|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
4-511 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 998.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 4 LTISSDEIRSAIANYTSSYSAEASREEVGVVISAADGIAQVSGLPSVMANELLEFPGGVIGVAQNLDTNSIGVVVLGNYE 83
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 84 SLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIG 163
Cdd:PRK09281 81 DIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 164 RGQRQLIIGDRKTGKTAVTIDTILNQKanwesgdkDKQVRCIYVAIGQKGSTIASVRRTLEEHGALDYTTIVAAPASDSA 243
Cdd:PRK09281 161 RGQRELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 244 GYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDDMGAGS 323
Cdd:PRK09281 233 PLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 324 MTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKKVAGNLRLDLAAYRDL 403
Cdd:PRK09281 313 LTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYREL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 404 QAFAAFASDLDAASKAQLERGSRLVELLKQSESSPQPVEYQMVSIYLAEAGIFDVVPVEDVRRFEAEVHEYLNANTPEVF 483
Cdd:PRK09281 393 EAFAQFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLL 472
|
490 500
....*....|....*....|....*...
gi 552765665 484 EQIAGGKALSDESKEALEAAAKEFAPTF 511
Cdd:PRK09281 473 EEIRETKDLSDEIEAKLKAAIEEFKKTF 500
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
4-515 |
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: 980.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 4 LTISSDEIRSAIANYTSSYSAEASREEVGVVISAADGIAQVSGLPSVMANELLEFPGGVIGVAQNLDTNSIGVVVLGNYE 83
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 84 SLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIG 163
Cdd:COG0056 81 GIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 164 RGQRQLIIGDRKTGKTAVTIDTILNQKanwesgdkDKQVRCIYVAIGQKGSTIASVRRTLEEHGALDYTTIVAAPASDSA 243
Cdd:COG0056 161 RGQRELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 244 GYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDDMGAGS 323
Cdd:COG0056 233 PLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 324 MTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKKVAGNLRLDLAAYRDL 403
Cdd:COG0056 313 LTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYREL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 404 QAFAAFASDLDAASKAQLERGSRLVELLKQSESSPQPVEYQMVSIYLAEAGIFDVVPVEDVRRFEAEVHEYLNANTPEVF 483
Cdd:COG0056 393 EAFAQFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLL 472
|
490 500 510
....*....|....*....|....*....|..
gi 552765665 484 EQIAGGKALSDESKEALEAAAKEFAPTFRTSE 515
Cdd:COG0056 473 KEIRETGKLDDEIEEKLKAAIEEFKKTFAASA 504
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
5-511 |
0e+00 |
|
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273365 [Multi-domain] Cd Length: 501 Bit Score: 831.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 5 TISSDEIRSAIANYTSSYSAEASREEVGVVISAADGIAQVSGLPSVMANELLEFPGGVIGVAQNLDTNSIGVVVLGNYES 84
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 85 LKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIGR 164
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 165 GQRQLIIGDRKTGKTAVTIDTILNQKANWesgdkdkqVRCIYVAIGQKGSTIASVRRTLEEHGALDYTTIVAAPASDSAG 244
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSD--------VYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSAS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 245 YKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDDMGAGSM 324
Cdd:TIGR00962 233 LQYLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 325 TALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKKVAGNLRLDLAAYRDLQ 404
Cdd:TIGR00962 313 TALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 405 AFAAFASDLDAASKAQLERGSRLVELLKQSESSPQPVEYQMVSIYLAEAGIFDVVPVEDVRRFEAEVHEYLNANTPEVFE 484
Cdd:TIGR00962 393 AFSQFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILE 472
|
490 500
....*....|....*....|....*..
gi 552765665 485 QIAGGKALSDESKEALEAAAKEFAPTF 511
Cdd:TIGR00962 473 EINTTKKLTEELEAKLKEALKNFKKTF 499
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
4-513 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 744.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 4 LTISSDEIRSAIANYTSSYSAEASREEVGVVISAADGIAQVSGLPSVMANELLEFPGGVIGVAQNLDTNSIGVVVLGNYE 83
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 84 SLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIG 163
Cdd:PRK13343 81 DILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 164 RGQRQLIIGDRKTGKTAVTIDTILNQKanwesgdkDKQVRCIYVAIGQKGSTIASVRRTLEEHGALDYTTIVAAPASDSA 243
Cdd:PRK13343 161 RGQRELIIGDRQTGKTAIAIDAIINQK--------DSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 244 GYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDDMGAGS 323
Cdd:PRK13343 233 GLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 324 MTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKKVAGNLRLDLAAYRDL 403
Cdd:PRK13343 313 LTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLEL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 404 QAFAAFASDLDAASKAQLERGSRLVELLKQSESSPQPVEYQMVSIYLAEAGIFDVVPVEDVRRFEAEVHEYLNANTPEVF 483
