|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
4-511 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 1013.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 4 LTINADDVRNALNEFAASYEPgNAERVEVGRVASASDGIARVEGLPSVMANELLRFEDGTLGLAQNLDTRDIGVIILGDF 83
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDA-EAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 84 TGIEEGQEVHRTGEVLSVPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPI 163
Cdd:PRK09281 80 EDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 164 GRGQRQLIIGDRQTGKTAIAVDTILNQKDnwatgdpnKQVRCVYVAIGQKASTIAAVRETLKQQGALEYTTIVASPASDA 243
Cdd:PRK09281 160 GRGQRELIIGDRQTGKTAIAIDTIINQKG--------KDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 244 AGFKYLAPYTGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDELGAG 323
Cdd:PRK09281 232 APLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 324 SMTGFPIIETKANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAMKKVSGTLKLDLAQYRA 403
Cdd:PRK09281 312 SLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 404 MEAFAMFASDLDDASKAQLTRGARLTELLRQPQYTPYAVEDQVVSIWAGTNGYLDDLEVSDVLRFESEFLDHLRRS-TSV 482
Cdd:PRK09281 392 LEAFAQFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNhADL 471
|
490 500
....*....|....*....|....*....
gi 2509359131 483 LQDIAASGKLEDETVAALKTAIVDFKQGF 511
Cdd:PRK09281 472 LEEIRETKDLSDEIEAKLKAAIEEFKKTF 500
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
4-514 |
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: 998.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 4 LTINADDVRNALNEFAASYEPGnAERVEVGRVASASDGIARVEGLPSVMANELLRFEDGTLGLAQNLDTRDIGVIILGDF 83
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPE-VEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 84 TGIEEGQEVHRTGEVLSVPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPI 163
Cdd:COG0056 80 EGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 164 GRGQRQLIIGDRQTGKTAIAVDTILNQKDnwatgdpnKQVRCVYVAIGQKASTIAAVRETLKQQGALEYTTIVASPASDA 243
Cdd:COG0056 160 GRGQRELIIGDRQTGKTAIAIDTIINQKG--------KDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 244 AGFKYLAPYTGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDELGAG 323
Cdd:COG0056 232 APLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 324 SMTGFPIIETKANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAMKKVSGTLKLDLAQYRA 403
Cdd:COG0056 312 SLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 404 MEAFAMFASDLDDASKAQLTRGARLTELLRQPQYTPYAVEDQVVSIWAGTNGYLDDLEVSDVLRFESEFLDHLRRS-TSV 482
Cdd:COG0056 392 LEAFAQFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKhPDL 471
|
490 500 510
....*....|....*....|....*....|..
gi 2509359131 483 LQDIAASGKLEDETVAALKTAIVDFKQGFRSE 514
Cdd:COG0056 472 LKEIRETGKLDDEIEEKLKAAIEEFKKTFAAS 503
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
5-511 |
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: 823.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 5 TINADDVRNALNEFAASYEPgNAERVEVGRVASASDGIARVEGLPSVMANELLRFEDGTLGLAQNLDTRDIGVIILGDFT 84
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNV-DSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 85 GIEEGQEVHRTGEVLSVPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIG 164
Cdd:TIGR00962 80 DIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 165 RGQRQLIIGDRQTGKTAIAVDTILNQKDNWatgdpnkqVRCVYVAIGQKASTIAAVRETLKQQGALEYTTIVASPASDAA 244
Cdd:TIGR00962 160 RGQRELIIGDRQTGKTAVAIDTIINQKDSD--------VYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 245 GFKYLAPYTGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDELGAGS 324
Cdd:TIGR00962 232 SLQYLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 325 MTGFPIIETKANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAMKKVSGTLKLDLAQYRAM 404
Cdd:TIGR00962 312 LTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYREL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 405 EAFAMFASDLDDASKAQLTRGARLTELLRQPQYTPYAVEDQVVSIWAGTNGYLDDLEVSDVLRFESEFLDHLRRS-TSVL 483
Cdd:TIGR00962 392 EAFSQFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANhPDIL 471
|
490 500
....*....|....*....|....*...
gi 2509359131 484 QDIAASGKLEDETVAALKTAIVDFKQGF 511
Cdd:TIGR00962 472 EEINTTKKLTEELEAKLKEALKNFKKTF 499
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
30-511 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 756.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 30 VEVGRVASASDGIARVEGLPSVMANELLRFEDGTLGLAQNLDTRDIGVIILGDFTGIEEGQEVHRTGEVLSVPVGDAYLG 109
Cdd:CHL00059 5 VNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 110 RVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQTGKTAIAVDTILN 189
Cdd:CHL00059 85 RVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 190 QKdnwatgdpNKQVRCVYVAIGQKASTIAAVRETLKQQGALEYTTIVASPASDAAGFKYLAPYTGSAIGQHWMYGGKHVL 269
Cdd:CHL00059 165 QK--------GQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 270 IIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDELGAGSMTGFPIIETKANDVSAFIPTNVISI 349
Cdd:CHL00059 237 IIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 350 TDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAMKKVSGTLKLDLAQYRAMEAFAMFASDLDDASKAQLTRGARLT 429
Cdd:CHL00059 317 TDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 430 ELLRQPQYTPYAVEDQVVSIWAGTNGYLDDLEVSDVLRFESEFLDHLRRSTSVLQDIAASGK-LEDETVAALKTAIVDFK 508
Cdd:CHL00059 397 ELLKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKtFTEEAEALLKEAIQEQL 476
|
...
