|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
40-546 |
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: 1007.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 40 RSAEISSILEERILGASSKANLEETGRVLSIGDGIARVYGLKNIQADEMVEFSSGLKGMALNLEPDNVGIVVFGNDRHIK 119
Cdd:COG0056 4 RPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEGIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 120 EGDIVKRTGAIVDVPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQ 199
Cdd:COG0056 84 EGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 200 RELIIGDRQTGKTALAIDTIINQKrfneggdeNKKLYCIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAAPLQ 279
Cdd:COG0056 164 RELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 280 YLAPYSGCAMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNKSLGGGSLTA 359
Cdd:COG0056 236 YIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 360 LPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAF 439
Cdd:COG0056 316 LPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 440 AQFGSDLDAATQQLLNRGVRLTELLKQGQYVPMAIEEQVAVIYCGVRGYLDKMDPAKITAFEKEFLAHIKATQQDLLATI 519
Cdd:COG0056 396 AQFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEI 475
|
490 500
....*....|....*....|....*..
gi 269784695 520 AKENIISEASDAKLKKVVTDFLSSFGA 546
Cdd:COG0056 476 RETGKLDDEIEEKLKAAIEEFKKTFAA 502
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
40-546 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 1005.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 40 RSAEISSILEERILGASSKANLEETGRVLSIGDGIARVYGLKNIQADEMVEFSSGLKGMALNLEPDNVGIVVFGNDRHIK 119
Cdd:PRK09281 4 NPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 120 EGDIVKRTGAIVDVPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQ 199
Cdd:PRK09281 84 EGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 200 RELIIGDRQTGKTALAIDTIINQKrfneggdeNKKLYCIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAAPLQ 279
Cdd:PRK09281 164 RELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 280 YLAPYSGCAMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNKSLGGGSLTA 359
Cdd:PRK09281 236 YLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 360 LPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAF 439
Cdd:PRK09281 316 LPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 440 AQFGSDLDAATQQLLNRGVRLTELLKQGQYVPMAIEEQVAVIYCGVRGYLDKMDPAKITAFEKEFLAHIKATQQDLLATI 519
Cdd:PRK09281 396 AQFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEI 475
|
490 500
....*....|....*....|....*..
gi 269784695 520 AKENIISEASDAKLKKVVTDFLSSFGA 546
Cdd:PRK09281 476 RETKDLSDEIEAKLKAAIEEFKKTFAA 502
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
40-546 |
0e+00 |
|
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273365 [Multi-domain] Cd Length: 501 Bit Score: 818.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 40 RSAEISSILEERILGASSKANLEETGRVLSIGDGIARVYGLKNIQADEMVEFSSGLKGMALNLEPDNVGIVVFGNDRHIK 119
Cdd:TIGR00962 3 KLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 120 EGDIVKRTGAIVDVPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQ 199
Cdd:TIGR00962 83 EGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 200 RELIIGDRQTGKTALAIDTIINQKrfneggdeNKKLYCIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAAPLQ 279
Cdd:TIGR00962 163 RELIIGDRQTGKTAVAIDTIINQK--------DSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 280 YLAPYSGCAMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNKSLGGGSLTA 359
Cdd:TIGR00962 235 YLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 360 LPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAF 439
Cdd:TIGR00962 315 LPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 440 AQFGSDLDAATQQLLNRGVRLTELLKQGQYVPMAIEEQVAVIYCGVRGYLDKMDPAKITAFEKEFLAHIKATQQDLLATI 519
Cdd:TIGR00962 395 SQFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEI 474
|
490 500
....*....|....*....|....*..
gi 269784695 520 AKENIISEASDAKLKKVVTDFLSSFGA 546
Cdd:TIGR00962 475 NTTKKLTEELEAKLKEALKNFKKTFAW 501
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
64-546 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 752.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 64 TGRVLSIGDGIARVYGLKNIQADEMVEFSSGLKGMALNLEPDNVGIVVFGNDRHIKEGDIVKRTGAIVDVPVGNELLGRV 143
Cdd:CHL00059 7 TGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 144 VDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTALAIDTIINQK 223
Cdd:CHL00059 87 VNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 224 rfneggdeNKKLYCIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAAPLQYLAPYSGCAMGEFFRDNGKHALII 303
Cdd:CHL00059 167 --------GQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLII 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 304 YDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNKSLGGGSLTALPVIETQAGDVSAYIPTNVISITD 383
Cdd:CHL00059 239 YDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 384 GQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDAATQQLLNRGVRLTEL 463
Cdd:CHL00059 319 GQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLREL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 464 LKQGQYVPMAIEEQVAVIYCGVRGYLDKMDPAKITAFEKEFLAHIKATQQDLLATIAKENIISEASDAKLKKVVTDFLSS 543
Cdd:CHL00059 399 LKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQLEL 478
|
...
