|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-503 |
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: 1010.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 1 MRVNPDELTKVIEERIKSYESG-EIKEIGWVMQVSDGIVRAYGLKDVMTNELVEIETSegekIYGIAMNLEEDNVGIITL 79
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEvEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGG----VYGMALNLEEDNVGVVLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 80 GDYKGIKEGDKLVRTNRIIEVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDAL 159
Cdd:COG0056 77 GDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 160 IPIGRGQRELIIGDRQTGKTAIATDTIINQKGKNVFCIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQY 239
Cdd:COG0056 157 IPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 240 IAPYAGAAIGEYFMFNGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRLNENYGNGSLTAL 319
Cdd:COG0056 237 IAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 320 PIIETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQYRELESFT 399
Cdd:COG0056 317 PIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 400 QFAADLDEATKKQLTKGEKLTELMKQPQYSPMEMEEQVAVIYAANEGYLDQIPTDRISDFERQFLAYLKENYRDTLNKIR 479
Cdd:COG0056 397 QFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIR 476
|
490 500
....*....|....*....|....
gi 1334587689 480 ESKDITDEIKKELNEAISKFLNVF 503
Cdd:COG0056 477 ETGKLDDEIEEKLKAAIEEFKKTF 500
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-503 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 983.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 1 MRVNPDELTKVIEERIKSYESG-EIKEIGWVMQVSDGIVRAYGLKDVMTNELVEIETSegekIYGIAMNLEEDNVGIITL 79
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAEaEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGG----VYGIALNLEEDNVGAVIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 80 GDYKGIKEGDKLVRTNRIIEVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDAL 159
Cdd:PRK09281 77 GDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 160 IPIGRGQRELIIGDRQTGKTAIATDTIINQKGKNVFCIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQY 239
Cdd:PRK09281 157 IPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 240 IAPYAGAAIGEYFMFNGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRLNENYGNGSLTAL 319
Cdd:PRK09281 237 LAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 320 PIIETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQYRELESFT 399
Cdd:PRK09281 317 PIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 400 QFAADLDEATKKQLTKGEKLTELMKQPQYSPMEMEEQVAVIYAANEGYLDQIPTDRISDFERQFLAYLKENYRDTLNKIR 479
Cdd:PRK09281 397 QFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIR 476
|
490 500
....*....|....*....|....
gi 1334587689 480 ESKDITDEIKKELNEAISKFLNVF 503
Cdd:PRK09281 477 ETKDLSDEIEAKLKAAIEEFKKTF 500
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
3-503 |
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: 815.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 3 VNPDELTKVIEERIKSYE-SGEIKEIGWVMQVSDGIVRAYGLKDVMTNELVEIETSegekIYGIAMNLEEDNVGIITLGD 81
Cdd:TIGR00962 2 LKLEEISELIKQEIKNFNvDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGG----VQGIALNLEEDSVGAVIMGD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 82 YKGIKEGDKLVRTNRIIEVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIP 161
Cdd:TIGR00962 78 YSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 162 IGRGQRELIIGDRQTGKTAIATDTIINQKGKNVFCIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQYIA 241
Cdd:TIGR00962 158 IGRGQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 242 PYAGAAIGEYFMFNGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRLNENYGNGSLTALPI 321
Cdd:TIGR00962 238 PYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 322 IETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQYRELESFTQF 401
Cdd:TIGR00962 318 IETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 402 AADLDEATKKQLTKGEKLTELMKQPQYSPMEMEEQVAVIYAANEGYLDQIPTDRISDFERQFLAYLKENYRDTLNKIRES 481
Cdd:TIGR00962 398 ASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTT 477
|
490 500
....*....|....*....|..
gi 1334587689 482 KDITDEIKKELNEAISKFLNVF 503
Cdd:TIGR00962 478 KKLTEELEAKLKEALKNFKKTF 499
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-503 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 789.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 1 MRVNPDELTKVIEERIKSYESG-EIKEIGWVMQVSDGIVRAYGLKDVMTNELVEIEtsegEKIYGIAMNLEEDNVGIITL 79
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQpDAREIGRVESVGDGIAFVSGLPDAALDELLRFE----GGSRGFAFNLEEELVGAVLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 80 GDYKGIKEGDKLVRTNRIIEVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDAL 159
Cdd:PRK13343 77 DDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 160 IPIGRGQRELIIGDRQTGKTAIATDTIINQKGKNVFCIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQY 239
Cdd:PRK13343 157 IPIGRGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 240 IAPYAGAAIGEYFMFNGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRLNENYGNGSLTAL 319
Cdd:PRK13343 237 LAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 320 PIIETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQYRELESFT 399
Cdd:PRK13343 317 PIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 400 QFAADLDEATKKQLTKGEKLTELMKQPQYSPMEMEEQVAVIYAANEGYLDQIPTDRISDFERQFLAYLKENYRDTLNKIR 479
Cdd:PRK13343 397 RFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALE 476
|
490 500
....*....|....*....|....
gi 1334587689 480 ESKDITDEIKKELNEAISKFLNVF 503
Cdd:PRK13343 477 SPRELDEAWLAALEEILREAGERF 500
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
27-503 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 751.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 27 IGWVMQVSDGIVRAYGLKDVMTNELVEIEtsegEKIYGIAMNLEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPVGENM 106
Cdd:CHL00059 7 TGTVLQVGDGIARIYGLDEVMAGELVEFE----DGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 107 LGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGKTAIATDTI 186
Cdd:CHL00059 83 LGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 187 INQKGKNVFCIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQYIAPYAGAAIGEYFMFNGKDALVIYDDL 266
Cdd:CHL00059 163 LNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 267 TKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRLNENYGNGSLTALPIIETQANDISAYIPTNVISITDGQIY 346
Cdd:CHL00059 243 SKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 347 LETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQYRELESFTQFAADLDEATKKQLTKGEKLTELMKQP 426
Cdd:CHL00059 323 LSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQS 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1334587689 427 QYSPMEMEEQVAVIYAANEGYLDQIPTDRISDFERQFLAYLKENYRDTLNKIRESKDITDEIKKELNEAISKFLNVF 503
Cdd:CHL00059 403 QSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQLELF 479
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
6-487 |
0e+00 |
|
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic species, including Methanosarcina barkeri, have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 alpha subunit of this apparent second ATP synthase.
