|
Name |
Accession |
Description |
Interval |
E-value |
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
23-333 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 722.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 23 EVKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSE 102
Cdd:CHL00059 1 EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 103 AYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 182
Cdd:CHL00059 81 AYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 183 TILNQQGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTSIIYD 262
Cdd:CHL00059 161 TILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 385267629 263 DPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSNLGEGSMTALPIVETQSGDVSAYIPT 333
Cdd:CHL00059 241 DLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPT 311
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
3-333 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 666.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 3 TIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLM 82
Cdd:PRK09281 2 QINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 83 IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR 162
Cdd:PRK09281 82 IKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 163 GQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYT 242
Cdd:PRK09281 162 GQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 243 GAALAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSNLGEGSMTALPIVET 322
Cdd:PRK09281 242 GCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIET 321
|
330
....*....|.
gi 385267629 323 QSGDVSAYIPT 333
Cdd:PRK09281 322 QAGDVSAYIPT 332
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
3-333 |
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: 663.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 3 TIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLM 82
Cdd:COG0056 2 QIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 83 IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR 162
Cdd:COG0056 82 IKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 163 GQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYT 242
Cdd:COG0056 162 GQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 243 GAALAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSNLGEGSMTALPIVET 322
Cdd:COG0056 242 GCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIET 321
|
330
....*....|.
gi 385267629 323 QSGDVSAYIPT 333
Cdd:COG0056 322 QAGDVSAYIPT 332
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
3-333 |
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: 570.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 3 TIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLM 82
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 83 IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR 162
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 163 GQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYT 242
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 243 GAALAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSNLGEGSMTALPIVET 322
Cdd:TIGR00962 241 GCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIET 320
|
330
....*....|.
gi 385267629 323 QSGDVSAYIPT 333
Cdd:TIGR00962 321 QAGDVSAYIPT 331
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
4-333 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 526.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 4 IRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMI 83
Cdd:PRK13343 3 SNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 84 QEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRG 163
Cdd:PRK13343 83 LAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 164 QRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYTG 243
Cdd:PRK13343 163 QRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 244 AALAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSNLGEGSMTALPIVETQ 323
Cdd:PRK13343 243 CAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETL 322
|
330
....*....|
gi 385267629 324 SGDVSAYIPT 333
Cdd:PRK13343 323 AGELSAYIPT 332
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
95-333 |
3.53e-175 |
|
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: 486.30 E-value: 3.53e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 95 IAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQT 174
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 175 GKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRE 254
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385267629 255 RHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSNLGEGSMTALPIVETQSGDVSAYIPT 333
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPT 239
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
7-333 |
1.34e-139 |
|
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: 404.53 E-value: 1.34e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 7 DEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEG 86
Cdd:TIGR03324 6 DKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 87 SSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRE 166
Cdd:TIGR03324 86 DEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 167 LIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYTGAAL 246
Cdd:TIGR03324 166 LILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 247 AEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSNLGEGSMTALPIVETQSGD 326
Cdd:TIGR03324 246 GEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQN 325
|
....*..
gi 385267629 327 VSAYIPT 333
Cdd:TIGR03324 326 ISAYIPT 332
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
150-333 |
7.54e-87 |
|
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: 259.98 E-value: 7.54e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 150 GLIAIDSMIPIGRGQRELIIGDRQTGKTAVAtDTILNQQGQNViCVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETA 229
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 230 DSPATLQYLAPYTGAALAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSnl 309
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKG-- 156
|
170 180
....*....|....*....|....
