|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-510 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 1022.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 1 MQLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADCMQGEMIALPGNRYAIALNLERDSVGAVVMGPYA 80
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 81 DLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIG 160
Cdd:PRK09281 81 DIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 161 RGQRELIIGDRQTGKTALAIDAIINQRDSGIKCVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPY 240
Cdd:PRK09281 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 241 AGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNVEyveaftkgevkGK 320
Cdd:PRK09281 241 AGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDE-----------LG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 321 TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQY 400
Cdd:PRK09281 310 GGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 401 RELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIGSFEAALLAYVDRDHA 480
Cdd:PRK09281 390 RELEAFAQFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHA 469
|
490 500 510
....*....|....*....|....*....|
gi 1340026348 481 PLMQEINQSGGYNDEIEGKLKGILDSFKAT 510
Cdd:PRK09281 470 DLLEEIRETKDLSDEIEAKLKAAIEEFKKT 499
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-513 |
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: 996.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 1 MQLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADCMQGEMIALPGNRYAIALNLERDSVGAVVMGPYA 80
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 81 DLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIG 160
Cdd:COG0056 81 GIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 161 RGQRELIIGDRQTGKTALAIDAIINQRDSGIKCVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPY 240
Cdd:COG0056 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 241 AGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNVEYveaftkgevkgK 320
Cdd:COG0056 241 AGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEL-----------G 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 321 TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQY 400
Cdd:COG0056 310 GGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 401 RELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIGSFEAALLAYVDRDHA 480
Cdd:COG0056 390 RELEAFAQFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHP 469
|
490 500 510
....*....|....*....|....*....|...
gi 1340026348 481 PLMQEINQSGGYNDEIEGKLKGILDSFKATQSW 513
Cdd:COG0056 470 DLLKEIRETGKLDDEIEEKLKAAIEEFKKTFAA 502
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
2-513 |
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: 937.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 2 QLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADCMQGEMIALPGNRYAIALNLERDSVGAVVMGPYAD 81
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 82 LAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGR 161
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 162 GQRELIIGDRQTGKTALAIDAIINQRDSGIKCVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYA 241
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 242 GCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNVEyveaftkgevKGKt 321
Cdd:TIGR00962 241 GCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDE----------KGG- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 322 GSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYR 401
Cdd:TIGR00962 310 GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 402 ELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIGSFEAALLAYVDRDHAP 481
Cdd:TIGR00962 390 ELEAFSQFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPD 469
|
490 500 510
....*....|....*....|....*....|..
gi 1340026348 482 LMQEINQSGGYNDEIEGKLKGILDSFKATQSW 513
Cdd:TIGR00962 470 ILEEINTTKKLTEELEAKLKEALKNFKKTFAW 501
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-513 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 786.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 1 MQLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADCMQGEMIALPGNRYAIALNLERDSVGAVVMGPYA 80
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 81 DLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIG 160
Cdd:PRK13343 81 DILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 161 RGQRELIIGDRQTGKTALAIDAIINQRDSGIKCVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPY 240
Cdd:PRK13343 161 RGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 241 AGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNVEYveaftkgevkgK 320
Cdd:PRK13343 241 AGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPEL-----------G 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 321 TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQY 400
Cdd:PRK13343 310 GGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 401 RELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIGSFEAALLAYVDRDHA 480
Cdd:PRK13343 390 LELEAFTRFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFA 469
|
490 500 510
....*....|....*....|....*....|...
gi 1340026348 481 PLMQEINQSGGYNDEIEGKLKGILDSFKATQSW 513
Cdd:PRK13343 470 ALSLALESPRELDEAWLAALEEILREAGERFAA 502
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
27-512 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 681.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 27 NEGTIVSVSDGVIRIHGLADCMQGEMIALPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGR 106
Cdd:CHL00059 6 NTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 107 VVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALAIDAIINQ 186
Cdd:CHL00059 86 VVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 187 RDSGIKCVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQ 266
Cdd:CHL00059 166 KGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 267 AVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNVEYveaftkGEvkgktGSLTALPIIETQAGDVSAFVPTNVI 346
Cdd:CHL00059 246 AQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQL------GE-----GSMTALPIVETQAGDVSAYIPTNVI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 347 SITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRELAAFSQFASDLDDATRKQLDHGQK 426
Cdd:CHL00059 315 SITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 427 VTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIGSFEAALLAYVDRDHAPLMQEINQSGGYNDEIEGKLKGILDS 506
Cdd:CHL00059 395 LRELLKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQE 474
|
....*.