gi 269784695 544 FGA 546
Cdd:CHL00059 479 FLL 481
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
41-546 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 742.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 41 SAEISSILEERILGASSKANLEETGRVLSIGDGIARVYGLKNIQADEMVEFSSGLKGMALNLEPDNVGIVVFGNDRHIKE 120
Cdd:PRK13343 5 ADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 121 GDIVKRTGAIVDVPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQR 200
Cdd:PRK13343 85 GTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 201 ELIIGDRQTGKTALAIDTIINQKrfneggdeNKKLYCIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAAPLQY 280
Cdd:PRK13343 165 ELIIGDRQTGKTAIAIDAIINQK--------DSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 281 LAPYSGCAMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNKSLGGGSLTAL 360
Cdd:PRK13343 237 LAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 361 PVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFA 440
Cdd:PRK13343 317 PIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 441 QFGSDLDAATQQLLNRGVRLTELLKQGQYVPMAIEEQVAVIYCGVRGYLDKMDPAKITAFEKEFLAHIKATQQDLLATIA 520
Cdd:PRK13343 397 RFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALE 476
|
490 500
....*....|....*....|....*.
gi 269784695 521 KENIISEASDAKLKKVVTDFLSSFGA 546
Cdd:PRK13343 477 SPRELDEAWLAALEEILREAGERFAA 502
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
130-411 |
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: 604.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 130 IVDVPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQT 209
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 210 GKTALAIDTIINQKRfneggdenKKLYCIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAAPLQYLAPYSGCAM 289
Cdd:cd01132 81 GKTAIAIDTIINQKG--------KKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 290 GEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNKSLGGGSLTALPVIETQAGD 369
Cdd:cd01132 153 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 269784695 370 VSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVG 411
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
48-527 |
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: 542.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 48 LEERILGASSKANLEETGRVLSIGDGIARVYGLKNIQADEMVEFSSGLKGMALNLEPDNVGIVVFGNDRHIKEGDIVKRT 127
Cdd:TIGR03324 12 LDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 128 GAIVDVPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQRELIIGDR 207
Cdd:TIGR03324 92 GRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 208 QTGKTALAIDTIINQKRFNeggdenkkLYCIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAAPLQYLAPYSGC 287
Cdd:TIGR03324 172 QTGKTAIAIDTILNQKGRN--------VLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 288 AMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNKSLGGGSLTALPVIETQA 367
Cdd:TIGR03324 244 SIGEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 368 GDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDLD 447
Cdd:TIGR03324 324 QNISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 448 AATQQLLNRGVRLTELLKQGQYVPMAIEEQVAVIYCGVRGYLDKMDPAKITAFEKEFLAHIKATQQDLLATIAKENIISE 527
Cdd:TIGR03324 404 ENTRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSD 483
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
132-410 |
4.16e-127 |
|
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: 372.56 E-value: 4.16e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 132 DVPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGK 211
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 212 TALAIDTIINQKrfneggdENKKLYCIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAAPLQYLAPYSGCAMGE 291
Cdd:cd19476 81 TVLAMQLARNQA-------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 292 FFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNKslGGGSLTALPVIETQAGDVS 371
Cdd:cd19476 154 YFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLT 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 269784695 372 AYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 410
Cdd:cd19476 232 DPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
97-501 |
5.68e-123 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 373.22 E-value: 5.68e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 97 GMALNLEPDN-VGIVVFGNDRHIKEGDIVKRTGAIVDVPVGNELLGRVVDALGNPIDgKGPLNNKLRF--------RIGT 167
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVP-VGLLTRSRALleseqtlgKVDA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 168 KAPGIIPRESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTALAIDTIINQKRFNEGGDENKKLYCIYVAVGQKRS 247
Cdd:PTZ00185 159 GAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVISIYVSIGQRCS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 248 TVAQIVKRLTDAGAINYSIIVSATASDAAPLQYLAPYSGCAMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGR 327
Cdd:PTZ00185 239 NVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 328 EAYPGDVFYLHSRLLERAAKMNKSLGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSV 407
Cdd:PTZ00185 319 EAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSV 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 408 SRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDAATqqlLNRGVRLTELLKQGQyvPMAIEEQVAVIYCGVRG 487
Cdd:PTZ00185 399 SRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNALVSLYACLNG 473
|
410
....*....|....
gi 269784695 488 YLDKMDPAKITAFE 501
Cdd:PTZ00185 474 YLDDVKVNYAKLYE 487
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
185-408 |
2.84e-113 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 334.71 E-value: 2.84e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 185 GIKAVDSLVPIGRGQRELIIGDRQTGKTALAiDTIINQKRFNeggdenkklYCIYVAVGQKRSTVAQIVKRLTDAGAINY 264
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD---------VVVYALIGERGREVREFIEELLGSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 265 SIIVSATASDAAPLQYLAPYSGCAMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLER 344
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784695 345 AAKMNKslGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVS 408
Cdd:pfam00006 151 AGRVKG--KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
66-466 |
8.06e-101 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 313.83 E-value: 8.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 66 RVLSIGDGIARVYGLKNIQADEMVEFSS--GLKGMALNLEPDNVGIVVFGNDRHIKEGDIVKRTGAIVDVPVGNELLGRV 143
Cdd:PRK07165 4 KIKSIFDYIVEVKGEYDYQQNQFFTLKNnpNVKAFVISATEDKAYLLINNEKGKIKINDELIELNNTNKVKTSKEYFGKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 144 VDALGNPI--DGKGPLNNKLRFRIGT---KAPGIIPRESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTALAIDT 218
Cdd:PRK07165 84 IDIDGNIIypEAQNPLSKKFLPNTSSifnLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 219 IINQKrfneggDENKKlyCIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSAtASDAAPLQYLAPYSGCAMGE---FFRD 295
Cdd:PRK07165 164 IINQK------NTNVK--CIYVAIGQKRENLSRIYETLKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAEnisYNDD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 296 ngkhALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMnksLGGGSLTALPVIETQAGDVSAYIP 375
Cdd:PRK07165 235 ----VLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKF---KNRKTITALPILQTVDNDITSLIS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 376 TNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDAATQQLLN 455
Cdd:PRK07165 308 SNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLF 387
|
410
....*....|.