gi 2509359131 509 QGF 511
Cdd:CHL00059 477 ELF 479
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
31-513 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 749.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 31 EVGRVASASDGIARVEGLPSVMANELLRFEDGTLGLAQNLDTRDIGVIILGDFTGIEEGQEVHRTGEVLSVPVGDAYLGR 110
Cdd:PRK13343 27 EIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 111 VVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQTGKTAIAVDTILNQ 190
Cdd:PRK13343 107 VIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIINQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 191 KDnwatgdpnKQVRCVYVAIGQKASTIAAVRETLKQQGALEYTTIVASPASDAAGFKYLAPYTGSAIGQHWMYGGKHVLI 270
Cdd:PRK13343 187 KD--------SDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 271 IFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDELGAGSMTGFPIIETKANDVSAFIPTNVISIT 350
Cdd:PRK13343 259 VYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETLAGELSAYIPTNLISIT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 351 DGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAMKKVSGTLKLDLAQYRAMEAFAMFASDLDDASKAQLTRGARLTE 430
Cdd:PRK13343 339 DGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLLDAGTQKQITRGRRLRE 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 431 LLRQPQYTPYAVEDQVVSIWAGTNGYLDDLEVSDVLRFESEFLDHLRRSTS-VLQDIAASGKLEDETVAALKTAIVDFKQ 509
Cdd:PRK13343 419 LLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAaLSLALESPRELDEAWLAALEEILREAGE 498
|
....
gi 2509359131 510 GFRS 513
Cdd:PRK13343 499 RFAA 502
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
98-379 |
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: 550.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 98 VLSVPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQT 177
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 178 GKTAIAVDTILNQKdnwatgdpNKQVRCVYVAIGQKASTIAAVRETLKQQGALEYTTIVASPASDAAGFKYLAPYTGSAI 257
Cdd:cd01132 81 GKTAIAIDTIINQK--------GKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 258 GQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDELGAGSMTGFPIIETKAND 337
Cdd:cd01132 153 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2509359131 338 VSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVG 379
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
32-469 |
1.47e-122 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 371.68 E-value: 1.47e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 32 VGRVASASDGIARV---EGLPSVMANELLRFEDG----TLGLAQNLDTRD-IGVIILGDFTGIEEGQEVHRTGEVLSVPV 103
Cdd:PTZ00185 40 IGYVHSIDGTIATLipaPGNPGVAYNTIIMIQVSpttfAAGLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 104 GDAYLGRVVDPLGNPIDdLGEIeAEGRRALELQ---------APGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGD 174
Cdd:PTZ00185 120 GAGVLGKVVNPLGHEVP-VGLL-TRSRALLESEqtlgkvdagAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 175 RQTGKTAIAVDTILNQKDNWATGDPNKQVRCVYVAIGQKASTIAAVRETLKQQGALEYTTIVASPASDAAGFKYLAPYTG 254
Cdd:PTZ00185 198 RQTGKTSIAVSTIINQVRINQQILSKNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 255 SAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDELGAGSMTGFPIIETK 334
Cdd:PTZ00185 278 VTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 335 ANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAMKKVSGTLKLDLAQYRAMEAFAMFASDL 414
Cdd:PTZ00185 358 SNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQV 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2509359131 415 ddaSKAQLTRGARLTELLRQPQytPYAVEDQVVSIWAGTNGYLDDLEVSDVLRFE 469
Cdd:PTZ00185 438 ---QTVPMIRGARFVALFNQKN--PSFFMNALVSLYACLNGYLDDVKVNYAKLYE 487
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
153-376 |
4.05e-104 |
|
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: 311.21 E-value: 4.05e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 153 GLKAIDAMIPIGRGQRQLIIGDRQTGKTAIAvDTILNQKDnwatgdpnKQVrCVYVAIGQKASTIAAVRETLKQQGALEY 232
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQAS--------ADV-VVYALIGERGREVREFIEELLGSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 233 TTIVASPASDAAGFKYLAPYTGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLER 312
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2509359131 313 CAKLSDElgAGSMTGFPIIETKANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVS 376
Cdd:pfam00006 151 AGRVKGK--GGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
107-474 |
2.93e-103 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 319.61 E-value: 2.93e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 107 YLGRVVDPLGNPI-----DDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQTGKTA 181
Cdd:PRK07165 79 YFGKIIDIDGNIIypeaqNPLSKKFLPNTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTH 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 182 IAVDTILNQKDNwatgdpnkQVRCVYVAIGQKASTIAAVRETLKQQGALEYTTIVASPaSDAAGFKYLAPYTGSAIGQHW 261
Cdd:PRK07165 159 IALNTIINQKNT--------NVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAP-STSPYEQYLAPYVAMAHAENI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 262 MYGgKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDElgaGSMTGFPIIETKANDVSAF 341
Cdd:PRK07165 230 SYN-DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNR---KTITALPILQTVDNDITSL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 342 IPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAMKKVSGTLKLDLAQYRAMEAFAMFASDLDDASKAQ 421
Cdd:PRK07165 306 ISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDL 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2509359131 422 LTRGARLTELLRQPQYTPYAVEDQVVSIWAGTNGYLDDL-EVSDVLRFESEFLD 474
Cdd:PRK07165 386 LFKGKMIEKMFNQKGFSLYSYRFVLLISKLISWGLLKDVkDEQKALDFIDYLIE 439
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
100-378 |
4.82e-93 |
|
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: 285.12 E-value: 4.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 100 SVPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQTGK 179
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 180 TAIAVDTILNQKDnwatgdPNKQVrCVYVAIGQKASTIAAVRETLKQQGALEYTTIVASPASDAAGFKYLAPYTGSAIGQ 259