Cdd:PRK13343 393 EAFTRFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALS 472
|
490 500 510
....*....|....*....|....*....|
gi 552765665 484 EQIAGGKALSDESKEALEAAAKEFAPTFRT 513
Cdd:PRK13343 473 LALESPRELDEAWLAALEEILREAGERFAA 502
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
31-515 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 717.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 31 VGVVISAADGIAQVSGLPSVMANELLEFPGGVIGVAQNLDTNSIGVVVLGNYESLKEGDEVKRTGEVLSIPVGEDFLGRV 110
Cdd:CHL00059 7 TGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 111 INPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIGRGQRQLIIGDRKTGKTAVTIDTILNQK 190
Cdd:CHL00059 87 VNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 191 anwesgdkDKQVRCIYVAIGQKGSTIASVRRTLEEHGALDYTTIVAAPASDSAGYKWLAPFSGAALGQQWMYQGNHVLVI 270
Cdd:CHL00059 167 --------GQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLII 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 271 YDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDDMGAGSMTALPIIETKANDVSAFIPTNVISITD 350
Cdd:CHL00059 239 YDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 351 GQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKKVAGNLRLDLAAYRDLQAFAAFASDLDAASKAQLERGSRLVEL 430
Cdd:CHL00059 319 GQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLREL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 431 LKQSESSPQPVEYQMVSIYLAEAGIFDVVPVEDVRRFEAEVHEYLNANTPEVFEQIAGGKALSDESKEALEAAAKEFAPT 510
Cdd:CHL00059 399 LKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQLEL 478
|
....*
gi 552765665 511 FRTSE 515
Cdd:CHL00059 479 FLLQE 483
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
4-505 |
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: 559.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 4 LTISSDEIRSAIANYTSSYSAEASREEVGVVISAADGIAQVSGLPSVMANELLEFPGGVIGVAQNLDTNSIGVVVLGNYE 83
Cdd:TIGR03324 1 LTEVLDKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 84 SLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIG 163
Cdd:TIGR03324 81 HLQAGDEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 164 RGQRQLIIGDRKTGKTAVTIDTILNQKanwesgdkDKQVRCIYVAIGQKGSTIASVRRTLEEHGALDYTTIVAAPASDSA 243
Cdd:TIGR03324 161 RGQRELILGDRQTGKTAIAIDTILNQK--------GRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 244 GYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDDMGAGS 323
Cdd:TIGR03324 233 GLQYIAPYAATSIGEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 324 MTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKKVAGNLRLDLAAYRDL 403
Cdd:TIGR03324 313 LTALPIIETEAQNISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEEL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 404 QAFAAFASDLDAASKAQLERGSRLVELLKQSESSPQPVEYQMVSIYLAEAGIFDVVPVEDVRRFEAEVHEYLNANTPEVF 483
Cdd:TIGR03324 393 ETFARFGARLDENTRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLR 472
|
490 500
....*....|....*....|..
gi 552765665 484 EQIAGGKALSDESKEALEAAAK 505
Cdd:TIGR03324 473 ERLQSGKKLSDEDREQILDIAR 494
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
97-378 |
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: 548.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 97 VLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIGRGQRQLIIGDRKT 176
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 177 GKTAVTIDTILNQKanwesgdkDKQVRCIYVAIGQKGSTIASVRRTLEEHGALDYTTIVAAPASDSAGYKWLAPFSGAAL 256
Cdd:cd01132 81 GKTAIAIDTIINQK--------GKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 257 GQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDDMGAGSMTALPIIETKAND 336
Cdd:cd01132 153 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 552765665 337 VSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVG 378
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
64-468 |
1.65e-117 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 358.97 E-value: 1.65e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 64 GVAQNLDTNS-IGVVVLGNYESLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPID-GL-----GPIESEEER-VLELQ 135
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvGLltrsrALLESEQTLgKVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 136 APSVLQRQPVEEPMQTGIKAIDAMTPIGRGQRQLIIGDRKTGKTAVTIDTILNQKANWESGDKDKQVRCIYVAIGQKGST 215
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 216 IASVRRTLEEHGALDYTTIVAAPASDSAGYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGRE 295
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGRE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 296 AYPGDVFYLHSRLLERAAKLSDDMGAGSMTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVS 375
Cdd:PTZ00185 320 AYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVS 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 376 RVGGAAQTKGMKKVAGNLRLDLAAYRDLQAFAAFASDLDAASkaqLERGSRLVELLKQSEssPQPVEYQMVSIYLAEAGI 455
Cdd:PTZ00185 400 RVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNALVSLYACLNGY 474
|
410
....*....|...