gi 269784695 456 RGVRLTELLKQ 466
Cdd:PRK07165 388 KGKMIEKMFNQ 398
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
419-544 |
4.84e-66 |
|
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: 209.91 E-value: 4.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 419 MKQVAGSMKLELAQYREVAAFAQFGSDLDAATQQLLNRGVRLTELLKQGQYVPMAIEEQVAVIYCGVRGYLDKMDPAKIT 498
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 269784695 499 AFEKEFLAHIKATQQDLLATIAKENIISEASDAKLKKVVTDFLSSF 544
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
415-540 |
3.62e-65 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 207.68 E-value: 3.62e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 415 QTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDAATQQLLNRGVRLTELLKQGQYVPMAIEEQVAVIYCGVRGYLDKMDP 494
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 269784695 495 AKITAFEKEFLAHIKATQQDLLATIAKENIISEASDAKLKKVVTDF 540
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
133-410 |
2.77e-49 |
|
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: 171.20 E-value: 2.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 133 VPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 212
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 213 ALaIDTIINqkrfNEGGDENkklycIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAAPLQYLAPYSGCAMGEF 292
Cdd:cd01136 82 TL-LGMIAR----NTDADVN-----VIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 293 FRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNKslggGSLTALPVIETQAGDVSA 372
Cdd:cd01136 152 FRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----GSITAFYTVLVEGDDFND 227
|
250 260 270
....*....|....*....|....*....|....*...
gi 269784695 373 YIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 410
Cdd:cd01136 228 PIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
61-481 |
4.86e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 167.21 E-value: 4.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 61 LEETGRVLSIGDgIARVY----GLKNIQAdEMVEFSSglkgmalnlepDNVGIVVFGNDRHIKEGDIVKRTGAIVDVPVG 136
Cdd:PRK07721 30 IESKGPESSIGD-VCYIHtkggGDKAIKA-EVVGFKD-----------EHVLLMPYTEVAEIAPGCLVEATGKPLEVKVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 137 NELLGRVVDALGNPIDGKgPLNNKLR-FRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTala 215
Cdd:PRK07721 97 SGLIGQVLDALGEPLDGS-ALPKGLApVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKS--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 216 idTIINQKRFNEGGDENkklycIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAAPLQYLAPYSGCAMGEFFRD 295
Cdd:PRK07721 173 --TLMGMIARNTSADLN-----VIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 296 NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNKslggGSLTALPVIETQAGDVSAYIP 375
Cdd:PRK07721 246 QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS----GSITAFYTVLVDGDDMNEPIA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 376 TNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGS-------DLDA 448
Cdd:PRK07721 322 DTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAykrgssrEIDE 401
|
410 420 430
....*....|....*....|....*....|...
gi 269784695 449 ATQqllnRGVRLTELLKQGQYVPMAIEEQVAVI 481
Cdd:PRK07721 402 AIQ----FYPQIISFLKQGTDEKATFEESIQAL 430
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
124-482 |
7.44e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 166.85 E-value: 7.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 124 VKRTGAIVDVPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQRELI 203
Cdd:PRK06936 88 VSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 204 IGDRQTGKTALaIDTIInqkrfnEGGDENkklYCIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAAPLQYLAP 283
Cdd:PRK06936 168 FAAAGGGKSTL-LASLI------RSAEVD---VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 284 YSGCAMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNKslggGSLTALPVI 363
Cdd:PRK06936 238 FVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDK----GSITALYTV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 364 ETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFG 443
Cdd:PRK06936 314 LVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIG 393
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 269784695 444 S---DLDAATQQLLNRGVRLTELLKQGQYVPMAIEEQVAVIY 482
Cdd:PRK06936 394 EyqkGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLE 435
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
42-466 |
2.87e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 162.68 E-value: 2.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 42 AEISSILEERILGASSK-ANLEETGRVLSIGDGIARVyGLKNIQADEMVEFS-SGLKGMALNLEPDNVGIVVFGNDRHIK 119
Cdd:PRK06820 7 ARLTPRLQQQLTRPSAPpEGLRYRGPIVEIGPTLLRA-SLPGVAQGELCRIEpQGMLAEVVSIEQEMALLSPFASSDGLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 120 EGDIVKRTGAIVDVPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTkAPGIIPRESVREPMQTGIKAVDSLVPIGRGQ 199
Cdd:PRK06820 86 CGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWRELDCP-PPSPLTRQPIEQMLTTGIRAIDGILSCGEGQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 200 RELIIGDRQTGKTAL--------AIDTIInqkrfneggdenkklyciYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSAT 271
Cdd:PRK06820 165 RIGIFAAAGVGKSTLlgmlcadsAADVMV------------------LALIGERGREVREFLEQVLTPEARARTVVVVAT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 272 aSDAAPLQYL-APYSGCAMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNK 350
Cdd:PRK06820 227 -SDRPALERLkGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 351 slggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLEL 430
Cdd:PRK06820 306 ----GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRML 381
|
410 420 430
....*....|....*....|....*....|....*....