Pssm-ID: 132367 [Multi-domain] Cd Length: 497 Bit Score: 619.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 6 DELTKVIEERIKSYESG-EIKEIGWVMQVSDGIVRAYGLKDVMTNELVEIETSegekIYGIAMNLEEDNVGIITLGDYKG 84
Cdd:TIGR03324 6 DKAFQQLDQARESFQPQlTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGG----LLGIAFNVDEDEVGVVLLGEYSH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 85 IKEGDKLVRTNRIIEVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGR 164
Cdd:TIGR03324 82 LQAGDEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 165 GQRELIIGDRQTGKTAIATDTIINQKGKNVFCIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQYIAPYA 244
Cdd:TIGR03324 162 GQRELILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 245 GAAIGEYFMFNGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRLNENYGNGSLTALPIIET 324
Cdd:TIGR03324 242 ATSIGEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIET 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 325 QANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQYRELESFTQFAAD 404
Cdd:TIGR03324 322 EAQNISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGAR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 405 LDEATKKQLTKGEKLTELMKQPQYSPMEMEEQVAVIYAANEGYLDQIPTDRISDFERQFLAYLKENYRDTLNKIRESKDI 484
Cdd:TIGR03324 402 LDENTRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKL 481
|
...
gi 1334587689 485 TDE 487
Cdd:TIGR03324 482 SDE 484
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
97-370 |
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: 561.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 97 IIEVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQT 176
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 177 GKTAIATDTIINQKGKNVFCIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQYIAPYAGAAIGEYFMFNG 256
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 257 KDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRLNENYGNGSLTALPIIETQANDISAYIPTN 336
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 1334587689 337 VISITDGQIYLETGLFNAGVRPAVNIGLSVSRVG 370
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
27-460 |
6.10e-126 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 379.00 E-value: 6.10e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 27 IGWVMQVSDGI---VRAYGLKDVMTNELVEIETSEGEKIYGIAMNLEEDN-VGIITLGDYKGIKEGDKLVRTNRIIEVPV 102
Cdd:PTZ00185 40 IGYVHSIDGTIatlIPAPGNPGVAYNTIIMIQVSPTTFAAGLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 103 GENMLGRVVNPLGMP------------LDGKGEINTndfypIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELI 170
Cdd:PTZ00185 120 GAGVLGKVVNPLGHEvpvglltrsralLESEQTLGK-----VDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 171 IGDRQTGKTAIATDTIINQKGKN--------VFCIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQYIAP 242
Cdd:PTZ00185 195 VGDRQTGKTSIAVSTIINQVRINqqilsknaVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 243 YAGAAIGEYFMFNGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRLNENYGNGSLTALPII 322
Cdd:PTZ00185 275 YSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 323 ETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQYRELesftqfA 402
Cdd:PTZ00185 355 ETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRKL------A 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1334587689 403 ADLDEATKKQ---LTKGEKLTELMKQPQysPMEMEEQVAVIYAANEGYLDQIPTDRISDFE 460
Cdd:PTZ00185 429 ADSVGGSQVQtvpMIRGARFVALFNQKN--PSFFMNALVSLYACLNGYLDDVKVNYAKLYE 487
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
152-367 |
5.47e-115 |
|
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: 337.79 E-value: 5.47e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 152 GLKVLDALIPIGRGQRELIIGDRQTGKTAIAtDTIINQKGKNVfCIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADA 231
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 232 SDPASLQYIAPYAGAAIGEYFMFNGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRLNEny 311
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKG-- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1334587689 312 GNGSLTALPIIETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVS 367
Cdd:pfam00006 157 KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
85-501 |
3.78e-109 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 333.86 E-value: 3.78e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 85 IKEGDKLVRTNRIIEVPVGENMLGRVVNPLGMPLDGKGEINTN-DFYPIERK----AMGVVTRKPVDTPLQTGLKVLDAL 159
Cdd:PRK07165 58 IKINDELIELNNTNKVKTSKEYFGKIIDIDGNIIYPEAQNPLSkKFLPNTSSifnlAHGLMTVKTLNEQLYTGIIAIDLL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 160 IPIGRGQRELIIGDRQTGKTAIATDTIINQKGKNVFCIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASlQY 239
Cdd:PRK07165 138 IPIGKGQRELIIGDRQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSPYE-QY 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 240 IAPYAGAAIGEYFMFNgKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRLNenyGNGSLTAL 319
Cdd:PRK07165 217 LAPYVAMAHAENISYN-DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFK---NRKTITAL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 320 PIIETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQYRELESFT 399
Cdd:PRK07165 293 PILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 400 QFAADLDEATKKQLTKGEKLTELMKQPQYSPMEMEEQVAVIYAANEGYLDQiptdrISDFER--QFLAYLKENYRDT--- 474
Cdd:PRK07165 373 MLDYDLNKETSDLLFKGKMIEKMFNQKGFSLYSYRFVLLISKLISWGLLKD-----VKDEQKalDFIDYLIENDPDAkki 447
|
410 420
....*....|....*....|....*...
gi 1334587689 475 LNKIRESKDITDEI-KKELNEAISKFLN 501
Cdd:PRK07165 448 FNKIKNNEDVDDELmKNYFAFLLNQYSD 475
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
100-369 |
6.12e-105 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 314.39 E-value: 6.12e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 100 VPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGKT 179
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 180 AIATDTIINQKGKNVF-CIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQYIAPYAGAAIGEYFMFNGKD 258
Cdd:cd19476 82 VLAMQLARNQAKAHAGvVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 259 ALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRLNEnyGNGSLTALPIIETQANDISAYIPTNVI 338
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNTF 239
|
250 260 270
....*....|....*....|....*....|.