Cdd:cd19476 81 TVLAMQLARNQAK------AHAGV-VVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 260 HWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDelGAGSMTGFPIIETKANDVS 339
Cdd:cd19476 154 YFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLT 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 2509359131 340 AFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRV 378
Cdd:cd19476 232 DPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
387-511 |
3.71e-64 |
|
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: 204.91 E-value: 3.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 387 MKKVSGTLKLDLAQYRAMEAFAMFASDLDDASKAQLTRGARLTELLRQPQYTPYAVEDQVVSIWAGTNGYLDDLEVSDVL 466
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2509359131 467 RFESEFLDHLRRS-TSVLQDIAASGKLEDETVAALKTAIVDFKQGF 511
Cdd:cd18113 81 EFEKELLEYLRSNhPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
383-507 |
5.92e-64 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 204.60 E-value: 5.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 383 QTKAMKKVSGTLKLDLAQYRAMEAFAMFASDLDDASKAQLTRGARLTELLRQPQYTPYAVEDQVVSIWAGTNGYLDDLEV 462
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2509359131 463 SDVLRFESEFLDHLRRS-TSVLQDIAASGKLEDETVAALKTAIVDF 507
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNhPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
100-378 |
2.52e-48 |
|
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: 168.51 E-value: 2.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 100 SVPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQTGK 179
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 180 TaiavdTILNQKDNWATGDPNkqvrcVYVAIGQKASTIAAVRETLKQQGALEYTTIVASPASDAAGFKYLAPYTGSAIGQ 259
Cdd:cd01136 81 S-----TLLGMIARNTDADVN-----VIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 260 HWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSdelgAGSMTGFPIIETKANDVS 339
Cdd:cd01136 151 YFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGE----KGSITAFYTVLVEGDDFN 226
|
250 260 270
....*....|....*....|....*....|....*....
gi 2509359131 340 AFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRV 378
Cdd:cd01136 227 DPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
13-405 |
2.60e-44 |
|
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: 162.12 E-value: 2.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 13 NALNEFAASYEPGNAERVeVGRVASASDGIARVEGlPSVMANELLRFE--DGTLGLAQNLDTRDIGVII--LGDFTGIEE 88
Cdd:COG1157 2 DRLARLLARLEELPPVRV-SGRVTRVVGLLIEAVG-PDASIGELCEIEtaDGRPVLAEVVGFRGDRVLLmpLGDLEGISP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 89 GQEVHRTGEVLSVPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQR 168
Cdd:COG1157 80 GARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 169 QLIIGDRQTGKTaiavdTILNQKDNWATGDpnkqvrcVYVaigqkastIAA-------VRE----TLKQQGaLEYTTIVA 237
Cdd:COG1157 160 IGIFAGSGVGKS-----TLLGMIARNTEAD-------VNV--------IALigergreVREfiedDLGEEG-LARSVVVV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 238 SPASDAAGFKYLAPYTGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKls 317
Cdd:COG1157 219 ATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN-- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 318 deLGAGSMTGF------------PIIETkandvsafiptnVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTK 385
Cdd:COG1157 297 --GGKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSP 362
|
410 420
....*....|....*....|
gi 2509359131 386 AMKKVSGTLKLDLAQYRAME 405
Cdd:COG1157 363 EHRALARRLRRLLARYEENE 382
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
80-449 |
2.20e-40 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 151.83 E-value: 2.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 80 LGDFTGIEEGQEVHRTGEVLSVPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDA 159
Cdd:PRK06936 76 LGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 160 MIPIGRGQRQLIIGDRQTGKTaiavdTILNQKDNWATGDPnkqvrCVYVAIGQKAStiaAVRE----TLKQQGaLEYTTI 235
Cdd:PRK06936 156 LLTCGEGQRMGIFAAAGGGKS-----TLLASLIRSAEVDV-----TVLALIGERGR---EVREfiesDLGEEG-LRKAVL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 236 VASPASDAAGFKYLAPYTGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERcAK 315
Cdd:PRK06936 222 VVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMER-AG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 316 LSDElgaGSMTGFPIIETKANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAMKKVSGTLK 395
Cdd:PRK06936 301 QSDK---GSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLR 377
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2509359131 396 LDLAQYRAMEAFAM---FASDLDDASKAQLTRGARLTELLRQPQYTPYAVEDQVVSI 449
Cdd:PRK06936 378 ELLAKYEEVELLLQigeYQKGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLL 434
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
33-440 |
3.28e-38 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 145.68 E-value: 3.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 33 GRVASASDGIARVEGLpSVMANEL--LRFEDGTLGLAQNLD--TRDIGVII-LGDFTGIEEGQEVHRTGEVLSVPVGDAY 107
Cdd:PRK09099 26 GKVVEVIGTLLRVSGL-DVTLGELceLRQRDGTLLQRAEVVgfSRDVALLSpFGELGGLSRGTRVIGLGRPLSVPVGPAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 108 LGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQTGKTaiavdTI 187
Cdd:PRK09099 105 LGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKS-----TL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 188 LNQKDNWATGDPNkqvrcVYVAIGQKASTIAAVRETLKQQGALEYTTIVASPASDAAGFKYLAPYTGSAIGQHWMYGGKH 267
Cdd:PRK09099 180 MGMFARGTQCDVN-----VIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 268 VLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERcAKLSDelgAGSMTGFPIIETKANDVSAFIPTNVI 347
Cdd:PRK09099 255 VLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLER-AGMGE---TGSITALYTVLAEDESGSDPIAEEVR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 348 SITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAMKKVSGTLKLDLAQYRAMEAFAM---FASDLDDASKAQLTR 424
Cdd:PRK09099 331 GILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQvgeYRAGSDPVADEAIAK 410
|
410
....*....|....*...
