|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
34-538 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 998.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 34 SEVSKILEERILGTETGINLEETGKVLSIGDGIARVYGLKNIQAEEMVEFDSGIKGMAMNLDVDNVGVVVFGNDKVIREG 113
Cdd:PRK09281 6 EEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIKEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 114 DIVKRTGAIVDVPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRE 193
Cdd:PRK09281 86 DTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 194 LIIGDRQTGKTAIAIDTIINQKrfndagddKKKLFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFL 273
Cdd:PRK09281 166 LIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 274 APYSGCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNNSLGGGSLTALP 353
Cdd:PRK09281 238 APYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 354 VIETQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQ 433
Cdd:PRK09281 318 IIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 434 FGSDLDASTQQLLNRGVRLTELLKQGQYVPMGIEEQVGVIYAGVKGYLDKVDPSAITKFEKEFLAHLRSSQQALLKTIRE 513
Cdd:PRK09281 398 FGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRE 477
|
490 500
....*....|....*....|....*
gi 71988063 514 EGQISPQTDAQLKDVVVNFLATFKP 538
Cdd:PRK09281 478 TKDLSDEIEAKLKAAIEEFKKTFAA 502
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
34-538 |
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: 995.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 34 SEVSKILEERILGTETGINLEETGKVLSIGDGIARVYGLKNIQAEEMVEFDSGIKGMAMNLDVDNVGVVVFGNDKVIREG 113
Cdd:COG0056 6 EEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEGIKEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 114 DIVKRTGAIVDVPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRE 193
Cdd:COG0056 86 DTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 194 LIIGDRQTGKTAIAIDTIINQKrfndagddKKKLFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFL 273
Cdd:COG0056 166 LIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 274 APYSGCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNNSLGGGSLTALP 353
Cdd:COG0056 238 APYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 354 VIETQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQ 433
Cdd:COG0056 318 IIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 434 FGSDLDASTQQLLNRGVRLTELLKQGQYVPMGIEEQVGVIYAGVKGYLDKVDPSAITKFEKEFLAHLRSSQQALLKTIRE 513
Cdd:COG0056 398 FGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRE 477
|
490 500
....*....|....*....|....*
gi 71988063 514 EGQISPQTDAQLKDVVVNFLATFKP 538
Cdd:COG0056 478 TGKLDDEIEEKLKAAIEEFKKTFAA 502
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
35-538 |
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: 818.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 35 EVSKILEERILGTETGINLEETGKVLSIGDGIARVYGLKNIQAEEMVEFDSGIKGMAMNLDVDNVGVVVFGNDKVIREGD 114
Cdd:TIGR00962 6 EISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIREGS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 115 IVKRTGAIVDVPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQREL 194
Cdd:TIGR00962 86 TVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQREL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 195 IIGDRQTGKTAIAIDTIINQKrfndagddKKKLFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFLA 274
Cdd:TIGR00962 166 IIGDRQTGKTAVAIDTIINQK--------DSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 275 PYSGCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNNSLGGGSLTALPV 354
Cdd:TIGR00962 238 PYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 355 IETQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQF 434
Cdd:TIGR00962 318 IETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 435 GSDLDASTQQLLNRGVRLTELLKQGQYVPMGIEEQVGVIYAGVKGYLDKVDPSAITKFEKEFLAHLRSSQQALLKTIREE 514
Cdd:TIGR00962 398 ASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTT 477
|
490 500
....*....|....*....|....
gi 71988063 515 GQISPQTDAQLKDVVVNFLATFKP 538
Cdd:TIGR00962 478 KKLTEELEAKLKEALKNFKKTFAW 501
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
51-537 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 754.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 51 INLEETGKVLSIGDGIARVYGLKNIQAEEMVEFDSGIKGMAMNLDVDNVGVVVFGNDKVIREGDIVKRTGAIVDVPVGDG 130
Cdd:CHL00059 2 VKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 131 LLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDT 210
Cdd:CHL00059 82 YLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 211 IINQKrfndagddKKKLFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAMGEHFRDNGK 290
Cdd:CHL00059 162 ILNQK--------GQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 291 HALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNNSLGGGSLTALPVIETQAGDVSAYIPTNV 370
Cdd:CHL00059 234 HTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 371 ISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDASTQQLLNRGV 450
Cdd:CHL00059 314 ISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 451 RLTELLKQGQYVPMGIEEQVGVIYAGVKGYLDKVDPSAITKFEKEFLAHLRSSQQALLKTIREEGQISPQTDAQLKDVVV 530
Cdd:CHL00059 394 RLRELLKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQ 473
|
....*..
gi 71988063 531 NFLATFK 537
Cdd:CHL00059 474 EQLELFL 480
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
31-538 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 742.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 31 ASGSEVSKILEERILGTETGINLEETGKVLSIGDGIARVYGLKNIQAEEMVEFDSGIKGMAMNLDVDNVGVVVFGNDKVI 110
Cdd:PRK13343 3 SNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 111 REGDIVKRTGAIVDVPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRG 190
Cdd:PRK13343 83 LAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 191 QRELIIGDRQTGKTAIAIDTIINQKrfndagddKKKLFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPL 270
Cdd:PRK13343 163 QRELIIGDRQTGKTAIAIDAIINQK--------DSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 271 QFLAPYSGCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNNSLGGGSLT 350
Cdd:PRK13343 235 QYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 351 ALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAA 430
Cdd:PRK13343 315 ALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 431 FAQFGSDLDASTQQLLNRGVRLTELLKQGQYVPMGIEEQVGVIYAGVKGYLDKVDPSAITKFEKEFLAHLRSSQQALLKT 510
Cdd:PRK13343 395 FTRFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLA 474
|
490 500
....*....|....*....|....*...