gi 1334587689 339 SITDGQIYLETGLFNAGVRPAVNIGLSVSRV 369
Cdd:cd19476 240 AILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
378-503 |
6.63e-71 |
|
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: 221.47 E-value: 6.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 378 MKRVAGSLKLDLAQYRELESFTQFAADLDEATKKQLTKGEKLTELMKQPQYSPMEMEEQVAVIYAANEGYLDQIPTDRIS 457
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1334587689 458 DFERQFLAYLKENYRDTLNKIRESKDITDEIKKELNEAISKFLNVF 503
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
374-499 |
1.01e-70 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 221.16 E-value: 1.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 374 QTKAMKRVAGSLKLDLAQYRELESFTQFAADLDEATKKQLTKGEKLTELMKQPQYSPMEMEEQVAVIYAANEGYLDQIPT 453
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1334587689 454 DRISDFERQFLAYLKENYRDTLNKIRESKDITDEIKKELNEAISKF 499
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
24-435 |
1.78e-58 |
|
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: 199.49 E-value: 1.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 24 IKEIGWVMQVSDGIVRAYGLkDVMTNELVEIETSEGEKIYGIAMNLEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPVG 103
Cdd:COG1157 17 VRVSGRVTRVVGLLIEAVGP-DASIGELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 104 ENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQReliIG----------- 172
Cdd:COG1157 96 DGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR---IGifagsgvgkst 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 173 -----DRQTgktaiATDTI----INQKGKNV--FcIYVSIGqkSSGLARtidnlekygamdyTVVVAADASDPASLQYIA 241
Cdd:COG1157 173 llgmiARNT-----EADVNvialIGERGREVreF-IEDDLG--EEGLAR-------------SVVVVATSDEPPLMRLRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 242 PYAGAAIGEYFMFNGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASrlneNYGNGSLTAL-- 319
Cdd:COG1157 232 AYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAG----NGGKGSITAFyt 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 320 ----------PIIETqandisayiptnVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDL 389
Cdd:COG1157 308 vlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLL 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1334587689 390 AQYRELESFTQFAA-------DLDEATKKQltkgEKLTELMKQPQYSPMEMEE 435
Cdd:COG1157 376 ARYEENEDLIRIGAyqpgsdpELDEAIALI----PAIEAFLRQGMDERVSFEE 424
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
28-425 |
1.76e-52 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 183.73 E-value: 1.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 28 GWVMQVSDGIVRAYGLKdVMTNELVEIETSEGEK-IYGIAMNLEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPVGENM 106
Cdd:PRK08472 20 GSITKISPTIIEADGLN-PSVGDIVKIESSDNGKeCLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 107 LGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGKTAIATDTI 186
Cdd:PRK08472 99 LGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 187 INQKGKnvfcIYVS--IGQKSSGLARTID-NLEkyGAMDYTVVVAADASDPASLQYIAPYAGAAIGEYFMFNGKDALVIY 263
Cdd:PRK08472 179 KGCLAP----IKVValIGERGREIPEFIEkNLG--GDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 264 DDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRlneNYGNGSLTALPIIETQANDISAYIPTNVISITDG 343
Cdd:PRK08472 253 DSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 344 QIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQYRELESFTQFAA-------DLDEAtkkqLTKG 416
Cdd:PRK08472 330 HIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAyqkgndkELDEA----ISKK 405
|
....*....
gi 1334587689 417 EKLTELMKQ 425
Cdd:PRK08472 406 EFMEQFLKQ 414
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
99-369 |
2.48e-52 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 178.14 E-value: 2.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 99 EVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGK 178
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 179 TaiatdTIINQKGKNVFC-IYVS--IGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQYIAPYAGAAIGEYFMFN 255
Cdd:cd01136 81 S-----TLLGMIARNTDAdVNVIalIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 256 GKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASrlneNYGNGSLTALPIIETQANDISAYIPT 335
Cdd:cd01136 156 GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAG----NGEKGSITAFYTVLVEGDDFNDPIAD 231
|
250 260 270
....*....|....*....|....*....|....
gi 1334587689 336 NVISITDGQIYLETGLFNAGVRPAVNIGLSVSRV 369
Cdd:cd01136 232 EVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
6-443 |
2.55e-50 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 178.02 E-value: 2.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 6 DELTKVIEERIKSYESGEIKeiGWVMQVSDGIVRAYgLKDVMTNELVEIETSEGE-KIYGIAMNLEEDNVGIITLGDYKG 84
Cdd:PRK06936 5 DYIPHHLRHAIVGSRLIQIR--GRVTQVTGTILKAV-VPGVRIGELCYLRNPDNSlSLQAEVIGFAQHQALLTPLGEMYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 85 IKEGDKLVRTNRIIEVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGR 164
Cdd:PRK06936 82 ISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 165 GQRELIIGDRQTGKTAIATDTIinqKGKNV-FCIYVSIGQKSSGLARTID-NLEKYGaMDYTVVVAADASDPASLQYIAP 242
Cdd:PRK06936 162 GQRMGIFAAAGGGKSTLLASLI---RSAEVdVTVLALIGERGREVREFIEsDLGEEG-LRKAVLVVATSDRPSMERAKAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 243 YAGAAIGEYFMFNGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASrlneNYGNGSLTALPII 322
Cdd:PRK06936 238 FVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG----QSDKGSITALYTV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 323 ETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQYRELESFTQ-- 400
Cdd:PRK06936 314 LVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQig 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1334587689 401 -FAADLDEATKKQLTKGEKLTELMKQPQYSPMEMEEQVAVIYAA 443
Cdd:PRK06936 394 eYQKGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETL 437
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
24-435 |
1.03e-45 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 165.77 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 24 IKEIGWVMQVSDGIVRAYGLKDVMTNELVEIETSEGEKIYGIAMNLEEDNVGIITLGDYKGIKEGDKLVR-TNRIIEVPV 102
Cdd:PRK04196 1 LKEYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRfTGEPLKLPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 103 GENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQR------------ELi 170
Cdd:PRK04196 81 SEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnEL- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 171 igdrqtgKTAIATDTIINQKGKNVFCIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQYIAPYAGAAIGE 250
Cdd:PRK04196 160 -------AAQIARQAKVLGEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 251 YFMFN-GKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGdifYLHSRL---LERASRLNENygNGSLTALPIIETQA 326
Cdd:PRK04196 233 YLAFEkGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 327 NDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAM-----KRVAGSLKLDLAQYRELESFTQF 401
Cdd:PRK04196 308 DDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKtredhKDVANQLYAAYARGKDLRELAAI 387
|
410 420 430
....*....|....*....|....*....|....*..
