|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
3-438 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 942.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 3 NIRPDEISNIIRQQIESYDQEVQIDNVGTVLQVGDGIARVYGLEQVMAGELLEFEDKTVGIALNLENDNVGVVLMGPGLD 82
Cdd:PRK09281 2 QINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 83 ILEGGSVRSTGKIAQIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGR 162
Cdd:PRK09281 82 IKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 163 GQRELIIGDRQTGKTSVAIDTIINQKSEDVICVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYT 242
Cdd:PRK09281 162 GQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 243 GAALAEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDALGGGSMTALPIIET 322
Cdd:PRK09281 242 GCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIET 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 323 QAGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELEAFSQFASD 402
Cdd:PRK09281 322 QAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSD 401
|
410 420 430
....*....|....*....|....*....|....*.
gi 2493022 403 LDAATQAELARGQRLREMLKQPQNSPIPVEEQVALI 438
Cdd:PRK09281 402 LDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVIL 437
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
4-438 |
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: 936.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 4 IRPDEISNIIRQQIESYDQEVQIDNVGTVLQVGDGIARVYGLEQVMAGELLEFEDKTVGIALNLENDNVGVVLMGPGLDI 83
Cdd:COG0056 3 IRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 84 LEGGSVRSTGKIAQIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRG 163
Cdd:COG0056 83 KEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 164 QRELIIGDRQTGKTSVAIDTIINQKSEDVICVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTG 243
Cdd:COG0056 163 QRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 244 AALAEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDALGGGSMTALPIIETQ 323
Cdd:COG0056 243 CAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 324 AGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELEAFSQFASDL 403
Cdd:COG0056 323 AGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDL 402
|
410 420 430
....*....|....*....|....*....|....*
gi 2493022 404 DAATQAELARGQRLREMLKQPQNSPIPVEEQVALI 438
Cdd:COG0056 403 DEATRAQLERGERLVELLKQPQYSPLSVEEQVAIL 437
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
23-438 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 932.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 23 EVQIDNVGTVLQVGDGIARVYGLEQVMAGELLEFEDKTVGIALNLENDNVGVVLMGPGLDILEGGSVRSTGKIAQIPVGD 102
Cdd:CHL00059 1 EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 103 GFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGDRQTGKTSVAID 182
Cdd:CHL00059 81 AYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 183 TIINQKSEDVICVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTGAALAEYFMYKGKATLIIYD 262
Cdd:CHL00059 161 TILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 263 DLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDALGGGSMTALPIIETQAGDVSAYIPTNVISITDGQ 342
Cdd:CHL00059 241 DLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 343 IFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELEAFSQFASDLDAATQAELARGQRLREMLK 422
Cdd:CHL00059 321 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLK 400
|
410
....*....|....*.
gi 2493022 423 QPQNSPIPVEEQVALI 438
Cdd:CHL00059 401 QSQSAPLTVEEQVATI 416
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
4-438 |
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: 811.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 4 IRPDEISNIIRQQIESYDQEVQIDNVGTVLQVGDGIARVYGLEQVMAGELLEFEDKTVGIALNLENDNVGVVLMGPGLDI 83
Cdd:TIGR00962 2 LKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 84 LEGGSVRSTGKIAQIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRG 163
Cdd:TIGR00962 82 REGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 164 QRELIIGDRQTGKTSVAIDTIINQKSEDVICVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTG 243
Cdd:TIGR00962 162 QRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 244 AALAEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDALGGGSMTALPIIETQ 323
Cdd:TIGR00962 242 CTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIETQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 324 AGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELEAFSQFASDL 403
Cdd:TIGR00962 322 AGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASDL 401
|
410 420 430
....*....|....*....|....*....|....*
gi 2493022 404 DAATQAELARGQRLREMLKQPQNSPIPVEEQVALI 438
Cdd:TIGR00962 402 DEATKKQLERGQRVVELLKQPQYKPLSVEEQVVIL 436
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
7-438 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 725.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 7 DEISNIIRQQIESYDQEVQIDNVGTVLQVGDGIARVYGLEQVMAGELLEFEDKTVGIALNLENDNVGVVLMGPGLDILEG 86
Cdd:PRK13343 6 DEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 87 GSVRSTGKIAQIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQRE 166
Cdd:PRK13343 86 TEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 167 LIIGDRQTGKTSVAIDTIINQKSEDVICVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTGAAL 246
Cdd:PRK13343 166 LIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 247 AEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDALGGGSMTALPIIETQAGD 326
Cdd:PRK13343 246 AEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETLAGE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 327 VSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELEAFSQFASDLDAA 406
Cdd:PRK13343 326 LSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLLDAG 405
|
410 420 430
....*....|....*....|....*....|..