gi 385267629 310 GEGSMTALPIVETQSGDVSAYIPT 333
Cdd:pfam00006 157 KGGSITALPTVLVPGDDITDPIPD 180
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
62-333 |
1.99e-86 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 270.76 E-value: 1.99e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 62 GIALNLESNN-VGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDgRGEISASESRL--------IES 132
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVP-VGLLTRSRALLeseqtlgkVDA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 133 PAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQQGQN--------VICVYVAIGQKAS 204
Cdd:PTZ00185 159 GAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINqqilsknaVISIYVSIGQRCS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 205 SVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGR 284
Cdd:PTZ00185 239 NVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGR 318
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 385267629 285 EAYPGDVFYLHSRLLERAAKSSSNLGEGSMTALPIVETQSGDVSAYIPT 333
Cdd:PTZ00185 319 EAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVT 367
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
97-333 |
1.06e-82 |
|
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: 251.61 E-value: 1.06e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 97 QIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 177 TAVATDTILNQQGQNV-ICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRER 255
Cdd:cd19476 81 TVLAMQLARNQAKAHAgVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 385267629 256 HTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKssSNLGEGSMTALPIVETQSGDVSAYIPT 333
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGK--VKDGGGSITAIPAVSTPGDDLTDPIPD 236
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
97-331 |
3.37e-75 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 239.87 E-value: 3.37e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 97 QIPVSEAYLGRVINALAKPIDGRGEISASESRLI-ESP----APGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGD 171
Cdd:PRK07165 72 KVKTSKEYFGKIIDIDGNIIYPEAQNPLSKKFLPnTSSifnlAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGD 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 172 RQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATlQYLAPYTGAALAEYFM 251
Cdd:PRK07165 152 RQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAENIS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 252 YRErHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSssnLGEGSMTALPIVETQSGDVSAYI 331
Cdd:PRK07165 231 YND-DVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKF---KNRKTITALPILQTVDNDITSLI 306
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
97-317 |
1.47e-35 |
|
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: 129.60 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 97 QIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 177 TavatdTILNQQGQNV---ICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYR 253
Cdd:cd01136 81 S-----TLLGMIARNTdadVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 385267629 254 ERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsnlgEGSMTAL 317
Cdd:cd01136 156 GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGE----KGSITAF 215
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
13-317 |
3.18e-34 |
|
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: 129.77 E-value: 3.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 13 IRERIEQYNRevkIVNTGTVLQVGDGIARIHGLDeVMAGELVEFEEGT--------IGIalnlesNNVGVVLM--GDGLM 82
Cdd:COG1157 7 LLARLEELPP---VRVSGRVTRVVGLLIEAVGPD-ASIGELCEIETADgrpvlaevVGF------RGDRVLLMplGDLEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 83 IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR 162
Cdd:COG1157 77 ISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 163 GQReliIGdr---qtGKTavatdTILNQQGQNV---ICVyVA-IGqkassvaqvvttfqERG--------------AMEY 221
Cdd:COG1157 157 GQR---IGifagsgvGKS-----TLLGMIARNTeadVNV-IAlIG--------------ERGrevrefieddlgeeGLAR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 222 TIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLER 301
Cdd:COG1157 214 SVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLER 293
|
330
....*....|....*.
gi 385267629 302 AAKSssnlGEGSMTAL 317
Cdd:COG1157 294 AGNG----GKGSITAF 305
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
5-325 |
3.73e-33 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 127.19 E-value: 3.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 5 RADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIHGLDeVMAGELVEF--EEGTIGIALNLESNNVGVVLM---GD 79
Cdd:PRK09099 1 ALAELSRLADALERELAALPAVRRTGKVVEVIGTLLRVSGLD-VTLGELCELrqRDGTLLQRAEVVGFSRDVALLspfGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 80 GLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIP 159
Cdd:PRK09099 80 LGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 160 IGRGQRELIIGDRQTGKTavatdTILNQQGQNVIC---VYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQ 236
Cdd:PRK09099 160 LGEGQRMGIFAPAGVGKS-----TLMGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIER 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 237 YLAPYTGAALAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSnlgeGSMTA 316
Cdd:PRK09099 235 AKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGET----GSITA 310
|
330
....*....|.
gi 385267629 317 LPIV--ETQSG 325
Cdd:PRK09099 311 LYTVlaEDESG 321
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
28-94 |
2.28e-32 |
|
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: 115.24 E-value: 2.28e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 385267629 28 NTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGR 94
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
95-332 |
1.06e-29 |
|
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: 114.63 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 95 IAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGD--- 171
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGsgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 172 ----------RQTGktavatdtiLNQQGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPY 241
Cdd:cd01135 81 phnelaaqiaRQAG---------VVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 242 TGAALAEYFMY-RERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKSSSNlgEGSMTAL 317
Cdd:cd01135 152 MALTTAEYLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQI 226
|
250
....*....|....*
gi 385267629 318 PIVETQSGDVSAYIP 332
Cdd:cd01135 227 PILTMPNDDITHPIP 241
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
77-328 |
1.75e-29 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 117.16 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 77 MGDGLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDS 156
Cdd:PRK06936 76 LGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 157 MIPIGRGQRELIIGDRQTGKTAVATDTILNQQGQnvICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQ 236
Cdd:PRK06936 156 LLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVD--VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMER 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 237 YLAPYTGAALAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsnlgEGSMTA 316
Cdd:PRK06936 234 AKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSD----KGSITA 309
|
250
....*....|..
