|
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: 1025.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 1 MQLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADCMQGEMISLPGNRYAIALNLERDSVGAVVMGPYA 80
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 81 DLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIG 160
Cdd:PRK09281 81 DIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 161 RGQRELIIGDRQTGKTALAIDAIINQRDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPY 240
Cdd:PRK09281 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 241 AGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNAEyveaftkgevkGK 320
Cdd:PRK09281 241 AGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDE-----------LG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 321 TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQY 400
Cdd:PRK09281 310 GGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 401 RELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIGSFEAALLAYVDRDHA 480
Cdd:PRK09281 390 RELEAFAQFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHA 469
|
490 500 510
....*....|....*....|....*....|
gi 1861313569 481 PLMQEINQTGGYNDEIEGKLKGILDSFKAT 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: 1000.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 1 MQLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADCMQGEMISLPGNRYAIALNLERDSVGAVVMGPYA 80
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 81 DLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIG 160
Cdd:COG0056 81 GIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 161 RGQRELIIGDRQTGKTALAIDAIINQRDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPY 240
Cdd:COG0056 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 241 AGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNAEYveaftkgevkgK 320
Cdd:COG0056 241 AGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEL-----------G 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 321 TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQY 400
Cdd:COG0056 310 GGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 401 RELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIGSFEAALLAYVDRDHA 480
Cdd:COG0056 390 RELEAFAQFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHP 469
|
490 500 510
....*....|....*....|....*....|...
gi 1861313569 481 PLMQEINQTGGYNDEIEGKLKGILDSFKATQSW 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: 940.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 2 QLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADCMQGEMISLPGNRYAIALNLERDSVGAVVMGPYAD 81
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 82 LAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGR 161
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 162 GQRELIIGDRQTGKTALAIDAIINQRDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYA 241
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 242 GCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNAEyveaftkgevKGKt 321
Cdd:TIGR00962 241 GCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDE----------KGG- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 322 GSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYR 401
Cdd:TIGR00962 310 GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 402 ELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIGSFEAALLAYVDRDHAP 481
Cdd:TIGR00962 390 ELEAFSQFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPD 469
|
490 500 510
....*....|....*....|....*....|..
gi 1861313569 482 LMQEINQTGGYNDEIEGKLKGILDSFKATQSW 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: 789.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 1 MQLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADCMQGEMISLPGNRYAIALNLERDSVGAVVMGPYA 80
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 81 DLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIG 160
Cdd:PRK13343 81 DILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 161 RGQRELIIGDRQTGKTALAIDAIINQRDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPY 240
Cdd:PRK13343 161 RGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 241 AGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNAEYveaftkgevkgK 320
Cdd:PRK13343 241 AGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPEL-----------G 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 321 TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQY 400
Cdd:PRK13343 310 GGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 401 RELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIGSFEAALLAYVDRDHA 480
Cdd:PRK13343 390 LELEAFTRFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFA 469
|
490 500 510
....*....|....*....|....*....|...
gi 1861313569 481 PLMQEINQTGGYNDEIEGKLKGILDSFKATQSW 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: 684.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 27 NEGTIVSVSDGVIRIHGLADCMQGEMISLPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGR 106
Cdd:CHL00059 6 NTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 107 VVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTALAIDAIINQ 186
Cdd:CHL00059 86 VVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 187 RDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQ 266
Cdd:CHL00059 166 KGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 267 AVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNAEYveaftkGEvkgktGSLTALPIIETQAGDVSAFVPTNVI 346
Cdd:CHL00059 246 AQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQL------GE-----GSMTALPIVETQAGDVSAYIPTNVI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 347 SITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRELAAFSQFASDLDDATRKQLDHGQK 426
Cdd:CHL00059 315 SITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 427 VTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIGSFEAALLAYVDRDHAPLMQEINQTGGYNDEIEGKLKGILDS 506
Cdd:CHL00059 395 LRELLKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQE 474
|
....*.