gi 1334587689 402 --AADLDEATKKQLTKGEKL-TELMKQPQYSPMEMEE 435
Cdd:PRK04196 388 vgEEALSERDRKYLKFADAFeREFVNQGFDENRSIEE 424
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
28-432 |
1.74e-45 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 164.94 E-value: 1.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 28 GWVMQVSDGIVRAYGLkDVMTNELVEIETSEGEKI-YGIAMNLEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPVGENM 106
Cdd:PRK09099 26 GKVVEVIGTLLRVSGL-DVTLGELCELRQRDGTLLqRAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGPAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 107 LGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGKTaiatdTI 186
Cdd:PRK09099 105 LGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKS-----TL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 187 INQKGKNVFC---IYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAAdASDPASLQYI-APYAGAAIGEYFMFNGKDALVI 262
Cdd:PRK09099 180 MGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCA-TSDRSSIERAkAAYVATAIAEYFRDRGLRVLLM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 263 YDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRlnenYGNGSLTALPIIETQANDISAYIPTNVISITD 342
Cdd:PRK09099 259 MDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM----GETGSITALYTVLAEDESGSDPIAEEVRGILD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 343 GQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQYRELESFTQ---FAADLDEATKKQLTKGEKL 419
Cdd:PRK09099 335 GHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQvgeYRAGSDPVADEAIAKIDAI 414
|
410
....*....|....*
gi 1334587689 420 TELMKQP--QYSPME 432
Cdd:PRK09099 415 RDFLSQRtdEYSDPD 429
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
94-440 |
1.06e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 157.19 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 94 TNRIIEVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGD 173
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 174 RQTGKTA----IATDT--------IINQKGKNV--FcIYVSIGQKssGLARTIdnlekygamdytvVVAADASDPASLQY 239
Cdd:PRK07721 167 SGVGKSTlmgmIARNTsadlnviaLIGERGREVreF-IERDLGPE--GLKRSI-------------VVVATSDQPALMRI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 240 IAPYAGAAIGEYFMFNGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRlNEnygNGSLTAL 319
Cdd:PRK07721 231 KGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGT-NA---SGSITAF 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 320 PIIETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQYRELESFT 399
Cdd:PRK07721 307 YTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLI 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1334587689 400 QFAA-------DLDEATKKQltkgEKLTELMKQPQYSPMEMEEQVAVI 440
Cdd:PRK07721 387 NIGAykrgssrEIDEAIQFY----PQIISFLKQGTDEKATFEESIQAL 430
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
28-411 |
1.47e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 156.90 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 28 GWVMQVSDGIVRAyGLKDVMTNELVEIETSegeKIYGIAMNLEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPVGENML 107
Cdd:PRK06820 31 GPIVEIGPTLLRA-SLPGVAQGELCRIEPQ---GMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 108 GRVVNPLGMPLDGkGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGKTAIATdTII 187
Cdd:PRK06820 107 GRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLG-MLC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 188 NQKGKNVFCIYVsIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQYIAPYAGAAIGEYFMFNGKDALVIYDDLT 267
Cdd:PRK06820 185 ADSAADVMVLAL-IGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 268 KHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASrlneNYGNGSLTALPIIETQANDISAYIPTNVISITDGQIYL 347
Cdd:PRK06820 264 RYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG----NSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVL 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1334587689 348 ETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQYRELESFTQF-----AADL--DEATKK 411
Cdd:PRK06820 340 SRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVgeyqaGEDLqaDEALQR 410
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
51-381 |
4.23e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 152.93 E-value: 4.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 51 LVEIETSEGEKIYGIaMNLEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPVGENMLGRVVNPLGMPLDGKGEINTNDFY 130
Cdd:PRK08972 49 LCSIETMAGELEAEV-VGFDGDLLYLMPIEELRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 131 PIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQR-----------ELIIGDRQTGKTA-IATDTIINQKGKNV--Fc 196
Cdd:PRK08972 128 SRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRmglfagsgvgkSVLLGMMTRGTTAdVIVVGLVGERGREVkeF- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 197 IYVSIGQKssGLARTidnlekygamdytVVVAADASDPASLQYIAPYAGAAIGEYFMFNGKDALVIYDDLTKHAAAYREI 276
Cdd:PRK08972 207 IEEILGEE--GRARS-------------VVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 277 SLLLRRPPGREAYPGDIFYLHSRLLERASrlNENYGNGSLTALPIIETQANDISAYIPTNVISITDGQIYLETGLFNAGV 356
Cdd:PRK08972 272 ALAVGEPPATKGYPPSVFAKLPALVERAG--NGGPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGH 349
|
330 340
....*....|....*....|....*....
gi 1334587689 357 RPAVNIGLSVSRVG----GDAQTKAMKRV 381
Cdd:PRK08972 350 YPAIDIEASISRVMpmviSEEHLEAMRRV 378
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
67-405 |
4.11e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 150.65 E-value: 4.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 67 MNLEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVD 146
Cdd:PRK05688 70 MGFSGDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPIS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 147 TPLQTGLKVLDALIPIGRGQRELIIGDRQTGK-------TAIATDTIInqkgknvfcIYVSIGQKSSGLARTIDNLEKYG 219
Cdd:PRK05688 150 EPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKsvllgmmTRFTEADII---------VVGLIGERGREVKEFIEHILGEE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 220 AMDYTVVVAADASDPASLQYIAPYAGAAIGEYFMFNGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSR 299
Cdd:PRK05688 221 GLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 300 LLERASrlNENYGNGSLTALPIIETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVggdaqtkaMK 379
Cdd:PRK05688 301 LVERAG--NAEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV--------MP 370
|
330 340
....*....|....*....|....*..