gi 552765665 456 FDVVPVEDVRRFE 468
Cdd:PTZ00185 475 LDDVKVNYAKLYE 487
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
80-531 |
4.78e-106 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 327.32 E-value: 4.78e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 80 GNYESLKEGDEVKRTGEVLSIPVGEDFLGRVINplgqpIDGlGPIESEEERVLELQ-----------APSVLQRQPVEEP 148
Cdd:PRK07165 53 NEKGKIKINDELIELNNTNKVKTSKEYFGKIID-----IDG-NIIYPEAQNPLSKKflpntssifnlAHGLMTVKTLNEQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 149 MQTGIKAIDAMTPIGRGQRQLIIGDRKTGKTAVTIDTILNQKanwesgdkDKQVRCIYVAIGQKGSTIASVRRTLEEHGA 228
Cdd:PRK07165 127 LYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQK--------NTNVKCIYVAIGQKRENLSRIYETLKEHDA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 229 LDYTTIVAAPaSDSAGYKWLAPFSGAALGQQWMYQgNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRL 308
Cdd:PRK07165 199 LKNTIIIDAP-STSPYEQYLAPYVAMAHAENISYN-DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 309 LERAAKLsddMGAGSMTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKK 388
Cdd:PRK07165 277 LERAGKF---KNRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 389 VAGNLRLDLAAYRDLQAFAAFASDLDAASKAQLERGSRLVELLKQSESSPQPVEYQMVSIYLAEAGIF-DVVPVEDVRRF 467
Cdd:PRK07165 354 VAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKGKMIEKMFNQKGFSLYSYRFVLLISKLISWGLLkDVKDEQKALDF 433
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552765665 468 EAEVHEYlNANTPEVFEQIAGGKALSDE-SKEALEAAAKEFaptfrtSEGHNLGTEEPVD----PLDEN 531
Cdd:PRK07165 434 IDYLIEN-DPDAKKIFNKIKNNEDVDDElMKNYFAFLLNQY------SDYVNLNWKIENEhsflKLSEE 495
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
152-375 |
1.07e-104 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 313.14 E-value: 1.07e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 152 GIKAIDAMTPIGRGQRQLIIGDRKTGKTaVTIDTILNQKAnwesgdKDKqvrCIYVAIGQKGSTIASVRRTLEEHGALDY 231
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKT-VLAGMIARQAS------ADV---VVYALIGERGREVREFIEELLGSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 232 TTIVAAPASDSAGYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLER 311
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552765665 312 AAKLSDdmGAGSMTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVS 375
Cdd:pfam00006 151 AGRVKG--KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
99-377 |
3.00e-96 |
|
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: 293.59 E-value: 3.00e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 99 SIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIGRGQRQLIIGDRKTGK 178
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 179 TAVTIDTILNQKanwesgDKDKQVrCIYVAIGQKGSTIASVRRTLEEHGALDYTTIVAAPASDSAGYKWLAPFSGAALGQ 258
Cdd:cd19476 81 TVLAMQLARNQA------KAHAGV-VVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 259 QWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDdmGAGSMTALPIIETKANDVS 338
Cdd:cd19476 154 YFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLT 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 552765665 339 AFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRV 377
Cdd:cd19476 232 DPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
382-507 |
5.92e-59 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 191.50 E-value: 5.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 382 QTKGMKKVAGNLRLDLAAYRDLQAFAAFASDLDAASKAQLERGSRLVELLKQSESSPQPVEYQMVSIYLAEAGIFDVVPV 461
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 552765665 462 EDVRRFEAEVHEYLNANTPEVFEQIAGGKALSDESKEALEAAAKEF 507
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
386-511 |
2.20e-57 |
|
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: 187.57 E-value: 2.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 386 MKKVAGNLRLDLAAYRDLQAFAAFASDLDAASKAQLERGSRLVELLKQSESSPQPVEYQMVSIYLAEAGIFDVVPVEDVR 465
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 552765665 466 RFEAEVHEYLNANTPEVFEQIAGGKALSDESKEALEAAAKEFAPTF 511
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
79-442 |
2.39e-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: 175.99 E-value: 2.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 79 LGNYESLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDA 158
Cdd:COG1157 71 LGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 159 MTPIGRGQRQLIIGDRKTGKTavtidTILNQKANWESGDkdkqvrcIYVA--IGQKGStiaSVR----RTLEEHGaLDYT 232
Cdd:COG1157 151 LLTVGRGQRIGIFAGSGVGKS-----TLLGMIARNTEAD-------VNVIalIGERGR---EVRefieDDLGEEG-LARS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 233 TIVAAPASDSAGYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERA 312
Cdd:COG1157 215 VVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 313 AKlsddMGAGSMTAL------------PIIETkandvsafiptnVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGA 380
Cdd:COG1157 295 GN----GGKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPD 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552765665 381 AQTKGMKKVAGNLRLDLAAY---RDLQAFAAFAS----DLDAAskaqLERGSRLVELLKQSESSPQPVE 442
Cdd:COG1157 359 IVSPEHRALARRLRRLLARYeenEDLIRIGAYQPgsdpELDEA----IALIPAIEAFLRQGMDERVSFE 423
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
99-377 |
1.55e-47 |
|
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: 166.20 E-value: 1.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 99 SIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIGRGQRQLIIGDRKTGK 178
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 179 TavtidTILNQKANWESGDkdkqvrcIYVA--IGQKGStiaSVRRTLEEH---GALDYTTIVAAPASDSAGYKWLAPFSG 253
Cdd:cd01136 81 S-----TLLGMIARNTDAD-------VNVIalIGERGR---EVREFIEKDlgeEGLKRSVLVVATSDESPLLRVRAAYTA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 254 AALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAKLSddmgAGSMTALPIIETK 333