gi 71988063 511 IREEGQISPQTDAQLKDVVVNFLATFKP 538
Cdd:PRK13343 475 LESPRELDEAWLAALEEILREAGERFAA 502
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
122-403 |
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: 603.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 122 IVDVPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQT 201
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 202 GKTAIAIDTIINQKRfndagddkKKLFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAM 281
Cdd:cd01132 81 GKTAIAIDTIINQKG--------KKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 282 GEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNNSLGGGSLTALPVIETQAGD 361
Cdd:cd01132 153 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 71988063 362 VSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVG 403
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
89-493 |
1.75e-124 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 376.69 E-value: 1.75e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 89 GMAMNLDVDN-VGVVVFGNDKVIREGDIVKRTGAIVDVPVGDGLLGRVVDALGNPIdgkgPIANARRSR----------- 156
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEV----PVGLLTRSRalleseqtlgk 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 157 VEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTIINQKRFNDAGDDKKKLFCIYVAVGQ 236
Cdd:PTZ00185 156 VDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVISIYVSIGQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 237 KRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRP 316
Cdd:PTZ00185 236 RCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 317 PGREAYPGDVFYLHSRLLERAAKMNNSLGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVG 396
Cdd:PTZ00185 316 PGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 397 LSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDASTqqlLNRGVRLTELLKQGQyvPMGIEEQVGVIYAG 476
Cdd:PTZ00185 396 LSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNALVSLYAC 470
|
410
....*....|....*..
gi 71988063 477 VKGYLDKVDPSAITKFE 493
Cdd:PTZ00185 471 LNGYLDDVKVNYAKLYE 487
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
124-402 |
4.01e-124 |
|
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: 364.85 E-value: 4.01e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 124 DVPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGK 203
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 204 TAIAIDTIINQKRfndagddKKKLFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAMGE 283
Cdd:cd19476 81 TVLAMQLARNQAK-------AHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 284 HFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNNslGGGSLTALPVIETQAGDVS 363
Cdd:cd19476 154 YFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLT 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 71988063 364 AYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRV 402
Cdd:cd19476 232 DPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
177-400 |
2.98e-113 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 334.71 E-value: 2.98e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 177 GVKAVDSLVPIGRGQRELIIGDRQTGKTAIAiDTIINQkrfndAGDDKkklfCIYVAVGQKRSTVAQIVKRLTDAGAMDY 256
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQ-----ASADV----VVYALIGERGREVREFIEELLGSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 257 TIVVSATASDAAPLQFLAPYSGCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLER 336
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71988063 337 AAKMNNslGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVS 400
Cdd:pfam00006 151 AGRVKG--KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
58-458 |
5.54e-100 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 311.14 E-value: 5.54e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 58 KVLSIGDGIARVYGLKNIQAEEM--VEFDSGIKGMAMNLDVDNVGVVVFGNDKVIREGDIVKRTGAIVDVPVGDGLLGRV 135
Cdd:PRK07165 4 KIKSIFDYIVEVKGEYDYQQNQFftLKNNPNVKAFVISATEDKAYLLINNEKGKIKINDELIELNNTNKVKTSKEYFGKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 136 VDALGNPIDGKGPI-----ANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDT 210
Cdd:PRK07165 84 IDIDGNIIYPEAQNplskkFLPNTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 211 IINQKRfndagDDKKklfCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSAtASDAAPLQFLAPYSGCAMGEHFRDNgK 290
Cdd:PRK07165 164 IINQKN-----TNVK---CIYVAIGQKRENLSRIYETLKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAENISYN-D 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 291 HALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNNslgGGSLTALPVIETQAGDVSAYIPTNV 370
Cdd:PRK07165 234 DVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKN---RKTITALPILQTVDNDITSLISSNI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 371 ISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDASTQQLLNRGV 450
Cdd:PRK07165 311 ISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKGK 390
|
....*...
