q 422
Cdd:PRK06820 420 Q 420
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-442 |
7.37e-50 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 176.87 E-value: 7.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 29 GTVIQVGDGIARAhGLDNVMAGELVEFSNG---------VMGLAQNleenNVGIIILGPYTEIREGDEVRRTGRIMQVPV 99
Cdd:PRK06936 25 GRVTQVTGTILKA-VVPGVRIGELCYLRNPdnslslqaeVIGFAQH----QALLTPLGEMYGISSNTEVSPTGTMHQVGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 100 GKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTAVa 179
Cdd:PRK06936 100 GEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTL- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 180 LDTIINQKDEDmICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNGKHVLVV 259
Cdd:PRK06936 179 LASLIRSAEVD-VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 260 YDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKlSDArggGSLTALPFIETQAGDVSAYIPTNVISITD 339
Cdd:PRK06936 258 MDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ-SDK---GSITALYTVLVEGDDMTEPVADETRSILD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 340 GQIFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASYRELEAFAQFGS---DLDKATQAKLNRGART 416
Cdd:PRK06936 334 GHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEyqkGQDKEADQAIERIGAI 413
|
410 420
....*....|....*....|....*.
gi 228817196 417 VEVLKQGLHKPLRVEKQVIILYALTR 442
Cdd:PRK06936 414 RGFLRQGTHELSHFNETLNLLETLTQ 439
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
74-443 |
1.33e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 167.98 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 74 IILGPYTEIRE---GDEVRRTGRIMQVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGI 150
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 151 KAIDALVPIGRGQRELIIGDRQTGKTAVaLDTIINQKDEDMICIYVaIGQKESTVRNVVETLRKHGALEYTIVVTASASQ 230
Cdd:PRK07721 147 RAIDSLLTVGKGQRVGIFAGSGVGKSTL-MGMIARNTSADLNVIAL-IGERGREVREFIERDLGPEGLKRSIVVVATSDQ 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 231 PAPLLYLAPYAGVTMGEEFMYNGKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAklsdARGG 310
Cdd:PRK07721 225 PALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG----TNAS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 311 GSLTALPFIETQAGDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASYR 390
Cdd:PRK07721 301 GSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQ 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 391 ELEAFAQFGS-------DLDKATQAKlnrgARTVEVLKQGLHKPLRVEKQVIILYALTRG 443
Cdd:PRK07721 381 NSEDLINIGAykrgssrEIDEAIQFY----PQIISFLKQGTDEKATFEESIQALLSLFGK 436
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
25-399 |
1.82e-44 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 162.24 E-value: 1.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 25 VSDVGTVIQVGDGIARAHGLDnVMAGELVEFSNGVMGLAQNLEEnnVG----IIILGPY---TEIREGDEVRRTGRIMQV 97
Cdd:PRK09099 22 VRRTGKVVEVIGTLLRVSGLD-VTLGELCELRQRDGTLLQRAEV--VGfsrdVALLSPFgelGGLSRGTRVIGLGRPLSV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 98 PVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGK-T 176
Cdd:PRK09099 99 PVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKsT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 177 AVALDTIINQKDEDMIciyVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNGKHV 256
Cdd:PRK09099 179 LMGMFARGTQCDVNVI---ALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 257 LVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAkLSDArggGSLTALPFIETQAGDVSAYIPTNVIS 336
Cdd:PRK09099 256 LLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-MGET---GSITALYTVLAEDESGSDPIAEEVRG 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 228817196 337 ITDGQIFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASYRELEAFAQFG 399
Cdd:PRK09099 332 ILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVG 394
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
29-368 |
4.11e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 155.61 E-value: 4.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 29 GTVIQVGDGIARAHGLdNVMAGELV-----EFSNGVMGLAQNLEENNVGIIILGPYTEIREGDEVRRTGRIMQVPVGKEL 103
Cdd:PRK08472 20 GSITKISPTIIEADGL-NPSVGDIVkiessDNGKECLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 104 IGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTavALDTI 183
Cdd:PRK08472 99 LGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKS--TLMGM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 184 INQKDEDMICIYVAIGQKEstvRNVVETLRKH--GALEYTIVVTASaSQPAPLL--YLApYAGVTMGEEFMYNGKHVLVV 259
Cdd:PRK08472 177 IVKGCLAPIKVVALIGERG---REIPEFIEKNlgGDLENTVIVVAT-SDDSPLMrkYGA-FCAMSVAEYFKNQGLDVLFI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 260 YDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKlsdARGGGSLTALPFIETQAGDVSAYIPTNVISITD 339
Cdd:PRK08472 252 MDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTVLVEGDDMSDPIADQSRSILD 328
|
330 340
....*....|....*....|....*....