gi 269784695 431 AQYREVAAFAQFG---SDLDAATQQLLNRGVRLTELLKQ 466
Cdd:PRK06820 382 ACYQEIELLVRVGeyqAGEDLQADEALQRYPAICAFLQQ 420
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
112-476 |
2.61e-43 |
|
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: 159.43 E-value: 2.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 112 FGNDRHIKEGDIVKRTGAIVDVPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDS 191
Cdd:COG1157 71 LGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 192 LVPIGRGQReliIGdrqtgktalaIdtiinqkrFNEGGdenkklyciyvaVGqK--------RSTVAQIV---------- 253
Cdd:COG1157 151 LLTVGRGQR---IG----------I--------FAGSG------------VG-KstllgmiaRNTEADVNvialigergr 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 254 -------KRLTDAGAINySIIVSATASDAAPLQYLAPYSGCAMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPG 326
Cdd:COG1157 197 evrefieDDLGEEGLAR-SVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 327 REAYPGDVFYLHSRLLERAAKMnkslGGGSLTAL------------PVIETqagdvsayiptnVISITDGQIFLETELFY 394
Cdd:COG1157 276 TRGYPPSVFALLPRLLERAGNG----GKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 395 KGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVA------AFAQfGSD--LDAAtqqlLNRGVRLTELLKQ 466
Cdd:COG1157 340 RGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEdlirigAYQP-GSDpeLDEA----IALIPAIEAFLRQ 414
|
410
....*....|
gi 269784695 467 GQYVPMAIEE 476
Cdd:COG1157 415 GMDERVSFEE 424
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
48-443 |
1.16e-42 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 158.01 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 48 LEERILGAsskANLEETGRVLSIGDGIARVYGLKN---------------IQADEMVEFSsglKGMALnLEPdnvgivvF 112
Cdd:PRK09099 12 LERELAAL---PAVRRTGKVVEVIGTLLRVSGLDVtlgelcelrqrdgtlLQRAEVVGFS---RDVAL-LSP-------F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 113 GNDRHIKEGDIVKRTGAIVDVPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSL 192
Cdd:PRK09099 78 GELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 193 VPIGRGQRELIIGDRQTGKTALaidtiinQKRFNEGG--DENkklycIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSA 270
Cdd:PRK09099 158 MTLGEGQRMGIFAPAGVGKSTL-------MGMFARGTqcDVN-----VIALIGERGREVREFIELILGEDGMARSVVVCA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 271 TASDAAPLQYLAPYSGCAMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNK 350
Cdd:PRK09099 226 TSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-MGE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 351 SlggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLEL 430
Cdd:PRK09099 305 T---GSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLL 381
|
410
....*....|...
gi 269784695 431 AQYREVAAFAQFG 443
Cdd:PRK09099 382 AKHREVETLLQVG 394
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
57-467 |
1.52e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 154.84 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 57 SKANLEETGRVLSIGDgIARVyglknIQADEMvefSSGLkGMALNLEPDNVGIVVFGNDRHIKEGDIVKRTGAIVDVPVG 136
Cdd:PRK08472 26 SPTIIEADGLNPSVGD-IVKI-----ESSDNG---KECL-GMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 137 NELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTALaI 216
Cdd:PRK08472 96 RNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTL-M 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 217 DTIInqkrfnEGGDENKKLyciyVA-VGQKRSTVAQ-IVKRLtdAGAINYSIIVSATASDAAPLQYLAPYSGCAMGEFFR 294
Cdd:PRK08472 175 GMIV------KGCLAPIKV----VAlIGERGREIPEfIEKNL--GGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 295 DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNkslGGGSLTALPVIETQAGDVSAYI 374
Cdd:PRK08472 243 NQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEE---GKGSITAFFTVLVEGDDMSDPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 375 PTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYRE------VAAFaQFGSD--L 446
Cdd:PRK08472 320 ADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKEnevlirIGAY-QKGNDkeL 398
|
410 420
....*....|....*....|.
gi 269784695 447 DAAtqqlLNRGVRLTELLKQG 467
Cdd:PRK08472 399 DEA----ISKKEFMEQFLKQN 415
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
133-473 |
6.12e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 142.18 E-value: 6.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 133 VPVGNELLGRVVDALGNPIDGKGPLnnKLRFRIGTKAPGIIP--RESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTG 210
Cdd:PRK05688 103 LPMGMSMLGRVLDGAGRALDGKGPM--KAEDWVPMDGPTINPlnRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 211 KTALaidtIINQKRFNEGGdenkklycIYVA--VGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAaPLQYLAPYSGCA 288
Cdd:PRK05688 181 KSVL----LGMMTRFTEAD--------IIVVglIGERGREVKEFIEHILGEEGLKRSVVVASPADDA-PLMRLRAAMYCT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 289 -MGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNKSLGGGSLTALPVIETQA 367
Cdd:PRK05688 248 rIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 368 GDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYRE------VAAFAQ 441
Cdd:PRK05688 326 DDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQsrdlisVGAYVA 405
|
330 340 350
....*....|....*....|....*....|....