gi 71988063 451 RLTELLKQ 458
Cdd:PRK07165 391 MIEKMFNQ 398
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
411-536 |
1.26e-65 |
|
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349748 [Multi-domain] Cd Length: 126 Bit Score: 208.76 E-value: 1.26e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 411 MKQVAGSMKLELAQYREVAAFAQFGSDLDASTQQLLNRGVRLTELLKQGQYVPMGIEEQVGVIYAGVKGYLDKVDPSAIT 490
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 71988063 491 KFEKEFLAHLRSSQQALLKTIREEGQISPQTDAQLKDVVVNFLATF 536
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
407-532 |
1.33e-64 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 206.14 E-value: 1.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 407 QTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDASTQQLLNRGVRLTELLKQGQYVPMGIEEQVGVIYAGVKGYLDKVDP 486
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 71988063 487 SAITKFEKEFLAHLRSSQQALLKTIREEGQISPQTDAQLKDVVVNF 532
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
125-402 |
1.44e-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: 168.89 E-value: 1.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 125 VPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGKT 204
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 205 aiaidTIINQKRFNDAGDdkkklfcIYVA--VGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAMG 282
Cdd:cd01136 82 -----TLLGMIARNTDAD-------VNVIalIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 283 EHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNNslggGSLTALPVIETQAGDV 362
Cdd:cd01136 150 EYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----GSITAFYTVLVEGDDF 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 71988063 363 SAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRV 402
Cdd:cd01136 226 NDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
101-468 |
2.88e-45 |
|
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: 164.82 E-value: 2.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 101 VVVFGNDKV----------IREGDIVKRTGAIVDVPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSV 170
Cdd:COG1157 58 VVGFRGDRVllmplgdlegISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 171 REPMVTGVKAVDSLVPIGRGQReliigdrqtgktaIAIdtiinqkrFNDAGddkkklfciyvaVGqK--------RSTVA 242
Cdd:COG1157 138 TEPLDTGVRAIDGLLTVGRGQR-------------IGI--------FAGSG------------VG-KstllgmiaRNTEA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 243 QIV-----------------KRLTDAGaMDYTIVVSATASDAAPLQFLAPYSGCAMGEHFRDNGKHALIIFDDLSKQAVA 305
Cdd:COG1157 184 DVNvialigergrevrefieDDLGEEG-LARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 306 YRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmnNSlGGGSLTAL------------PVIETqagdvsayiptnVISI 373
Cdd:COG1157 263 QREIGLAAGEPPATRGYPPSVFALLPRLLERAG---NG-GKGSITAFytvlvegddmndPIADA------------VRGI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 374 TDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVA------AFAQfGSD--LDAStqql 445
Cdd:COG1157 327 LDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEdlirigAYQP-GSDpeLDEA---- 401
|
410 420
....*....|....*....|...
gi 71988063 446 LNRGVRLTELLKQGQYVPMGIEE 468
Cdd:COG1157 402 IALIPAIEAFLRQGMDERVSFEE 424
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
57-458 |
1.58e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 163.06 E-value: 1.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 57 GKVLSIGDGIARVyGLKNIQAEEMVEFD-SGIKGMAMNLDVDNVGVVVFGNDKVIREGDIVKRTGAIVDVPVGDGLLGRV 135
Cdd:PRK06820 31 GPIVEIGPTLLRA-SLPGVAQGELCRIEpQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 136 VDALGNPIDGKGPIANARRSrVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGKTaiaidTIINQK 215
Cdd:PRK06820 110 LDGLGAPIDGGPPLTGQWRE-LDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKS-----TLLGML 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 216 RFNDAGDdkkklFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATaSDAAPLQFL-APYSGCAMGEHFRDNGKHALI 294
Cdd:PRK06820 184 CADSAAD-----VMVLALIGERGREVREFLEQVLTPEARARTVVVVAT-SDRPALERLkGLSTATTIAEYFRDRGKKVLL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 295 IFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNNslggGSLTALPVIETQAGDVSAYIPTNVISIT 374
Cdd:PRK06820 258 MADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDR----GSITAFYTVLVEGDDMNEPVADEVRSLL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 375 DGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFG---SDLDASTQQLLNRGVR 451
Cdd:PRK06820 334 DGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGeyqAGEDLQADEALQRYPA 413
|
....*..
gi 71988063 452 LTELLKQ 458
Cdd:PRK06820 414 ICAFLQQ 420
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
116-470 |
7.09e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 161.07 E-value: 7.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 116 VKRTGAIVDVPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELI 195
Cdd:PRK06936 88 VSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 196 IGDRQTGKTAIaIDTIInqkRFNDAGddkkklFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFLAP 275
Cdd:PRK06936 168 FAAAGGGKSTL-LASLI---RSAEVD------VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 276 YSGCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNNslggGSLTALPVI 355
Cdd:PRK06936 238 FVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDK----GSITALYTV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 356 ETQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFG 435
Cdd:PRK06936 314 LVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIG 393
|
330 340 350
....*....|....*....|....*....|....*...
gi 71988063 436 S---DLDASTQQLLNRGVRLTELLKQGQYVPMGIEEQV 470
Cdd:PRK06936 394 EyqkGQDKEADQAIERIGAIRGFLRQGTHELSHFNETL 431
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
104-435 |
2.86e-42 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 156.85 E-value: 2.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 104 FGNDKVIREGDIVKRTGAIVDVPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDS 183
Cdd:PRK09099 77 FGELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 184 LVPIGRGQRELIIGDRQTGKTaiaidTIINQKRFNDAGDdkkklFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSAT 263
Cdd:PRK09099 157 LMTLGEGQRMGIFAPAGVGKS-----TLMGMFARGTQCD-----VNVIALIGERGREVREFIELILGEDGMARSVVVCAT 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 264 ASDAAPLQFLAPYSGCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNNS 343
Cdd:PRK09099 227 SDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-MGET 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 344 lggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELA 423
Cdd:PRK09099 306 ---GSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLA 382
|
330
....*....|..