gi 228817196 340 GQIFLQSDLFFSGVRPAIDAGTSVSRVGG 368
Cdd:PRK08472 329 GHIVLSRELTDFGIYPPINILNSASRVMN 357
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-408 |
7.09e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 155.11 E-value: 7.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 29 GTVIQVGDGIARAHgLDNVMAGELVEFSNGvMGLAQNleennVGI----IILGPYTE---IREGDEVRRTGRIMQVPVGK 101
Cdd:PRK07594 23 GRIQDVSATLLNAW-LPGVFMGELCCIKPG-EELAEV-----VGIngskALLSPFTStigLHCGQQVMALRRRHQVPVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 102 ELIGRVVNPLGQPVDGLgPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTAVaLD 181
Cdd:PRK07594 96 ALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 182 TIINQKDEDmICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNGKHVLVVYD 261
Cdd:PRK07594 174 MLCNAPDAD-SNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLAD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 262 DLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDarggGSLTALPFIETQAGDVSAYIPTNVISITDGQ 341
Cdd:PRK07594 253 SLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEK----GSITAFYTVLVEGDDMNEPLADEVRSLLDGH 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 228817196 342 IFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASYRELEAFAQFG-------SDLDKATQA 408
Cdd:PRK07594 329 IVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGeyqrgvdTDTDKAIDT 402
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
44-399 |
1.16e-41 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 154.00 E-value: 1.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 44 LDNVMAGELVE-----FSNGVMGLAQ-----------NLEENNVGI---IILGPyteiregdevrrTGRIMQVPVGKELI 104
Cdd:PRK08149 22 LPDVAIGEICEiragwHSNEVIARAQvvgfqrertilSLIGNAQGLsrqVVLKP------------TGKPLSVWVGEALL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 105 GRVVNPLGQPVDGLGPINT----TNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTAVaL 180
Cdd:PRK08149 90 GAVLDPTGKIVERFDAPPTvgpiSEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSL-M 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 181 DTIINQKDEDmicIYVA--IGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNGKHVLV 258
Cdd:PRK08149 169 NMLIEHSEAD---VFVIglIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 259 VYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDarggGSLTALPFIETQAGDVSAYIPTNVISIT 338
Cdd:PRK08149 246 FIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA----GSITAFYTVLLESEEEPDPIGDEIRSIL 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 228817196 339 DGQIFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASYRELEAFAQFG 399
Cdd:PRK08149 322 DGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLG 382
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
48-440 |
1.86e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 154.09 E-value: 1.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 48 MAGELVEfsnGVMGLAQNleennvgIIILGPYTEIR---EGDEVRRTGRIMQVPVGKELIGRVVNPLGQPVDGLGPINTT 124
Cdd:PRK08972 55 MAGELEA---EVVGFDGD-------LLYLMPIEELRgvlPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 125 NTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTaVALDTIINQKDEDMICIYVaIGQKEST 204
Cdd:PRK08972 125 QRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKS-VLLGMMTRGTTADVIVVGL-VGERGRE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 205 VRNVVETLRKHGALEYTIVVTASASQpAPLLYL-APYAGVTMGEEFMYNGKHVLVVYDDLSKQAAAYRELSLLLRRPPGR 283
Cdd:PRK08972 203 VKEFIEEILGEEGRARSVVVAAPADT-SPLMRLkGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPAT 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 284 EAYPGDVFYLHSRLLERAAKLSDarGGGSLTALPFIETQAGDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGTSV 363
Cdd:PRK08972 282 KGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASI 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 364 SRVG----GSAQIKAMSKVSGTLRL-----DLASyreLEAFAQfGSD--LDKA--TQAKLNrgartvEVLKQGLHKPLRV 430
Cdd:PRK08972 360 SRVMpmviSEEHLEAMRRVKQVYSLyqqnrDLIS---IGAYKQ-GSDprIDNAirLQPAMN------AFLQQTMKEAVPY 429
|
410
....*....|
gi 228817196 431 EKQVIILYAL 440
Cdd:PRK08972 430 DMSVNMLKQL 439
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