gi 1861313569 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: 557.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 94 ILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQT 173
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 174 GKTALAIDAIINQRDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRG 253
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 254 EDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNAEYveaftkgevkgKTGSLTALPIIETQ 333
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEL-----------GGGSLTALPIIETQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1861313569 334 AGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVG 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: 527.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 29 GTIVSVSDGVIRIHGLADCMQGEMISLPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVV 108
Cdd:TIGR03324 29 GTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERTGRVMDVPVGDGLLGRVV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 109 NTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTALAIDAIINQRD 188
Cdd:TIGR03324 109 DPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDRQTGKTAIAIDTILNQKG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 189 SGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAV 268
Cdd:TIGR03324 189 RNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSIGEHFMEQGRDVLIVYDDLTQHAR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 269 AYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNAEYveaftkgevkgKTGSLTALPIIETQAGDVSAFVPTNVISI 348
Cdd:TIGR03324 269 AYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEEL-----------GGGSLTALPIIETEAQNISAYIPTNLISI 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 349 TDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRELAAFSQFASDLDDATRKQLDHGQKVT 428
Cdd:TIGR03324 338 TDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDENTRKTIEHGRRIR 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861313569 429 ELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIGSFEAALLAYVDRDHAPLMQEINQTGGYNDE 495
Cdd:TIGR03324 418 ACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSDE 484
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
61-472 |
2.60e-116 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 354.73 E-value: 2.60e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 61 AIALNLERDS-VGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPID------GKGPLDHDG-FSAVEAI 132
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQtLGKVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 133 APGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTALAIDAIINQ--------RDSGIKCIYVAIGQKAST 204
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 205 ISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGRE 284
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGRE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 285 AFPGDVFYLHSRLLERAARVNAeyveafTKGevkgkTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGI 364
Cdd:PTZ00185 320 AYPGDVFYLHSRLLERAAMLSP------GKG-----GGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQ 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 365 RPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRELAAFSQFASDLDDATrkqLDHGQKVTELLKQKQyaPMSVAQQ 444
Cdd:PTZ00185 389 RPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNA 463
|
410 420
....*....|....*....|....*...
gi 1861313569 445 SLVLFAAERGYLADVELSKIGSFEAALL 472
Cdd:PTZ00185 464 LVSLYACLNGYLDDVKVNYAKLYEYLLV 491
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
149-375 |
1.11e-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: 334.71 E-value: 1.11e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 149 GYKAVDSMIPIGRGQRELIIGDRQTGKTALAiDAIINQRDSGIkCIYVAIGQKASTISNVVRKLEEHGALANTIVVVATA 228
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 229 SESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARvnaey 308
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGR----- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861313569 309 veaftkgeVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVS 375
Cdd:pfam00006 154 --------VKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
30-440 |
2.29e-109 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 334.63 E-value: 2.29e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 30 TIVSVSDGVIRIHGLADCMQGEMISLPGNRYAIA--LNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRV 107
Cdd:PRK07165 4 KIKSIFDYIVEVKGEYDYQQNQFFTLKNNPNVKAfvISATEDKAYLLINNEKGKIKINDELIELNNTNKVKTSKEYFGKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 108 VNTLGAPI---------DGKGPLDHDGFsaveAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTAL 178
Cdd:PRK07165 84 IDIDGNIIypeaqnplsKKFLPNTSSIF----NLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 179 AIDAIINQRDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVAtASESAALQYLAPYAGCAMGE---YFrdrgED 255
Cdd:PRK07165 160 ALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAEnisYN----DD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 256 ALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvnaeyveaftkGEVKGKTgSLTALPIIETQAG 335
Cdd:PRK07165 235 VLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERA-------------GKFKNRK-TITALPILQTVDN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 336 DVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRELAAFSQFASDLDD 415
Cdd:PRK07165 301 DITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNK 380
|
410 420
....*....|....*....|....*
gi 1861313569 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 |