gi 71988063 424 QYREVAAFAQFG 435
Cdd:PRK09099 383 KHREVETLLQVG 394
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
50-470 |
3.70e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 156.42 E-value: 3.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 50 GINLEETGKVLSIGDgIARVY----GLKNIQAEeMVEFDSgikgmamnldvDNVGVVVFGNDKVIREGDIVKRTGAIVDV 125
Cdd:PRK07721 27 GLMIESKGPESSIGD-VCYIHtkggGDKAIKAE-VVGFKD-----------EHVLLMPYTEVAEIAPGCLVEATGKPLEV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 126 PVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGKTa 205
Cdd:PRK07721 94 KVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKS- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 206 iaidTIINQKRFNDAGDdkkklFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAMGEHF 285
Cdd:PRK07721 173 ----TLMGMIARNTSAD-----LNVIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 286 RDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNNslggGSLTALPVIETQAGDVSAY 365
Cdd:PRK07721 244 RDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS----GSITAFYTVLVDGDDMNEP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 366 IPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDASTQQL 445
Cdd:PRK07721 320 IADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRGSSREI 399
|
410 420
....*....|....*....|....*...
gi 71988063 446 ---LNRGVRLTELLKQGQYVPMGIEEQV 470
Cdd:PRK07721 400 deaIQFYPQIISFLKQGTDEKATFEESI 427
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
49-459 |
7.55e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 149.84 E-value: 7.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 49 TGINLEETGKVLSIGDgIARVyglkniqaeEMVEFDSGIKGMAMNLDVDNVGVVVFGNDKVIREGDIVKRTGAIVDVPVG 128
Cdd:PRK08472 26 SPTIIEADGLNPSVGD-IVKI---------ESSDNGKECLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 129 DGLLGRVVDALGNPIDGKGPIANARRSRVeVKAP------GIIprlsvREPMVTGVKAVDSLVPIGRGQRELIIGDRQTG 202
Cdd:PRK08472 96 RNLLGRVVDPLGRPIDGKGAIDYERYAPI-MKAPiaamkrGLI-----DEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 203 KTAIaIDTIInqkrfndagddKKKLFCIYVA--VGQKRSTVAQ-IVKRLtdAGAMDYTIVVSATASDAAPLQFLAPYSGC 279
Cdd:PRK08472 170 KSTL-MGMIV-----------KGCLAPIKVValIGERGREIPEfIEKNL--GGDLENTVIVVATSDDSPLMRKYGAFCAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 280 AMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNnslGGGSLTALPVIETQA 359
Cdd:PRK08472 236 SVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEE---GKGSITAFFTVLVEG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 360 GDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYRE------VAAFaQ 433
Cdd:PRK08472 313 DDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKEnevlirIGAY-Q 391
|
410 420
....*....|....*....|....*...
gi 71988063 434 FGSD--LDastqQLLNRGVRLTELLKQG 459
Cdd:PRK08472 392 KGNDkeLD----EAISKKEFMEQFLKQN 415
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
101-459 |
2.35e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 140.64 E-value: 2.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 101 VVVFGNDKV----------IREGDIVKRTGAIVDVPVGDGLLGRVVDALGNPIDGKGPIANarRSRVEVKAPGIIP--RL 168
Cdd:PRK05688 69 VMGFSGDKVflmpvgsvagIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKA--EDWVPMDGPTINPlnRH 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 169 SVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGKTAIaidtIINQKRFNDAGddkkklfcIYVA--VGQKRSTVAQIVK 246
Cdd:PRK05688 147 PISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVL----LGMMTRFTEAD--------IIVVglIGERGREVKEFIE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 247 RLTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDV 326
Cdd:PRK05688 215 HILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 327 FYLHSRLLERAAkmNNSLGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAA 406
Cdd:PRK05688 295 FAKLPKLVERAG--NAEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQV 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 71988063 407 QTKAMKQVAGSMKLELAQYRE------VAAFAQFGsdlDASTQQLLNRGVRLTELLKQG 459
Cdd:PRK05688 373 VDPEHLRRAQRFKQLWSRYQQsrdlisVGAYVAGG---DPETDLAIARFPHLVQFLRQG 428
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
57-427 |
9.65e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 138.98 E-value: 9.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 57 GKVLSIGDGIARVYGL-KNIQAEEMVEFDSG---IKGMAMNLDVDNVGVVVFGNDKVIREGDIVKRTGAIVDVPvGDGLL 132
Cdd:PRK06002 28 GTVSEVTASHYRVRGLsRFVRLGDFVAIRADggtHLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGPLRIRP-DPSWK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 133 GRVVDALGNPIDGKGPIANARRSR-VEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGKT------- 204
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKStllamla 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 205 -AIAIDTIInqkrfndagddkkklfciyVA-VGQKRSTVAQIVKRlTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAMG 282
Cdd:PRK06002 187 rADAFDTVV-------------------IAlVGERGREVREFLED-TLADNLKKAVAVVATSDESPMMRRLAPLTATAIA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 283 EHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmnNSLGGGSLTALPVIETQAGDV 362
Cdd:PRK06002 247 EYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGP--GAEGGGSITGIFSVLVDGDDH 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71988063 363 SAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYRE 427
Cdd:PRK06002 325 NDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEE 389
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
101-435 |
1.24e-35 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 138.20 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 101 VVVFGNDKVI-----------REgDIVKRTGAIVDVPVGDGLLGRVVDALGN---PIDGKGPIANARRSR-VEVKAPGII 165
Cdd:PRK08149 48 VVGFQRERTIlslignaqglsRQ-VVLKPTGKPLSVWVGEALLGAVLDPTGKiveRFDAPPTVGPISEERvIDVAPPSYA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 166 PRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGKTAIaIDTIINQkrfNDAGddkkklfcIYVA--VGQKRSTVAQ 243
Cdd:PRK08149 127 ERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSL-MNMLIEH---SEAD--------VFVIglIGERGREVTE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 244 IVKRLTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYP 323
Cdd:PRK08149 195 FVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 324 GDVFYLHSRLLERAAKmnnsLGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVG 403
Cdd:PRK08149 275 ASVFDSLPRLLERPGA----TLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVF 350
|
330 340 350
....*....|....*....|....*....|..