94-370 |
3.16e-41 |
|
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: 149.29 E-value: 3.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 94 IMQVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDrqT 173
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSG--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 174 GKTA------VALDTIINQKDEDMICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTMGE 247
Cdd:cd01135 79 GLPHnelaaqIARQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 248 EFMY-NGKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSDArgGGSLTALPFIETQA 323
Cdd:cd01135 159 YLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTMPN 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 228817196 324 GDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGTSVSRVGGSA 370
Cdd:cd01135 234 DDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSG 280
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
96-407 |
4.80e-38 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 144.93 E-value: 4.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 96 QVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 176 TaVALDTIINQKDEDMICIYVaIGQKESTVRNVVETLRKHGALEYTIVVTASASQpAPLLYL--APYAgVTMGEEFMYNG 253
Cdd:PRK07960 189 S-VLLGMMARYTQADVIVVGL-IGERGREVKDFIENILGAEGRARSVVIAAPADV-SPLLRMqgAAYA-TRIAEDFRDRG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 254 KHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDARGGGSLTALPFIETQAGDVSAYIPTN 333
Cdd:PRK07960 265 QHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG--NGISGGGSITAFYTVLTEGDDQQDPIADS 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 334 VISITDGQIFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASY---REL---EAFAQfGSD--LDKA 405
Cdd:PRK07960 343 ARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFqrnRDLvsvGAYAK-GSDpmLDKA 421
|
..
gi 228817196 406 TQ 407
Cdd:PRK07960 422 IA 423
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
95-427 |
3.25e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 139.48 E-value: 3.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 95 MQVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTG 174
Cdd:PRK05688 101 GRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 175 KTaVALDTIINQKDEDMICIYVaIGQKESTVRNVVETLRKHGALEYTIVVtASASQPAPLLYL-APYAGVTMGEEFMYNG 253
Cdd:PRK05688 181 KS-VLLGMMTRFTEADIIVVGL-IGERGREVKEFIEHILGEEGLKRSVVV-ASPADDAPLMRLrAAMYCTRIAEYFRDKG 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 254 KHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDARGGGSLTALPFIETQAGDVSAYIPTN 333
Cdd:PRK05688 258 KNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEGDDQQDPIADS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 334 VISITDGQIFLQSDLFFSGVRPAIDAGTSVSRVggsaqikaMSKVSGTLRLDLASY-RELEAFAQFGSDL---------- 402
Cdd:PRK05688 336 ARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV--------MPQVVDPEHLRRAQRfKQLWSRYQQSRDLisvgayvagg 407
|
330 340
....*....|....*....|....*
gi 228817196 403 DKATQAKLNRGARTVEVLKQGLHKP 427
Cdd:PRK05688 408 DPETDLAIARFPHLVQFLRQGLREN 432
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
76-428 |
5.28e-36 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 138.88 E-value: 5.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 76 LGPYTEIREGDEVRRTGRIMQVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDA 155
Cdd:PRK05922 71 LSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 156 LVPIGRGQRELIIGDRQTGKTavALDTIINQKDEDMICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLL 235
Cdd:PRK05922 151 FLTLGKGQRIGVFSEPGSGKS--SLLSTIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 236 YLAPYAGVTMGEEFMYNGKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKlsdaRGGGSLTA 315
Cdd:PRK05922 229 VIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN----NDKGSITA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 316 LPFIETQAGDVSAYIPTnVISITDGQIFL--QSDLFFSgvrPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASYRELE 393
Cdd:PRK05922 305 LYAILHYPNHPDIFTDY-LKSLLDGHFFLtpQGKALAS---PPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEAL 380
|
330 340 350