gi 2493022 407 TQAELARGQRLREMLKQPQNSPIPVEEQVALI 438
Cdd:PRK13343 406 TQKQITRGRRLRELLKQPRFSPLSVEEQIALL 437
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
95-368 |
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: 581.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 95 IAQIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGDRQT 174
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 175 GKTSVAIDTIINQKSEDVICVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTGAALAEYFMYKG 254
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 255 KATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDALGGGSMTALPIIETQAGDVSAYIPTN 334
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 2493022 335 VISITDGQIFLSGDLFNAGIRPAINVGISVSRVG 368
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
7-438 |
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: 557.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 7 DEISNIIRQQIESYDQEVQIDNVGTVLQVGDGIARVYGLEQVMAGELLEFEDKTVGIALNLENDNVGVVLMGPGLDILEG 86
Cdd:TIGR03324 6 DKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 87 GSVRSTGKIAQIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQRE 166
Cdd:TIGR03324 86 DEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 167 LIIGDRQTGKTSVAIDTIINQKSEDVICVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTGAAL 246
Cdd:TIGR03324 166 LILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 247 AEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDALGGGSMTALPIIETQAGD 326
Cdd:TIGR03324 246 GEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 327 VSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELEAFSQFASDLDAA 406
Cdd:TIGR03324 326 ISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDEN 405
|
410 420 430
....*....|....*....|....*....|..
gi 2493022 407 TQAELARGQRLREMLKQPQNSPIPVEEQVALI 438
Cdd:TIGR03324 406 TRKTIEHGRRIRACLKQTQSSPLTVPQQIAIL 437
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
62-427 |
1.83e-117 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 355.12 E-value: 1.83e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 62 GIALNLENDN-VGVVLMGPGLDILEGGSVRSTGKIAQIPVGDGFLGRVVDSLARPID------GKGDIDATESR-LVESM 133
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQTLgKVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 134 APGIITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGDRQTGKTSVAIDTIINQ--------KSEDVICVYVAIGQKASS 205
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 206 VASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTGAALAEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGRE 285
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGRE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 286 AYPGDVFYLHSRLLERAAKLSDALGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVS 365
Cdd:PTZ00185 320 AYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVS 399
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2493022 366 RVGSAAQTKAMKQVAGKLKLELAQFAELEAFSQFASDLDAATqaeLARGQRLREMLKQPQNS 427
Cdd:PTZ00185 400 RVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKNPS 458
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
150-365 |
3.33e-112 |
|
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: 328.16 E-value: 3.33e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 150 GITAIDSMIPIGRGQRELIIGDRQTGKTSVAiDTIINQKSEDViCVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNA 229
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 230 DDPATLQYIAPYTGAALAEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDal 309
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKG-- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2493022 310 GGGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVS 365
Cdd:pfam00006 157 KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
134-424 |
6.73e-106 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 323.08 E-value: 6.73e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 134 APGIITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGDRQTGKTSVAIDTIINQKSEDVICVYVAIGQKASSVASIVTTL 213
Cdd:PRK07165 114 AHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 214 EEKGALGYTIVVASNADDPATlQYIAPYTGAALAEYFMYKGKAtLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFY 293
Cdd:PRK07165 194 KEHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAENISYNDDV-LIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFF 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 294 LHSRLLERAAKLsdaLGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQT 373
Cdd:PRK07165 272 AHSKLLERAGKF---KNRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQS 348
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2493022 374 KAMKQVAGKLKLELAQFAELEAFSQFASDLDAATQAELARGQRLREMLKQP 424
Cdd:PRK07165 349 KTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKGKMIEKMFNQK 399
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
97-367 |
4.31e-103 |
|
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: 307.46 E-value: 4.31e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 97 QIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 177 TSVAIDTIINQKSEDV-ICVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTGAALAEYFMYKGK 255
Cdd:cd19476 81 TVLAMQLARNQAKAHAgVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 256 ATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDalGGGSMTALPIIETQAGDVSAYIPTNV 335
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 2493022 336 ISITDGQIFLSGDLFNAGIRPAINVGISVSRV 367
Cdd:cd19476 239 FAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
97-367 |
2.75e-51 |
|
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: 173.90 E-value: 2.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 97 QIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 177 tSVAIDTIINQKSEDVIcVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTGAALAEYFMYKGKA 256
Cdd:cd01136 81 -STLLGMIARNTDADVN-VIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 257 TLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDalggGSMTALPIIETQAGDVSAYIPTNVI 336
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----GSITAFYTVLVEGDDFNDPIADEVR 234
|
250 260 270
....*....|....*....|....*....|.
gi 2493022 337 SITDGQIFLSGDLFNAGIRPAINVGISVSRV 367
Cdd:cd01136 235 SILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
30-433 |
9.86e-51 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 177.31 E-value: 9.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 30 GTVLQVGDGIARVyGLEQVMAGELLEFEDKtvgialNLENDNVGV----VLMGP-----GLDIleGGSVRSTGKIAQIPV 100
Cdd:PRK06820 31 GPIVEIGPTLLRA-SLPGVAQGELCRIEPQ------GMLAEVVSIeqemALLSPfassdGLRC--GQWVTPLGHMHQVQV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 101 GDGFLGRVVDSLARPIDGkGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGDRQTGKtSVA 180
Cdd:PRK06820 102 GADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGK-STL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 181 IDTIINQKSEDVIcVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTGAALAEYFMYKGKATLII 260
Cdd:PRK06820 180 LGMLCADSAADVM-VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 261 YDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlSDAlggGSMTALPIIETQAGDVSAYIPTNVISITD 340
Cdd:PRK06820 259 ADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGN-SDR---GSITAFYTVLVEGDDMNEPVADEVRSLLD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 341 GQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELEAFSQ---FASDLDAATQAELARGQRL 417
Cdd:PRK06820 335 GHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRvgeYQAGEDLQADEALQRYPAI 414
|
410
....*....|....*.