gi 71988063 404 SAAQTKAMKQVAGSMKLELAQYREVAAFAQFG 435
Cdd:PRK08149 351 GQVTDPKHRQLAAAFRKLLTRLEELQLFIDLG 382
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
127-458 |
7.43e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 136.17 E-value: 7.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 127 VGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGKTAI 206
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 207 aIDTIinqKRFNDAGddkkklFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATAsDAAPLQFLAPYSGC-AMGEHF 285
Cdd:PRK07196 172 -LGMI---TRYTQAD------VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPA-DESPLMRIKATELChAIATYY 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 286 RDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmnNSLGGGSLTALPVIETQAGDVSAY 365
Cdd:PRK07196 241 RDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQDP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 366 IPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDL---DAST 442
Cdd:PRK07196 318 IVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVagaDPMA 397
|
330
....*....|....*.
gi 71988063 443 QQLLNRGVRLTELLKQ 458
Cdd:PRK07196 398 DQAVHYYPAITQFLRQ 413
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
125-459 |
4.01e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 134.06 E-value: 4.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 125 VPVGDGLLGRVVDALGNPIDGKGPI-ANARRSRvevKAPGIIP--RLSVREPMVTGVKAVDSLVPIGRGQR--------- 192
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIyTDQRASR---HSPPINPlsRRPITEPLDVGVRAINAMLTVGKGQRmglfagsgv 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 193 --ELIIGDRQTGKTAiaiDTIInqkrfndagddkkklfciyVA-VGQKRSTVAQIVKRLTDAGAMDYTIVVSATAsDAAP 269
Cdd:PRK08972 174 gkSVLLGMMTRGTTA---DVIV-------------------VGlVGERGREVKEFIEEILGEEGRARSVVVAAPA-DTSP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 270 LQFLapySGC----AMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNNSLG 345
Cdd:PRK08972 231 LMRL---KGCetatTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAG--NGGPG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 346 GGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQY 425
Cdd:PRK08972 306 QGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLY 385
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 71988063 426 RE------VAAFAQfGSdlDASTQQLLNRGVRLTELLKQG 459
Cdd:PRK08972 386 QQnrdlisIGAYKQ-GS--DPRIDNAIRLQPAMNAFLQQT 422
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
125-467 |
1.14e-33 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 132.77 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 125 VPVGDGLLGRVVDALGNPIDGKgPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGK- 203
Cdd:PRK07594 91 VPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKs 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 204 TAIAIDTiinqkrfNDAGDDKKKLfciyVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAMGE 283
Cdd:PRK07594 170 TLLAMLC-------NAPDADSNVL----VLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 284 HFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNNSlggGSLTALPVIETQAGDVS 363
Cdd:PRK07594 239 FFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-MGEK---GSITAFYTVLVEGDDMN 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 364 AYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGS---DLDA 440
Cdd:PRK07594 315 EPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEyqrGVDT 394
|
330 340
....*....|....*....|....*..
gi 71988063 441 STQQLLNRGVRLTELLKQGQYVPMGIE 467
Cdd:PRK07594 395 DTDKAIDTYPDICTFLRQSKDEVCGPE 421
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
125-401 |
4.87e-32 |
|
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: 124.64 E-value: 4.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 125 VPVGDGLLGRVVDALGNPIDGKGPIANarRSRVEVKAPGIIP--RLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTG 202
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDGGPPILP--EDYLDINGPPINPvaRIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 203 KTAIAIdTIINQKRFNDAGDDKKKLFciyVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAMG 282
Cdd:cd01135 82 HNELAA-QIARQAGVVGSEENFAIVF---AAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 283 EHFR-DNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMNNSlgGGSLTALPVIETQ 358
Cdd:cd01135 158 EYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTMP 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 71988063 359 AGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSR 401
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
55-121 |
8.09e-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: 116.78 E-value: 8.09e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71988063 55 ETGKVLSIGDGIARVYGLKNIQAEEMVEFDSGIKGMAMNLDVDNVGVVVFGNDKVIREGDIVKRTGA 121
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
49-469 |
2.08e-30 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 123.74 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 49 TGINLEETGKVLSIGDG--IARVYGLKNIQAE-EMVEFDsGIKGMAMNLDvdNVGVVVFGNdKVIREGDIVKRTGAIVDV 125
Cdd:PRK07960 35 TGLVLEATGLQLPLGATcvIERQNGSETHEVEsEVVGFN-GQRLFLMPLE--EVEGILPGA-RVYARNISGEGLQSGKQL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 126 PVGDGLLGRVVDALGNPIDGKGPIANARRsrvevkAPGIIP------RLSVREPMVTGVKAVDSLVPIGRGQRELIIGDR 199
Cdd:PRK07960 111 PLGPALLGRVLDGSGKPLDGLPAPDTGET------GALITPpfnplqRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 200 QTGKTAIaidtIINQKRFNDAGddkkklfCIYVA-VGQKRSTVAQIVKRLTDAGAMDYTIVVSATAsDAAPLQFL--APY 276
Cdd:PRK07960 185 GVGKSVL----LGMMARYTQAD-------VIVVGlIGERGREVKDFIENILGAEGRARSVVIAAPA-DVSPLLRMqgAAY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 277 SgCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNNSLGGGSLTALPVIE 356
Cdd:PRK07960 253 A-TRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG--NGISGGGSITAFYTVL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 357 TQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYRE------VAA 430
Cdd:PRK07960 330 TEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFQRnrdlvsVGA 409
|
410 420 430
....*....|....*....|....*....|....*....