....*....|....*....|....*....|....*
gi 228817196 394 AFAQFGSdLDKATQAKLNRGARTVEVLKQGLHKPL 428
Cdd:PRK05922 381 DIIQLGA-YVPGQDAHLDRAVKLLPSIKQFLSQPL 414
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
29-407 |
7.68e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 138.59 E-value: 7.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 29 GTVIQVGDGIARAHGL-DNVMAGELVEF-SNGVMGLAQ--NLEENNVGIIILGPYTEIREGDEVRRTGRiMQVPVGKELI 104
Cdd:PRK06002 28 GTVSEVTASHYRVRGLsRFVRLGDFVAIrADGGTHLGEvvRVDPDGVTVKPFEPRIEIGLGDAVFRKGP-LRIRPDPSWK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 105 GRVVNPLGQPVDGLGPINT-TNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKT------- 176
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKStllamla 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 177 -AVALDTIInqkdedmiciyVA-IGQKESTVRNVVE-TLRKHgaLEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNG 253
Cdd:PRK06002 187 rADAFDTVV-----------IAlVGERGREVREFLEdTLADN--LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 254 KHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDARGGGSLTALPFIETQAGDVSAYIPTN 333
Cdd:PRK06002 254 ENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAG--PGAEGGGSITGIFSVLVDGDDHNDPVADS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 334 VISITDGQIFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASY---RELEAFA--QFGSD--LDKAT 406
Cdd:PRK06002 332 IRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFeetRDLRLIGgyRAGSDpdLDQAV 411
|
.
gi 228817196 407 Q 407
Cdd:PRK06002 412 D 412
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
43-365 |
8.74e-34 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 133.03 E-value: 8.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 43 GLDNVMAGELVEF--SNGVMGLAQNLE--ENNVGIIILGPYTEI-REGDEVRRTGRIMQVPVGKELIGRVVNPLGQPVDG 117
Cdd:PRK04196 19 GVEGVAYGEIVEIelPNGEKRRGQVLEvsEDKAVVQVFEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 118 LGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQR------------ELIIgdrQTGKTAVALDTiin 185
Cdd:PRK04196 99 GPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnELAA---QIARQAKVLGE--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 186 qkDEDMICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYN-GKHVLVVYDDLS 264
Cdd:PRK04196 173 --EENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFEkGMHVLVILTDMT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 265 KQAAAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSDARggGSLTALPFIETQAGDVSAYIPTNVISITDGQ 341
Cdd:PRK04196 251 NYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGKK--GSITQIPILTMPDDDITHPIPDLTGYITEGQ 325
|
330 340
....*....|....*....|....
gi 228817196 342 IFLQSDLFFSGVRPAIDAGTSVSR 365
Cdd:PRK04196 326 IVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| 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 |
1.39e-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: 121.41 E-value: 1.39e-33
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 228817196 27 DVGTVIQVGDGIARAHGLDNVMAGELVEFSNGVMGLAQNLEENNVGIIILGPYTEIREGDEVRRTGR 93
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
99-429 |
1.71e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 128.86 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 99 VGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTaV 178
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKS-V 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 179 ALDTIINQKDEDMICIYVaIGQKESTVRNVVETLRKHGALEYTIVVTASASQpAPLLYL-APYAGVTMGEEFMYNGKHVL 257
Cdd:PRK07196 171 LLGMITRYTQADVVVVGL-IGERGREVKEFIEHSLQAAGMAKSVVVAAPADE-SPLMRIkATELCHAIATYYRDKGHDVL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 258 VVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAklsDARGGGSLTALPFIETQAGDVSAYIPTNVISI 337
Cdd:PRK07196 249 LLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQDPIVDCARAV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 338 TDGQIFLQSDLFFSGVRPAIDAGTSVSR----VGGSAQIKAMSKVSGTLRlDLASYRELEAFAQFGSDLDKATQAKLNRG 413
Cdd:PRK07196 326 LDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCYA-DYMAIKPLIPLGGYVAGADPMADQAVHYY 404
|
330
....*....|....*.