gi 269784695 442 FGsdlDAATQQLLNRGVRLTELLKQG--QYVPMA 473
Cdd:PRK05688 406 GG---DPETDLAIARFPHLVQFLRQGlrENVSLA 436
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
63-129 |
9.73e-37 |
|
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: 130.27 E-value: 9.73e-37
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784695 63 ETGRVLSIGDGIARVYGLKNIQADEMVEFSSGLKGMALNLEPDNVGIVVFGNDRHIKEGDIVKRTGA 129
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
133-475 |
3.70e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 139.70 E-value: 3.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 133 VPVGNELLGRVVDALGNPIDGKgPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 212
Cdd:PRK07594 91 VPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 213 alaidTIINQKRFNEGGDENkklycIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAAPLQYLAPYSGCAMGEF 292
Cdd:PRK07594 170 -----TLLAMLCNAPDADSN-----VLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEF 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 293 FRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNKslggGSLTALPVIETQAGDVSA 372
Cdd:PRK07594 240 FRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEK----GSITAFYTVLVEGDDMNE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 373 YIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGS---DLDAA 449
Cdd:PRK07594 316 PLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEyqrGVDTD 395
|
330 340
....*....|....*....|....*.
gi 269784695 450 TQQLLNRGVRLTELLKQGQYVPMAIE 475
Cdd:PRK07594 396 TDKAIDTYPDICTFLRQSKDEVCGPE 421
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
133-467 |
4.33e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 139.84 E-value: 4.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 133 VPVGNELLGRVVDALGNPIDGKGPLNNKLRfrIGTKAPGIIP--RESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTG 210
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIYTDQR--ASRHSPPINPlsRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 211 KTAL-------AIDTIINQKRFNEGGDENKK-LYCIYVAVGQKRSTVaqivkrltdagainysiiVSATAsDAAPLQYLa 282
Cdd:PRK08972 175 KSVLlgmmtrgTTADVIVVGLVGERGREVKEfIEEILGEEGRARSVV------------------VAAPA-DTSPLMRL- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 283 pySGC----AMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNKSLGGGSLT 358
Cdd:PRK08972 235 --KGCetatTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAG--NGGPGQGSIT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 359 ALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYRE--- 435
Cdd:PRK08972 311 AFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQnrd 390
|
330 340 350
....*....|....*....|....*....|....*
gi 269784695 436 ---VAAFAQfGSdlDAATQQLLNRGVRLTELLKQG 467
Cdd:PRK08972 391 lisIGAYKQ-GS--DPRIDNAIRLQPAMNAFLQQT 422
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
65-466 |
1.20e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 138.59 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 65 GRVLSIGDGIARVYGL-KNIQADEMVEFSSGLK---GMALNLEPDNVGIVVFGNDRHIKEGDIVKRTGAIVDVPvGNELL 140
Cdd:PRK06002 28 GTVSEVTASHYRVRGLsRFVRLGDFVAIRADGGthlGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGPLRIRP-DPSWK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 141 GRVVDALGNPIDGKGPLNNKLRFR-IGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTAL----- 214
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLlamla 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 215 ---AIDTIInqkrfneggdenkklyciyVA-VGQKRSTVAQIVKRlTDAGAINYSIIVSATASDAAPLQYLAPYSGCAMG 290
Cdd:PRK06002 187 radAFDTVV-------------------IAlVGERGREVREFLED-TLADNLKKAVAVVATSDESPMMRRLAPLTATAIA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 291 EFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNKslGGGSLTALPVIETQAGDV 370
Cdd:PRK06002 247 EYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLVDGDDH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 371 SAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYRE------VAAFaQFGS 444
Cdd:PRK06002 325 NDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdlrlIGGY-RAGS 403
|
410 420
....*....|....*....|....
gi 269784695 445 D--LDAATQQLlnrgVRLTELLKQ 466
Cdd:PRK06002 404 DpdLDQAVDLV----PRIYEALRQ 423
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
133-424 |
1.37e-33 |
|
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: 128.88 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 133 VPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 212
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLPHN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 213 ALAIdTIINQKRFnEGGDENKKLycIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAAPLQYLAPYSGCAMGEF 292
Cdd:cd01135 84 ELAA-QIARQAGV-VGSEENFAI--VFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 293 FR-DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMNKSlgGGSLTALPVIETQAG 368
Cdd:cd01135 160 LAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTMPND 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 269784695 369 DVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVgsaaqtkaMKQVAG 424
Cdd:cd01135 235 DITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRL--------MKSGIG 282
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
135-466 |
1.72e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 132.32 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 135 VGNELLGRVVDALGNPIDGKGPLNNKLRFRigTKAPGIIP--RESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 212
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQ--QQLPQIHPlqRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 213 ALaIDTIinqKRFNEGGdenkklYCIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSATAsDAAPLQYLAPYSGC-AMGE 291
Cdd:PRK07196 170 VL-LGMI---TRYTQAD------VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPA-DESPLMRIKATELChAIAT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 292 FFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmnKSLGGGSLTALPVIETQAGDVS 371
Cdd:PRK07196 239 YYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQ 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 372 AYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDL---DA 448
Cdd:PRK07196 316 DPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVagaDP 395
|
330
....*....|....*...