Cdd:cd01136 146 TAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGE----KGSITAFYTVLVE 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 552765665 334 ANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRV 377
Cdd:cd01136 222 GDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
62-442 |
3.57e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 164.86 E-value: 3.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 62 VIGVAQNLDTNSIGVVVLGNYESLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQ 141
Cdd:PRK08472 54 CLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 142 RQPVEEPMQTGIKAIDAMTPIGRGQRQLIIGDRKTGKTAVTIDTILNQKAnwesgdkdkQVRCIYVaIGQKGSTIAS-VR 220
Cdd:PRK08472 134 RGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLA---------PIKVVAL-IGERGREIPEfIE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 221 RTLEehGALDYTTIVAAPASDSAGYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGD 300
Cdd:PRK08472 204 KNLG--GDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 301 VFYLHSRLLERAAKlsdDMGAGSMTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGA 380
Cdd:PRK08472 282 VLSLLPQLMERAGK---EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMND 358
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552765665 381 AQTKGMKKVAGNLR------------LDLAAYRdlqafAAFASDLDAAskaqLERGSRLVELLKQSESSPQPVE 442
Cdd:PRK08472 359 IISPEHKLAARKFKrlysllkenevlIRIGAYQ-----KGNDKELDEA----ISKKEFMEQFLKQNPNELFPFE 423
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
97-391 |
2.52e-44 |
|
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: 158.15 E-value: 2.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 97 VLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIGRGQRQLIIGDrkT 176
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSG--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 177 GKTAVTI-DTILNQKANWESGDKDKQVrciYVAIGQKGSTIASVRRTLEEHGALDYTTIVAAPASDSAGYKWLAPFSGAA 255
Cdd:cd01135 79 GLPHNELaAQIARQAGVVGSEENFAIV---FAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 256 LGQQWMYQ-GNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSDDmgAGSMTALPIIE 331
Cdd:cd01135 156 TAEYLAYEkGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILT 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 332 TKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVggaaqtkgMKKVAG 391
Cdd:cd01135 231 MPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRL--------MKSGIG 282
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
79-438 |
1.98e-40 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 151.83 E-value: 1.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 79 LGNYESLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDA 158
Cdd:PRK06936 76 LGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 159 MTPIGRGQRQLIIGDRKTGKTAVTIDTILNQKANwesgdkdkqvRCIYVAIGQKGSTIAS-VRRTLEEHGaLDYTTIVAA 237
Cdd:PRK06936 156 LLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVD----------VTVLALIGERGREVREfIESDLGEEG-LRKAVLVVA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 238 PASDSAGYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAKlSD 317
Cdd:PRK06936 225 TSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ-SD 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 318 dmgAGSMTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKKVAGNLRLDL 397
Cdd:PRK06936 304 ---KGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELL 380
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 552765665 398 AAYRD---LQAFAAFASDLDAASKAQLERGSRLVELLKQSESSP 438
Cdd:PRK06936 381 AKYEEvelLLQIGEYQKGQDKEADQAIERIGAIRGFLRQGTHEL 424
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
85-442 |
3.55e-40 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 151.12 E-value: 3.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 85 LKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGlGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIGR 164
Cdd:PRK06820 84 LRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 165 GQRQLIIGDRKTGKTavtidTILNQKANwesgdkDKQVRCIYVA-IGQKGStiaSVRRTLEEH---GALDYTTIVAAPAS 240
Cdd:PRK06820 163 GQRIGIFAAAGVGKS-----TLLGMLCA------DSAADVMVLAlIGERGR---EVREFLEQVltpEARARTVVVVATSD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 241 DSAGYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAklsdDMG 320
Cdd:PRK06820 229 RPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG----NSD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 321 AGSMTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKKVAGNLRLDLAAY 400
Cdd:PRK06820 305 RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACY 384
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 552765665 401 RDLQAF---AAFASDLDAASKAQLERGSRLVELLKQSESSPQPVE 442
Cdd:PRK06820 385 QEIELLvrvGEYQAGEDLQADEALQRYPAICAFLQQDHSETAHLE 429
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
80-404 |
1.22e-39 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 149.53 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 80 GNYESLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAM 159
Cdd:PRK09099 78 GELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 160 TPIGRGQRQLIIGDRKTGKTavtidTILNQKANWESGDKDkqvrcIYVAIGQKGSTIAS-VRRTLEEHGaLDYTTIVAAP 238
Cdd:PRK09099 158 MTLGEGQRMGIFAPAGVGKS-----TLMGMFARGTQCDVN-----VIALIGERGREVREfIELILGEDG-MARSVVVCAT 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 239 ASDSAGYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAklsdd 318
Cdd:PRK09099 227 SDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG----- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 319 MGA-GSMTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKKVAGNLRLDL 397
Cdd:PRK09099 302 MGEtGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLL 381
|
....*..