1.10e-105 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 316.70 E-value: 1.10e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 97 VPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKT 176
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 177 ALAIDAIINQ-RDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGED 255
Cdd:cd19476 82 VLAMQLARNQaKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 256 ALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARvnaeyveaftkgeVKGKTGSLTALPIIETQAG 335
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGK-------------VKDGGGSITAIPAVSTPGD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1861313569 336 DVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRV 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 |
1.93e-63 |
|
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349748 [Multi-domain] Cd Length: 126 Bit Score: 202.60 E-value: 1.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 386 MKKLSGGIRTALAQYRELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIG 465
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1861313569 466 SFEAALLAYVDRDHAPLMQEINQTGGYNDEIEGKLKGILDSFKAT 510
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKS 125
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
382-507 |
2.90e-62 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 199.59 E-value: 2.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 382 QTKIMKKLSGGIRTALAQYRELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVEL 461
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1861313569 462 SKIGSFEAALLAYVDRDHAPLMQEINQTGGYNDEIEGKLKGILDSF 507
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
96-377 |
5.70e-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: 5.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 96 EVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGK 175
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 176 TALaIDAIINQRDSGIKCIyVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGED 255
Cdd:cd01136 81 STL-LGMIARNTDADVNVI-ALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 256 ALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvnaeyveaftkgevKGKTGSLTALPIIETQAG 335
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAG---------------NGEKGSITAFYTVLVEGD 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1861313569 336 DVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRV 377
Cdd:cd01136 224 DFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
28-402 |
1.38e-47 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 170.60 E-value: 1.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 28 EGTIVSVSDGVIRIHGLaDCMQGE--MISLPGNRYAIA--LNLERDSVgaVVMgPYAD---LAEGMKVKCTGRILEVPVG 100
Cdd:COG1157 20 SGRVTRVVGLLIEAVGP-DASIGElcEIETADGRPVLAevVGFRGDRV--LLM-PLGDlegISPGARVVPTGRPLSVPVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 101 RGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQReliIGdr---qtGKTA 177
Cdd:COG1157 96 DGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR---IGifagsgvGKST 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 178 LaIDAIINQRDSGIkciyvaigqkastisNVV---------------RKLEEHGaLANTIVVVATASESAALQYLAPYAG 242
Cdd:COG1157 173 L-LGMIARNTEADV---------------NVIaligergrevrefieDDLGEEG-LARSVVVVATSDEPPLMRLRAAYTA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 243 CAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvnaeyveaftkGevKGKTG 322
Cdd:COG1157 236 TAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERA-------------G--NGGKG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 323 SLTAL------------PIIETqagdvsafvptnVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLS 390
Cdd:COG1157 301 SITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALA 368
|
410
....*....|..
gi 1861313569 391 GGIRTALAQYRE 402
Cdd:COG1157 369 RRLRRLLARYEE 380
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
29-408 |
3.54e-47 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 169.56 E-value: 3.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 29 GTIVSVSDGVIRIHGLaDCMQGEMISLPGNRYAIalnLERDSV-----GAVVMGPYADLAE---GMKVKCTGRILEVPVG 100
Cdd:PRK09099 26 GKVVEVIGTLLRVSGL-DVTLGELCELRQRDGTL---LQRAEVvgfsrDVALLSPFGELGGlsrGTRVIGLGRPLSVPVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 101 RGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTALai 180
Cdd:PRK09099 102 PALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTL-- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 181 daiINQRDSGIKC---IYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDAL 257
Cdd:PRK09099 180 ---MGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 258 IIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARvnaeyveaftkgevkGKTGSLTALPIIETQAGDV 337
Cdd:PRK09099 257 LMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM---------------GETGSITALYTVLAEDESG 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861313569 338 SAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRELAAFSQ 408
Cdd:PRK09099 322 SDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQ 392
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
1-446 |
4.28e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 166.91 E-value: 4.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 1 MQLNSTE-ISELIKQRIAQFN-VVSEAHNEGTIVSVSDGVIRIhGLADCMQGEMISLPGNRY-AIALNLERDSVgavVMG 77
Cdd:PRK06820 1 MKLPDIArLTPRLQQQLTRPSaPPEGLRYRGPIVEIGPTLLRA-SLPGVAQGELCRIEPQGMlAEVVSIEQEMA---LLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 78 PYAD---LAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDgFSAVEAIAPGVIERQSVDQPVQTGYKAVD 154