gi 2509359131 425 GARLTELLRQP--QYTPY 440
Cdd:PRK09099 411 IDAIRDFLSQRtdEYSDP 428
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
98-377 |
5.27e-38 |
|
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: 141.21 E-value: 5.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 98 VLSVPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQT 177
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 178 GKTAIAVdTILNQKDNWATGDpNKQVrcVYVAIGQKASTIAAVRETLKQQGALEYTTIVASPASDAAGFKYLAPYTGSAI 257
Cdd:cd01135 81 PHNELAA-QIARQAGVVGSEE-NFAI--VFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 258 GQHWMY-GGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGdvfYLHSRL---LERCAKLSDElgAGSMTGFPIIET 333
Cdd:cd01135 157 AEYLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTM 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2509359131 334 KANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSR 377
Cdd:cd01135 232 PNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
85-405 |
4.65e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 139.56 E-value: 4.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 85 GIEEGQEVHRTGEVLSVPVGDAYLGRVVDPLGNPIDDlGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIG 164
Cdd:PRK06820 83 GLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 165 RGQRQLIIGDRQTGKTaiavdTILNQKDNWATGDPnkqvrCVYVAIGQKASTiaaVRETLKQQGALE--YTTIVASPASD 242
Cdd:PRK06820 162 EGQRIGIFAAAGVGKS-----TLLGMLCADSAADV-----MVLALIGERGRE---VREFLEQVLTPEarARTVVVVATSD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 243 AAGFKYL-APYTGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERcAKLSDElg 321
Cdd:PRK06820 229 RPALERLkGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLER-TGNSDR-- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 322 aGSMTGFPIIETKANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAMKKVSGTLKLDLAQY 401
Cdd:PRK06820 306 -GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACY 384
|
....
gi 2509359131 402 RAME 405
Cdd:PRK06820 385 QEIE 388
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
45-377 |
3.89e-35 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 137.26 E-value: 3.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 45 VEGLPSVMANELLRFE--DGTLGLAQNLDTR-DIGVI-ILGDFTGIE-EGQEVHRTGEVLSVPVGDAYLGRVVDPLGNPI 119
Cdd:PRK04196 17 VEGVEGVAYGEIVEIElpNGEKRRGQVLEVSeDKAVVqVFEGTTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 120 DDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQR----------------QLIigdRQTgktaia 183
Cdd:PRK04196 97 DGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnelaaQIA---RQA------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 184 vdTILNQKDNWATgdpnkqvrcVYVAIGQKASTIAAVRETLKQQGALEYTTIVASPASDAAGFKYLAPYTGSAIGQHWMY 263
Cdd:PRK04196 168 --KVLGEEENFAV---------VFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 264 G-GKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGdvfYLHSRL---LERCAKLSDElgAGSMTGFPIIETKANDVS 339
Cdd:PRK04196 237 EkGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDIT 311
|
330 340 350
....*....|....*....|....*....|....*...