gi 269784695 449 ATQQLLNRGVRLTELLKQ 466
Cdd:PRK07196 396 MADQAVHYYPAITQFLRQ 413
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
123-476 |
3.29e-33 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 131.27 E-value: 3.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 123 IVKRTGAIVDVPVGNELLGRVVDALGNpIDGK-----GPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGR 197
Cdd:PRK08149 72 VLKPTGKPLSVWVGEALLGAVLDPTGK-IVERfdappTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 198 GQRELIIGDRQTGKTALaIDTIINQKRFNeggdenkklycIYVA--VGQKRSTVAQIVKRLTDAGAINYSIIVSATaSDA 275
Cdd:PRK08149 151 GQRMGIFASAGCGKTSL-MNMLIEHSEAD-----------VFVIglIGERGREVTEFVESLRASSRREKCVLVYAT-SDF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 276 APLQYL-APYSGCAMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmnksLGG 354
Cdd:PRK08149 218 SSVDRCnAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGA----TLA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 355 GSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYR 434
Cdd:PRK08149 294 GSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLE 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 269784695 435 EVAAFAQFG-------SDLDAAtqqlLNRGVRLTELLKQGQYVPMAIEE 476
Cdd:PRK08149 374 ELQLFIDLGeyrrgenADNDRA----MDKRPALEAFLKQDVAEKSSFSD 418
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
99-477 |
7.94e-32 |
|
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: 127.91 E-value: 7.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 99 ALNLEPDNVGIVVFGNDRHIKEGDIVKRTGAIVDVPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESV 178
Cdd:TIGR01039 44 AQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 179 REPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTALAIDTIINQKRFNEGgdenkklYCIYVAVGQKRSTVAQIVKRLTD 258
Cdd:TIGR01039 124 VEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGG-------YSVFAGVGERTREGNDLYHEMKE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 259 AGAINYSIIVSATASDAAPLQYLAPYSGCAMGEFFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYL 337
Cdd:TIGR01039 197 SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 338 HSRLLERAAkmnkSLGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQT- 416
Cdd:TIGR01039 277 MGELQERIT----STKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVg 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784695 417 KAMKQVAGSMKLELAQYREVA-AFAQFGSD-LDAATQQLLNRGVRLTELLKQgqyvPMAIEEQ 477
Cdd:TIGR01039 353 EEHYDVARGVQQILQRYKELQdIIAILGMDeLSEEDKLTVERARRIQRFLSQ----PFFVAEV 411
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
133-451 |
3.33e-31 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 126.05 E-value: 3.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 133 VPVGNELLGRVVDALGNPIDGKGPLNNklrfriGTKAPGIIP------RESVREPMQTGIKAVDSLVPIGRGQRELIIGD 206
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDT------GETGALITPpfnplqRTPIEHVLDTGVRAINALLTVGRGQRMGLFAG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 207 RQTGKTALaidtIINQKRFNEGGdenkklyCIYVA-VGQKRSTVAQIVKRLTDAGAINYSIIVSATAsDAAPLQYL--AP 283
Cdd:PRK07960 184 SGVGKSVL----LGMMARYTQAD-------VIVVGlIGERGREVKDFIENILGAEGRARSVVIAAPA-DVSPLLRMqgAA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 284 YSgCAMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNKSLGGGSLTALPVI 363
Cdd:PRK07960 252 YA-TRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG--NGISGGGSITAFYTV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 364 ETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYRE------VA 437
Cdd:PRK07960 329 LTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFQRnrdlvsVG 408
|
330
....*....|....*.
gi 269784695 438 AFAQfGSD--LDAATQ 451
Cdd:PRK07960 409 AYAK-GSDpmLDKAIA 423
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
100-482 |
1.85e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 123.55 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 100 LNLEPDNVGIVVFGNDRHIKEGDIVKRTGAIVDVPVGNELLGRVVDALGNPIDGKGPlNNKLRfRIGTKAPGI--IPRES 177
Cdd:PRK06793 58 IAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAE-NIPLQ-KIKLDAPPIhaFEREE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 178 VREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTalaidTIINQKRFNEGGDENkklycIYVAVGQKRSTVAQIVKRLT 257
Cdd:PRK06793 136 ITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKS-----TLLGMIAKNAKADIN-----VISLVGERGREVKDFIRKEL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 258 DAGAINYSIIVSATASDAAPLQYLAPYSGCAMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPgreaYPGDVFYL 337
Cdd:PRK06793 206 GEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 338 HS---RLLERAAKMNKslggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAA 414
Cdd:PRK06793 282 ESymkKLLERSGKTQK----GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEI 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784695 415 QTKAMKQVAGSMKLELAQYREVAAFAQFGS----DLDAATQQLLNRGVRLTELLKQGQYVPMAIEEQVAVIY 482
Cdd:PRK06793 358 VSPNHWQLANEMRKILSIYKENELYFKLGTiqenAENAYIFECKNKVEGINTFLKQGRSDSFQFDDIVEAMH 429
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
133-466 |
3.58e-30 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 122.71 E-value: 3.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 133 VPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 212
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 213 ALaIDTIinqkrfnegGDENKKLYCIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAAPLQYLAPYSGCAMGEF 292
Cdd:PRK05922 172 SL-LSTI---------AKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 293 FRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNKslggGSLTALPVIETQAGDVSA 372
Cdd:PRK05922 242 FRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDK----GSITALYAILHYPNHPDI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 373 YIPTnVISITDGQIFL---ETELFykgiRPAINVGLSVSRvgSAAQTKAMKQVAGSMKLE--LAQYREVAAFAQFGSDLD 447
Cdd:PRK05922 318 FTDY-LKSLLDGHFFLtpqGKALA----SPPIDILTSLSR--SARQLALPHHYAAAEELRslLKAYHEALDIIQLGAYVP 390
|
330
....*....|....*....