gi 385267629 317 LPIVETQSGDVS 328
Cdd:PRK06936 310 LYTVLVEGDDMT 321
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
17-317 |
7.14e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 115.48 E-value: 7.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 17 IEQYNREVKIVNT-GTVLQVGDGIARIHGL-DEVMAGELVEFEEGT---IGIALNLESNNVGVVLMGDGLMIQEGSSVKA 91
Cdd:PRK06002 14 VERYAAPEPLVRIgGTVSEVTASHYRVRGLsRFVRLGDFVAIRADGgthLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 92 TGRiAQIPVSEAYLGRVINALAKPIDGRGEI-SASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIG 170
Cdd:PRK06002 94 KGP-LRIRPDPSWKGRVINALGEPIDGLGPLaPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 171 DRQTGKT--------AVATDTIlnqqgqnvicVYVAIGQKASSVAQvvttFQE---RGAMEYTIVVAETADSPATLQYLA 239
Cdd:PRK06002 173 GSGVGKStllamlarADAFDTV----------VIALVGERGREVRE----FLEdtlADNLKKAVAVVATSDESPMMRRLA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 385267629 240 PYTGAALAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSnlGEGSMTAL 317
Cdd:PRK06002 239 PLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGI 314
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
9-320 |
8.90e-29 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 114.91 E-value: 8.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 9 ISNIIRERIEQYNREVK-IVNTGTVLQVGDGIARIhGLDEVMAGELVEFE-EGTIGIALNLESNNVGVVLMGDGLMIQEG 86
Cdd:PRK06820 9 LTPRLQQQLTRPSAPPEgLRYRGPIVEIGPTLLRA-SLPGVAQGELCRIEpQGMLAEVVSIEQEMALLSPFASSDGLRCG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 87 SSVKATGRIAQIPVSEAYLGRVINALAKPIDGrGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRE 166
Cdd:PRK06820 88 QWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 167 LIIGDRQTGKTAVATdTILNQQGQNVIcVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYTGAAL 246
Cdd:PRK06820 167 GIFAAAGVGKSTLLG-MLCADSAADVM-VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTI 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 385267629 247 AEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsnlgEGSMTALPIV 320
Cdd:PRK06820 245 AEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSD----RGSITAFYTV 314
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
16-332 |
3.04e-28 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 113.77 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 16 RIEQYNREVKivnTGTVLQVGDGIArihgldevmageLVEFEEGTIGIALnlesnnvgvvlmgdglmiqEGSSVKATGRI 95
Cdd:PRK04196 30 EIELPNGEKR---RGQVLEVSEDKA------------VVQVFEGTTGLDL-------------------KDTKVRFTGEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 96 AQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR---------- 165
Cdd:PRK04196 76 LKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 166 --EL---IIgdRQTgktavatdTILNQQGQNVIcVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAP 240
Cdd:PRK04196 156 hnELaaqIA--RQA--------KVLGEEENFAV-VFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 241 YTGAALAEYFMY-RERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKSSSNlgEGSMTA 316
Cdd:PRK04196 225 RMALTAAEYLAFeKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQ 299
|
330
....*....|....*.
gi 385267629 317 LPIVETQSGDVSAYIP 332
Cdd:PRK04196 300 IPILTMPDDDITHPIP 315
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
83-320 |
4.09e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 113.28 E-value: 4.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 83 IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR 162
Cdd:PRK07721 78 IAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 163 GQRELIIGDRQTGKTAVATDTILNQQGQ-NVICVyvaIGQKASSVAQvvttFQERG----AMEYTIVVAETADSPATLQY 237
Cdd:PRK07721 158 GQRVGIFAGSGVGKSTLMGMIARNTSADlNVIAL---IGERGREVRE----FIERDlgpeGLKRSIVVVATSDQPALMRI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 238 LAPYTGAALAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSnlgeGSMTAL 317
Cdd:PRK07721 231 KGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS----GSITAF 306
|
...