Cdd:PRK06820 77 PFASsdgLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQ-WRELDCPPPSPLTRQPIEQMLTTGIRAID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 155 SMIPIGRGQRELIIGDRQTGKTALaIDAIINQRDSGIkCIYVAIGQKASTisnvVRKLEEHG----ALANTIVVVATaSE 230
Cdd:PRK06820 156 GILSCGEGQRIGIFAAAGVGKSTL-LGMLCADSAADV-MVLALIGERGRE----VREFLEQVltpeARARTVVVVAT-SD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 231 SAALQYL-APYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvNAEyv 309
Cdd:PRK06820 229 RPALERLkGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG--NSD-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 310 eaftkgevkgkTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKL 389
Cdd:PRK06820 305 -----------RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAM 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861313569 390 SGGIRTALAQYRE---LAAFSQFASDLDDATRKQLDHGQKVTELLKQK--QYAPMSVAQQSL 446
Cdd:PRK06820 374 AQKLRRMLACYQEielLVRVGEYQAGEDLQADEALQRYPAICAFLQQDhsETAHLETTLEHL 435
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
74-449 |
3.80e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 164.13 E-value: 3.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 74 VVMGPYADLAE---GMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGY 150
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 151 KAVDSMIPIGRGQRELIIGDRQTGKTALaIDAIINQRDSGIKCIYVaIGQKASTISNVV-RKLEEHGaLANTIVVVATAS 229
Cdd:PRK07721 147 RAIDSLLTVGKGQRVGIFAGSGVGKSTL-MGMIARNTSADLNVIAL-IGERGREVREFIeRDLGPEG-LKRSIVVVATSD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 230 ESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArVNAEyv 309
Cdd:PRK07721 224 QPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG-TNAS-- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 310 eaftkgevkgktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKL 389
Cdd:PRK07721 301 ------------GSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEA 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861313569 390 SGGIRTALAQYRE------LAAFSQFAS-DLDDATRKQldhgQKVTELLKQKQYAPMSVAQQSLVLF 449
Cdd:PRK07721 369 ANRFRELLSTYQNsedlinIGAYKRGSSrEIDEAIQFY----PQIISFLKQGTDEKATFEESIQALL 431
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
87-443 |
8.75e-45 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 163.38 E-value: 8.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 87 KVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQREL 166
Cdd:PRK06936 87 EVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 167 IIGDRQTGKTALaIDAIINQRDSGIkCIYVAIGQKASTisnvVRKLEEHG----ALANTIVVVATASESAALQYLAPYAG 242
Cdd:PRK06936 167 IFAAAGGGKSTL-LASLIRSAEVDV-TVLALIGERGRE----VREFIESDlgeeGLRKAVLVVATSDRPSMERAKAGFVA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 243 CAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvnaeyveaftkgevKGKTG 322
Cdd:PRK06936 241 TSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG---------------QSDKG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 323 SLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRE 402
Cdd:PRK06936 306 SITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEE 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1861313569 403 ---LAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQ 443
Cdd:PRK06936 386 velLLQIGEYQKGQDKEADQAIERIGAIRGFLRQGTHELSHFNE 429
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
10-384 |
2.71e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 161.78 E-value: 2.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 10 ELIKQRIAQFNVVSEAhneGTIVSVSDGVIRIHGL----ADCMQgeMISLPGNRYAIALNLERDSVGAVVMgPYAdLAEG 85
Cdd:PRK08472 4 ESLKNKLQKFNLSPRF---GSITKISPTIIEADGLnpsvGDIVK--IESSDNGKECLGMVVVIEKEQFGIS-PFS-FIEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 86 MK----VKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGR 161
Cdd:PRK08472 77 FKigdkVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 162 GQRELIIGDRQTGKTALaIDAIINQRDSGIKCIYVaIGQKASTISNVVRKlEEHGALANTIVVVATASESAALQYLAPYA 241
Cdd:PRK08472 157 GQKLGIFAGSGVGKSTL-MGMIVKGCLAPIKVVAL-IGERGREIPEFIEK-NLGGDLENTVIVVATSDDSPLMRKYGAFC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 242 GCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvnaeyveaftkGEVKGKt 321
Cdd:PRK08472 234 AMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERA-------------GKEEGK- 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861313569 322 GSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTK 384
Cdd:PRK08472 300 GSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-438 |
9.39e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 143.94 E-value: 9.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 29 GTIVSVSDGVIRIHgLADCMQGEMISL-PGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRV 107
Cdd:PRK07594 23 GRIQDVSATLLNAW-LPGVFMGELCCIkPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 108 VNTLGAPIDGKgPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTALaIDAIINQR 187
Cdd:PRK07594 102 IDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLCNAP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 188 DSGIKcIYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQA 267
Cdd:PRK07594 180 DADSN-VLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 268 VAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvnaeyveaftkgevKGKTGSLTALPIIETQAGDVSAFVPTNVIS 347
Cdd:PRK07594 259 RAAREIALAAGETAVSGEYPPGVFSALPRLLERTG---------------MGEKGSITAFYTVLVEGDDMNEPLADEVRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 348 ITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRE---LAAFSQFASDLDDATRKQLDHG 424
Cdd:PRK07594 324 LLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEvelLIRIGEYQRGVDTDTDKAIDTY 403
|
410
....*....|....