gi 269784695 448 AATQQlLNRGVRLTELLKQ 466
Cdd:PRK05922 391 GQDAH-LDRAVKLLPSIKQ 408
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
77-409 |
4.41e-29 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 119.93 E-value: 4.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 77 VYGLKNIQADEMVEFSSG----LKGMALNLEPDNVGIVVFGNDRHIKEGDI-VKRTGAIVDVPVGNELLGRVVDALGNPI 151
Cdd:PRK04196 17 VEGVEGVAYGEIVEIELPngekRRGQVLEVSEDKAVVQVFEGTTGLDLKDTkVRFTGEPLKLPVSEDMLGRIFDGLGRPI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 152 DGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQReLII--GdrqTGKTA--LAIDtIINQKRFnE 227
Cdd:PRK04196 97 DGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQK-LPIfsG---SGLPHneLAAQ-IARQAKV-L 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 228 GGDENkkLYCIYVAVGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAAPLQYLAPYSGCAMGEFFR-DNGKHALIIYDD 306
Cdd:PRK04196 171 GEEEN--FAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMHVLVILTD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 307 LSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMNKSlgGGSLTALPVIETQAGDVSAYIPTNVISITD 383
Cdd:PRK04196 249 MTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHPIPDLTGYITE 323
|
330 340
....*....|....*....|....*.
gi 269784695 384 GQIFLETELFYKGIRPAINVGLSVSR 409
Cdd:PRK04196 324 GQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
140-476 |
1.98e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 114.69 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 140 LGRVVDALGNPIDGKGPL-NNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTAL---- 214
Cdd:PRK08927 99 LGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLlsml 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 215 ----AIDTIInqkrfneggdenkklycIYVaVGQKRSTVAQIVKR-LTDAGaINYSIIVSATASDAAPLQYLAPYSGCAM 289
Cdd:PRK08927 179 arnaDADVSV-----------------IGL-IGERGREVQEFLQDdLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 290 GEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmnKSLGGGSLTALPVIETQAGD 369
Cdd:PRK08927 240 AEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGP--GPIGEGTITGLFTVLVDGDD 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 370 VSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSdLDAA 449
Cdd:PRK08927 318 HNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGA-YRAG 396
|
330 340 350
....*....|....*....|....*....|.
gi 269784695 450 TQQLLNRGVR----LTELLKQGQYVPMAIEE 476
Cdd:PRK08927 397 SDPEVDEAIRlnpaLEAFLRQGKDEATSLAE 427
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
127-419 |
9.71e-23 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 101.34 E-value: 9.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 127 TGAIVDVPVGNELLGRVVDALGNPIDgKGPLNNKLRFRIGTKAPgIIPRESV--REPMQTGIKAVDSLVPIGRGQRELII 204
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPID-KGPPVLAEDYLDINGQP-INPYARIypEEMIQTGISAIDVMNSIARGQKIPIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 205 GD-------------RQTGKTALAidtiinQKRFNEGGDENkklYCI-YVAVGQKRSTvAQIVKR-LTDAGAINYSIIVS 269
Cdd:TIGR01040 148 SAaglphneiaaqicRQAGLVKLP------TKDVHDGHEDN---FAIvFAAMGVNMET-ARFFKQdFEENGSMERVCLFL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 270 ATASDAAPLQYLAPYSGCAMGEFFR-DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKM 348
Cdd:TIGR01040 218 NLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269784695 349 NKSlgGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAM 419
Cdd:TIGR01040 298 EGR--NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
133-410 |
2.88e-22 |
|
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: 96.52 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 133 VPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 212
Cdd:cd01133 2 VPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 213 ALAIDTIINQKRFNEGgdenkklYCIYVAVGQKRSTVAQIVKRLTDAGAINYSIIvSATAsdaapLQY-----------L 281
Cdd:cd01133 82 VLIMELINNIAKAHGG-------YSVFAGVGERTREGNDLYHEMKESGVINLDGL-SKVA-----LVYgqmneppgaraR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 282 APYSGCAMGEFFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmnkSLGGGSLTAL 360
Cdd:cd01133 149 VALTGLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERIT----STKKGSITSV 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 269784695 361 PVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 410
Cdd:cd01133 225 QAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
100-388 |
1.45e-21 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 97.41 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 100 LNLEPDNVGIVVFGNDRHIKEGDIVKRTGAIVDVPVGNELLGRVVDALGNPIDGkGPLNNKLRFRIGTK----APGIIPR 175
Cdd:PRK02118 43 IRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GPELEGEPIEIGGPsvnpVKRIVPR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 176 ESVRepmqTGIKAVD---SLV-----PI----GRGQRELIIgdrqtgKTALA--IDTIInqkrfnEGGdenkklyciyva 241
Cdd:PRK02118 122 EMIR----TGIPMIDvfnTLVesqkiPIfsvsGEPYNALLA------RIALQaeADIII------LGG------------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 242 VGQKRSTVAQIVKRLTDAGAINYSIIVSATASDAAPLQYLAPYSGCAMGEFFR-DNGKHALIIYDDLSKQAVAYRQMSLL 320
Cdd:PRK02118 174 MGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISIT 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 269784695 321 LRRPPGREAYPGDvfyLHSRLLERAAKMNKSLGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFL 388
Cdd:PRK02118 254 MDQIPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
419-486 |
3.19e-21 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 87.50 E-value: 3.19e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 419 MKQVAGSMKLELAQYREVAAFAQFGSD--LDAATQQLLNRGVRLTELLKQGQYVPMAIEEQVAVIYCGVR 486
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
62-128 |
5.63e-19 |
|
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: 81.05 E-value: 5.63e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 269784695 62 EETGRVLSIGDGIARVYGLKNIQADEMVEFSSGLKGMALNLEPDNVGIVVFGNDRHIKEGDIVKRTG 128
Cdd:pfam02874 3 QVIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
121-214 |
2.81e-18 |
|
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: 87.45 E-value: 2.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 121 GDIVKRTGAIVDVPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGRGqr 200
Cdd:COG0055 69 GMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKG-- 146
|
90
....*....|....