gi 228817196 414 ARTVEVLKQGLHKPLR 429
Cdd:PRK07196 405 PAITQFLRQEVGHPAL 420
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
23-393 |
1.97e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 128.94 E-value: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 23 IEVSDVGTVIQVGDGIARAHGLDNVMAGELVEFSNgvmglaqnleeNNVGIIILGPYTEIREGDEVRRTGRIMQVPVGKE 102
Cdd:PRK08927 29 VEVAGPIHALSVGARIVVETRGGRPVPCEVVGFRG-----------DRALLMPFGPLEGVRRGCRAVIANAAAAVRPSRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 103 LIGRVVNPLGQPVDGLGPI-NTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTaVALD 181
Cdd:PRK08927 98 WLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKS-VLLS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 182 TIINQKDEDMICIYVaIGQKESTVRNVVE-TLRKHGaLEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNGKHVLVVY 260
Cdd:PRK08927 177 MLARNADADVSVIGL-IGERGREVQEFLQdDLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 261 DDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDARGGGSLTALPFIETQAGDVSAYIPTNVISITDG 340
Cdd:PRK08927 255 DSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDG 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 228817196 341 QIFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSKVSGTLRLDLASYRELE 393
Cdd:PRK08927 333 HIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADME 385
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
59-449 |
2.07e-31 |
|
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: 125.99 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 59 VMGLAQNLEENNVGIIILGPYTEIREGDEVRRTGRIMQVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMD 138
Cdd:TIGR01039 40 TLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 139 RKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTAVALDTIIN-QKDEDMICIYVAIGQKESTVRNVVETLRKHGA 217
Cdd:TIGR01039 120 QSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKESGV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 218 LEYTIVVTASASQPAPLLYLAPYAGVTMGEEFM-YNGKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSR 296
Cdd:TIGR01039 200 IDKTALVYGQMNEPPGARMRVALTGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 297 LLERAAklsdARGGGSLTALPFIETQAGDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGTSVSR-----VGGSAQ 371
Cdd:TIGR01039 280 LQERIT----STKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRlldpsVVGEEH 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 372 IKAMSKVSGTLRldlaSYREL-EAFAQFG----SDLDKATqakLNRGARTVEVLKQGLH----------KPLRVEKQVII 436
Cdd:TIGR01039 356 YDVARGVQQILQ----RYKELqDIIAILGmdelSEEDKLT---VERARRIQRFLSQPFFvaevftgqpgKYVPLKDTIRG 428
|
410
....*....|...