gi 1861313569 425 QKVTELLKQKQYAP 438
Cdd:PRK07594 404 PDICTFLRQSKDEV 417
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
29-402 |
1.12e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 140.90 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 29 GTIVSVSDGVIRIHGLADCMQ-GEMISLP-GNRYAIA--LNLERDSVGAVVMGPYADLAEGMKVKCTGRiLEVPVGRGLL 104
Cdd:PRK06002 28 GTVSEVTASHYRVRGLSRFVRlGDFVAIRaDGGTHLGevVRVDPDGVTVKPFEPRIEIGLGDAVFRKGP-LRIRPDPSWK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 105 GRVVNTLGAPIDGKGPLDH-DGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGK-TALAIDA 182
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKsTLLAMLA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 183 iinqRDSGIKCIYVA-IGQKASTisnvVRK-LEEH--GALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALI 258
Cdd:PRK06002 187 ----RADAFDTVVIAlVGERGRE----VREfLEDTlaDNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 259 IYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvnaeyveaftKGEvKGkTGSLTALPIIETQAGDVS 338
Cdd:PRK06002 259 IVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAG-----------PGA-EG-GGSITGIFSVLVDGDDHN 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861313569 339 AFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRE 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 |
4.92e-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: 135.43 E-value: 4.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 94 ILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQT 173
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 174 GKTALAI----DAIINQRDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYF 249
Cdd:cd01135 81 PHNELAAqiarQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 250 R-DRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAarvnaeyveaftkGEVKGKTGSLT 325
Cdd:cd01135 161 AyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERA-------------GRVEGRKGSIT 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1861313569 326 ALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSR 376
Cdd:cd01135 225 QIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
82-433 |
4.54e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 136.17 E-value: 4.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 82 LAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGR 161
Cdd:PRK07196 75 VLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 162 GQRELIIGDRQTGKTALAidAIINQRDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYA 241
Cdd:PRK07196 155 GQRVGLMAGSGVGKSVLL--GMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATEL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 242 GCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvNAEyveaftkgevkgKT 321
Cdd:PRK07196 233 CHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG--NSS------------GN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 322 GSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSR----VGGAAQTKIMKKLSGGIrTAL 397
Cdd:PRK07196 299 GTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCY-ADY 377
|
330 340 350
....*....|....*....|....*....|....*.
gi 1861313569 398 AQYRELAAFSQFASDLDDATRKQLDHGQKVTELLKQ 433
Cdd:PRK07196 378 MAIKPLIPLGGYVAGADPMADQAVHYYPAITQFLRQ 413
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
62-377 |
1.66e-33 |
|
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: 132.15 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 62 IALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQS 141
Cdd:TIGR01039 43 VAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQST 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 142 VDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTALAIDAI--INQRDSGIKcIYVAIGQKASTISNVVRKLEEHGALA 219
Cdd:TIGR01039 123 KVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELInnIAKEHGGYS-VFAGVGERTREGNDLYHEMKESGVID 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 220 NTIVVVATASESAALQYLAPYAGCAMGEYFRD-RGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLL 298
Cdd:TIGR01039 202 KTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQ 281
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861313569 299 ERAARVnaeyveaftkgevkgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRV 377
Cdd:TIGR01039 282 ERITST---------------KTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRL 345
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
91-443 |
9.40e-33 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 129.73 E-value: 9.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 91 TGRILEVPVGRGLLGRVVNTLGApIDGK-----GPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRE 165
Cdd:PRK08149 76 TGKPLSVWVGEALLGAVLDPTGK-IVERfdappTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 166 LIIGDRQTGKTALaIDAIINQRDSGIkciYVA--IGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGC 243
Cdd:PRK08149 155 GIFASAGCGKTSL-MNMLIEHSEADV---FVIglIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVAT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 244 AMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVnaeyveaftkgevkgKTGS 323
Cdd:PRK08149 231 TVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT---------------LAGS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 324 LTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYREL 403
Cdd:PRK08149 296 ITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEEL 375
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1861313569 404 AAFSQFA-------SDLDDATRKQldhgQKVTELLKQKQYAPMSVAQ 443
Cdd:PRK08149 376 QLFIDLGeyrrgenADNDRAMDKR----PALEAFLKQDVAEKSSFSD 418
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
85-451 |
2.73e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 128.66 E-value: 2.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 85 GMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPL--DHDGFSAVEAIAPgvIERQSVDQPVQTGYKAVDSMIPIGRG 162
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIytDQRASRHSPPINP--LSRRPITEPLDVGVRAINAMLTVGKG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 163 QRELIIGDRQTGKTALaidAIINQRDSGIKCIYVA-IGQKASTISNVVRK-LEEHGaLANTIVVVATASESAALQYLAPY 240
Cdd:PRK08972 163 QRMGLFAGSGVGKSVL---LGMMTRGTTADVIVVGlVGERGREVKEFIEEiLGEEG-RARSVVVAAPADTSPLMRLKGCE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 241 AGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvnaeyveaftkGEVKGK 320
Cdd:PRK08972 239 TATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERA-------------GNGGPG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 321 TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQY 400
Cdd:PRK08972 306 QGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLY 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861313569 401 RE------LAAFSQfASD--LDDATRKQldhgQKVTELLKQ--KQYAPMSVAQQSLVLFAA 451
Cdd:PRK08972 386 QQnrdlisIGAYKQ-GSDprIDNAIRLQ----PAMNAFLQQtmKEAVPYDMSVNMLKQLAA 441
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
29-418 |
1.12e-31 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 126.56 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 29 GTIVSVSDGVIRIHGLADCMqGEM--ISLP--GNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLL 104
Cdd:PRK05922 21 GLLSRVSGNLLEAQGLSACL-GELcqISLSksPPILAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 105 GRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTALaIDAII 184
Cdd:PRK05922 100 GRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSL-LSTIA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 185 NQRDSGIKCIYVaIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLS 264
Cdd:PRK05922 179 KGSKSTINVIAL-IGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 265 KQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvnaeyveaftkgevKGKTGSLTALPIIETQAGDVSAFVPTn 344
Cdd:PRK05922 258 RWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG---------------NNDKGSITALYAILHYPNHPDIFTDY- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 345 VISITDGQIFLeTNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRE------LAAFSQ-FASDLDDAT 417
Cdd:PRK05922 322 LKSLLDGHFFL-TPQGKALASPPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEaldiiqLGAYVPgQDAHLDRAV 400
|
.