gi 2493022 418 REMLKQPQNSPIPVEE 433
Cdd:PRK06820 415 CAFLQQDHSETAHLET 430
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
7-438 |
2.85e-50 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 176.10 E-value: 2.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 7 DEISNIIRQQIESYDQeVQIDnvGTVLQVGDGIARVYgLEQVMAGELLEFEDKtvGIALNLENDNVGVV----LMGPgLD 82
Cdd:PRK06936 5 DYIPHHLRHAIVGSRL-IQIR--GRVTQVTGTILKAV-VPGVRIGELCYLRNP--DNSLSLQAEVIGFAqhqaLLTP-LG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 83 ILEGGS----VRSTGKIAQIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMI 158
Cdd:PRK06936 78 EMYGISsnteVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 159 PIGRGQRELIIGDRQTGKtSVAIDTIINQKSEDViCVYVAIGQKASSVAS-IVTTLEEKGaLGYTIVVASNADDPATLQY 237
Cdd:PRK06936 158 TCGEGQRMGIFAAAGGGK-STLLASLIRSAEVDV-TVLALIGERGREVREfIESDLGEEG-LRKAVLVVATSDRPSMERA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 238 IAPYTGAALAEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlSDAlggGSMTAL 317
Cdd:PRK06936 235 KAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ-SDK---GSITAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 318 PIIETQAGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELEAFS 397
Cdd:PRK06936 311 YTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2493022 398 Q---FASDLDAATQAELARGQRLREMLKQPQNSPIPVEEQVALI 438
Cdd:PRK06936 391 QigeYQKGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLL 434
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
29-433 |
4.55e-49 |
|
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: 172.52 E-value: 4.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 29 VGTVLQVGDGIARVYGLeQVMAGELLEFEDKT--------VGIalnlENDNVGVVLMGPGLDILEGGSVRSTGKIAQIPV 100
Cdd:COG1157 20 SGRVTRVVGLLIEAVGP-DASIGELCEIETADgrpvlaevVGF----RGDRVLLMPLGDLEGISPGARVVPTGRPLSVPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 101 GDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQReliIGdr---qtGKt 177
Cdd:COG1157 95 GDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR---IGifagsgvGK- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 178 SVAIDTIINQKSEDVIcVyVA-IGQKASSVAS-IVTTLEEKGaLGYTIVVASNADDPATLQYIAPYTGAALAEYFMYKGK 255
Cdd:COG1157 171 STLLGMIARNTEADVN-V-IAlIGERGREVREfIEDDLGEEG-LARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 256 ATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlsdaLGGGSMTAL------------PIIETq 323
Cdd:COG1157 248 NVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN----GGKGSITAFytvlvegddmndPIADA- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 324 agdvsayiptnVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELE------AFs 397
Cdd:COG1157 323 -----------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEdlirigAY- 390
|
410 420 430
....*....|....*....|....*....|....*...
gi 2493022 398 QFASD--LDAAtqaeLARGQRLREMLKQPQNSPIPVEE 433
Cdd:COG1157 391 QPGSDpeLDEA----IALIPAIEAFLRQGMDERVSFEE 424
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
30-438 |
2.51e-45 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 163.02 E-value: 2.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 30 GTVLQVGDGIARVYGLeQVMAGELLEFEDKTVgiALNLENDNVG----VVLMGP--GLDILEGGS-VRSTGKIAQIPVGD 102
Cdd:PRK09099 26 GKVVEVIGTLLRVSGL-DVTLGELCELRQRDG--TLLQRAEVVGfsrdVALLSPfgELGGLSRGTrVIGLGRPLSVPVGP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 103 GFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGDRQTGKTsvaid 182
Cdd:PRK09099 103 ALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKS----- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 183 TIINQKSEDVIC---VYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTGAALAEYFMYKGKATLI 259
Cdd:PRK09099 178 TLMGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 260 IYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkLSDAlggGSMTALPIIETQAGDVSAYIPTNVISIT 339
Cdd:PRK09099 258 MMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-MGET---GSITALYTVLAEDESGSDPIAEEVRGIL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 340 DGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELEAFSQ---FASDLDAATQAELARGQR 416
Cdd:PRK09099 334 DGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQvgeYRAGSDPVADEAIAKIDA 413
|
410 420
....*....|....*....|..
gi 2493022 417 LREMLKQPQNSPIPVEEQVALI 438
Cdd:PRK09099 414 IRDFLSQRTDEYSDPDATLAAL 435
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
97-438 |
6.56e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 161.78 E-value: 6.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 97 QIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:PRK08472 91 NIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 177 TSVAidTIINQKSEDVICVYVAIGQKASSVASIVttleEK---GALGYTIVVASNADDPATLQYIAPYTGAALAEYFMYK 253
Cdd:PRK08472 171 STLM--GMIVKGCLAPIKVVALIGERGREIPEFI----EKnlgGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQ 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 254 GKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSdalGGGSMTALPIIETQAGDVSAYIPT 333
Cdd:PRK08472 245 GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEE---GKGSITAFFTVLVEGDDMSDPIAD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 334 NVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELEAFSQFAS-------DLDAA 406
Cdd:PRK08472 322 QSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAyqkgndkELDEA 401
|
330 340 350
....*....|....*....|....*....|..