gi 552765665 398 AAYRDLQ 404
Cdd:PRK09099 382 AKHREVE 388
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
44-415 |
1.43e-39 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 149.98 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 44 VSGLPSVMANELLEF--PGGVIGVAQNLDTNSIGVV--VLGNYESLK-EGDEVKRTGEVLSIPVGEDFLGRVINPLGQPI 118
Cdd:PRK04196 17 VEGVEGVAYGEIVEIelPNGEKRRGQVLEVSEDKAVvqVFEGTTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 119 DGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIGRGQRQLIIgdrkTG------KTAVTI---DTILNq 189
Cdd:PRK04196 97 DGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIF----SGsglphnELAAQIarqAKVLG- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 190 kanwesgdKDKQVRCIYVAIGQKGSTIASVRRTLEEHGALDYTTIVAAPASDSAGYKWLAPFSGAALGQQWMYQ-GNHVL 268
Cdd:PRK04196 172 --------EEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFEkGMHVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 269 VIYDDLTKQAEAYRAISLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSDDmgAGSMTALPIIETKANDVSAFIPTNV 345
Cdd:PRK04196 244 VILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHPIPDLT 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552765665 346 ISITDGQVFLESDLFNQGVRPAINVGVSVSRVggaaqtkgMKKV--AGNLRLDLAAYRDlQAFAAFASDLDA 415
Cdd:PRK04196 319 GYITEGQIVLSRELHRKGIYPPIDVLPSLSRL--------MKDGigEGKTREDHKDVAN-QLYAAYARGKDL 381
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
88-439 |
6.43e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 145.14 E-value: 6.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 88 GDEVKRTGEvLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERV-LELQAPSVLQRQPVEEPMQTGIKAIDAMTPIGRGQ 166
Cdd:PRK06002 88 GDAVFRKGP-LRIRPDPSWKGRVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQ 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 167 RQLIIGDRKTGKTavtidTILNQKAnwESGDKDKQVrciyVA-IGQKGStiaSVRRTLEEH--GALDYTTIVAAPASDSA 243
Cdd:PRK06002 167 RIGIFAGSGVGKS-----TLLAMLA--RADAFDTVV----IAlVGERGR---EVREFLEDTlaDNLKKAVAVVATSDESP 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 244 GYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDdmGAGS 323
Cdd:PRK06002 233 MMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 324 MTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKKVAGNLRLDLAAY--- 400
Cdd:PRK06002 311 ITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFeet 390
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 552765665 401 RDLQAFAAFASDLDaaskAQLERGSRLV----ELLKQSESSPQ 439
Cdd:PRK06002 391 RDLRLIGGYRAGSD----PDLDQAVDLVpriyEALRQSPGDPP 429
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
79-440 |
5.23e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 142.56 E-value: 5.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 79 LGNYESLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDA 158
Cdd:PRK05688 82 VGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSING 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 159 MTPIGRGQRQLIIGDRKTGKTavtidTILNQKANWESGDkdkqvrcIYVA--IGQKGSTIAS-VRRTLEEHGaLDYTTIV 235
Cdd:PRK05688 162 LLTVGRGQRLGLFAGTGVGKS-----VLLGMMTRFTEAD-------IIVVglIGERGREVKEfIEHILGEEG-LKRSVVV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 236 AAPASDSAGYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAkl 315
Cdd:PRK05688 229 ASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG-- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 316 SDDMGAGSMTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKKVAGNLRL 395
Cdd:PRK05688 307 NAEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQ 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 552765665 396 DLAAY---RDLQAFAAFASDLDAASKAQLERGSRLVELLKQSESSPQP 440
Cdd:PRK05688 387 LWSRYqqsRDLISVGAYVAGGDPETDLAIARFPHLVQFLRQGLRENVS 434
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
77-433 |
2.00e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 140.63 E-value: 2.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 77 VVLGNYESLKE---GDEVKRTGEVLSIPVGEDFLGRVINPLGQPID------GLGPIESEEErvlelqAPSVLQRQPVEE 147
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDgsalpkGLAPVSTDQD------PPNPLKRPPIRE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 148 PMQTGIKAIDAMTPIGRGQRQLIIGDRKTGKTavtidTILNQKANWESGDKDkqvrcIYVAIGQKGSTIAS-VRRTLEEH 226
Cdd:PRK07721 141 PMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKS-----TLMGMIARNTSADLN-----VIALIGERGREVREfIERDLGPE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 227 GaLDYTTIVAAPASDSAGYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHS 306
Cdd:PRK07721 211 G-LKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILP 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 307 RLLERAAKlsddMGAGSMTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGM 386
Cdd:PRK07721 290 KLLERTGT----NASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEH 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 552765665 387 KKVAGNLRLDLAAY---RDLQAFAAF----ASDLDAAskaqLERGSRLVELLKQ 433
Cdd:PRK07721 366 KEAANRFRELLSTYqnsEDLINIGAYkrgsSREIDEA----IQFYPQIISFLKQ 415
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
94-408 |
2.84e-36 |
|
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: 140.63 E-value: 2.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 94 TGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIGRGQRQLIIGD 173
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 174 -------------RKTGKTAVTIDTILNqkanwesgDKDKQVRCIYVAIGQKGSTIASVRRTLEEHGALDYTTIVAAPAS 240
Cdd:TIGR01040 150 aglphneiaaqicRQAGLVKLPTKDVHD--------GHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLAN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 241 DSAGYKWLAPFSGAALGQQWMYQ-GNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDDm 319
Cdd:TIGR01040 222 DPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 320 gAGSMTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKK-----VAGNLR 394
Cdd:TIGR01040 301 -NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRkdhsdVSNQLY 379
|
330
....*....|....