gi 1340026348 507 FKATQS 512
Cdd:CHL00059 475 QLELFL 480
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
94-378 |
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: 555.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 94 ILEVPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQT 173
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 174 GKTALAIDAIINQRDSGIKCVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRG 253
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 254 EDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNVEYveaftkgevkgKTGSLTALPIIETQ 333
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEL-----------GGGSLTALPIIETQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1340026348 334 AGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRVG 378
Cdd:cd01132 230 AGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
29-495 |
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: 528.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 29 GTIVSVSDGVIRIHGLADCMQGEMIALPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVV 108
Cdd:TIGR03324 29 GTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERTGRVMDVPVGDGLLGRVV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 109 NTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALAIDAIINQRD 188
Cdd:TIGR03324 109 DPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDRQTGKTAIAIDTILNQKG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 189 SGIKCVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAV 268
Cdd:TIGR03324 189 RNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSIGEHFMEQGRDVLIVYDDLTQHAR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 269 AYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNVEYveaftkgevkgKTGSLTALPIIETQAGDVSAFVPTNVISI 348
Cdd:TIGR03324 269 AYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEEL-----------GGGSLTALPIIETEAQNISAYIPTNLISI 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 349 TDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRELAAFSQFASDLDDATRKQLDHGQKVT 428
Cdd:TIGR03324 338 TDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDENTRKTIEHGRRIR 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1340026348 429 ELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIGSFEAALLAYVDRDHAPLMQEINQSGGYNDE 495
Cdd:TIGR03324 418 ACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSDE 484
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
61-472 |
4.21e-115 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 351.65 E-value: 4.21e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 61 AIALNLERDS-VGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPID------GKGPLEHDG-FSAVEAI 132
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQtLGKVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 133 APGVIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALAIDAIINQ--------RDSGIKCVYVAIGQKAST 204
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 205 ISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGRE 284
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGRE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 285 AFPGDVFYLHSRLLERAARVNveyveaftkgevKGK-TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSG 363
Cdd:PTZ00185 320 AYPGDVFYLHSRLLERAAMLS------------PGKgGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 364 IRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRELAAFSQFASDLDDATrkqLDHGQKVTELLKQKQyaPMSVAQ 443
Cdd:PTZ00185 388 QRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMN 462
|
410 420
....*....|....*....|....*....
gi 1340026348 444 QSLVLFAAERGYLADVELSKIGSFEAALL 472
Cdd:PTZ00185 463 ALVSLYACLNGYLDDVKVNYAKLYEYLLV 491
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
149-375 |
1.87e-113 |
|
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: 334.32 E-value: 1.87e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 149 GYKSVDAMIPIGRGQRELIIGDRQTGKTALAiDAIINQRDSGIkCVYVAIGQKASTISNVVRKLEEHGALANTIVVVATA 228
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 229 SESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARvnvey 308
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGR----- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1340026348 309 veaftkgeVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVS 375
Cdd:pfam00006 154 --------VKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
30-440 |
1.62e-109 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 335.02 E-value: 1.62e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 30 TIVSVSDGVIRIHGLADCMQGEMIALPGNRYAIA--LNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRV 107
Cdd:PRK07165 4 KIKSIFDYIVEVKGEYDYQQNQFFTLKNNPNVKAfvISATEDKAYLLINNEKGKIKINDELIELNNTNKVKTSKEYFGKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 108 VNTLGAPI---------DGKGPLEHDGFsaveAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTAL 178
Cdd:PRK07165 84 IDIDGNIIypeaqnplsKKFLPNTSSIF----NLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 179 AIDAIINQRDSGIKCVYVAIGQKASTISNVVRKLEEHGALANTIVVVAtASESAALQYLAPYAGCAMGE---YFrdrgED 255
Cdd:PRK07165 160 ALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAEnisYN----DD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 256 ALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvnveyveaftkGEVKGKTgSLTALPIIETQAG 335
Cdd:PRK07165 235 VLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERA-------------GKFKNRK-TITALPILQTVDN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 336 DVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRELAAFSQFASDLDD 415
Cdd:PRK07165 301 DITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNK 380
|
410 420
....*....|....*....|....*
gi 1340026348 416 ATRKQLDHGQKVTELLKQKQYAPMS 440
Cdd:PRK07165 381 ETSDLLFKGKMIEKMFNQKGFSLYS 405