gi 2493022 407 tqaeLARGQRLREMLKQPQNSPIPVEEQVALI 438
Cdd:PRK08472 402 ----ISKKEFMEQFLKQNPNELFPFEQTFEQL 429
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
74-438 |
1.49e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 157.96 E-value: 1.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 74 VVLMgPGLDILE---GGSVRSTGKIAQIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTG 150
Cdd:PRK07721 67 VLLM-PYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 151 ITAIDSMIPIGRGQRELIIGDRQTGKtSVAIDTIINQKSEDvICVYVAIGQKASSVAS-IVTTLEEKGaLGYTIVVASNA 229
Cdd:PRK07721 146 VRAIDSLLTVGKGQRVGIFAGSGVGK-STLMGMIARNTSAD-LNVIALIGERGREVREfIERDLGPEG-LKRSIVVVATS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 230 DDPATLQYIAPYTGAALAEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsdAL 309
Cdd:PRK07721 223 DQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG----TN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 310 GGGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQ 389
Cdd:PRK07721 299 ASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLST 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2493022 390 FAELE------AFSQFAS-DLDAATQAELArgqrLREMLKQPQNSPIPVEEQVALI 438
Cdd:PRK07721 379 YQNSEdlinigAYKRGSSrEIDEAIQFYPQ----IISFLKQGTDEKATFEESIQAL 430
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
95-366 |
6.71e-42 |
|
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: 149.68 E-value: 6.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 95 IAQIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGD--- 171
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGsgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 172 ----------RQTGktsvaidtiINQKSEDVICVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPY 241
Cdd:cd01135 81 phnelaaqiaRQAG---------VVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 242 TGAALAEYFMY-KGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSDAlgGGSMTAL 317
Cdd:cd01135 152 MALTTAEYLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQI 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2493022 318 PIIETQAGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSR 366
Cdd:cd01135 227 PILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
372-438 |
1.75e-40 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 140.66 E-value: 1.75e-40
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2493022 372 QTKAMKQVAGKLKLELAQFAELEAFSQFASDLDAATQAELARGQRLREMLKQPQNSPIPVEEQVALI 438
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIIL 67
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
42-420 |
1.94e-40 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 149.98 E-value: 1.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 42 VYGLEQVMAGELLEFEDKT----VGIALNLENDNVGV-VLMGP-GLDiLEGGSVRSTGKIAQIPVGDGFLGRVVDSLARP 115
Cdd:PRK04196 17 VEGVEGVAYGEIVEIELPNgekrRGQVLEVSEDKAVVqVFEGTtGLD-LKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 116 IDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQR------------EL---IIgdRQTgktsva 180
Cdd:PRK04196 96 IDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnELaaqIA--RQA------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 181 idTIINQKSEDVIcVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTGAALAEYFMY-KGKATLI 259
Cdd:PRK04196 168 --KVLGEEENFAV-VFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFeKGMHVLV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 260 IYDDLSKQASAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSDAlgGGSMTALPIIETQAGDVSAYIPTNVI 336
Cdd:PRK04196 245 ILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHPIPDLTG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 337 SITDGQIFLSGDLFNAGIRPAINVGISVSRVgsaaqtkaMKQVAGKLKLElaqfaelEAFSQFASDLDAAtqaeLARGQR 416
Cdd:PRK04196 320 YITEGQIVLSRELHRKGIYPPIDVLPSLSRL--------MKDGIGEGKTR-------EDHKDVANQLYAA----YARGKD 380
|
....
gi 2493022 417 LREM 420
Cdd:PRK04196 381 LREL 384
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
376-438 |
1.08e-39 |
|
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: 138.65 E-value: 1.08e-39
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2493022 376 MKQVAGKLKLELAQFAELEAFSQFASDLDAATQAELARGQRLREMLKQPQNSPIPVEEQVALI 438
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAIL 63
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
83-379 |
1.43e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 147.54 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 83 ILEGGSVRSTGKIAQIPVGDGFLGRVVDSLARPIDGKGDI--DATESRLVESMAPgiITRKSVCEPVQTGITAIDSMIPI 160
Cdd:PRK08972 82 VLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIytDQRASRHSPPINP--LSRRPITEPLDVGVRAINAMLTV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 161 GRGQRELIIGDRQTGKtSVAIDTIINQKSEDVICVYVaIGQKASSVAS-IVTTLEEKGaLGYTIVVASNADDPATLQYIA 239
Cdd:PRK08972 160 GKGQRMGLFAGSGVGK-SVLLGMMTRGTTADVIVVGL-VGERGREVKEfIEEILGEEG-RARSVVVAAPADTSPLMRLKG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 240 PYTGAALAEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDalGGGSMTALPI 319
Cdd:PRK08972 237 CETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYT 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2493022 320 IETQAGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRVG----SAAQTKAMKQV 379
Cdd:PRK08972 315 VLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMpmviSEEHLEAMRRV 378
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
89-433 |
2.77e-38 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 143.60 E-value: 2.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 89 VRSTGKIAQIPVGDGFLGRVVDSLARpIDGKGDIDAT-----ESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRG 163
Cdd:PRK08149 73 LKPTGKPLSVWVGEALLGAVLDPTGK-IVERFDAPPTvgpisEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 164 QRELIIGDRQTGKTSVaIDTIINQKSEDViCVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTG 243
Cdd:PRK08149 152 QRMGIFASAGCGKTSL-MNMLIEHSEADV-FVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 244 AALAEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsdALGGGSMTALPIIETQ 323
Cdd:PRK08149 230 TTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPG----ATLAGSITAFYTVLLE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 324 AGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELEAFSQFA--- 400
Cdd:PRK08149 306 SEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGeyr 385
|
330 340 350
....*....|....*....|....*....|....*..