gi 269784695 201 eliigdrqtGKTAL 214
Cdd:COG0055 147 ---------GKIGL 151
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
180-409 |
5.29e-13 |
|
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: 69.53 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 180 EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTalaidtIINQK--RFNEGgDENkklycIYVAVGQKRSTVAQIVKRL- 256
Cdd:cd01134 58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKT------VISQSlsKWSNS-DVV-----IYVGCGERGNEMAEVLEEFp 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 257 ------TDAGAINYSIIVSATASDAAPLQYLAPYSGCAMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY 330
Cdd:cd01134 126 elkdpiTGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGY 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 331 PGdvfYLHSRL---LERAAKMnKSLGG----GSLTALPVIETQAGDVSAYIPTNVISITdgQIF--LETELFYKGIRPAI 401
Cdd:cd01134 206 PA---YLGARLaefYERAGRV-RCLGSpgreGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSI 279
|
....*...
gi 269784695 402 NVGLSVSR 409
Cdd:cd01134 280 NWLISYSK 287
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
118-402 |
9.34e-13 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 70.45 E-value: 9.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 118 IKEGDIVKRTGAIVDVPVGNELLGRVVDALGNPIDGKGPLNNKLRFRIGTKAPGIIPRESVREPMQTGIKAVDSLVPIGR 197
Cdd:CHL00060 81 LMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 198 GQRELIIGDRQTGKTALAIDTIINQKRFNEGgdenkklYCIYVAVGQKRSTVAQIVKRLTDAGAINYSIIvsaTASDAAP 277
Cdd:CHL00060 161 GGKIGLFGGAGVGKTVLIMELINNIAKAHGG-------VSVFGGVGERTREGNDLYMEMKESGVINEQNI---AESKVAL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 278 L--QYLAP--------YSGCAMGEFFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAA 346
Cdd:CHL00060 231 VygQMNEPpgarmrvgLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERIT 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 269784695 347 kmnkSLGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAIN 402
Cdd:CHL00060 311 ----STKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 362
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
238-422 |
9.55e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 58.11 E-value: 9.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 238 IYVAVGQKRSTVAQIVK---RLTDAGA----INYSIIVSATASDAAPLQYLAPYSGCAMGEFFRDNGKHALIIYDDLSKQ 310
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEefpKLKDPKTgkplMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 311 AVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMnKSLGG----GSLTALPVIETQAGDVSAYIPTNVISITD 383
Cdd:PRK14698 766 AEALREISGRLEEMPGEEGYPA---YLASKLaefYERAGRV-VTLGSdyrvGSVSVIGAVSPPGGDFSEPVVQNTLRVVK 841
|
170 180 190
....*....|....*....|....*....|....*....
gi 269784695 384 GQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQV 422
Cdd:PRK14698 842 VFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNV 880
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
284-359 |
1.48e-08 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 57.48 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 284 YSGCAMGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMnKSLGG--GSLT 358
Cdd:PRK04192 310 YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASRLaefYERAGRV-KTLGGeeGSVT 385
|
.
gi 269784695 359 A 359
Cdd:PRK04192 386 I 386
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
64-129 |
1.26e-03 |
|
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: 37.68 E-value: 1.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784695 64 TGRVLSIGDGIARVYGLKNIQADEMVEF-------SSGLKGMALNLEPDNVGIVVFGNDRHIKEGDIVKRTGA 129
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIergdgnnETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
85-214 |
2.06e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 40.45 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784695 85 ADEMVEFSSGLKGMALNLE------PDNVGIVVFGNDRH-IKEGDIVKrtgAIVDVPVGNELLGRVVDALGNPIDgkgPL 157
Cdd:PRK12608 19 VLGVLEILGDGFGFLRSARrnylpsPDDVFVPPALIRRFnLRTGDVVE---GVARPRERYRVLVRVDSVNGTDPE---KL 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 269784695 158 NNKLRFRIGTKapgIIPRESVRepMQTG-----IKAVDSLVPIGRGQRELIIGDRQTGKTAL 214
Cdd:PRK12608 93 ARRPHFDDLTP---LHPRERLR--LETGsddlsMRVVDLVAPIGKGQRGLIVAPPRAGKTVL 149
|
|
| |