gi 228817196 437 LYALTRGFLDDIP 449
Cdd:TIGR01039 429 FKEILEGKYDHLP 441
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
91-377 |
3.24e-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: 119.83 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 91 TGRIMQVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGD 170
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 171 -------------RQTGKTAVALDTIINQKDEDMICIYVAIGQKESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYL 237
Cdd:TIGR01040 150 aglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERII 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 238 APYAGVTMGEEFMYN-GKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLsDARgGGSLTAL 316
Cdd:TIGR01040 230 TPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV-EGR-NGSITQI 307
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 228817196 317 PFIETQAGDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGTSVSRVGGSAQIKAMSK 377
Cdd:TIGR01040 308 PILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTR 368
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
45-365 |
1.86e-28 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 117.44 E-value: 1.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 45 DNVMAGEL--VEFSNGVMgLAQ--NLEENNVGIIILGPYTEIREGDEVRRTGRIMQVPVGKELIGRVVNPLGQPVDGlGP 120
Cdd:PRK02118 21 EGVGYGELatVERKDGSS-LAQviRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 121 INTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTAVaLDTIINQKDEDMIcIYVAIGQ 200
Cdd:PRK02118 99 ELEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNAL-LARIALQAEADII-ILGGMGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 201 KESTVRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNG-KHVLVVYDDLSKQAAAYRELSLLLRR 279
Cdd:PRK02118 177 TFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLTDMTNFADALKEISITMDQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 280 PPGREAYPGDvfyLHSRLLERAAKLSDARGGGSLTALPFIETQAGDVSAYIPTNVISITDGQIFLQSDlffsgvrpAIDA 359
Cdd:PRK02118 257 IPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLRRG--------RIDP 325
|
....*.
gi 228817196 360 GTSVSR 365
Cdd:PRK02118 326 FGSLSR 331
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-366 |
3.53e-23 |
|
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: 99.22 E-value: 3.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 96 QVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGK 175
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 176 TAVALDTIIN-QKDEDMICIYVAIGQ------------KESTVRNVvetlrkhGALEYTIVVTASASQPAPLLYLAPYAG 242
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGErtregndlyhemKESGVINL-------DGLSKVALVYGQMNEPPGARARVALTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 243 VTMGEEFM-YNGKHVLVVYDDLSKQAAAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDarggGSLTALPFIET 321
Cdd:cd01133 154 LTMAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKK----GSITSVQAVYV 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 228817196 322 QAGDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGTSVSRV 366
Cdd:cd01133 230 PADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
45-423 |
6.56e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 100.82 E-value: 6.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 45 DNVMAGElvefsNGVMGLAQNLEENNVGIIILGPYTEIREGDEVRRTGRIMQVPVGKELIGRVVNPLGQPVDGLGPINTT 124
Cdd:PRK06793 44 DVCFVGE-----HNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 125 NTRPIESPAPGVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTAVaLDTIINQKDEDMICIYVaIGQKEST 204
Cdd:PRK06793 119 QKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTL-LGMIAKNAKADINVISL-VGERGRE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 205 VRNVVETLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNGKHVLVVYDDLSKQAAAYRELSLLLRRPPgre 284
Cdd:PRK06793 197 VKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP--- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 285 aYPGDVFYLHS---RLLERAAKLSDarggGSLTALPFIETQAGDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGT 361
Cdd:PRK06793 274 -IGGKTLLMESymkKLLERSGKTQK----GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLD 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 228817196 362 SVSRVGGSAQIKAMSKVSGTLRLDLASYRELEAFAQFGSDLDKATQAKLNRGARTVE----VLKQG 423
Cdd:PRK06793 349 SVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTIQENAENAYIFECKNKVEgintFLKQG 414
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
64-393 |
3.23e-19 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 90.49 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 64 QNLEENNVGIIILGPYTEIREGDEVRRTGRIMQVPVGKELIGRVVNPLGQPVDGLGPINTTNTRPIESPAPGVMDRKSVH 143
Cdd:CHL00060 63 QLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 144 EPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTAVALDTIIN-QKDEDMICIYVAIGQ------------KESTVRNVVE 210
Cdd:CHL00060 143 SIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGErtregndlymemKESGVINEQN 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 211 TLRKHGALEYtivvtasaSQ----PAPLLYLAPYAgVTMGEEFM-YNGKHVLVVYDDLSKQAAAYRELSLLLRRPPGREA 285
Cdd:CHL00060 223 IAESKVALVY--------GQmnepPGARMRVGLTA-LTMAEYFRdVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 286 YPGDVFYLHSRLLERAAKLSDarggGSLTALPFIETQAGDVSAYIPTNVISITDGQIFLQSDLFFSGVRPAIDAGTSVS- 364
Cdd:CHL00060 294 YQPTLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSt 369
|
330 340 350
....*....|....*....|....*....|...