gi 385267629 318 PIV 320
Cdd:PRK07721 307 YTV 309
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
30-328 |
1.40e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 111.70 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 30 GTVLQVGDGIARIHGLdEVMAGELVEFEEG-----TIGIALNLESNNVGVVLMG--DGLMIqeGSSVKATGRIAQIPVSE 102
Cdd:PRK08472 20 GSITKISPTIIEADGL-NPSVGDIVKIESSdngkeCLGMVVVIEKEQFGISPFSfiEGFKI--GDKVFISKEGLNIPVGR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 103 AYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 182
Cdd:PRK08472 97 NLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 183 TILNQQGQnvICVYVAIGQKASSVAQvvttFQER---GAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTSI 259
Cdd:PRK08472 177 IVKGCLAP--IKVVALIGERGREIPE----FIEKnlgGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLF 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385267629 260 IYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsnlGEGSMTALPIVETQSGDVS 328
Cdd:PRK08472 251 IMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEE---GKGSITAFFTVLVEGDDMS 316
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
41-316 |
1.22e-26 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 108.93 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 41 RIHG------LDEVMAGELVE-----FEEGTIGIALNLESNNVGVVL--MGDGLMIQEGSSVKATGRIAQIPVSEAYLGR 107
Cdd:PRK08149 12 RIQGpiieaeLPDVAIGEICEiragwHSNEVIARAQVVGFQRERTILslIGNAQGLSRQVVLKPTGKPLSVWVGEALLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 108 VINALAKpIDGR-----GEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVAtd 182
Cdd:PRK08149 92 VLDPTGK-IVERfdappTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLM-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 183 TILNQQGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTSIIYD 262
Cdd:PRK08149 169 NMLIEHSEADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFID 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 385267629 263 DPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERaaksSSNLGEGSMTA 316
Cdd:PRK08149 249 SMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLER----PGATLAGSITA 298
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
86-326 |
1.55e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 105.94 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 86 GSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR 165
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 166 ELIIGDRQTGKTaVATDTILNQQGQNVICVYVaIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYTGAA 245
Cdd:PRK08972 165 MGLFAGSGVGKS-VLLGMMTRGTTADVIVVGL-VGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 246 LAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSnlGEGSMTALPIVETQSG 325
Cdd:PRK08972 243 IAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVLTEGD 320
|
.
gi 385267629 326 D 326
Cdd:PRK08972 321 D 321
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
87-332 |
4.21e-25 |
|
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: 105.19 E-value: 4.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 87 SSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRE 166
Cdd:TIGR01040 65 TTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 167 LIIGD-------------RQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPA 233
Cdd:TIGR01040 145 PIFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 234 TLQYLAPYTGAALAEYFMY-RERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSNlgEG 312
Cdd:TIGR01040 225 IERIITPRLALTTAEYLAYqCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR--NG 302
|
250 260
....*....|....*....|
gi 385267629 313 SMTALPIVETQSGDVSAYIP 332
Cdd:TIGR01040 303 SITQIPILTMPNDDITHPIP 322
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-328 |
6.11e-25 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 104.26 E-value: 6.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 29 TGTVLQVGDGIARIHgLDEVMAGELVEFE-EGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGR 107
Cdd:PRK07594 22 WGRIQDVSATLLNAW-LPGVFMGELCCIKpGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 108 VINALAKPIDGRgEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATdTILNQ 187
Cdd:PRK07594 101 VIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLA-MLCNA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 188 QGQNViCVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTSIIYDDPSKQ 267
Cdd:PRK07594 179 PDADS-NVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRY 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 385267629 268 AQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAksssnLGE-GSMTALPIVETQSGDVS 328
Cdd:PRK07594 258 ARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTVLVEGDDMN 314
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
31-317 |
6.50e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 101.21 E-value: 6.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 31 TVLQVGDGIARIHGLDEVMAGELVEFEEGTigialnlesnnvgVVLMGDGLM--IQEGSSVKATGRIAQIPVSEAYLGRV 108
Cdd:PRK08927 36 HALSVGARIVVETRGGRPVPCEVVGFRGDR-------------ALLMPFGPLegVRRGCRAVIANAAAAVRPSRAWLGRV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 109 INALAKPIDGRGEISASES-RLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTavatdTILNQ 187
Cdd:PRK08927 103 VNALGEPIDGKGPLPQGPVpYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKS-----VLLSM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 188 QGQNVIC---VYVAIGQKASSVAQVVT-TFQERGaMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTSIIYDD 263
Cdd:PRK08927 178 LARNADAdvsVIGLIGERGREVQEFLQdDLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDS 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 385267629 264 PSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsnLGEGSMTAL 317