gi 2493022 401 ----SDLDAAtqaeLARGQRLREMLKQPQNSPIPVEE 433
Cdd:PRK08149 386 rgenADNDRA----MDKRPALEAFLKQDVAEKSSFSD 418
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
98-436 |
7.65e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 142.95 E-value: 7.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 98 IPVGDGFLGRVVDSLARPIDGKGDIDAtESRLveSMAPGIIT---RKSVCEPVQTGITAIDSMIPIGRGQRELIIGDRQT 174
Cdd:PRK05688 103 LPMGMSMLGRVLDGAGRALDGKGPMKA-EDWV--PMDGPTINplnRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 175 GKtSVAIDTIINQKSEDVICVYVaIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTGAALAEYFMYKG 254
Cdd:PRK05688 180 GK-SVLLGMMTRFTEADIIVVGL-IGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKG 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 255 KATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDALGGGSMTALPIIETQAGDVSAYIPTN 334
Cdd:PRK05688 258 KNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEGDDQQDPIADS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 335 VISITDGQIFLSGDLFNAGIRPAINVGISVSRVgsaaqtkaMKQVAGKLKLELAQ-FAELEAFSQFASDL---------- 403
Cdd:PRK05688 336 ARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV--------MPQVVDPEHLRRAQrFKQLWSRYQQSRDLisvgayvagg 407
|
330 340 350
....*....|....*....|....*....|...
gi 2493022 404 DAATQAELARGQRLREMLKQPQNSPIPVEEQVA 436
Cdd:PRK05688 408 DPETDLAIARFPHLVQFLRQGLRENVSLAQSRE 440
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
30-432 |
8.69e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 142.40 E-value: 8.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 30 GTVLQVGDGIARVYgLEQVMAGELLEFE-DKTVGIALNLENDNVGVVLMGPGLDILEGGSVRSTGKIAQIPVGDGFLGRV 108
Cdd:PRK07594 23 GRIQDVSATLLNAW-LPGVFMGELCCIKpGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 109 VDSLARPIDGKGDIDATESRLvESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGDRQTGKTSVaIDTIINQK 188
Cdd:PRK07594 102 IDGFGRPLDGRELPDVCWKDY-DAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLCNAP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 189 SEDViCVYVAIGQKASSVASIVT-TLEEKGALGYTIVVASnADDPATLQYIAPYTGAALAEYFMYKGKATLIIYDDLSKQ 267
Cdd:PRK07594 180 DADS-NVLVLIGERGREVREFIDfTLSEETRKRCVIVVAT-SDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 268 ASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsdaLGG-GSMTALPIIETQAGDVSAYIPTNVISITDGQIFLS 346
Cdd:PRK07594 258 ARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 347 GDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELEAF---SQFASDLDAATQAELARGQRLREMLKQ 423
Cdd:PRK07594 333 RRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLiriGEYQRGVDTDTDKAIDTYPDICTFLRQ 412
|
....*....
gi 2493022 424 PQNSPIPVE 432
Cdd:PRK07594 413 SKDEVCGPE 421
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
83-436 |
2.62e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 135.40 E-value: 2.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 83 ILEGGSVRSTGKIAQIPVGDGFLGRVVDSLARPIDGKGDIDAteSRLVESMAPGI--ITRKSVCEPVQTGITAIDSMIPI 160
Cdd:PRK07196 75 VLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGG--STPLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLTI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 161 GRGQRELIIGDRQTGKtSVAIDTIINQKSEDVICVYVaIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAP 240
Cdd:PRK07196 153 GKGQRVGLMAGSGVGK-SVLLGMITRYTQADVVVVGL-IGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKAT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 241 YTGAALAEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsDALGGGSMTALPII 320
Cdd:PRK07196 231 ELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 321 ETQAGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAE---LEAFS 397
Cdd:PRK07196 308 LAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAikpLIPLG 387
|
330 340 350
....*....|....*....|....*....|....*....