gi 2509359131 340 AFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSR 377
Cdd:PRK04196 312 HPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
59-436 |
8.09e-33 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 130.11 E-value: 8.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 59 FEDGTLGLAQNLDTRDIGVII--LGDFTGIEEGQEVHRTGEVLSVPVGDAYLGRVVDPLGNPIDDLGEIEAEG----RRA 132
Cdd:PRK08149 38 HSNEVIARAQVVGFQRERTILslIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVGpiseERV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 133 LELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQTGKTaiavdTILNQKDNWATGDpnkqvrcVYVA--I 210
Cdd:PRK08149 118 IDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKT-----SLMNMLIEHSEAD-------VFVIglI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 211 GQKASTIAAVRETLKQQGALEYTTIVASPASDAAGFKYLAPYTGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLR 290
Cdd:PRK08149 186 GERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 291 RPPGREAYPGDVFYLHSRLLERCAKLSdelgAGSMTGFPIIETKANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVD 370
Cdd:PRK08149 266 ELPARRGYPASVFDSLPRLLERPGATL----AGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAID 341
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2509359131 371 VGISVSRVGG-------AAQTKAMKKVSGTLK-----LDLAQYRAMEafamfASDLDDASKAQltrgARLTELLRQPQ 436
Cdd:PRK08149 342 VLKSVSRVFGqvtdpkhRQLAAAFRKLLTRLEelqlfIDLGEYRRGE-----NADNDRAMDKR----PALEAFLKQDV 410
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
82-378 |
1.03e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 130.21 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 82 DFTGIEEGQEVHRTGEVLSVPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMI 161
Cdd:PRK08972 78 ELRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 162 PIGRGQRQLIIGDRQTGKTaiavdTILNQKDNWATGDpnkqvrcVYVA--IGQKASTIAA-VRETLKQQGaLEYTTIVAS 238
Cdd:PRK08972 158 TVGKGQRMGLFAGSGVGKS-----VLLGMMTRGTTAD-------VIVVglVGERGREVKEfIEEILGEEG-RARSVVVAA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 239 PASDAAGFKYLAPYTGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSD 318
Cdd:PRK08972 225 PADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 319 elGAGSMTGFPIIETKANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRV 378
Cdd:PRK08972 305 --GQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRV 362
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
22-444 |
4.65e-32 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 128.15 E-value: 4.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 22 YEPGNAERVeVGRVASASDGIARVEgLPSVMANELLRFEDGTlGLAQ--NLDTRDIGVIILGDFTGIEEGQEVHRTGEVL 99
Cdd:PRK07594 13 YPPPDGYCR-WGRIQDVSATLLNAW-LPGVFMGELCCIKPGE-ELAEvvGINGSKALLSPFTSTIGLHCGQQVMALRRRH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 100 SVPVGDAYLGRVVDPLGNPIDDLgEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQTGK 179
Cdd:PRK07594 90 QVPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 180 TaiavdTILNQKDNWATGDPNkqvrcVYVAIGQKASTiaaVRE----TLKQQGALEYTTIVASpaSDAAGFKYL-APYTG 254
Cdd:PRK07594 169 S-----TLLAMLCNAPDADSN-----VLVLIGERGRE---VREfidfTLSEETRKRCVIVVAT--SDRPALERVrALFVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 255 SAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAklsdeLGA-GSMTGFPIIET 333
Cdd:PRK07594 234 TTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTVLV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 334 KANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAMKKVSGTLKLDLAQYRAMEAF---AMF 410
Cdd:PRK07594 309 EGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLiriGEY 388
|
410 420 430
....*....|....*....|....*....|....
gi 2509359131 411 ASDLDDASKAQLTRGARLTELLRQPQYTPYAVED 444
Cdd:PRK07594 389 QRGVDTDTDKAIDTYPDICTFLRQSKDEVCGPEL 422
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
33-395 |
3.23e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 125.57 E-value: 3.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 33 GRVASASDGIARVEGL-PSVmaNELLRFEDG-----TLGLAQNLDTRDIGVIILGDFTGIEEGQEVHRTGEVLSVPVGDA 106
Cdd:PRK08472 20 GSITKISPTIIEADGLnPSV--GDIVKIESSdngkeCLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 107 YLGRVVDPLGNPIDDLGEIEAEgRRALELQAP-GVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQTGKTAIAVD 185
Cdd:PRK08472 98 LLGRVVDPLGRPIDGKGAIDYE-RYAPIMKAPiAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 186 TILNQKdnwatgDPNKqvrcVYVAIGQKASTIAA-VRETLKqqGALEYTTIVASPASDAAGFKYLAPYTGSAIGQHWMYG 264
Cdd:PRK08472 177 IVKGCL------APIK----VVALIGERGREIPEfIEKNLG--GDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 265 GKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKlsdELGAGSMTGFPIIETKANDVSAFIPT 344
Cdd:PRK08472 245 GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTVLVEGDDMSDPIAD 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2509359131 345 NVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAMKKVSGTLK 395
Cdd:PRK08472 322 QSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFK 372
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
78-405 |
4.15e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 125.61 E-value: 4.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 78 IILGDFTGIEE---GQEVHRTGEVLSVPVGDAYLGRVVDPLGNPIDdlGEIEAEGRRAL--ELQAPGVTQRKSVHEPLQT 152
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLD--GSALPKGLAPVstDQDPPNPLKRPPIREPMEV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 153 GLKAIDAMIPIGRGQRQLIIGDRQTGKTaiavdTILNQKDNWATGDPNkqvrcVYVAIGQKASTiaaVRE----TLKQQG 228
Cdd:PRK07721 145 GVRAIDSLLTVGKGQRVGIFAGSGVGKS-----TLMGMIARNTSADLN-----VIALIGERGRE---VREfierDLGPEG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 229 aLEYTTIVASPASDAAGFKYLAPYTGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSR 308
Cdd:PRK07721 212 -LKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 309 LLERcaklSDELGAGSMTGFPIIETKANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAMK 388
Cdd:PRK07721 291 LLER----TGTNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHK 366
|
330
....*....|....*..