gi 71988063 431 FAQfGSDldastqQLLNRGVRLTELLKqgQYVPMGIEEQ 469
Cdd:PRK07960 410 YAK-GSD------PMLDKAIALWPQLE--AFLQQGIFER 439
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
125-458 |
1.01e-29 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 121.55 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 125 VPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGKT 204
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 205 AIaIDTIinqkrfndAGDDKKKLFCIYVaVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAMGEH 284
Cdd:PRK05922 172 SL-LSTI--------AKGSKSTINVIAL-IGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 285 FRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNNSlgGGSLTALPVIETQAGDVSA 364
Cdd:PRK05922 242 FRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG--NND--KGSITALYAILHYPNHPDI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 365 YIPTnVISITDGQIFL---ETELFykgvRPAINVGLSVSRvgSAAQTKAMKQVAGSMKLE--LAQYREVAAFAQFGSDLD 439
Cdd:PRK05922 318 FTDY-LKSLLDGHFFLtpqGKALA----SPPIDILTSLSR--SARQLALPHHYAAAEELRslLKAYHEALDIIQLGAYVP 390
|
330
....*....|....*....
gi 71988063 440 ASTQQlLNRGVRLTELLKQ 458
Cdd:PRK05922 391 GQDAH-LDRAVKLLPSIKQ 408
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
125-459 |
2.52e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 117.39 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 125 VPVGDGLLGRVVDALGNPIDGKGPIANARRSRVeVKA--PGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTG 202
Cdd:PRK08927 92 VRPSRAWLGRVVNALGEPIDGKGPLPQGPVPYP-LRAppPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 203 KTaiaidTIINQKRFNDAGDdkkklfciyVAV----GQKRSTVAQIVKR-LTDAGaMDYTIVVSATASDAAPLQFLAPYS 277
Cdd:PRK08927 171 KS-----VLLSMLARNADAD---------VSVigliGERGREVQEFLQDdLGPEG-LARSVVVVATSDEPALMRRQAAYL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 278 GCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmnNSLGGGSLTALPVIET 357
Cdd:PRK08927 236 TLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGP--GPIGEGTITGLFTVLV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 358 QAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSd 437
Cdd:PRK08927 314 DGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGA- 392
|
330 340
....*....|....*....|....*.
gi 71988063 438 LDASTQQLLNRGVR----LTELLKQG 459
Cdd:PRK08927 393 YRAGSDPEVDEAIRlnpaLEAFLRQG 418
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
113-460 |
2.76e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 114.30 E-value: 2.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 113 GDIVKRTGAIVDVPVGDGLLGRVVDALGNPIDgkGPIANARRSRVEVKAPGI--IPRLSVREPMVTGVKAVDSLVPIGRG 190
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLN--EEAENIPLQKIKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 191 QRELIIGDRQTGKTaiaidTIINQKRFNDAGDdkkklFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPL 270
Cdd:PRK06793 157 QKIGIFAGSGVGKS-----TLLGMIAKNAKAD-----INVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 271 QFLAPYSGCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPgreaYPGDVFYLHS---RLLERAAKMNNslggG 347
Cdd:PRK06793 227 QLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK----G 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 348 SLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYRE 427
Cdd:PRK06793 299 SITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKE 378
|
330 340 350
....*....|....*....|....*....|....*..