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
97-377 |
3.72e-104 |
|
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: 312.85 E-value: 3.72e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 97 VPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKT 176
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 177 ALAIDAIINQ-RDSGIKCVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGED 255
Cdd:cd19476 82 VLAMQLARNQaKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 256 ALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARvnveyveaftkgeVKGKTGSLTALPIIETQAG 335
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGK-------------VKDGGGSITAIPAVSTPGD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1340026348 336 DVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRV 377
Cdd:cd19476 229 DLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
386-510 |
5.26e-63 |
|
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349748 [Multi-domain] Cd Length: 126 Bit Score: 201.44 E-value: 5.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 386 MKKLSGGIRTALAQYRELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIG 465
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1340026348 466 SFEAALLAYVDRDHAPLMQEINQSGGYNDEIEGKLKGILDSFKAT 510
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKS 125
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
382-507 |
6.11e-62 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 198.43 E-value: 6.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 382 QTKIMKKLSGGIRTALAQYRELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVEL 461
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1340026348 462 SKIGSFEAALLAYVDRDHAPLMQEINQSGGYNDEIEGKLKGILDSF 507
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
96-377 |
1.47e-50 |
|
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: 173.90 E-value: 1.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 96 EVPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGK 175
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 176 TALaIDAIINQRDSGIKcVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGED 255
Cdd:cd01136 81 STL-LGMIARNTDADVN-VIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 256 ALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvnveyveaftkgevKGKTGSLTALPIIETQAG 335
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAG---------------NGEKGSITAFYTVLVEGD 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1340026348 336 DVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRV 377
Cdd:cd01136 224 DFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
29-408 |
5.16e-47 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 169.18 E-value: 5.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 29 GTIVSVSDGVIRIHGLaDCMQGEMIALPGNRYAIalnLERDSV-----GAVVMGPYADLAE---GMKVKCTGRILEVPVG 100
Cdd:PRK09099 26 GKVVEVIGTLLRVSGL-DVTLGELCELRQRDGTL---LQRAEVvgfsrDVALLSPFGELGGlsrGTRVIGLGRPLSVPVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 101 RGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALai 180
Cdd:PRK09099 102 PALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTL-- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 181 daiINQRDSGIKC---VYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDAL 257
Cdd:PRK09099 180 ---MGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 258 IIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARvnveyveaftkgevkGKTGSLTALPIIETQAGDV 337
Cdd:PRK09099 257 LMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM---------------GETGSITALYTVLAEDESG 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1340026348 338 SAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRELAAFSQ 408
Cdd:PRK09099 322 SDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQ 392
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
28-402 |
9.48e-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: 168.29 E-value: 9.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 28 EGTIVSVSDGVIRIHGLaDCMQGE--MIALPGNRYAIA--LNLERDSVgaVVMgPYAD---LAEGMKVKCTGRILEVPVG 100
Cdd:COG1157 20 SGRVTRVVGLLIEAVGP-DASIGElcEIETADGRPVLAevVGFRGDRV--LLM-PLGDlegISPGARVVPTGRPLSVPVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 101 RGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQReliIGdr---qtGKTA 177
Cdd:COG1157 96 DGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR---IGifagsgvGKST 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 178 LaIDAIINQRDSGIkcvyvaigqkastisNVV---------------RKLEEHGaLANTIVVVATASESAALQYLAPYAG 242
Cdd:COG1157 173 L-LGMIARNTEADV---------------NVIaligergrevrefieDDLGEEG-LARSVVVVATSDEPPLMRLRAAYTA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 243 CAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvnveyveaftkGevKGKTG 322
Cdd:COG1157 236 TAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERA-------------G--NGGKG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 323 SLTAL------------PIIETqagdvsafvptnVISITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKLS 390
Cdd:COG1157 301 SITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALA 368
|
410
....*....|..
gi 1340026348 391 GGIRTALAQYRE 402
Cdd:COG1157 369 RRLRRLLARYEE 380
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
87-443 |
3.23e-45 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 164.54 E-value: 3.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 87 KVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQREL 166
Cdd:PRK06936 87 EVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 167 IIGDRQTGKTALaIDAIINQRDSGIkCVYVAIGQKASTisnvVRKLEEHG----ALANTIVVVATASESAALQYLAPYAG 242