gi 2509359131 389 KVSGTLKLDLAQYRAME 405
Cdd:PRK07721 367 EAANRFRELLSTYQNSE 383
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
94-434 |
2.24e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 123.46 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 94 RTGEVLsvpVGDAYLGRVVDPLGNPIDDLGEIEaeGRRALELQAPGVT--QRKSVHEPLQTGLKAIDAMIPIGRGQRQLI 171
Cdd:PRK07196 86 QDGELL---IGDSWLGRVINGLGEPLDGKGQLG--GSTPLQQQLPQIHplQRRAVDTPLDVGVNAINGLLTIGKGQRVGL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 172 IGDRQTGKTAI-AVDTILNQKDNWATGdpnkqvrcvyvAIGQKASTIAAVRETLKQQGALEYTTIVASPASDAAGFKYLA 250
Cdd:PRK07196 161 MAGSGVGKSVLlGMITRYTQADVVVVG-----------LIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 251 PYTGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAklsDELGAGSMTGFPI 330
Cdd:PRK07196 230 TELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYT 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 331 IETKANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSR----VGGAAQTKAMKKVSGTLKlDLAQYRAMEA 406
Cdd:PRK07196 307 VLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCYA-DYMAIKPLIP 385
|
330 340
....*....|....*....|....*...
gi 2509359131 407 FAMFASDLDDASKAQLTRGARLTELLRQ 434
Cdd:PRK07196 386 LGGYVAGADPMADQAVHYYPAITQFLRQ 413
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
80-378 |
5.31e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 116.75 E-value: 5.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 80 LGDFTGIEEGQEVHRTGEVLSVPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDA 159
Cdd:PRK05688 82 VGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSING 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 160 MIPIGRGQRQLIIGDRQTGKTaiavdTILNQKDNWATGDPnkqvrCVYVAIGQKASTIAAVRETLKQQGALEYTTIVASP 239
Cdd:PRK05688 162 LLTVGRGQRLGLFAGTGVGKS-----VLLGMMTRFTEADI-----IVVGLIGERGREVKEFIEHILGEEGLKRSVVVASP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 240 ASDAAGFKYLAPYTGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAklSDE 319
Cdd:PRK05688 232 ADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAE 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2509359131 320 LGAGSMTGFPIIETKANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRV 378
Cdd:PRK05688 310 PGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV 368
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
33-417 |
1.42e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 115.48 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 33 GRVASASDGIARVEGL-PSVMANELLRFE-DGTLGLAQNLDTRDIGVIIL----GDFTGIeeGQEVHRTGEvLSVPVGDA 106
Cdd:PRK06002 28 GTVSEVTASHYRVRGLsRFVRLGDFVAIRaDGGTHLGEVVRVDPDGVTVKpfepRIEIGL--GDAVFRKGP-LRIRPDPS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 107 YLGRVVDPLGNPIDDLGEI-EAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQTGKTAIAvd 185
Cdd:PRK06002 105 WKGRVINALGEPIDGLGPLaPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLL-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 186 TILNQKDNWATgdpnkqvrcVYVA-IGQKAStiaAVRETLKQ--QGALEYTTIVASPASDAAGFKYLAPYTGSAIGQHWM 262
Cdd:PRK06002 183 AMLARADAFDT---------VVIAlVGERGR---EVREFLEDtlADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 263 YGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDelGAGSMTGFPIIETKANDVSAFI 342
Cdd:PRK06002 251 DRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLVDGDDHNDPV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 343 PTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAMKKVSGTLKLDLAQY------RAMEAF-AMFASDLD 415
Cdd:PRK06002 329 ADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFeetrdlRLIGGYrAGSDPDLD 408
|
..
gi 2509359131 416 DA 417
Cdd:PRK06002 409 QA 410
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
95-387 |
1.72e-27 |
|
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: 115.20 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 95 TGEVLSVPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGD 174
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 175 -------------RQTGKTAIAVDTILN-QKDNWATgdpnkqvrcVYVAIGQKASTIAAVRETLKQQGALEYTTIVASPA 240
Cdd:TIGR01040 150 aglphneiaaqicRQAGLVKLPTKDVHDgHEDNFAI---------VFAAMGVNMETARFFKQDFEENGSMERVCLFLNLA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 241 SDAAGFKYLAPYTGSAIGQHWMYG-GKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLsdE 319
Cdd:TIGR01040 221 NDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV--E 298
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2509359131 320 LGAGSMTGFPIIETKANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAM 387
Cdd:TIGR01040 299 GRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
31-96 |
1.57e-25 |
|
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: 99.45 E-value: 1.57e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2509359131 31 EVGRVASASDGIARVEGLPSVMANELLRFEDGTLGLAQNLDTRDIGVIILGDFTGIEEGQEVHRTG 96
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTG 66
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
101-378 |
6.26e-25 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 107.56 E-value: 6.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 101 VPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQTGKT 180