gi 1861313569 418 R 418
Cdd:PRK05922 401 K 401
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
73-404 |
1.26e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 123.94 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 73 AVVMgPYADLaEGMKVKCTGRILE----VPVGRGLLGRVVNTLGAPIDGKGPLDHDGFS-AVEAIAPGVIERQSVDQPVQ 147
Cdd:PRK08927 66 ALLM-PFGPL-EGVRRGCRAVIANaaaaVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPyPLRAPPPPAHSRARVGEPLD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 148 TGYKAVDSMIPIGRGQRELIIGDRQTGKTALaIDAIINQRDSGIKCIYVaIGQKASTISNVVRK-LEEHGaLANTIVVVA 226
Cdd:PRK08927 144 LGVRALNTFLTCCRGQRMGIFAGSGVGKSVL-LSMLARNADADVSVIGL-IGERGREVQEFLQDdLGPEG-LARSVVVVA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 227 TASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvna 306
Cdd:PRK08927 221 TSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERA----- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 307 eyveaftkGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIM 386
Cdd:PRK08927 296 --------GPGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEE 367
|
330
....*....|....*...
gi 1861313569 387 KKLSGGIRTALAQYRELA 404
Cdd:PRK08927 368 NPLVRRARQLMATYADME 385
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
84-376 |
1.64e-30 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 123.78 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 84 EGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAV--EAIAPgvIERQSVDQPVQTGYKAVDSMIPIGR 161
Cdd:PRK04196 65 KDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDIngAPINP--VAREYPEEFIQTGISAIDGLNTLVR 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 162 GQR------------ELiigdrqtgktALAI--DAIINQRDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVAT 227
Cdd:PRK04196 143 GQKlpifsgsglphnEL----------AAQIarQAKVLGEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 228 ASESAALQYLAPYAGCAMGEYFR-DRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAar 303
Cdd:PRK04196 213 ADDPAIERILTPRMALTAAEYLAfEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERA-- 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861313569 304 vnaeyveaftkGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSR 376
Cdd:PRK04196 288 -----------GRIKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
86-377 |
9.58e-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: 115.97 E-value: 9.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 86 MKVKC--TGRILEVPVGRGLLGRVVNTLGAPIDgKGP-------LDHDGfsavEAIAPgvIERQSVDQPVQTGYKAVDSM 156
Cdd:TIGR01040 63 KKTTCefTGDILRTPVSEDMLGRVFNGSGKPID-KGPpvlaedyLDING----QPINP--YARIYPEEMIQTGISAIDVM 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 157 IPIGRGQRELIIGD-------------RQTGKTALAIDAIINQRDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIV 223
Cdd:TIGR01040 136 NSIARGQKIPIFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 224 VVATASESAALQYLAPYAGCAMGEYFR-DRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAA 302
Cdd:TIGR01040 216 FLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAG 295
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861313569 303 RVnaeyveaftkgevKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRV 377
Cdd:TIGR01040 296 RV-------------EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 357
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
76-377 |
3.38e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 114.06 E-value: 3.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 76 MGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDS 155
Cdd:PRK05688 82 VGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSING 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 156 MIPIGRGQRELIIGDRQTGKTALaidAIINQRDSGIKCIYVA-IGQKASTISNVVRKLEEHGALANTIVVVATASESAAL 234
Cdd:PRK05688 162 LLTVGRGQRLGLFAGTGVGKSVL---LGMMTRFTEADIIVVGlIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLM 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 235 QYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAArvNAEyveaftK 314
Cdd:PRK05688 239 RLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAE------P 310
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861313569 315 GEvkgktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRV 377
Cdd:PRK05688 311 GG-----GSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV 368
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
27-93 |
2.86e-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: 101.38 E-value: 2.86e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861313569 27 NEGTIVSVSDGVIRIHGLADCMQGEMISLPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGR 93
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
82-402 |
7.20e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 109.68 E-value: 7.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 82 LAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGkgPLDHDGFSAVEAIAPGV--IERQSVDQPVQTGYKAVDSMIPI 159