Cdd:PRK06936 167 IFAAAGGGKSTL-LASLIRSAEVDV-TVLALIGERGRE----VREFIESDlgeeGLRKAVLVVATSDRPSMERAKAGFVA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 243 CAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvnveyveaftkgevKGKTG 322
Cdd:PRK06936 241 TSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG---------------QSDKG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 323 SLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRE 402
Cdd:PRK06936 306 SITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEE 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1340026348 403 ---LAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQ 443
Cdd:PRK06936 386 velLLQIGEYQKGQDKEADQAIERIGAIRGFLRQGTHELSHFNE 429
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
1-446 |
1.56e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 162.68 E-value: 1.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 1 MQLNSTE-ISELIKQRIAQFN-VVSEAHNEGTIVSVSDGVIRIhGLADCMQGEMIALPGNRY-AIALNLERDSVgavVMG 77
Cdd:PRK06820 1 MKLPDIArLTPRLQQQLTRPSaPPEGLRYRGPIVEIGPTLLRA-SLPGVAQGELCRIEPQGMlAEVVSIEQEMA---LLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 78 PYAD---LAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLEHDgFSAVEAIAPGVIERQSVDQPVQTGYKSVD 154
Cdd:PRK06820 77 PFASsdgLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQ-WRELDCPPPSPLTRQPIEQMLTTGIRAID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 155 AMIPIGRGQRELIIGDRQTGKTALaIDAIINQRDSGIkCVYVAIGQKASTisnvVRKLEEHG----ALANTIVVVATaSE 230
Cdd:PRK06820 156 GILSCGEGQRIGIFAAAGVGKSTL-LGMLCADSAADV-MVLALIGERGRE----VREFLEQVltpeARARTVVVVAT-SD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 231 SAALQYL-APYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvnveyv 309
Cdd:PRK06820 229 RPALERLkGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 310 eaftkgevKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKL 389
Cdd:PRK06820 302 --------NSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAM 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1340026348 390 SGGIRTALAQYRE---LAAFSQFASDLDDATRKQLDHGQKVTELLKQK--QYAPMSVAQQSL 446
Cdd:PRK06820 374 AQKLRRMLACYQEielLVRVGEYQAGEDLQADEALQRYPAICAFLQQDhsETAHLETTLEHL 435
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
10-384 |
5.86e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 161.01 E-value: 5.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 10 ELIKQRIAQFNVVSEAhneGTIVSVSDGVIRIHGL----ADCMQgeMIALPGNRYAIALNLERDSVGAVVMgPYAdLAEG 85
Cdd:PRK08472 4 ESLKNKLQKFNLSPRF---GSITKISPTIIEADGLnpsvGDIVK--IESSDNGKECLGMVVVIEKEQFGIS-PFS-FIEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 86 MK----VKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGR 161
Cdd:PRK08472 77 FKigdkVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 162 GQRELIIGDRQTGKTALaIDAIINQRDSGIKCVYVaIGQKASTISNVVRKlEEHGALANTIVVVATASESAALQYLAPYA 241
Cdd:PRK08472 157 GQKLGIFAGSGVGKSTL-MGMIVKGCLAPIKVVAL-IGERGREIPEFIEK-NLGGDLENTVIVVATSDDSPLMRKYGAFC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 242 GCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvnveyveaftkGEVKGKt 321
Cdd:PRK08472 234 AMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERA-------------GKEEGK- 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1340026348 322 GSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTK 384
Cdd:PRK08472 300 GSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
74-449 |
1.11e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 160.27 E-value: 1.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 74 VVMGPYADLAE---GMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKgPLEHdGFSAV--EAIAPGVIERQSVDQPVQT 148
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGS-ALPK-GLAPVstDQDPPNPLKRPPIREPMEV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 149 GYKSVDAMIPIGRGQRELIIGDRQTGKTALAidAIINQRDSGIKCVYVAIGQKASTISNVV-RKLEEHGaLANTIVVVAT 227
Cdd:PRK07721 145 GVRAIDSLLTVGKGQRVGIFAGSGVGKSTLM--GMIARNTSADLNVIALIGERGREVREFIeRDLGPEG-LKRSIVVVAT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 228 ASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvnve 307
Cdd:PRK07721 222 SDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG----- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 308 yveaftkgevKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMK 387
Cdd:PRK07721 297 ----------TNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHK 366
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1340026348 388 KLSGGIRTALAQYRE------LAAFSQFAS-DLDDATRKQldhgQKVTELLKQKQYAPMSVAQQSLVLF 449
Cdd:PRK07721 367 EAANRFRELLSTYQNsedlinIGAYKRGSSrEIDEAIQFY----PQIISFLKQGTDEKATFEESIQALL 431
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-438 |
7.03e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 143.94 E-value: 7.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 29 GTIVSVSDGVIRIHgLADCMQGEMIAL-PGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRV 107
Cdd:PRK07594 23 GRIQDVSATLLNAW-LPGVFMGELCCIkPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 108 VNTLGAPIDGKgPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALaIDAIINQR 187
Cdd:PRK07594 102 IDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLCNAP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 188 DSGIKcVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQA 267
Cdd:PRK07594 180 DADSN-VLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 268 VAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvnveyveaftkgevKGKTGSLTALPIIETQAGDVSAFVPTNVIS 347
Cdd:PRK07594 259 RAAREIALAAGETAVSGEYPPGVFSALPRLLERTG---------------MGEKGSITAFYTVLVEGDDMNEPLADEVRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 348 ITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRE---LAAFSQFASDLDDATRKQLDHG 424
Cdd:PRK07594 324 LLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEvelLIRIGEYQRGVDTDTDKAIDTY 403
|
410
....*....|....