gi 2493022 398 QFASDLDAATQAELARGQRLREMLKQPQNSPIPVEEQVA 436
Cdd:PRK07196 388 GYVAGADPMADQAVHYYPAITQFLRQEVGHPALFSASVE 426
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
30-392 |
1.34e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 133.97 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 30 GTVLQVGDGIARVYGLEQ-VMAGELLEFEDKT---VGIALNLENDNVGVVLMGPGLDILEGGSVRSTGKiAQIPVGDGFL 105
Cdd:PRK06002 28 GTVSEVTASHYRVRGLSRfVRLGDFVAIRADGgthLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGP-LRIRPDPSWK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 106 GRVVDSLARPIDGKGDIDA-TESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGDRQTGKTsvaidTI 184
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKS-----TL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 185 INQ--KSEDVICVYVA-IGQKASSVASIvttLEE--KGALGYTIVVASNADDPATLQYIAPYTGAALAEYFMYKGKATLI 259
Cdd:PRK06002 182 LAMlaRADAFDTVVIAlVGERGREVREF---LEDtlADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 260 IYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDalGGGSMTALPIIETQAGDVSAYIPTNVISIT 339
Cdd:PRK06002 259 IVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLVDGDDHNDPVADSIRGTL 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2493022 340 DGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAE 392
Cdd:PRK06002 337 DGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEE 389
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
92-376 |
8.74e-32 |
|
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: 126.38 E-value: 8.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 92 TGKIAQIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGD 171
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 172 -------------RQTGKTSVAIDTIINQKSEDVICVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYI 238
Cdd:TIGR01040 150 aglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERII 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 239 APYTGAALAEYFMY-KGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDAlgGGSMTAL 317
Cdd:TIGR01040 230 TPRLALTTAEYLAYqCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR--NGSITQI 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2493022 318 PIIETQAGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAM 376
Cdd:TIGR01040 308 PILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
28-94 |
8.81e-30 |
|
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: 110.24 E-value: 8.81e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2493022 28 NVGTVLQVGDGIARVYGLEQVMAGELLEFEDKTVGIALNLENDNVGVVLMGPGLDILEGGSVRSTGK 94
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
86-370 |
1.29e-29 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 119.89 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 86 GGSVRSTGKiaQIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQR 165
Cdd:PRK07960 100 SGEGLQSGK--QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 166 ELIIGDRQTGKtSVAIDTIINQKSEDVICVYVaIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTGAA 245
Cdd:PRK07960 178 MGLFAGSGVGK-SVLLGMMARYTQADVIVVGL-IGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 246 LAEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDalGGGSMTALPIIETQAG 325
Cdd:PRK07960 256 IAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGD 333
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2493022 326 DVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSA 370
Cdd:PRK07960 334 DQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTA 378
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
24-394 |
3.89e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 118.16 E-value: 3.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 24 VQIDNVGTVLQVGDGIARVYGLEQVMAGELLEFEDKTVgialnlendnvgvVLM--GPGLDILEGGSVRSTGKIAQIPVG 101
Cdd:PRK08927 29 VEVAGPIHALSVGARIVVETRGGRPVPCEVVGFRGDRA-------------LLMpfGPLEGVRRGCRAVIANAAAAVRPS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 102 DGFLGRVVDSLARPIDGKGDI-DATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGDRQTGKtSVA 180
Cdd:PRK08927 96 RAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGK-SVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 181 IDTIINQKSEDVIcVYVAIGQKASSVASIVT-TLEEKGaLGYTIVVASNADDPATLQYIAPYTGAALAEYFMYKGKATLI 259
Cdd:PRK08927 175 LSMLARNADADVS-VIGLIGERGREVQEFLQdDLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 260 IYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDALGGGSMTALPIIETQAGDVSAYIPTNVISIT 339
Cdd:PRK08927 253 LMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVDGDDHNEPVADAVRGIL 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2493022 340 DGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELE 394
Cdd:PRK08927 331 DGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADME 385
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
86-435 |
2.98e-27 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 113.08 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 86 GGSVRSTGKIAQIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQR 165
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 166 ELIIGDRQTGKTSVAidTIINQKSEDVICVYVAIGQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTGAA 245
Cdd:PRK05922 160 IGVFSEPGSGKSSLL--STIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 246 LAEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlSDAlggGSMTALPIIETQAG 325
Cdd:PRK05922 238 IAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-NDK---GSITALYAILHYPN 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 326 DVSAYIPTnVISITDGQIFLS--GDLFNAgirPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELEAFSQFASdL 403
Cdd:PRK05922 314 HPDIFTDY-LKSLLDGHFFLTpqGKALAS---PPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGA-Y 388
|
330 340 350
....*....|....*....|....*....|....*.