Cdd:PRK06793 76 VCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIhaFEREEITDVFETGIKSIDSMLTI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 160 GRGQRELIIGDRQTGKTALaIDAIINQRDSGIKCIYVaIGQKASTISNVVRK-LEEHGaLANTIVVVATASESAALQYLA 238
Cdd:PRK06793 154 GIGQKIGIFAGSGVGKSTL-LGMIAKNAKADINVISL-VGERGREVKDFIRKeLGEEG-MRKSVVVVATSDESHLMQLRA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 239 PYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPgreaFPGDVFYLHS---RLLERAArvnaeyveaftkg 315
Cdd:PRK06793 231 AKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSG------------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 316 evKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRT 395
Cdd:PRK06793 294 --KTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRK 371
|
....*..
gi 1861313569 396 ALAQYRE 402
Cdd:PRK06793 372 ILSIYKE 378
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
96-377 |
1.81e-23 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 102.94 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 96 EVPVGRGLLGRVVNTLGAPIDGKGPLDhDGFSAVEAIAP-GVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTG 174
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPD-TGETGALITPPfNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 175 KTAL-AIDAIINQRDsgikCIYVA-IGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYL-APYAgCAMGEYFRD 251
Cdd:PRK07960 188 KSVLlGMMARYTQAD----VIVVGlIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQgAAYA-TRIAEDFRD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 252 RGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAarvnaeyveaftkGEVKGKTGSLTALPIIE 331
Cdd:PRK07960 263 RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERA-------------GNGISGGGSITAFYTVL 329
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1861313569 332 TQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRV 377
Cdd:PRK07960 330 TEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRA 375
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
62-403 |
2.41e-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: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 62 IALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQS 141
Cdd:COG0055 46 VAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQST 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 142 VDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTALaIDAIIN---QRDSGIkCIYVAIGQKASTISNVVRKLEEHGAL 218
Cdd:COG0055 126 KTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL-IMELIHniaKEHGGV-SVFAGVGERTREGNDLYREMKESGVL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 219 ANTIVVVATASESAALQYLAPYAGCAMGEYFRD-RGEDALIIYDDLSK--QAVAyrQISLLLRRPPGReafpgdVFY--- 292
Cdd:COG0055 204 DKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRftQAGS--EVSALLGRMPSA------VGYqpt 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 293 LHS---RLLERAARVnaeyveaftkgevkgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVN 369
Cdd:COG0055 276 LATemgALQERITST---------------KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVD 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1861313569 370 PGISVSR------VG----GAAQtkimkklsgGIRTALAQYREL 403
Cdd:COG0055 341 PLDSTSRildpliVGeehyRVAR---------EVQRILQRYKEL 375
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-377 |
1.04e-19 |
|
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: 89.20 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 96 EVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGK 175
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 176 TALAIDAIIN-QRDSGIKCIYVAIGQKASTISNVVRKLEEHG-----ALANTIVVVATASESAALQYLAPYAGCAMGEYF 249
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGERTREGNDLYHEMKESGvinldGLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 250 RD-RGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVnaeyveaftkgevkgKTGSLTALP 328
Cdd:cd01133 161 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST---------------KKGSITSVQ 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1861313569 329 IIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVNPGISVSRV 377
Cdd:cd01133 226 AVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
136-376 |
2.40e-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: 88.40 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 136 VIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTALaIDAIINQRDSGIkCIYVAIGQKASTISNVVR----- 210
Cdd:cd01134 50 VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVI-SQSLSKWSNSDV-VIYVGCGERGNEMAEVLEefpel 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 211 KLEEHGA--LANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPG 288
Cdd:cd01134 128 KDPITGEslMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 289 dvfYLHSRL---LERAARVNaeyveafTKGEvKGKTGSLTALPIIETQAGDVSAFVPTNVISITdgQIF--LETNLFNAG 363
Cdd:cd01134 208 ---YLGARLaefYERAGRVR-------CLGS-PGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRR 274
|
250
....*....|...