gi 1340026348 425 QKVTELLKQKQYAP 438
Cdd:PRK07594 404 PDICTFLRQSKDEV 417
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
29-402 |
9.03e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 143.98 E-value: 9.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 29 GTIVSVSDGVIRIHGLADCMQ-GEMIALP-GNRYAIA--LNLERDSVGAVVMGPYADLAEGMKVKCTGRiLEVPVGRGLL 104
Cdd:PRK06002 28 GTVSEVTASHYRVRGLSRFVRlGDFVAIRaDGGTHLGevVRVDPDGVTVKPFEPRIEIGLGDAVFRKGP-LRIRPDPSWK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 105 GRVVNTLGAPIDGKGPL-EHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGK-TALAIDA 182
Cdd:PRK06002 107 GRVINALGEPIDGLGPLaPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKsTLLAMLA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 183 iinqRDSGIKCVYVA-IGQKASTisnvVRK-LEEH--GALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALI 258
Cdd:PRK06002 187 ----RADAFDTVVIAlVGERGRE----VREfLEDTlaDNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 259 IYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvnveyveaftKGEvKGkTGSLTALPIIETQAGDVS 338
Cdd:PRK06002 259 IVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAG-----------PGA-EG-GGSITGIFSVLVDGDDHN 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1340026348 339 AFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRE 402
Cdd:PRK06002 326 DPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEE 389
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
94-376 |
2.93e-36 |
|
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: 135.81 E-value: 2.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 94 ILEVPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQT 173
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 174 GKTALAI----DAIINQRDSGIKCVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYF 249
Cdd:cd01135 81 PHNELAAqiarQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 250 R-DRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAarvnveyveaftkGEVKGKTGSLT 325
Cdd:cd01135 161 AyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERA-------------GRVEGRKGSIT 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1340026348 326 ALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSR 376
Cdd:cd01135 225 QIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
62-377 |
2.28e-34 |
|
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: 134.85 E-value: 2.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 62 IALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQS 141
Cdd:TIGR01039 43 VAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQST 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 142 VDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALAIDAI--INQRDSGIKcVYVAIGQKASTISNVVRKLEEHGALA 219
Cdd:TIGR01039 123 KVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELInnIAKEHGGYS-VFAGVGERTREGNDLYHEMKESGVID 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 220 NTIVVVATASESAALQYLAPYAGCAMGEYFRD-RGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLL 298
Cdd:TIGR01039 202 KTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQ 281
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1340026348 299 ERAARVnveyveaftkgevkgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRV 377
Cdd:TIGR01039 282 ERITST---------------KTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRL 345
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
82-433 |
3.45e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 133.86 E-value: 3.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 82 LAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLehdGFSAVEAIAPGVI---ERQSVDQPVQTGYKSVDAMIP 158
Cdd:PRK07196 75 VLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQL---GGSTPLQQQLPQIhplQRRAVDTPLDVGVNAINGLLT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 159 IGRGQRELIIGDRQTGKTALAidAIINQRDSGIKCVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLA 238
Cdd:PRK07196 152 IGKGQRVGLMAGSGVGKSVLL--GMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 239 PYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvnveyveaftKGEvk 318
Cdd:PRK07196 230 TELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG-----------NSS-- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 319 gKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSR----VGGAAQTKIMKKLSGGIr 394
Cdd:PRK07196 297 -GNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCY- 374
|
330 340 350
....*....|....*....|....*....|....*....
gi 1340026348 395 TALAQYRELAAFSQFASDLDDATRKQLDHGQKVTELLKQ 433
Cdd:PRK07196 375 ADYMAIKPLIPLGGYVAGADPMADQAVHYYPAITQFLRQ 413
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
91-443 |
9.12e-33 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 129.73 E-value: 9.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 91 TGRILEVPVGRGLLGRVVNTLGApIDGK-----GPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQRE 165
Cdd:PRK08149 76 TGKPLSVWVGEALLGAVLDPTGK-IVERfdappTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 166 LIIGDRQTGKTALaIDAIINQRDSGIkCVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAM 245
Cdd:PRK08149 155 GIFASAGCGKTSL-MNMLIEHSEADV-FVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTV 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 246 GEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVnveyveaftkgevkgKTGSLT 325
Cdd:PRK08149 233 AEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT---------------LAGSIT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 326 ALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRELAA 405
Cdd:PRK08149 298 AFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQL 377
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1340026348 406 FSQFA-------SDLDDATRKQldhgQKVTELLKQKQYAPMSVAQ 443
Cdd:PRK08149 378 FIDLGeyrrgenADNDRAMDKR----PALEAFLKQDVAEKSSFSD 418
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
85-451 |
1.07e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 126.74 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 85 GMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPL--EHDGFSAVEAIAPgvIERQSVDQPVQTGYKSVDAMIPIGRG 162
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIytDQRASRHSPPINP--LSRRPITEPLDVGVRAINAMLTVGKG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 163 QRELIIGDRQTGKTALAIdaiINQRDSGIKCVYVA-IGQKASTISNVVRK-LEEHGaLANTIVVVATASESAALQYLAPY 240
Cdd:PRK08972 163 QRMGLFAGSGVGKSVLLG---MMTRGTTADVIVVGlVGERGREVKEFIEEiLGEEG-RARSVVVAAPADTSPLMRLKGCE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 241 AGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvnveyveaftkGEVKGK 320
Cdd:PRK08972 239 TATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERA-------------GNGGPG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 321 TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQY 400
Cdd:PRK08972 306 QGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLY 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1340026348 401 RE------LAAFSQfASD--LDDATRKQldhgQKVTELLKQ--KQYAPMSVAQQSLVLFAA 451
Cdd:PRK08972 386 QQnrdlisIGAYKQ-GSDprIDNAIRLQ----PAMNAFLQQtmKEAVPYDMSVNMLKQLAA 441
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
84-376 |
2.64e-31 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 126.09 E-value: 2.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 84 EGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAV--EAIAPgvIERQSVDQPVQTGYKSVDAMIPIGR 161
Cdd:PRK04196 65 KDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDIngAPINP--VAREYPEEFIQTGISAIDGLNTLVR 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 162 GQR------------ELiigdrqtgktALAI--DAIINQRDSGIKCVYVAIGQKASTISNVVRKLEEHGALANTIVVVAT 227
Cdd:PRK04196 143 GQKlpifsgsglphnEL----------AAQIarQAKVLGEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 228 ASESAALQYLAPYAGCAMGEYFR-DRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAar 303
Cdd:PRK04196 213 ADDPAIERILTPRMALTAAEYLAfEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERA-- 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1340026348 304 vnveyveaftkGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSR 376
Cdd:PRK04196 288 -----------GRIKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
29-418 |
2.87e-31 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 125.40 E-value: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 29 GTIVSVSDGVIRIHGLADCMqGEMIALPGNRY----AIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLL 104
Cdd:PRK05922 21 GLLSRVSGNLLEAQGLSACL-GELCQISLSKSppilAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 105 GRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALaIDAII 184
Cdd:PRK05922 100 GRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSL-LSTIA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 185 NQRDSGIKcVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLS 264
Cdd:PRK05922 179 KGSKSTIN-VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 265 KQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvnveyveaftkgevKGKTGSLTALPIIETQAGDVSAFVPTn 344
Cdd:PRK05922 258 RWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG---------------NNDKGSITALYAILHYPNHPDIFTDY- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 345 VISITDGQIFLeTNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRE------LAAFSQ-FASDLDDAT 417
Cdd:PRK05922 322 LKSLLDGHFFL-TPQGKALASPPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEaldiiqLGAYVPgQDAHLDRAV 400
|
.
gi 1340026348 418 R 418
Cdd:PRK05922 401 K 401
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
73-404 |
1.73e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 123.55 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 73 AVVMgPYADLaEGMKVKCTGRILE----VPVGRGLLGRVVNTLGAPIDGKGPLEHDGFS-AVEAIAPGVIERQSVDQPVQ 147
Cdd:PRK08927 66 ALLM-PFGPL-EGVRRGCRAVIANaaaaVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPyPLRAPPPPAHSRARVGEPLD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 148 TGYKSVDAMIPIGRGQRELIIGDRQTGKTAL------AIDAIINqrdsgikcVYVAIGQKASTISNVVRK-LEEHGaLAN 220
Cdd:PRK08927 144 LGVRALNTFLTCCRGQRMGIFAGSGVGKSVLlsmlarNADADVS--------VIGLIGERGREVQEFLQDdLGPEG-LAR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 221 TIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLER 300
Cdd:PRK08927 215 SVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLER 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 301 AarvnveyveaftkGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRVGGA 380
Cdd:PRK08927 295 A-------------GPGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPG 361
|
330 340
....*....|....*....|....