Cdd:PRK08927 257 VTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGP--IGEGTITGL 308
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
86-317 |
1.22e-22 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 97.67 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 86 GSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR 165
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 166 ELIIGDRQTGKTA-VATDTILNQQGQNVICVyvaIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYTGA 244
Cdd:PRK05922 160 IGVFSEPGSGKSSlLSTIAKGSKSTINVIAL---IGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAM 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 385267629 245 ALAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAksssNLGEGSMTAL 317
Cdd:PRK05922 237 TIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG----NNDKGSITAL 305
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
86-326 |
5.79e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 95.73 E-value: 5.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 86 GSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR 165
Cdd:PRK07196 78 GARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 166 ELIIGDRQTGKTAVAtdTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYTGAA 245
Cdd:PRK07196 158 VGLMAGSGVGKSVLL--GMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 246 LAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSsnlGEGSMTALPIVETQSG 325
Cdd:PRK07196 236 IATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSS---GNGTMTAIYTVLAEGD 312
|
.
gi 385267629 326 D 326
Cdd:PRK07196 313 D 313
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
83-326 |
5.75e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 92.87 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 83 IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGR 162
Cdd:PRK05688 88 IAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 163 GQRELIIGDRQTGKTAVAtdTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYT 242
Cdd:PRK05688 168 GQRLGLFAGTGVGKSVLL--GMMTRFTEADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 243 GAALAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSnlGEGSMTALPIVET 322
Cdd:PRK05688 246 CTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEP--GGGSITAFYTVLS 323
|
....
gi 385267629 323 QSGD 326
Cdd:PRK05688 324 EGDD 327
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
60-287 |
3.71e-19 |
|
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: 87.85 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 60 TIGIALNLESNNVGVVLMG--DGLmiQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGI 137
Cdd:TIGR01039 40 TLEVAQHLGDDTVRTIAMGstDGL--VRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 138 ISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN-QQGQNVICVYVAIGQKASSVAQVVTTFQER 216
Cdd:TIGR01039 118 EEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKES 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 385267629 217 GAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTSIIY-DDPSKQAQAYRQMSLLLRRPPGREAY 287
Cdd:TIGR01039 198 GVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFiDNIFRFTQAGSEVSALLGRMPSAVGY 269
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
145-328 |
8.73e-18 |
|
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: 81.85 E-value: 8.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 145 EPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTavatdtILNQQ----GQNVICVYVAIGQKASSVAQVVTTFQE----- 215
Cdd:cd01134 58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKT------VISQSlskwSNSDVVIYVGCGERGNEMAEVLEEFPElkdpi 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 216 --RGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGdvfY 293
Cdd:cd01134 132 tgESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---Y 208
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 385267629 294 LHSRL---LERAAKsSSNLG----EGSMTALPIVETQSGDVS 328
Cdd:cd01134 209 LGARLaefYERAGR-VRCLGspgrEGSVTIVGAVSPPGGDFS 249
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
97-326 |
4.17e-17 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 81.75 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 97 QIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 177 TaVATDTILNQQGQNVICVYVaIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERH 256
Cdd:PRK07960 189 S-VLLGMMARYTQADVIVVGL-IGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQH 266
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 257 TSIIYDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSnlGEGSMTALPIVETQSGD 326
Cdd:PRK07960 267 VLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGDD 334
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
29-93 |
3.05e-16 |
|
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: 72.19 E-value: 3.05e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 385267629 29 TGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATG 93
Cdd:pfam02874 5 IGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
86-332 |
1.51e-15 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 76.94 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 86 GSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR 165
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 166 ELIIGDRQTGKTavatdTILNQQGQNV---ICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYT 242
Cdd:PRK06793 159 IGIFAGSGVGKS-----TLLGMIAKNAkadINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 243 GAALAEYFMYRERHTSIIYDDPSKQAQAYRQMSLLLRRPPgreaYPGDVFYLHS---RLLERAAKSSsnlgEGSMTALPI 319
Cdd:PRK06793 234 ATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQ----KGSITGIYT 305
|
250
....*....|...