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKS 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 181 aiavdTILNQKDNWATGDpnkqvrcVYVA--IGQKASTIAAVRETLKQQGALEYTTIVASPASDAAGFKYLAPYTGSAIG 258
Cdd:PRK07960 190 -----VLLGMMARYTQAD-------VIVVglIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 259 QHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDelGAGSMTGFPIIETKANDV 338
Cdd:PRK07960 258 EDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGDDQ 335
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2509359131 339 SAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRV 378
Cdd:PRK07960 336 QDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRA 375
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
100-377 |
3.26e-24 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 105.37 E-value: 3.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 100 SVPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQTGK 179
Cdd:PRK05922 91 SLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 180 TAIaVDTIlnqkdnwATGdpNKQVRCVYVAIGQKAStiaAVRETLKQQG---ALEYTTIVASPASDAAGFKYLAPYTGSA 256
Cdd:PRK05922 171 SSL-LSTI-------AKG--SKSTINVIALIGERGR---EVREYIEQHKeglAAQRTIIIASPAHETAPTKVIAGRAAMT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 257 IGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERcAKLSDElgaGSMTGFPIIETKAN 336
Cdd:PRK05922 238 IAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTER-AGNNDK---GSITALYAILHYPN 313
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2509359131 337 DVSAFIPTnVISITDGQIFLqSDLFNANQRPAVDVGISVSR 377
Cdd:PRK05922 314 HPDIFTDY-LKSLLDGHFFL-TPQGKALASPPIDILTSLSR 352
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
89-378 |
3.79e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 101.98 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 89 GQEVHRTGEVLSVPVGDAYLGRVVDPLGNPIDDlgEIEAEGRRALELQAPGVT--QRKSVHEPLQTGLKAIDAMIPIGRG 166
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIHafEREEITDVFETGIKSIDSMLTIGIG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 167 QRQLIIGDRQTGKTaiavdTILNQKDNWATGDPNkqvrcVYVAIGQKASTIAA-VRETLKQQGaLEYTTIVASPASDAAG 245
Cdd:PRK06793 157 QKIGIFAGSGVGKS-----TLLGMIAKNAKADIN-----VISLVGERGREVKDfIRKELGEEG-MRKSVVVVATSDESHL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 246 FKYLAPYTGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPgreaYPGDVFYLHS---RLLERCAKLSDelga 322
Cdd:PRK06793 226 MQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK---- 297
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2509359131 323 GSMTGFPIIETKANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRV 378
Cdd:PRK06793 298 GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRI 353
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
63-435 |
6.06e-22 |
|
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: 98.64 E-value: 6.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 63 TLGLAQNLDTRDIGVIILGDFTGIEEGQEVHRTGEVLSVPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQ 142
Cdd:TIGR01039 40 TLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 143 RKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQTGKTAIAVDTILN--QKDNWATgdpnkqvrcVYVAIGQKASTIAAV 220
Cdd:TIGR01039 120 QSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiaKEHGGYS---------VFAGVGERTREGNDL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 221 RETLKQQGALEYTTIVASPASDAAGFKYLAPYTGSAIGQHWM-YGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYP 299
Cdd:TIGR01039 191 YHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 300 GDVFYLHSRLLERCAKLSdelgAGSMTGFPIIETKANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSR-- 377
Cdd:TIGR01039 271 PTLATEMGELQERITSTK----TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRll 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2509359131 378 ---VGGAAQTKAMKKVSGTLKldlaQYRAM-EAFAMFASD-LDDASKAQLTRGARLTELLRQP 435
Cdd:TIGR01039 347 dpsVVGEEHYDVARGVQQILQ----RYKELqDIIAILGMDeLSEEDKLTVERARRIQRFLSQP 405
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
25-405 |
2.45e-20 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 93.51 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 25 GNAERVEV-GRVASASDGIARVEGLPSVMAnellrfedgtLGLAQNLDTRDIGVII---------------LGDFTGIEE 88
Cdd:PRK08927 10 GDIDTLVIyGRVVAVRGLLVEVAGPIHALS----------VGARIVVETRGGRPVPcevvgfrgdrallmpFGPLEGVRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 89 GQEVHRTGEVLSVPVGDAYLGRVVDPLGNPIDDLGEIeAEGRRALELQA--PGVTQRKSVHEPLQTGLKAIDAMIPIGRG 166
Cdd:PRK08927 80 GCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPL-PQGPVPYPLRAppPPAHSRARVGEPLDLGVRALNTFLTCCRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 167 QRQLIIGDRQTGKTaiavdTILNQKDNWATGDPNkqvrcVYVAIGQKAStiaAVRE----TLKQQGALEYTTIVASpaSD 242
Cdd:PRK08927 159 QRMGIFAGSGVGKS-----VLLSMLARNADADVS-----VIGLIGERGR---EVQEflqdDLGPEGLARSVVVVAT--SD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 243 A-AGFKYLAPYTGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAklSDELG 321
Cdd:PRK08927 224 EpALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 322 AGSMTGFPIIETKANDVSAFIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAMKKVSGTLKLDLAQY 401
Cdd:PRK08927 302 EGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATY 381
|
....