gi 552765665 395 LDLAAYRDLQAFAA 408
Cdd:TIGR01040 380 ACYAIGKDVQAMKA 393
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
47-438 |
3.10e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 140.09 E-value: 3.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 47 LPSVMANELLEF-PGGVIGVAQNLDTNSIGVVVLGNYESLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLgPIE 125
Cdd:PRK07594 37 LPGVFMGELCCIkPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 126 SEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIGRGQRQLIIGDRKTGKTavtidTILNQKANWESGDKDkqvrcI 205
Cdd:PRK07594 116 DVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKS-----TLLAMLCNAPDADSN-----V 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 206 YVAIGQKGSTIAS-VRRTLEEHGALDYTTIVAApaSDSAGYKWL-APFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRA 283
Cdd:PRK07594 186 LVLIGERGREVREfIDFTLSEETRKRCVIVVAT--SDRPALERVrALFVATTIAEFFRDNGKRVVLLADSLTRYARAARE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 284 ISLLLRRPPGREAYPGDVFYLHSRLLERAAklsddMGA-GSMTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQ 362
Cdd:PRK07594 264 IALAAGETAVSGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAER 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 552765665 363 GVRPAINVGVSVSRVGGAAQTKGMKKVAGNLRLDLAAYRDLQAF---AAFASDLDAASKAQLERGSRLVELLKQSESSP 438
Cdd:PRK07594 339 GHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLiriGEYQRGVDTDTDKAIDTYPDICTFLRQSKDEV 417
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
88-433 |
3.41e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 134.44 E-value: 3.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 88 GDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIGRGQR 167
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 168 QLIIGDRKTGKTavtidTILNQKANWESGDkdkqvrCIYVA-IGQKGSTIAS-VRRTLEEHGaLDYTTIVAAPASDSAGY 245
Cdd:PRK08972 165 MGLFAGSGVGKS-----VLLGMMTRGTTAD------VIVVGlVGERGREVKEfIEEILGEEG-RARSVVVAAPADTSPLM 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 246 KWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDdmGAGSMT 325
Cdd:PRK08972 233 RLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSIT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 326 ALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKKVAGNLRLDLAAY---RD 402
Cdd:PRK08972 311 AFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYqqnRD 390
|
330 340 350
....*....|....*....|....*....|....*
gi 552765665 403 LQAFAAFA--SD--LDAASKAQlergSRLVELLKQ 433
Cdd:PRK08972 391 LISIGAYKqgSDprIDNAIRLQ----PAMNAFLQQ 421
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
91-406 |
5.36e-34 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 133.58 E-value: 5.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 91 VKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESE----EERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIGRGQ 166
Cdd:PRK08149 73 LKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVgpisEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 167 RQLIIGDRKTGKTavtidTILNQKANWESGDkdkqvrcIYVA--IGQKGSTIASVRRTLEEHGALDYTTIVAAPASDSAG 244
Cdd:PRK08149 153 RMGIFASAGCGKT-----SLMNMLIEHSEAD-------VFVIglIGERGREVTEFVESLRASSRREKCVLVYATSDFSSV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 245 YKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAKLSddmgAGSM 324
Cdd:PRK08149 221 DRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATL----AGSI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 325 TALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKKVAGNLRLDLAAYRDLQ 404
Cdd:PRK08149 297 TAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQ 376
|
..
gi 552765665 405 AF 406
Cdd:PRK08149 377 LF 378
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
93-440 |
1.65e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 132.32 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 93 RTGEVLsipVGEDFLGRVINPLGQPIDGLGPIESEEerVLELQAPSV--LQRQPVEEPMQTGIKAIDAMTPIGRGQRQLI 170
Cdd:PRK07196 86 QDGELL---IGDSWLGRVINGLGEPLDGKGQLGGST--PLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLTIGKGQRVGL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 171 IGDRKTGKTaVTIDTIlnqkanwesgDKDKQVRCIYVA-IGQKGSTIAS-VRRTLEEHGaLDYTTIVAAPASDSAGYKWL 248
Cdd:PRK07196 161 MAGSGVGKS-VLLGMI----------TRYTQADVVVVGlIGERGREVKEfIEHSLQAAG-MAKSVVVAAPADESPLMRIK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 249 APFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAklsDDMGAGSMTALP 328
Cdd:PRK07196 229 ATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIY 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 329 IIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSR----VGGAAQTKGMKKVAGNLRlDLAAYRDLQ 404
Cdd:PRK07196 306 TVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCYA-DYMAIKPLI 384
|
330 340 350
....*....|....*....|....*....|....*.
gi 552765665 405 AFAAFASDLDAASKAQLERGSRLVELLKQSESSPQP 440
Cdd:PRK07196 385 PLGGYVAGADPMADQAVHYYPAITQFLRQEVGHPAL 420
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
100-414 |
1.53e-31 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 127.21 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 100 IPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIGRGQRQLIIGDRKTGKT 179
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKS 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 180 avtidTILNQKANWESGDkdkqvrCIYVA-IGQKGSTIAS-VRRTLEEHGaLDYTTIVAAPASDSAgykwLAPFSGAA-- 255
Cdd:PRK07960 190 -----VLLGMMARYTQAD------VIVVGlIGERGREVKDfIENILGAEG-RARSVVIAAPADVSP----LLRMQGAAya 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 256 --LGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDdmGAGSMTALPIIETK 333
Cdd:PRK07960 254 trIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 334 ANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKKVAGNLRLDLAAY---RDLQAFAAFA 410
Cdd:PRK07960 332 GDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFqrnRDLVSVGAYA 411
|
....