gi 71988063 428 VAAFAQFGS----DLDASTQQLLNRGVRLTELLKQGQ 460
Cdd:PRK06793 379 NELYFKLGTiqenAENAYIFECKNKVEGINTFLKQGR 415
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
107-479 |
1.73e-26 |
|
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: 112.12 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 107 DKVIReGDIVKRTGAIVDVPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVP 186
Cdd:TIGR01039 61 DGLVR-GLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 187 IGRGQRELIIGDRQTGKTAIAIDTIINQKRFNDAgddkkklFCIYVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASD 266
Cdd:TIGR01039 140 YAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGG-------YSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 267 AAPLQFLAPYSGCAMGEHFRD-NGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmnnSLG 345
Cdd:TIGR01039 213 PPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERIT----STK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 346 GGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQT-KAMKQVAGSMKLELAQ 424
Cdd:TIGR01039 289 TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVgEEHYDVARGVQQILQR 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 71988063 425 YREVA-AFAQFGSD-LDASTQQLLNRGVRLTELLKQgqyvPMGIEEQvgviYAGVKG 479
Cdd:TIGR01039 369 YKELQdIIAILGMDeLSEEDKLTVERARRIQRFLSQ----PFFVAEV----FTGQPG 417
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
69-401 |
2.52e-25 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 108.76 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 69 VYGLKNIQAEEMVEF--DSGIKGMAMNLDV--DNVGVVVFGNDKVIREGDI-VKRTGAIVDVPVGDGLLGRVVDALGNPI 143
Cdd:PRK04196 17 VEGVEGVAYGEIVEIelPNGEKRRGQVLEVseDKAVVQVFEGTTGLDLKDTkVRFTGEPLKLPVSEDMLGRIFDGLGRPI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 144 DGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQReLII--GdrqTGKTA--IAIDtIINQKRFnd 219
Cdd:PRK04196 97 DGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQK-LPIfsG---SGLPHneLAAQ-IARQAKV-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 220 AGDDKKklFCI-YVAVGQKRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAMGEHFR-DNGKHALIIFD 297
Cdd:PRK04196 170 LGEEEN--FAVvFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMHVLVILT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 298 DLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMNNSlgGGSLTALPVIETQAGDVSAYIPTNVISIT 374
Cdd:PRK04196 248 DMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHPIPDLTGYIT 322
|
330 340
....*....|....*....|....*..
gi 71988063 375 DGQIFLETELFYKGVRPAINVGLSVSR 401
Cdd:PRK04196 323 EGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
119-411 |
1.36e-23 |
|
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: 103.65 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 119 TGAIVDVPVGDGLLGRVVDALGNPIDgKGPIANARrSRVEVKAPGIIP--RLSVREPMVTGVKAVDSLVPIGRGQRELII 196
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPID-KGPPVLAE-DYLDINGQPINPyaRIYPEEMIQTGISAIDVMNSIARGQKIPIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 197 GDRQTGKTAIAIDTI----INQKRFNDAGDDKKKLFCI-YVAVGQKRSTvAQIVKR-LTDAGAMDYTIVVSATASDAAPL 270
Cdd:TIGR01040 148 SAAGLPHNEIAAQICrqagLVKLPTKDVHDGHEDNFAIvFAAMGVNMET-ARFFKQdFEENGSMERVCLFLNLANDPTIE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 271 QFLAPYSGCAMGEHFR-DNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNNSlgGGSL 349
Cdd:TIGR01040 227 RIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR--NGSI 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71988063 350 TALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRVGSAAQTKAM 411
Cdd:TIGR01040 305 TQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
93-380 |
1.54e-21 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 97.03 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 93 NLDVDNVGVVVFGNDKVIREGDIVKRTGAIVDVPVGDGLLGRVVDALGNPIDGkGPIANARRsrVEVKAPGIIP--RLSV 170
Cdd:PRK02118 44 RLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GPELEGEP--IEIGGPSVNPvkRIVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 171 REPMVTGVKAVD---SLVpigRGQReliigdrqtgktaIAIdtiinqkrFNDAGDDKKKLFC-----------IYVAVGQ 236
Cdd:PRK02118 121 REMIRTGIPMIDvfnTLV---ESQK-------------IPI--------FSVSGEPYNALLArialqaeadiiILGGMGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 237 KRSTVAQIVKRLTDAGAMDYTIVVSATASDAAPLQFLAPYSGCAMGEHFR-DNGKHALIIFDDLSKQAVAYRQMSLLLRR 315
Cdd:PRK02118 177 TFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQ 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71988063 316 PPGREAYPGDvfyLHSRLLERAAKMNNSLGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFL 380
Cdd:PRK02118 257 IPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
411-478 |
7.11e-21 |
|
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: 86.34 E-value: 7.11e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 411 MKQVAGSMKLELAQYREVAAFAQFGSD--LDASTQQLLNRGVRLTELLKQGQYVPMGIEEQVGVIYAGVK 478
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
125-401 |
6.59e-19 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 87.24 E-value: 6.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 125 VPVGDGLLGRVVDALGNPID----------GKGpiANARRSRVEVKAPgIIPRLSVREPMVTGVKAVDSLVPIGRGQREL 194
Cdd:cd01134 4 VELGPGLLGSIFDGIQRPLEviaetgsifiPRG--VNVQRWPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 195 IIGDRQTGKTaiaidtIINQK--RFNDAGddkkklFCIYVAVGQKRSTVAQIVKRL-------TDAGAMDYTIVVSATAS 265