gi 1334587689 380 RVAGSLKLDLAQY-RELESFTQFAADL 405
Cdd:PRK05688 371 QVVDPEHLRRAQRfKQLWSRYQQSRDL 397
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
97-383 |
4.44e-40 |
|
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: 146.21 E-value: 4.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 97 IIEVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDrqT 176
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSG--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 177 GKTA------IATDTIINQKGKNVFCIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQYIAPYAGAAIGE 250
Cdd:cd01135 79 GLPHnelaaqIARQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 251 YFMF-NGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGdifYLHSRL---LERASRLNENygNGSLTALPIIETQA 326
Cdd:cd01135 159 YLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTMPN 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1334587689 327 NDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVggdaqtkaMKRVAG 383
Cdd:cd01135 234 DDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRL--------MKSGIG 282
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
37-442 |
6.26e-39 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 146.68 E-value: 6.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 37 IVRAYgLKDVMTNELVEIETSEGEK-IYGIA--MNLEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPVGENMLGRVVNP 113
Cdd:PRK08149 17 IIEAE-LPDVAIGEICEIRAGWHSNeVIARAqvVGFQRERTILSLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 114 LGM---PLDGKGEINTNDFY-PIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGKTAIaTDTIINQ 189
Cdd:PRK08149 96 TGKiveRFDAPPTVGPISEErVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSL-MNMLIEH 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 190 KGKNVFCIYVsIGQKSSGLARTIDNLEKYGAMDYTVVVAAdASDPASLQYI-APYAGAAIGEYFMFNGKDALVIYDDLTK 268
Cdd:PRK08149 175 SEADVFVIGL-IGERGREVTEFVESLRASSRREKCVLVYA-TSDFSSVDRCnAALVATTVAEYFRDQGKRVVLFIDSMTR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 269 HAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRLnenyGNGSLTALPIIETQANDISAYIPTNVISITDGQIYLE 348
Cdd:PRK08149 253 YARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT----LAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 349 TGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLK------------LDLAQYRELESftqfaADLDEATKKQltkg 416
Cdd:PRK08149 329 RKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRklltrleelqlfIDLGEYRRGEN-----ADNDRAMDKR---- 399
|
410 420
....*....|....*....|....*.
gi 1334587689 417 EKLTELMKQPQYSPMEMEEQVAVIYA 442
Cdd:PRK08149 400 PALEAFLKQDVAEKSSFSDTLERLNE 425
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
48-438 |
4.41e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 138.87 E-value: 4.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 48 TNELVEIETSEGEKIYGIAMNLEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPVGENMLGRVVNPLGMPLDGKGEINTN 127
Cdd:PRK07196 38 IGQRCRIESVDETFIEAQVVGFDRDITYLMPFKHPGGVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 128 DFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGKTAIATdtIINQKGKNVFCIYVSIGQKSSG 207
Cdd:PRK07196 118 TPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLG--MITRYTQADVVVVGLIGERGRE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 208 LARTIDNLEKYGAMDYTVVVAADASDPASLQYIAPYAGAAIGEYFMFNGKDALVIYDDLTKHAAAYREISLLLRRPPGRE 287
Cdd:PRK07196 196 VKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 288 AYPGDIFYLHSRLLERASrlnENYGNGSLTALPIIETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVS 367
Cdd:PRK07196 276 GYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSIS 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1334587689 368 R----VGGDAQTKAMKRVAGSLKlDLAQYRELESFTQFAADLDEATKKQLTKGEKLTELMKQPQYSPMEMEEQVA 438
Cdd:PRK07196 353 RcmsqVIGSQQAKAASLLKQCYA-DYMAIKPLIPLGGYVAGADPMADQAVHYYPAITQFLRQEVGHPALFSASVE 426
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
28-434 |
1.34e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 137.78 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 28 GWVMQVSDGIVRAYgLKDVMTNELVEIETSEG-EKIYGIamnlEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPVGENM 106
Cdd:PRK07594 23 GRIQDVSATLLNAW-LPGVFMGELCCIKPGEElAEVVGI----NGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 107 LGRVVNPLGMPLDGKG--EINTNDFYPIERKAMgvvTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGKTAIATd 184
Cdd:PRK07594 98 LGRVIDGFGRPLDGRElpDVCWKDYDAMPPPAM---VRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLA- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 185 TIINQKGKNVfCIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQYIAPYAGAAIGEYFMFNGKDALVIYD 264
Cdd:PRK07594 174 MLCNAPDADS-NVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLAD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 265 DLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASrLNENygnGSLTALPIIETQANDISAYIPTNVISITDGQ 344
Cdd:PRK07594 253 SLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-MGEK---GSITAFYTVLVEGDDMNEPLADEVRSLLDGH 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 345 IYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQYRELESFT---QFAADLDEATKKQLTKGEKLTE 421
Cdd:PRK07594 329 IVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIrigEYQRGVDTDTDKAIDTYPDICT 408
|
410
....*....|...