gi 552765665 411 SDLD 414
Cdd:PRK07960 412 KGSD 415
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
62-433 |
3.65e-30 |
|
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: 123.29 E-value: 3.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 62 VIGVAQNLDTNSIGVVVLGNYESLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQ 141
Cdd:TIGR01039 40 TLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 142 RQPVEEPMQTGIKAIDAMTPIGRGQRQLIIGDRKTGKTaVTIDTILNQKANWESGdkdkqvRCIYVAIGQKGSTIASVRR 221
Cdd:TIGR01039 120 QSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKT-VLIQELINNIAKEHGG------YSVFAGVGERTREGNDLYH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 222 TLEEHGALDYTTIVAAPASDSAGYKWLAPFSGAALGQQWM-YQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYpgd 300
Cdd:TIGR01039 193 EMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGY--- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 301 vfylhsrllerAAKLSDDMG----------AGSMTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINV 370
Cdd:TIGR01039 270 -----------QPTLATEMGelqeritstkTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDP 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552765665 371 GVSVSRVgGAAQTKGMK--KVAGNLRLDLAAYRDLQAFAAF--ASDLDAASKAQLERGSRLVELLKQ 433
Cdd:TIGR01039 339 LDSTSRL-LDPSVVGEEhyDVARGVQQILQRYKELQDIIAIlgMDELSEEDKLTVERARRIQRFLSQ 404
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
30-95 |
1.45e-29 |
|
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: 110.62 E-value: 1.45e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552765665 30 EVGVVISAADGIAQVSGLPSVMANELLEFPGGVIGVAQNLDTNSIGVVVLGNYESLKEGDEVKRTG 95
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTG 66
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
84-438 |
3.23e-29 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 120.01 E-value: 3.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 84 SLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIG 163
Cdd:PRK05922 76 YVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 164 RGQRQLIIGDRKTGKTAVtIDTIlnqkanwESGdkDKQVRCIYVAIGQKGStiaSVRRTLEEHG---ALDYTTIVAAPAS 240
Cdd:PRK05922 156 KGQRIGVFSEPGSGKSSL-LSTI-------AKG--SKSTINVIALIGERGR---EVREYIEQHKeglAAQRTIIIASPAH 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 241 DSAGYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAklSDDmg 320
Cdd:PRK05922 223 ETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG--NND-- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 321 AGSMTALPIIETKANDVSAFIPTnVISITDGQVFLEsdlfNQG---VRPAINVGVSVSRVGGAAQTKGMKKVAGNLRLDL 397
Cdd:PRK05922 299 KGSITALYAILHYPNHPDIFTDY-LKSLLDGHFFLT----PQGkalASPPIDILTSLSRSARQLALPHHYAAAEELRSLL 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 552765665 398 AAYR---DLQAFAAFASDLDaaskAQLERGSRLVELLKQSESSP 438
Cdd:PRK05922 374 KAYHealDIIQLGAYVPGQD----AHLDRAVKLLPSIKQFLSQP 413
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
80-404 |
1.50e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 112.38 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 80 GNYESLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPI-ESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDA 158
Cdd:PRK08927 72 GPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 159 MTPIGRGQRQLIIGDRKTGKTavtidTILNQKAnwesgdkdKQVRCIYVAIGQKGSTIASVRRTLE----EHGaLDYTTI 234
Cdd:PRK08927 152 FLTCCRGQRMGIFAGSGVGKS-----VLLSMLA--------RNADADVSVIGLIGERGREVQEFLQddlgPEG-LARSVV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 235 VAAPASDSAGYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDVFYLHSRLLERAAk 314
Cdd:PRK08927 218 VVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 315 lSDDMGAGSMTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKKVAGNLR 394
Cdd:PRK08927 297 -PGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRAR 375
|
330
....*....|
gi 552765665 395 LDLAAYRDLQ 404
Cdd:PRK08927 376 QLMATYADME 385
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
83-402 |
3.70e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 108.14 E-value: 3.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 83 ESLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGlgPIESEEERVLELQAPSV--LQRQPVEEPMQTGIKAIDAMT 160
Cdd:PRK06793 74 EKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIhaFEREEITDVFETGIKSIDSML 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 161 PIGRGQRQLIIGDRKTGKTavtidTILNQKANWESGDKDkqvrcIYVAIGQKGSTIAS-VRRTLEEHGaLDYTTIVAAPA 239
Cdd:PRK06793 152 TIGIGQKIGIFAGSGVGKS-----TLLGMIAKNAKADIN-----VISLVGERGREVKDfIRKELGEEG-MRKSVVVVATS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 240 SDSAGYKWLAPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPgreaYPGDVFYLHS---RLLERAAKLS 316
Cdd:PRK06793 221 DESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 317 DdmgaGSMTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRVGGAAQTKGMKKVAGNLRLD 396
Cdd:PRK06793 297 K----GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKI 372
|
....*.
gi 552765665 397 LAAYRD 402
Cdd:PRK06793 373 LSIYKE 378
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
68-358 |
2.36e-23 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 102.80 E-value: 2.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 68 NLDTNSIGVVVLGNYESLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGlGPiESEEERVlELQAPSV--LQRQPV 145
Cdd:PRK02118 44 RLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GP-ELEGEPI-EIGGPSVnpVKRIVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 146 EEPMQTGIKAIDAMTPIGRGQRQLIIGDRKTGKTAVtidtiLNQKANWESGDKdkqvrCIYVAIGQKGSTIASVRRTLEE 225
Cdd:PRK02118 121 REMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNAL-----LARIALQAEADI-----IILGGMGLTFDDYLFFKDTFEN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 226 HGALDYTTIVAAPASDSAGYKWLAPFSGAALGQQWMYQGN-HVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGDvfyL 304
Cdd:PRK02118 191 AGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGKkKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGS---L 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 552765665 305 HSRLLERAAKLSDDMGAGSMTALPIIETKANDVSAFIPTNVISITDGQVFLESD 358
Cdd:PRK02118 268 YSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLRRG 321
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
62-165 |
3.05e-22 |
|
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: 99.78 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 62 VIGVAQNLDTNSIGVVVLGNYESLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQ 141
Cdd:COG0055 43 VLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEE 122
|
90 100
....*....|....*....|....