Cdd:cd01134 81 IPGPFGCGKT------VISQSlsKWSNSD------VVIYVGCGERGNEMAEVLEEFpelkdpiTGESLMERTVLIANTSN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 266 DAAPLQFLAPYSGCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAK--- 339
Cdd:cd01134 149 MPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYERAGRvrc 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71988063 340 MNNSLGGGSLTALPVIETQAGDVSAYIPTNVISITdgQIF--LETELFYKGVRPAINVGLSVSR 401
Cdd:cd01134 226 LGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
125-402 |
1.77e-17 |
|
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: 82.65 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 125 VPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGKT 204
Cdd:cd01133 2 VPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 205 AIAIDTIINQKRFNDAgddkkklFCIYVAVGQkRSTVAQ------IVKRLTDAGAMDYTIVVSATASDAAPLQFLAPYSG 278
Cdd:cd01133 82 VLIMELINNIAKAHGG-------YSVFAGVGE-RTREGNdlyhemKESGVINLDGLSKVALVYGQMNEPPGARARVALTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 279 CAMGEHFRD-NGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmnnSLGGGSLTALPVIET 357
Cdd:cd01133 154 LTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERIT----STKKGSITSVQAVYV 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 71988063 358 QAGDVSAYIPTNVISITDGQIFLETELFYKGVRPAINVGLSVSRV 402
Cdd:cd01133 230 PADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
91-190 |
1.33e-16 |
|
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: 82.44 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 91 AMNLDVDNVGVVVFGNDKVIREGDIVKRTGAIVDVPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGIIPRLSV 170
Cdd:COG0055 47 AQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTK 126
|
90 100
....*....|....*....|
gi 71988063 171 REPMVTGVKAVDSLVPIGRG 190
Cdd:COG0055 127 TEILETGIKVIDLLAPYAKG 146
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
54-120 |
1.21e-15 |
|
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: 71.42 E-value: 1.21e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71988063 54 EETGKVLSIGDGIARVYGLKNIQAEEMVEFDSGIKGMAMNLDVDNVGVVVFGNDKVIREGDIVKRTG 120
Cdd:pfam02874 3 QVIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
24-351 |
3.22e-12 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 69.04 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 24 TARGMAGASGSEVSKILEERILG-----------------TeTGINL----EETGKVLS----------IGDGIARvyGL 72
Cdd:PRK04192 16 VAEGMGGARMYEVVRVGEEGLIGeiiriegdkatiqvyeeT-SGIKPgepvEFTGEPLSvelgpgllgsIFDGIQR--PL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 73 KNIqAEEMVEF-DSGIKGMAMNLDV--DNVGVVVFGnDKVIReGDI---VKRTGAIVD---VPVGDGllGRVVDalgnpI 143
Cdd:PRK04192 93 DEL-AEKSGDFlERGVYVPALDREKkwEFTPTVKVG-DKVEA-GDIlgtVQETPSIEHkimVPPGVS--GTVKE-----I 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 144 DGKG------PIA---NARRSRVEV----KAPGIIPR-----LSVREPMVTGVKAVDSLVPIGRGQRELIIGDRQTGKT- 204
Cdd:PRK04192 163 VSEGdytvddTIAvleDEDGEGVELtmmqKWPVRRPRpykekLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTv 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 205 ---AIAidtiinqkRFNDAgdDkkklFCIYVAVGQKRSTVAQIVK---RLTD--AGA--MDYTIVVSAT-----ASDAAP 269
Cdd:PRK04192 243 tqhQLA--------KWADA--D----IVIYVGCGERGNEMTEVLEefpELIDpkTGRplMERTVLIANTsnmpvAAREAS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 270 LqflapYSGCAMGEHFRDNGKHALIIFDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMNNsLGG 346
Cdd:PRK04192 309 I-----YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASRLaefYERAGRVKT-LGG 379
|
....*..
gi 71988063 347 --GSLTA 351
Cdd:PRK04192 380 eeGSVTI 386
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
230-394 |
1.56e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 60.81 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 230 IYVAVGQKRSTVAQIVK---RLTDAGA----MDYTIVVSATASDAAPLQFLAPYSGCAMGEHFRDNGKHALIIFDDLSKQ 302
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEefpKLKDPKTgkplMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 303 AVAYRQMSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKMNNSLGGGSLTALPVIETQAGDVSAYIPTNVISITDG 376
Cdd:PRK14698 766 AEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKV 842
|
170
....*....|....*...
gi 71988063 377 QIFLETELFYKGVRPAIN 394
Cdd:PRK14698 843 FWALDADLARRRHFPAIN 860
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
105-213 |
1.60e-09 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 60.05 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 105 GNDKV----------IREGDIVKRTGAIVDVPVGDGLLGRVVDALGNPIDGKGPIANARRSRVEVKAPGII---PRLSVR 171
Cdd:CHL00060 66 GNNRVravamsatdgLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTKLSIF 145
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 71988063 172 EpmvTGVKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTIIN 213
Cdd:CHL00060 146 E---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINN 184
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
110-206 |
2.93e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 40.07 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988063 110 IREGDIVKrtgAIVDVPVGDGLLGRVVDalgnpIDGKGPIANARRSRVEVKAPgIIPRLSVRepMVTG-----VKAVDSL 184
Cdd:PRK12608 59 LRTGDVVE---GVARPRERYRVLVRVDS-----VNGTDPEKLARRPHFDDLTP-LHPRERLR--LETGsddlsMRVVDLV 127
|
90 100
....*....|....*....|..
gi 71988063 185 VPIGRGQRELIIGDRQTGKTAI 206
Cdd:PRK12608 128 APIGKGQRGLIVAPPRAGKTVL 149
|
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