gi 2493022 404 DAATQAELARGQRL----REMLKQPQNSPIPVEEQV 435
Cdd:PRK05922 389 VPGQDAHLDRAVKLlpsiKQFLSQPLSSYCALHNTL 424
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
60-424 |
3.98e-23 |
|
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: 101.33 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 60 TVGIALNLENDNVGVVLMGPGLDILEGGSVRSTGKIAQIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIIT 139
Cdd:TIGR01039 40 TLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 140 RKSVCEPVQTGITAIDSMIPIGRGQRELIIGDRQTGKTsVAIDTIINQ--KSEDVICVYVAIGQKASSVASIVTTLEEKG 217
Cdd:TIGR01039 120 QSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKT-VLIQELINNiaKEHGGYSVFAGVGERTREGNDLYHEMKESG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 218 ALGYTIVVASNADDPATLQYIAPYTGAALAEYFM-YKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHS 296
Cdd:TIGR01039 199 VIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 297 RLLERAAKLSdalgGGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQT-KA 375
Cdd:TIGR01039 279 ELQERITSTK----TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVgEE 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2493022 376 MKQVAGKLKLELAQFAELEAFSQF-----ASDLDAATqaeLARGQRLREMLKQP 424
Cdd:TIGR01039 355 HYDVARGVQQILQRYKELQDIIAIlgmdeLSEEDKLT---VERARRIQRFLSQP 405
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
86-438 |
6.80e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 100.44 E-value: 6.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 86 GGSVRSTGKIAQIPVGDGFLGRVVDSlarpidgKGDIDATESRLVESM-----APGI--ITRKSVCEPVQTGITAIDSMI 158
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSA-------NGEVLNEEAENIPLQkikldAPPIhaFEREEITDVFETGIKSIDSML 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 159 PIGRGQRELIIGDRQTGKTSVAIDTIINQKSEdvICVYVAIGQKASSVASIV-TTLEEKGaLGYTIVVASNADDPATLQY 237
Cdd:PRK06793 152 TIGIGQKIGIFAGSGVGKSTLLGMIAKNAKAD--INVISLVGERGREVKDFIrKELGEEG-MRKSVVVVATSDESHLMQL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 238 IAPYTGAALAEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPgreaYPGDVFYLHS---RLLERAAKLSDalggGSM 314
Cdd:PRK06793 229 RAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK----GSI 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 315 TALPIIETQAGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQTKAMKQVAGKLKLELAQFAELE 394
Cdd:PRK06793 301 TGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENE 380
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2493022 395 AFSQFASDLDAATQAEL----ARGQRLREMLKQPQNSPIPVEEQVALI 438
Cdd:PRK06793 381 LYFKLGTIQENAENAYIfeckNKVEGINTFLKQGRSDSFQFDDIVEAM 428
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
46-348 |
1.39e-21 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 96.26 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 46 EQVMAGELLEFEDKTVGI---ALNLENDNVGVVLMGPGLDILEGGSVRSTGKIAQIPVGDGFLGRVVDSLARPIDGKGDI 122
Cdd:PRK02118 21 EGVGYGELATVERKDGSSlaqVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 123 datESRLVESMAPGI--ITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGDrqTGKTSVAI-DTIINQKSEDVIcVYVAI 199
Cdd:PRK02118 101 ---EGEPIEIGGPSVnpVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSV--SGEPYNALlARIALQAEADII-ILGGM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 200 GQKASSVASIVTTLEEKGALGYTIVVASNADDPATLQYIAPYTGAALAEYFMYKG-KATLIIYDDLSKQASAYRQMSLLL 278
Cdd:PRK02118 175 GLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLTDMTNFADALKEISITM 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 279 RRPPGREAYPGDvfyLHSRLLERAAKLSDALGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSGD 348
Cdd:PRK02118 255 DQIPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLRRG 321
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
376-438 |
1.59e-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: 76.71 E-value: 1.59e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2493022 376 MKQVAGKLKLELAQFAELEAFSQFASD--LDAATQAELARGQRLREMLKQPQNSPIPVEEQVALI 438
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKL 65
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
97-367 |
2.06e-16 |
|
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: 79.19 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 97 QIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRGQRELIIGDRQTGK 176
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 177 TsVAIDTIINQ--KSEDVICVYVAIGQ------------KASSVasIVTTLEEKGALgytivVASNADDPATLQYIAPYT 242
Cdd:cd01133 81 T-VLIMELINNiaKAHGGYSVFAGVGErtregndlyhemKESGV--INLDGLSKVAL-----VYGQMNEPPGARARVALT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 243 GAALAEYFM-YKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklsdALGGGSMTALPIIE 321
Cdd:cd01133 153 GLTMAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERIT----STKKGSITSVQAVY 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2493022 322 TQAGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAINVGISVSRV 367
Cdd:cd01133 229 VPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
101-366 |
2.43e-16 |
|
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: 79.16 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 101 GDGFLGRVVDSLARPIDgkgDIDATESRL-----------VESMAPgIITRKSVCEPVQTGITAIDSMIPIGRGQRELII 169
Cdd:cd01134 7 GPGLLGSIFDGIQRPLE---VIAETGSIFiprgvnvqrwpVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 170 GDRQTGKTsVAIDTIINQKSEDVIcVYVAIGQKASSVASIVT-------TLEEKGALGYTIVVASNADDPATLQYIAPYT 242
Cdd:cd01134 83 GPFGCGKT-VISQSLSKWSNSDVV-IYVGCGERGNEMAEVLEefpelkdPITGESLMERTVLIANTSNMPVAAREASIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 243 GAALAEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSdALGG----GSMT 315
Cdd:cd01134 161 GITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYERAGRVR-CLGSpgreGSVT 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2493022 316 ALPIIETQAGDVSAYIPTNVISITdgQIF--LSGDLFNAGIRPAINVGISVSR 366