gi 1334587689 422 LMKQPQYSPMEME 434
Cdd:PRK07594 409 FLRQSKDEVCGPE 421
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
28-458 |
1.71e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 128.96 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 28 GWVMQVSDGIVRAYGL-KDVMTNELVEIETSEGEKIyGIAMNLEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPvGENM 106
Cdd:PRK06002 28 GTVSEVTASHYRVRGLsRFVRLGDFVAIRADGGTHL-GEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGPLRIRP-DPSW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 107 LGRVVNPLGMPLDGKGEINTNDF-YPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGKT------ 179
Cdd:PRK06002 106 KGRVINALGEPIDGLGPLAPGTRpMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKStllaml 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 180 --AIATDTII----NQKGKNVfciyvsigqkssglaRtiDNLEKY--GAMDYTVVVAADASDPASLQYIAPYAGAAIGEY 251
Cdd:PRK06002 186 arADAFDTVVialvGERGREV---------------R--EFLEDTlaDNLKKAVAVVATSDESPMMRRLAPLTATAIAEY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 252 FMFNGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRLNEnyGNGSLTALPIIETQANDISA 331
Cdd:PRK06002 249 FRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLVDGDDHND 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 332 YIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQY---RELESFTQFAA----D 404
Cdd:PRK06002 327 PVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFeetRDLRLIGGYRAgsdpD 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1334587689 405 LDEATKkqltkgekltelmkqpqyspmemeeQVAVIYAAnegyLDQIPTDRISD 458
Cdd:PRK06002 407 LDQAVD-------------------------LVPRIYEA----LRQSPGDPPSD 431
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
94-380 |
4.69e-30 |
|
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: 122.52 E-value: 4.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 94 TNRIIEVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGD 173
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 174 -------------RQTGKTAIATDTIINQKGKNVFCIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQYI 240
Cdd:TIGR01040 150 aglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERII 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 241 APYAGAAIGEYFMFN-GKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRLNENygNGSLTAL 319
Cdd:TIGR01040 230 TPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR--NGSITQI 307
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1334587689 320 PIIETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKR 380
Cdd:TIGR01040 308 PILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTR 368
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
65-455 |
1.12e-29 |
|
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: 121.36 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 65 IAMNLEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKP 144
Cdd:TIGR01039 43 VAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQST 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 145 VDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGKTAIATDTIIN-QKGKNVFCIYVSIGQKSSGLARTIDNLEKYGAMDY 223
Cdd:TIGR01039 123 KVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 224 TVVVAADASDPASLQYIAPYAGAAIGEYFM-FNGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLE 302
Cdd:TIGR01039 203 TALVYGQMNEPPGARMRVALTGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 303 RASRLNenygNGSLTALPIIETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVgGDAQTKAMK--R 380
Cdd:TIGR01039 283 RITSTK----TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRL-LDPSVVGEEhyD 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 381 VAGSLKLDLAQYRELESFTQFAA--DLDEATKKQLTKGEKLTELMKQP-----QYSPME-----MEEQVAVIYAANEGYL 448
Cdd:TIGR01039 358 VARGVQQILQRYKELQDIIAILGmdELSEEDKLTVERARRIQRFLSQPffvaeVFTGQPgkyvpLKDTIRGFKEILEGKY 437
|
....*..
gi 1334587689 449 DQIPTDR 455
Cdd:TIGR01039 438 DHLPEQA 444
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
99-435 |
7.53e-29 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 118.73 E-value: 7.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 99 EVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGK 178
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 179 TAI--------ATDTI----INQKGKNVFCIYVSIgQKSSGLARTidnlekygamdytVVVAAdasdPASLQYIAPYAGA 246
Cdd:PRK07960 189 SVLlgmmarytQADVIvvglIGERGREVKDFIENI-LGAEGRARS-------------VVIAA----PADVSPLLRMQGA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 247 A----IGEYFMFNGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASrlNENYGNGSLTALPII 322
Cdd:PRK07960 251 AyatrIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG--NGISGGGSITAFYTV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 323 ETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQY---RELESFT 399
Cdd:PRK07960 329 LTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFqrnRDLVSVG 408
|
330 340 350
....*....|....*....|....*....|....*.
gi 1334587689 400 QFAADLDEATKKQLTKGEKLTELMKQPQYSPMEMEE 435
Cdd:PRK07960 409 AYAKGSDPMLDKAIALWPQLEAFLQQGIFERADWED 444
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
25-410 |
8.17e-29 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 118.47 E-value: 8.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 25 KEIGWVMQVSDGIVRAYGLKDVMtNELVEIETSEGEKIYGIAMNLEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPVGE 104
Cdd:PRK05922 18 RECGLLSRVSGNLLEAQGLSACL-GELCQISLSKSPPILAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 105 NMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGKTAIAtd 184
Cdd:PRK05922 97 HLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLL-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 185 TIINQKGKNVFCIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQYIAPYAGAAIGEYFMFNGKDALVIYD 264
Cdd:PRK05922 175 STIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 265 DLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASrlneNYGNGSLTALPIIETQAN--DI-SAYIPtnviSIT 341
Cdd:PRK05922 255 SLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG----NNDKGSITALYAILHYPNhpDIfTDYLK----SLL 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1334587689 342 DGQIYLeTGLFNAGVRPAVNIGLSVSRvggDAQTKAMKR---VAGSLKLDLAQYRELESFTQFAA-------DLDEATK 410
Cdd:PRK05922 327 DGHFFL-TPQGKALASPPIDILTSLSR---SARQLALPHhyaAAEELRSLLKAYHEALDIIQLGAyvpgqdaHLDRAVK 401
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
28-425 |
1.40e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 117.77 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 28 GWVMQVSDGIVRAYGLKDVMT-NELVEIETSEGEKIYGIAMNLEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPVGENM 106
Cdd:PRK08927 19 GRVVAVRGLLVEVAGPIHALSvGARIVVETRGGRPVPCEVVGFRGDRALLMPFGPLEGVRRGCRAVIANAAAAVRPSRAW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 107 LGRVVNPLGMPLDGKGEINTNDF-YPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGKTAI---- 181
Cdd:PRK08927 99 LGRVVNALGEPIDGKGPLPQGPVpYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLlsml 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 182 ----ATDTI----INQKGKNV--FcIYVSIGQKssGLARTidnlekygamdytVVVAADASDPASLQYIAPYAGAAIGEY 251
Cdd:PRK08927 179 arnaDADVSviglIGERGREVqeF-LQDDLGPE--GLARS-------------VVVVATSDEPALMRRQAAYLTLAIAEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 252 FMFNGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASRLNEnyGNGSLTALPIIETQANDISA 331
Cdd:PRK08927 243 FRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPI--GEGTITGLFTVLVDGDDHNE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 332 YIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVAGSLKLDLAQYRELESFTQFAA-------D 404
Cdd:PRK08927 321 PVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGAyragsdpE 400
|
410 420
....*....|....*....|.