gi 385267629 320 VETQSGDVSAYIP 332
Cdd:PRK06793 306 VLVDGDDLNGPVP 318
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
145-328 |
7.56e-15 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 75.20 E-value: 7.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 145 EPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTavatdtILNQQ----GQNVICVYVAIGQKASSVAQVVTTFQE----- 215
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT------VTQHQlakwADADIVIYVGCGERGNEMTEVLEEFPElidpk 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 216 --RGAMEYTIVVAETADSP-----ATLqylapYTGAALAEYfmYRE--RHTSIIYDDPSKQAQAYRQMSLLLRRPPGREA 286
Cdd:PRK04192 283 tgRPLMERTVLIANTSNMPvaareASI-----YTGITIAEY--YRDmgYDVLLMADSTSRWAEALREISGRLEEMPGEEG 355
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 385267629 287 YPGdvfYLHSRL---LERAAKSSSNLG-EGSMTALPIVETQSGDVS 328
Cdd:PRK04192 356 YPA---YLASRLaefYERAGRVKTLGGeEGSVTIIGAVSPPGGDFS 398
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
51-332 |
7.72e-14 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 71.99 E-value: 7.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 51 GELVEFEE---GTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIsasES 127
Cdd:PRK02118 26 GELATVERkdgSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPEL---EG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 128 RLIE------SPAPGIISRRSVyeplQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATdTILNQQGQNVIcVYVAIGQ 201
Cdd:PRK02118 103 EPIEiggpsvNPVKRIVPREMI----RTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA-RIALQAEADII-ILGGMGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 202 KASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRE-RHTSIIYDDPSKQAQAYRQMSLLLRR 280
Cdd:PRK02118 177 TFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLTDMTNFADALKEISITMDQ 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 385267629 281 PPGREAYPGDvfyLHSRLLERAAKSSSNLGEGSMTALPIVETQSGDVSAYIP 332
Cdd:PRK02118 257 IPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVP 305
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
54-163 |
8.79e-14 |
|
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: 71.66 E-value: 8.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 54 VEFEEGTI-------------GIALNLE------SNNVGVVLMG--DGLmiQEGSSVKATGRIAQIPVSEAYLGRVINAL 112
Cdd:COG0055 18 VEFPEGELpaiynalevenegGGELVLEvaqhlgDNTVRCIAMDstDGL--VRGMEVIDTGAPISVPVGEATLGRIFNVL 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 385267629 113 AKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRG 163
Cdd:COG0055 96 GEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKG 146
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
97-287 |
2.51e-13 |
|
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: 69.17 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 97 QIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 177 TAVATDTILN-QQGQNVICVYVAIGQ------------KASSVAQVvttfqerGAMEYTIVVAETADSPATLQYLAPYTG 243
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGErtregndlyhemKESGVINL-------DGLSKVALVYGQMNEPPGARARVALTG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 385267629 244 AALAEYFMYRERHTSIIY-DDPSKQAQAYRQMSLLLRRPPGREAY 287
Cdd:cd01133 154 LTMAEYFRDEEGQDVLLFiDNIFRFTQAGSEVSALLGRIPSAVGY 198
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
29-94 |
5.48e-12 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 60.40 E-value: 5.48e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 385267629 29 TGTVLQVGDGIARIHGLDEVMAGELVEFEE-------GTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGR 94
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERgdgnnetVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
193-328 |
1.51e-11 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 65.43 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 193 ICVYVAIGQKASSVAQVVTTFQE-------RGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTSIIYDDPS 265
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTS 763
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385267629 266 KQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKSSSNLGEGSMTALPIVETQSGDVS 328
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFS 829
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
67-186 |
8.46e-10 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 59.67 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385267629 67 LESNNVGVVLMG--DGLMiqEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGII---SRR 141
Cdd:CHL00060 65 LGNNRVRAVAMSatDGLM--RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTKL 142
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 385267629 142 SVYEplqTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN 186
Cdd:CHL00060 143 SIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINN 184
|
|
| |