gi 2509359131 402 RAME 405
Cdd:PRK08927 382 ADME 385
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
46-166 |
4.76e-19 |
|
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: 89.76 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 46 EGLPSVmaNELLRFEDG-----TLGLAQNLDTRDIGVIILGDFTGIEEGQEVHRTGEVLSVPVGDAYLGRVVDPLGNPID 120
Cdd:COG0055 23 GELPAI--YNALEVENEgggelVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPID 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2509359131 121 DLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRG 166
Cdd:COG0055 101 GKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKG 146
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
66-359 |
3.45e-16 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 80.85 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 66 LAQ--NLDTRDIGVIILGDFTGIEEGQEVHRTGEVLSVPVGDAYLGRVVDPLGNPIDDLGEIEAEgrrALELQAPGV--T 141
Cdd:PRK02118 39 LAQviRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGE---PIEIGGPSVnpV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 142 QRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDrqtgktaiavdtilnqkdnwaTGDPNKQVrCVYVAIGQKASTI---- 217
Cdd:PRK02118 116 KRIVPREMIRTGIPMIDVFNTLVESQKIPIFSV---------------------SGEPYNAL-LARIALQAEADIIilgg 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 218 --------AAVRETLKQQGALEYTTIVASPASDAAGFKYLAPYTGSAIGQHW-MYGGKHVLIIFDDLSKQAEAYRAVSLL 288
Cdd:PRK02118 174 mgltfddyLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFaLEGKKKVLVLLTDMTNFADALKEISIT 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2509359131 289 LRRPPGREAYPGDvfyLHSRLLERCAKLSDELGAGSMTGFPIIETKANDVSAFIPTNVISITDGQIFLQSD 359
Cdd:PRK02118 254 MDQIPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLRRG 321
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
387-454 |
2.30e-15 |
|
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: 70.94 E-value: 2.30e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 387 MKKVSGTLKLDLAQYRAMEAFAMFASD--LDDASKAQLTRGARLTELLRQPQYTPYAVEDQVVSIWAGTN 454
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
100-189 |
1.84e-14 |
|
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: 73.79 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 100 SVPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQTGK 179
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90
....*....|
gi 2509359131 180 TAIAVDTILN 189
Cdd:cd01133 81 TVLIMELINN 90
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
85-189 |
2.05e-13 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 72.38 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 85 GIEEGQEVHRTGEVLSVPVGDAYLGRVVDPLGNPIDDLGEIEAEGRRALELQAPGVTQRKSVHEPLQTGLKAIDAMIPIG 164
Cdd:CHL00060 80 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYR 159
|
90 100
....*....|....*....|....*
gi 2509359131 165 RGQRQLIIGDRQTGKTAIAVDTILN 189
Cdd:CHL00060 160 RGGKIGLFGGAGVGKTVLIMELINN 184
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
99-377 |
1.77e-12 |
|
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: 67.98 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 99 LSVPVGDAYLGRVVDPLGNPIDDLGEieAEG---RRALELQ------APGVTQRKSVHEPLQTGLKAIDAMIPIGRGQRQ 169
Cdd:cd01134 2 LSVELGPGLLGSIFDGIQRPLEVIAE--TGSifiPRGVNVQrwpvrqPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 170 LIIGDRQTGKTaiavdTILNQKDNWATGDPNkqvrcVYVAIGQKASTIAAVRE-------TLKQQGALEYTTIVAS---- 238
Cdd:cd01134 80 AIPGPFGCGKT-----VISQSLSKWSNSDVV-----IYVGCGERGNEMAEVLEefpelkdPITGESLMERTVLIANtsnm 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 239 --PASDAAgfkylaPYTGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGdvfYLHSRLLE----- 311
Cdd:cd01134 150 pvAAREAS------IYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLAEfyera 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2509359131 312 ---RCAKLSDELGAGSMTGfpIIETKANDVSAFIPTNVISITdgQIF--LQSDLFNANQRPAVDVGISVSR 377
Cdd:cd01134 221 grvRCLGSPGREGSVTIVG--AVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
31-96 |
3.93e-12 |
|
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: 61.41 E-value: 3.93e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2509359131 31 EVGRVASASDGIARVEGLPSVMANELLRFEDGTLGLAQNLDTRDIGVIILGDFTGIEEGQEVHRTG 96
Cdd:pfam02874 4 VIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
206-409 |
3.03e-08 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 56.57 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 206 VYVAIGQKASTIAAVRETLKQ-------QGALEYTTIVASPASDAAGFKYLAPYTGSAIGQHWMYGGKHVLIIFDDLSKQ 278
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 279 AEAYRAVSLLLRRPPGREAYPGdvfYLHSRLLE------RCAKLSDELGAGSMTGFPIIETKANDVSAFIPTNVISITDG 352
Cdd:PRK14698 766 AEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKV 842
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2509359131 353 QIFLQSDLFNANQRPAVDVGISVSRVGGAAQTKAMKKVSgtlkldlAQYRAMEAFAM 409
Cdd:PRK14698 843 FWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNVD-------PEWKAMRDKAM 892
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
140-311 |
1.09e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 44.77 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 140 VTQRKSVHEPLQTGLKAIDAMIPIGRGQRQLIIGDRQTGKT----AIA----VDTIlnqkdnwatgdpnkqvrcVYVAIG 211
Cdd:PRK04192 201 YKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTvtqhQLAkwadADIV------------------IYVGCG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509359131 212 QKASTIAavrETLKQ----------QGALEYTTIVAS----P-----ASdaagfkylaPYTGSAIGQHWMYGGKHVLIIF 272
Cdd:PRK04192 263 ERGNEMT---EVLEEfpelidpktgRPLMERTVLIANtsnmPvaareAS---------IYTGITIAEYYRDMGYDVLLMA 330
|
170 180 190
....*....|....*....|....*....|....*....
gi 2509359131 273 DDLSKQAEAYRAVSLLLRRPPGREAYPGdvfYLHSRLLE 311
Cdd:PRK04192 331 DSTSRWAEALREISGRLEEMPGEEGYPA---YLASRLAE 366
|
|
| |