gi 1334587689 405 LDEATKKQltkgEKLTELMKQ 425
Cdd:PRK08927 401 VDEAIRLN----PALEAFLRQ 417
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
26-96 |
3.29e-24 |
|
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: 95.60 E-value: 3.29e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1334587689 26 EIGWVMQVSDGIVRAYGLKDVMTNELVEIETsegeKIYGIAMNLEEDNVGIITLGDYKGIKEGDKLVRTNR 96
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPG----GVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
38-350 |
6.01e-24 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 103.96 E-value: 6.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 38 VRAYGlkdVMTNELVEIETSEGEKiYGIAMNLEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPVGENMLGRVVNPLGMP 117
Cdd:PRK02118 18 VEAEG---VGYGELATVERKDGSS-LAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 118 LDGKGEINTNDFyPIERKAMGVVTRKPVDTPLQTGLKVLDAL--------IPI----GRGQRELIIgdrqtgKTAIATDT 185
Cdd:PRK02118 94 IDGGPELEGEPI-EIGGPSVNPVKRIVPREMIRTGIPMIDVFntlvesqkIPIfsvsGEPYNALLA------RIALQAEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 186 IInqkgknvfCIYVSIGQKSSGLARTIDNLEKYGAMDYTVVVAADASDPASLQYIAPYAGAAIGEYFMFNG-KDALVIYD 264
Cdd:PRK02118 167 DI--------IILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 265 DLTKHAAAYREISLLLRRPPGREAYPGDifyLHSRLLERASRLNENYGNGSLTALPIIETQANDISAYIPTNVISITDGQ 344
Cdd:PRK02118 239 DMTNFADALKEISITMDQIPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQ 315
|
....*.
gi 1334587689 345 IYLETG 350
Cdd:PRK02118 316 FYLRRG 321
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
99-369 |
1.33e-23 |
|
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: 100.37 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 99 EVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGK 178
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 179 TAIATDTIIN----QKGKNVFciyVSIGQkssglaRTIDNLEKYGAMDYTVVVAADASDPASLQY-----------IAPY 243
Cdd:cd01133 81 TVLIMELINNiakaHGGYSVF---AGVGE------RTREGNDLYHEMKESGVINLDGLSKVALVYgqmneppgaraRVAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 244 AGAAIGEYFM-FNGKDALVIYDDLTKHAAAYREISLLLRRPPGREAYPGDIFYLHSRLLERASrlneNYGNGSLTALPII 322
Cdd:cd01133 152 TGLTMAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERIT----STKKGSITSVQAV 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1334587689 323 ETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRV 369
Cdd:cd01133 228 YVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
67-398 |
3.40e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 95.81 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 67 MNLEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTRKPVD 146
Cdd:PRK06793 58 IAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEIT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 147 TPLQTGLKVLDALIPIGRGQRELIIGDRQTGKTAIATDTIINQKGK-NVFCIYVSIGQKSSGLARTidNLEKYGaMDYTV 225
Cdd:PRK06793 138 DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADiNVISLVGERGREVKDFIRK--ELGEEG-MRKSV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 226 VVAADASDPASLQYIAPYAGAAIGEYFMFNGKDALVIYDDLTKHAAAYREISLLLRRPPgreaYPGDIFYLHS---RLLE 302
Cdd:PRK06793 215 VVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 303 RASRLNenygNGSLTALPIIETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIGLSVSRVGGDAQTKAMKRVA 382
Cdd:PRK06793 291 RSGKTQ----KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLA 366
|
330
....*....|....*.
gi 1334587689 383 GSLKLDLAQYRELESF 398
Cdd:PRK06793 367 NEMRKILSIYKENELY 382
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
49-395 |
1.32e-20 |
|
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439825 [Multi-domain] Cd Length: 468 Bit Score: 94.39 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 49 NELVEIETSEGEKIYG-IAMNLEEDNVGIITLGDYKGIKEGDKLVRTNRIIEVPVGENMLGRVVNPLGMPLDGKGEINTN 127
Cdd:COG0055 29 YNALEVENEGGGELVLeVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 128 DFYPIERKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGKTAIATDTIIN----QKGKNVFCiyvSIGQ 203
Cdd:COG0055 109 ERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNiakeHGGVSVFA---GVGE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 204 kssglaRTIDNLEKY------GAMDYTVVVAADASDPASLQYIAPYAGAAIGEYFM-FNGKDALVIYDDLTKHAAAYREI 276
Cdd:COG0055 186 ------RTREGNDLYremkesGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRdEEGQDVLLFIDNIFRFTQAGSEV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 277 SLLLRRPPGREAY-P---GDIfylhSRLLER-ASRlnenyGNGSLTALPIIETQANDISAYIPTNVISITDGQIYLETGL 351
Cdd:COG0055 260 SALLGRMPSAVGYqPtlaTEM----GALQERiTST-----KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKI 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1334587689 352 FNAGVRPAVNIGLSVSR------VGgdaqtKAMKRVAGSLKLDLAQYREL 395
Cdd:COG0055 331 AELGIYPAVDPLDSTSRildpliVG-----EEHYRVAREVQRILQRYKEL 375
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
129-341 |
3.73e-17 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 81.85 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 129 FYPIeRKAMGVVTRKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGKTaiatdtIINQ---KGKNVFC-IYVSIGQK 204
Cdd:cd01134 41 RWPV-RQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKT------VISQslsKWSNSDVvIYVGCGER 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 205 SSGLARTIDNLEKY-------GAMDYTVVVAADASDPASLQYIAPYAGAAIGEYFMFNGKDALVIYDDLTKHAAAYREIS 277