gi 228817196 365 ----RVGGSAQIKAMSKVSGTLRldlaSYRELE 393
Cdd:CHL00060 370 mlqpRIVGEEHYETAQRVKQTLQ----RYKELQ 398
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
25-92 |
5.63e-19 |
|
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: 80.67 E-value: 5.63e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 228817196 25 VSDVGTVIQVGDGIARAHGLDNVMAGELVEFSNGVMGLAQNLEENNVGIIILGPYTEIREGDEVRRTG 92
Cdd:pfam02874 2 VQVIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
128-365 |
5.25e-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: 78.39 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 128 PIESPAPgVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTaVALDTIINQKDEDMIcIYVAIGQKESTVRN 207
Cdd:cd01134 43 PVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKT-VISQSLSKWSNSDVV-IYVGCGERGNEMAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 208 VVE-------TLRKHGALEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNGKHVLVVYDDLSKQAAAYRELSLLLRRP 280
Cdd:cd01134 120 VLEefpelkdPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEM 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 281 PGREAYPGdvfYLHSRL---LERAAK---LSDARGGGSLTALPFIETQAGDVSAYIPTNVISITdgQIF--LQSDLFFSG 352
Cdd:cd01134 200 PAEEGYPA---YLGARLaefYERAGRvrcLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRR 274
|
250
....*....|...
gi 228817196 353 VRPAIDAGTSVSR 365
Cdd:cd01134 275 HFPSINWLISYSK 287
|
|
| 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 |
9.06e-12 |
|
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: 60.54 E-value: 9.06e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 375 MSKVSGTLRLDLASYRELEAFAQFGSD--LDKATQAKLNRGARTVEVLKQGLHKPLRVEKQVIILYALTR 442
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
192-364 |
2.77e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 63.12 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 192 ICIYVAIGQKESTVRNVVETLRK-------HGALEYTIVVTASASQPAPLLYLAPYAGVTMGEEFMYNGKHVLVVYDDLS 264
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 265 KQAAAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERAAKL----SDARgGGSLTALPFIETQAGDVSAYIPTNVISI 337
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPA---YLASKLaefYERAGRVvtlgSDYR-VGSVSVIGAVSPPGGDFSEPVVQNTLRV 839
|
170 180
....*....|....*....|....*..
gi 228817196 338 TDGQIFLQSDLFFSGVRPAIDAGTSVS 364
Cdd:PRK14698 840 VKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
128-315 |
8.86e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 60.95 E-value: 8.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 128 PIESPAPgVMDRKSVHEPLQTGIKAIDALVPIGRGQRELIIGDRQTGKTaVALDTIINQKDEDmICIYVAIGQK--Estv 205
Cdd:PRK04192 194 PVRRPRP-YKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT-VTQHQLAKWADAD-IVIYVGCGERgnE--- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228817196 206 rnVVETLR--------KHGA--LEYTIVV--TAS---ASQPAPLlylapYAGVTMGEEFMYNGKHVLVVYDDLSKQAAAY 270
Cdd:PRK04192 268 --MTEVLEefpelidpKTGRplMERTVLIanTSNmpvAAREASI-----YTGITIAEYYRDMGYDVLLMADSTSRWAEAL 340
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 228817196 271 RELSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSdARGG--GSLTA 315
Cdd:PRK04192 341 REISGRLEEMPGEEGYPA---YLASRLaefYERAGRVK-TLGGeeGSVTI 386
|
|
| 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 |
3.48e-05 |
|
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: 41.91 E-value: 3.48e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 228817196 29 GTVIQVGDGIARAHGLDNVMAGELVEF-----SNGVMGLAQ--NLEENNVGIIILGPYTEIREGDEVRRTGR 93
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIGEVCEIergdgNNETVLKAEviGFRGDRAILQLFESTRGLSRGALVEPTGR 73
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