Cdd:cd01134 237 IVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
29-93 |
2.29e-14 |
|
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: 67.57 E-value: 2.29e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2493022 29 VGTVLQVGDGIARVYGLEQVMAGELLEFEDKTVGIALNLENDNVGVVLMGPGLDILEGGSVRSTG 93
Cdd:pfam02874 5 IGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
86-163 |
8.81e-12 |
|
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: 66.65 E-value: 8.81e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2493022 86 GGSVRSTGKIAQIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGIITRKSVCEPVQTGITAIDSMIPIGRG 163
Cdd:COG0055 69 GMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKG 146
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
189-393 |
9.68e-11 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 63.89 E-value: 9.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 189 SEDVICVYVAIGQKASSVASIVTTLEE-------KGALGYTIVVASNADDPATLQYIAPYTGAALAEYFMYKGKATLIIY 261
Cdd:PRK14698 680 SDAQVVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMA 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 262 DDLSKQASAYRQMSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKLSDALGGGSMTALPIIETQAGDVSAYIPTNV 335
Cdd:PRK14698 760 DSTSRWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNT 836
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2493022 336 ISITDGQIFLSGDLFNAGIRPAINVGISVSRVGSAAQT----------KAMKQVAGKLKLELAQFAEL 393
Cdd:PRK14698 837 LRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDwwhknvdpewKAMRDKAMELLQKEAELQEI 904
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
67-359 |
1.82e-09 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 59.67 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 67 LENDNVGVVLMGPGLDILEGGSVRSTGKIAQIPVGDGFLGRVVDSLARPIDGKGDIDATESRLVESMAPGII---TRKSV 143
Cdd:CHL00060 65 LGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTKLSI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 144 CEpvqTGITAIDSMIPIGRGQRELIIGDRQTGKTsVAIDTIINQ--KSEDVICVYVAIGQ------------KASSVASI 209
Cdd:CHL00060 145 FE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKT-VLIMELINNiaKAHGGVSVFGGVGErtregndlymemKESGVINE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 210 VTTLEEKGALGYtivvaSNADDPATLQYIAPYTGAALAEYF--MYKGKATLIIyDDLSKQASAYRQMSLLLRRPPGREAY 287
Cdd:CHL00060 221 QNIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFrdVNKQDVLLFI-DNIFRFVQAGSEVSALLGRMPSAVGY 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2493022 288 PGDVFYLHSRLLERAAKLSDalggGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLSGDLFNAGIRPAIN 359
Cdd:CHL00060 295 QPTLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 362
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
145-316 |
2.01e-08 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 56.33 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 145 EPVQTGITAIDSMIPIGRGQRELIIGDRQTGKTsVAIDTIINQKSEDVIcVYVAIGQKASSVasiVTTLEE--------- 215
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT-VTQHQLAKWADADIV-IYVGCGERGNEM---TEVLEEfpelidpkt 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 216 -KGALGYTIVVA--SN---ADDPATLqyiapYTGAALAEYFMYKGKATLIIYDDLSKQASAYRQMSLLLRRPPGREAYPG 289
Cdd:PRK04192 284 gRPLMERTVLIAntSNmpvAAREASI-----YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPA 358
|
170 180 190
....*....|....*....|....*....|..
gi 2493022 290 dvfYLHSRL---LERAAKLSdALGG--GSMTA 316
Cdd:PRK04192 359 ---YLASRLaefYERAGRVK-TLGGeeGSVTI 386
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
30-94 |
6.33e-06 |
|
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: 43.84 E-value: 6.33e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2493022 30 GTVLQVGDGIARVYGLEQVMAGELLEFE-----DKTVGIA--LNLENDNVGVVLMGPGLDILEGGSVRSTGK 94
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIGEVCEIErgdgnNETVLKAevIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
154-322 |
5.09e-04 |
|
transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]
Pssm-ID: 162030 [Multi-domain] Cd Length: 415 Bit Score: 41.98 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 154 IDSMIPIGRGQRELIIGDRQTGKTSV--AIDTIINQKSEDVICVYVAIGQKASSVASIVTTLeeKGAlgytiVVASNADD 231
Cdd:TIGR00767 159 LDLFAPIGKGQRGLIVAPPKAGKTVLlqKIAQAITRNHPEVELIVLLIDERPEEVTDMQRSV--KGE-----VVASTFDE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 232 PATLQyiapytgAALAEYFMYK-------GKATLIIYDDLSKQASAYRQMSlllrrPPGREAYPGDV----FYLHSRLLE 300
Cdd:TIGR00767 232 PASRH-------VQVAEMVIEKakrlvehKKDVVILLDSITRLARAYNTVT-----PASGKVLSGGVdanaLHRPKRFFG 299
|
170 180
....*....|....*....|....
gi 2493022 301 RAAKLSdalGGGSMT--ALPIIET 322
Cdd:TIGR00767 300 AARNIE---EGGSLTiiATALIDT 320
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
122-366 |
2.99e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 39.68 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 122 IDATESRLVESMAPGIITRksvcepvqtgitAIDSMIPIGRGQRELIIGDRQTGKTSV--AIDTIINQKSEDVICVYVAI 199
Cdd:PRK12608 104 LHPRERLRLETGSDDLSMR------------VVDLVAPIGKGQRGLIVAPPRAGKTVLlqQIAAAVAANHPEVHLMVLLI 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 200 GQKASSVASIVTTLEekgalgyTIVVASNADDPATlQYIapytgaALAEYFMYK-------GKATLIIYDDLSKQASAYR 272
Cdd:PRK12608 172 DERPEEVTDMRRSVK-------GEVYASTFDRPPD-EHI------RVAELVLERakrlveqGKDVVILLDSLTRLARAYN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2493022 273 QMSlllrRPPGREAYPGdvfyLHSRLLERAAKLSDAL----GGGSMT--ALPIIET--QAGDVsayIPTNVISITDGQIF 344
Cdd:PRK12608 238 NEV----ESSGRTLSGG----VDARALQRPKRLFGAArnieEGGSLTiiATALVDTgsRMDEV---IFEEFKGTGNMEIV 306
|
250 260
....*....|....*....|..
gi 2493022 345 LSGDLFNAGIRPAINVGISVSR 366
Cdd:PRK12608 307 LDRELADKRVFPAIDIAKSGTR 328
|
|
| |