Cdd:cd01134 114 GNEMAEVLEEFPELkdpitgeSLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREIS 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 278 LLLRRPPGREAYPGdifYLHSRL---LERASR---LNENYGNGSLTALPIIETQANDISAYIPTNVISIT 341
Cdd:cd01134 194 GRLEEMPAEEGYPA---YLGARLaefYERAGRvrcLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV 260
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
378-442 |
7.28e-17 |
|
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: 74.79 E-value: 7.28e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1334587689 378 MKRVAGSLKLDLAQYRELESFTQFAAD--LDEATKKQLTKGEKLTELMKQPQYSPMEMEEQVAVIYA 442
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYP 67
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
79-396 |
1.11e-14 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 76.23 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 79 LGDYK----------GIKEGDKLVRTNRIIEVPVGENMLGRVVNPLGMPLDGKGEINTNDFYPIERKAMGVVTrkpVDTP 148
Cdd:CHL00060 65 LGNNRvravamsatdGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQ---LDTK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 149 L---QTGLKVLDALIPIGRGQRELIIGDRQTGKTAIATDTIIN----QKGKNVFC-----------IYVSIgqKSSGLAR 210
Cdd:CHL00060 142 LsifETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakaHGGVSVFGgvgertregndLYMEM--KESGVIN 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 211 TiDNLEK------YGAMDYTvvvaadasdPASLQYIAPYAgAAIGEYFM-FNGKDALVIYDDLTKHAAAYREISLLLRRP 283
Cdd:CHL00060 220 E-QNIAEskvalvYGQMNEP---------PGARMRVGLTA-LTMAEYFRdVNKQDVLLFIDNIFRFVQAGSEVSALLGRM 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 284 PGREAYPGDIFYLHSRLLERASRLNEnygnGSLTALPIIETQANDISAYIPTNVISITDGQIYLETGLFNAGVRPAVNIG 363
Cdd:CHL00060 289 PSAVGYQPTLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPL 364
|
330 340 350
....*....|....*....|....*....|....*...
gi 1334587689 364 LSVS-----RVGGDAQTKAMKRVAGSLKldlaQYRELE 396
Cdd:CHL00060 365 DSTStmlqpRIVGEEHYETAQRVKQTLQ----RYKELQ 398
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
24-95 |
1.15e-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: 62.95 E-value: 1.15e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1334587689 24 IKEIGWVMQVSDGIVRAYGLKDVMTNELVEietsEGEKIYGIAMNLEEDNVGIITLGDYKGIKEGDKLVRTN 95
Cdd:pfam02874 2 VQVIGPVVDVEFGIGRLPGLLNALEVELVE----FGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
197-361 |
1.73e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 63.50 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 197 IYVSIGQKSSGLARTIDNLEKYG-------AMDYTVVVAADASDPASLQYIAPYAGAAIGEYFMFNGKDALVIYDDLTKH 269
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPKLKdpktgkpLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 270 AAAYREISLLLRRPPGREAYPGdifYLHSRL---LERASR---LNENYGNGSLTALPIIETQANDISAYIPTNVISITDG 343
Cdd:PRK14698 766 AEALREISGRLEEMPGEEGYPA---YLASKLaefYERAGRvvtLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKV 842
|
170
....*....|....*...
gi 1334587689 344 QIYLETGLFNAGVRPAVN 361
Cdd:PRK14698 843 FWALDADLARRRHFPAIN 860
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
86-318 |
2.15e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 59.80 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 86 KEGDKLVRTNRIIEVPVGENMLGRVVNPLGMP-----LDGKGEINTND-------------------FYPIeRKAMGVVT 141
Cdd:PRK04192 125 KVGDKVEAGDILGTVQETPSIEHKIMVPPGVSgtvkeIVSEGDYTVDDtiavlededgegveltmmqKWPV-RRPRPYKE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 142 RKPVDTPLQTGLKVLDALIPIGRGQRELIIGDRQTGKT----AIA----TDTIInqkgknvfciYVSIGQKSSGLARTID 213
Cdd:PRK04192 204 KLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTvtqhQLAkwadADIVI----------YVGCGERGNEMTEVLE 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 214 ---NLE--KYGA--MDYTVVVAADASDP-----ASLqyiapYAGAAIGEYFMFNGKDALVIYDDLTKHAAAYREISLLLR 281
Cdd:PRK04192 274 efpELIdpKTGRplMERTVLIANTSNMPvaareASI-----YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLE 348
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1334587689 282 RPPGREAYPGdifYLHSRL---LERASRLNENYGN-GSLTA 318
Cdd:PRK04192 349 EMPGEEGYPA---YLASRLaefYERAGRVKTLGGEeGSVTI 386
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
28-96 |
2.81e-07 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 47.69 E-value: 2.81e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1334587689 28 GWVMQVSDGIVRAYGLKDVMTNELVEIETSEGEK---IYGIAMNLEEDNVGIITLGDYKGIKEGDKLVRTNR 96
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIGEVCEIERGDGNNetvLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
400-495 |
5.83e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334587689 400 QFAADLDEATKKQLTKGEKLTELMKQ--PQYsPMEMEEqVAVIYAANEGY---LDQIPTDRISDFERQFLAYLKENYR-- 472
Cdd:COG4913 770 NLEERIDALRARLNRAEEELERAMRAfnREW-PAETAD-LDADLESLPEYlalLDRLEEDGLPEYEERFKELLNENSIef 847
|
90 100
....*....|....*....|....*.
gi 1334587689 473 --DTLNKIRES-KDITDEIkKELNEA 495
Cdd:COG4913 848 vaDLLSKLRRAiREIKERI-DPLNDS 872
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
130-190 |
8.86e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 38.58 E-value: 8.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1334587689 130 YPIERKAMGVVTRKPVDTplqtglKVLDALIPIGRGQRELIIGDRQTGKT----AIATDTIINQK 190
Cdd:PRK09376 140 YPNERLRLETGNPEDLST------RIIDLIAPIGKGQRGLIVAPPKAGKTvllqNIANSITTNHP 198
|
|
| |