gi 1861313569 364 IRPAVNPGISVSR 376
Cdd:cd01134 275 HFPSINWLISYSK 287
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
57-355 |
4.57e-18 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 86.63 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 57 GNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDgfsAVEAIAPGV 136
Cdd:PRK02118 36 GSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGE---PIEIGGPSV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 137 --IERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTALAIdAIINQRDSGIkCIYVAIGQKASTISNVVRKLEE 214
Cdd:PRK02118 113 npVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA-RIALQAEADI-IILGGMGLTFDDYLFFKDTFEN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 215 HGALANTIVVVATASESAALQYLAPYAGCAMGEYFR-DRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDvfyL 293
Cdd:PRK02118 191 AGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGS---L 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861313569 294 HSRLlerAARvnaeYVEA--FTKGevkgktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFL 355
Cdd:PRK02118 268 YSDL---ASR----YEKAvdFEDG------GSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
71-403 |
3.66e-15 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 77.77 E-value: 3.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 71 VGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGY 150
Cdd:CHL00060 70 VRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 151 KAVDSMIPIGRGQRELIIGDRQTGKTALAIDAI--INQRDSGIKcIYVAIGQKASTISNVVRKLEEHGalantIVVVATA 228
Cdd:CHL00060 150 KVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELInnIAKAHGGVS-VFGGVGERTREGNDLYMEMKESG-----VINEQNI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 229 SES-AALQY----LAPYA-------GCAMGEYFRD-RGEDALIIYDDLSKQAVAYRQISLLLRRppgreaFPGDVFY--- 292
Cdd:CHL00060 224 AESkVALVYgqmnEPPGArmrvgltALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGR------MPSAVGYqpt 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 293 LHSR---LLERAARVnaeyveaftkgevkgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLFNAGIRPAVN 369
Cdd:CHL00060 298 LSTEmgsLQERITST---------------KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 362
|
330 340 350
....*....|....*....|....*....|....*....
gi 1861313569 370 PGISVS-----RVGGAAQTKIMKKlsggIRTALAQYREL 403
Cdd:CHL00060 363 PLDSTStmlqpRIVGEEHYETAQR----VKQTLQRYKEL 397
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
29-92 |
1.31e-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: 59.87 E-value: 1.31e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861313569 29 GTIVSVSDGVIRIHGLADCMQGEMISLPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTG 92
Cdd:pfam02874 6 GPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
194-369 |
1.98e-11 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 66.58 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 194 IYVAIGQKASTISNVvrkLEEHGALAN----------TIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDL 263
Cdd:PRK14698 686 IYIGCGERGNEMTDV---LEEFPKLKDpktgkplmerTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADST 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 264 SKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAARV---NAEYveaftkgevkgKTGSLTALPIIETQAGDV 337
Cdd:PRK14698 763 SRWAEALREISGRLEEMPGEEGYPA---YLASKLaefYERAGRVvtlGSDY-----------RVGSVSVIGAVSPPGGDF 828
|
170 180 190
....*....|....*....|....*....|..
gi 1861313569 338 SAFVPTNVISITDGQIFLETNLFNAGIRPAVN 369
Cdd:PRK14698 829 SEPVVQNTLRVVKVFWALDADLARRRHFPAIN 860
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
136-376 |
5.76e-11 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 64.80 E-value: 5.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 136 VIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTALaIDAIINQRDSGIkCIYVAIGQKASTISNVVR---KL 212
Cdd:PRK04192 201 YKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVT-QHQLAKWADADI-VIYVGCGERGNEMTEVLEefpEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 213 EE----HGALANTIVVVAT------ASESAAlqylapYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPG 282
Cdd:PRK04192 279 IDpktgRPLMERTVLIANTsnmpvaAREASI------YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861313569 283 REAFPGdvfYLHSRL---LERAARVNaeyveafTKGevkGKTGSLTALPIIETQAGDVSAFVPTNVISITdgQIF--LET 357
Cdd:PRK04192 353 EEGYPA---YLASRLaefYERAGRVK-------TLG---GEEGSVTIIGAVSPPGGDFSEPVTQNTLRIV--KVFwaLDA 417
|
250
....*....|....*....
gi 1861313569 358 NLFNAGIRPAVNPGISVSR 376
Cdd:PRK04192 418 ELADRRHFPAINWLTSYSL 436
|
|
| 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 1861313569 386 MKKLSGGIRTALAQYRELAAFSQFASD--LDDATRKQLDHGQKVTELLKQKQYAPMSVAQQ 444
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDT 61
|
|
| |