gi 1340026348 381 AQTKIMKKLSGGIRTALAQYRELA 404
Cdd:PRK08927 362 CNDPEENPLVRRARQLMATYADME 385
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
86-377 |
3.07e-28 |
|
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: 117.13 E-value: 3.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 86 MKVKC--TGRILEVPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQ 163
Cdd:TIGR01040 63 KKTTCefTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 164 RELIIGD-------------RQTGKTALAIDAIINQRDSGIKCVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASE 230
Cdd:TIGR01040 143 KIPIFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLAND 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 231 SAALQYLAPYAGCAMGEYFR-DRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVnveyv 309
Cdd:TIGR01040 223 PTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV----- 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1340026348 310 eaftkgevKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRV 377
Cdd:TIGR01040 298 --------EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 357
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
76-377 |
4.53e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 113.67 E-value: 4.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 76 MGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDA 155
Cdd:PRK05688 82 VGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSING 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 156 MIPIGRGQRELIIGDRQTGKTALaIDAIINQRDSGIKCVYVaIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQ 235
Cdd:PRK05688 162 LLTVGRGQRLGLFAGTGVGKSVL-LGMMTRFTEADIIVVGL-IGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 236 YLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvnveyveaftkG 315
Cdd:PRK05688 240 LRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERA-------------G 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1340026348 316 EVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRV 377
Cdd:PRK05688 307 NAEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV 368
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
82-402 |
4.62e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 110.45 E-value: 4.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 82 LAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGkgPLEHDGFSAVEAIAPGV--IERQSVDQPVQTGYKSVDAMIPI 159
Cdd:PRK06793 76 VCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIhaFEREEITDVFETGIKSIDSMLTI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 160 GRGQRELIIGDRQTGKTALaIDAIINQRDSGIKCVYVaIGQKASTISNVVRK-LEEHGaLANTIVVVATASESAALQYLA 238
Cdd:PRK06793 154 GIGQKIGIFAGSGVGKSTL-LGMIAKNAKADINVISL-VGERGREVKDFIRKeLGEEG-MRKSVVVVATSDESHLMQLRA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 239 PYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPgreaFPGDVFYLHS---RLLERAArvnveyveaftkg 315
Cdd:PRK06793 231 AKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSG------------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 316 evKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRT 395
Cdd:PRK06793 294 --KTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRK 371
|
....*..
gi 1340026348 396 ALAQYRE 402
Cdd:PRK06793 372 ILSIYKE 378
|
|
| 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 |
6.74e-26 |
|
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: 100.22 E-value: 6.74e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1340026348 27 NEGTIVSVSDGVIRIHGLADCMQGEMIALPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGR 93
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
96-377 |
2.59e-23 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 102.55 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 96 EVPVGRGLLGRVVNTLGAPIDGKgPLEHDGFSAVEAIAP-GVIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTG 174
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGL-PAPDTGETGALITPPfNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 175 KTAL-AIDAIINQRDSgikCVYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYL-APYAgCAMGEYFRDR 252
Cdd:PRK07960 188 KSVLlGMMARYTQADV---IVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQgAAYA-TRIAEDFRDR 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 253 GEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvnveyveaftkGEVKGKTGSLTALPIIET 332
Cdd:PRK07960 264 GQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERA-------------GNGISGGGSITAFYTVLT 330
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1340026348 333 QAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRV 377
Cdd:PRK07960 331 EGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRA 375
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-377 |
1.36e-20 |
|
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: 91.51 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 96 EVPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGK 175
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 176 TALAIDAIIN-QRDSGIKCVYVAIGQKASTISNVVRKLEEHG-----ALANTIVVVATASESAALQYLAPYAGCAMGEYF 249
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGERTREGNDLYHEMKESGvinldGLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 250 RD-RGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVnveyveaftkgevkgKTGSLTALP 328
Cdd:cd01133 161 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST---------------KKGSITSVQ 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1340026348 329 IIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVNPGISVSRV 377
Cdd:cd01133 226 AVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
62-403 |
2.48e-20 |
|
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: 93.62 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 62 IALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQS 141
Cdd:COG0055 46 VAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQST 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 142 VDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALaIDAIIN---QRDSGIkCVYVAIGQKASTISNVVRKLEEHGAL 218
Cdd:COG0055 126 KTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL-IMELIHniaKEHGGV-SVFAGVGERTREGNDLYREMKESGVL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 219 ANTIVVVATASESAALQYLAPYAGCAMGEYFRD-RGEDALIIYDDLSK--QAVAyrQISLLLRRPPGReafpgdVFY--- 292
Cdd:COG0055 204 DKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRftQAGS--EVSALLGRMPSA------VGYqpt 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 293 LHS---RLLERAARVnveyveaftkgevkgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVN 369
Cdd:COG0055 276 LATemgALQERITST---------------KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVD 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1340026348 370 PGISVSR------VG----GAAQtkimkklsgGIRTALAQYREL 403
Cdd:COG0055 341 PLDSTSRildpliVGeehyRVAR---------EVQRILQRYKEL 375
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
136-376 |
3.74e-19 |
|
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: 87.63 E-value: 3.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 136 VIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALaIDAIINQRDSGIkCVYVAIGQKASTISNVVR----- 210
Cdd:cd01134 50 VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVI-SQSLSKWSNSDV-VIYVGCGERGNEMAEVLEefpel 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 211 KLEEHGA--LANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPG 288
Cdd:cd01134 128 KDPITGEslMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 289 dvfYLHSRL---LERAARVNveyveafTKGEvKGKTGSLTALPIIETQAGDVSAFVPTNVISITdgQIF--LETNLFNSG 363
Cdd:cd01134 208 ---YLGARLaefYERAGRVR-------CLGS-PGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRR 274
|
250
....*....|...
gi 1340026348 364 IRPAVNPGISVSR 376
Cdd:cd01134 275 HFPSINWLISYSK 287
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
57-355 |
2.29e-18 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 87.40 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 57 GNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLEHDgfsAVEAIAPGV 136
Cdd:PRK02118 36 GSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGE---PIEIGGPSV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 137 --IERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALAIdAIINQRDSGIkCVYVAIGQKASTISNVVRKLEE 214
Cdd:PRK02118 113 npVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA-RIALQAEADI-IILGGMGLTFDDYLFFKDTFEN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 215 HGALANTIVVVATASESAALQYLAPYAGCAMGEYFR-DRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDvfyL 293
Cdd:PRK02118 191 AGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGS---L 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1340026348 294 HSRLLERAARVnVEYVEAftkgevkgktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFL 355
Cdd:PRK02118 268 YSDLASRYEKA-VDFEDG----------GSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
71-403 |
1.76e-15 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 78.93 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 71 VGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLEHDGFSAVEAIAPGVIERQSVDQPVQTGY 150
Cdd:CHL00060 70 VRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 151 KSVDAMIPIGRGQRELIIGDRQTGKTALAIDAI--INQRDSGIKcVYVAIGQKASTISNVVRKLEEHGalantIVVVATA 228
Cdd:CHL00060 150 KVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELInnIAKAHGGVS-VFGGVGERTREGNDLYMEMKESG-----VINEQNI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 229 SES-AALQY----LAPYA-------GCAMGEYFRD-RGEDALIIYDDLSKQAVAYRQISLLLRRppgreaFPGDVFY--- 292
Cdd:CHL00060 224 AESkVALVYgqmnEPPGArmrvgltALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGR------MPSAVGYqpt 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 293 LHSR---LLERAARVnveyveaftkgevkgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNSGIRPAVN 369
Cdd:CHL00060 298 LSTEmgsLQERITST---------------KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 362
|
330 340 350
....*....|....*....|....*....|....*....
gi 1340026348 370 PGISVS-----RVGGAAQTKIMKKlsggIRTALAQYREL 403
Cdd:CHL00060 363 PLDSTStmlqpRIVGEEHYETAQR----VKQTLQRYKEL 397
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
194-369 |
2.39e-11 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 66.58 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 194 VYVAIGQKASTISNVvrkLEEHGALAN----------TIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDL 263
Cdd:PRK14698 686 IYIGCGERGNEMTDV---LEEFPKLKDpktgkplmerTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADST 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 264 SKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAARVnveyveaFTKGEvKGKTGSLTALPIIETQAGDVSAF 340
Cdd:PRK14698 763 SRWAEALREISGRLEEMPGEEGYPA---YLASKLaefYERAGRV-------VTLGS-DYRVGSVSVIGAVSPPGGDFSEP 831
|
170 180
....*....|....*....|....*....
gi 1340026348 341 VPTNVISITDGQIFLETNLFNSGIRPAVN 369
Cdd:PRK14698 832 VVQNTLRVVKVFWALDADLARRRHFPAIN 860
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
29-92 |
3.22e-11 |
|
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: 58.71 E-value: 3.22e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1340026348 29 GTIVSVSDGVIRIHGLADCMQGEMIALPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTG 92
Cdd:pfam02874 6 GPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
386-444 |
4.90e-10 |
|
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: 55.53 E-value: 4.90e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1340026348 386 MKKLSGGIRTALAQYRELAAFSQFASD--LDDATRKQLDHGQKVTELLKQKQYAPMSVAQQ 444
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDT 61
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
136-376 |
5.76e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 61.72 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 136 VIERQSVDQPVQTGYKSVDAMIPIGRGQRELIIGDRQTGKTALaIDAIINQRDSGIkCVYVAIGQKASTISNVVR---KL 212
Cdd:PRK04192 201 YKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVT-QHQLAKWADADI-VIYVGCGERGNEMTEVLEefpEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 213 EE----HGALANTIVVVAT------ASESAAlqylapYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPG 282
Cdd:PRK04192 279 IDpktgRPLMERTVLIANTsnmpvaAREASI------YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340026348 283 REAFPGdvfYLHSRL---LERAARVNveyveafTKGevkGKTGSLTALPIIETQAGDVSAFVPTNVISITdgQIF--LET 357
Cdd:PRK04192 353 EEGYPA---YLASRLaefYERAGRVK-------TLG---GEEGSVTIIGAVSPPGGDFSEPVTQNTLRIV--KVFwaLDA 417
|
250
....*....|....*....
gi 1340026348 358 NLFNSGIRPAVNPGISVSR 376
Cdd:PRK04192 418 ELADRRHFPAINWLTSYSL 436
|
|
| |