gi 552765665 142 RQPVEEPMQTGIKAIDAMTPIGRG 165
Cdd:COG0055 123 QSTKTEILETGIKVIDLLAPYAKG 146
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
99-377 |
7.29e-17 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 80.73 E-value: 7.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 99 SIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQPVEEPMQTGIKAIDAMTPIGRGQRQLIIGDRKTGK 178
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 179 TAVTIDTILNqkanwesgdkdkqvrciyVAIGQKG-STIASV-RRTLEEH--------------GALDYTTIVAAPASDS 242
Cdd:cd01133 81 TVLIMELINN------------------IAKAHGGySVFAGVgERTREGNdlyhemkesgvinlDGLSKVALVYGQMNEP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 243 AGYKWLAPFSGAALGQQWM-YQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYpgdvfylhsrllerAAKLSDDMGA 321
Cdd:cd01133 143 PGARARVALTGLTMAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGY--------------QPTLATEMGS 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552765665 322 ----------GSMTALPIIETKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVSRV 377
Cdd:cd01133 209 lqeritstkkGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
65-188 |
7.47e-17 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 83.17 E-value: 7.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 65 VAQNLDTNSIGVVVLGNYESLKEGDEVKRTGEVLSIPVGEDFLGRVINPLGQPIDGLGPIESEEERVLELQAPSVLQRQP 144
Cdd:CHL00060 61 VQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDT 140
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 552765665 145 VEEPMQTGIKAIDAMTPIGRGQRQLIIGDRKTGKTAVTIDTILN 188
Cdd:CHL00060 141 KLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINN 184
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
29-95 |
3.88e-15 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 70.27 E-value: 3.88e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552765665 29 EEVGVVISAADGIAQVSGLPSVMANELLEFPGGVIGVAQNLDTNSIGVVVLGNYESLKEGDEVKRTG 95
Cdd:pfam02874 3 QVIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
386-450 |
1.30e-11 |
|
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: 60.15 E-value: 1.30e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552765665 386 MKKVAGNLRLDLAAYRDLQAFAAFASD--LDAASKAQLERGSRLVELLKQSESSPQPVEYQMVSIYL 450
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYP 67
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
139-376 |
2.08e-11 |
|
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: 64.90 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 139 VLQRQPVEEPMQTGIKAIDAMTPIGRGQRQLIIGDRKTGKTavtidTILNQKANWESGDKdkqvrCIYVAIGQKGSTIAS 218
Cdd:cd01134 50 VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKT-----VISQSLSKWSNSDV-----VIYVGCGERGNEMAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 219 VRR-----TLEEHGA--LDYTTIVA------APASDSAGYkwlapfSGAALGQQWMYQGNHVLVIYDDLTKQAEAYRAIS 285
Cdd:cd01134 120 VLEefpelKDPITGEslMERTVLIAntsnmpVAAREASIY------TGITIAEYFRDMGYNVSLMADSTSRWAEALREIS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 286 LLLRRPPGREAYPGdvfYLHSRL---LERAAK---LSDDMGAGSMTALPIIETKANDVSAFIPTNVISITdgQVF--LES 357
Cdd:cd01134 194 GRLEEMPAEEGYPA---YLGARLaefYERAGRvrcLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDK 268
|
250
....*....|....*....
gi 552765665 358 DLFNQGVRPAINVGVSVSR 376
Cdd:cd01134 269 KLAQRRHFPSINWLISYSK 287
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
188-375 |
2.14e-08 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 57.34 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 188 NQKANWEsgdkDKQVrCIYVAIGQKGSTIASVrrtLEEHGAL----------DYTTIVAAPASDSAGYKWLAPFSGAALG 257
Cdd:PRK14698 674 HQLAKWS----DAQV-VIYIGCGERGNEMTDV---LEEFPKLkdpktgkplmERTVLIANTSNMPVAAREASIYTGITIA 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 258 QQWMYQGNHVLVIYDDLTKQAEAYRAISLLLRRPPGREAYPGdvfYLHSRLLE------RAAKLSDDMGAGSMTALPIIE 331
Cdd:PRK14698 746 EYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVS 822
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 552765665 332 TKANDVSAFIPTNVISITDGQVFLESDLFNQGVRPAINVGVSVS 375
Cdd:PRK14698 823 PPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
141-312 |
4.55e-05 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 46.31 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 141 QRQPVEEPMQTGIKAIDAMTPIGRGQRQLIIGDRKTGKTaVTIDTIlnqkANWESGDKdkqvrCIYVAIGQKGSTIASVr 220
Cdd:PRK04192 203 EKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT-VTQHQL----AKWADADI-----VIYVGCGERGNEMTEV- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 221 rtLEEHGAL----------DYTTI--------VAA-PASdsagykwlaPFSGAALGQQWMYQGNHVLVIYDDLTKQAEAY 281
Cdd:PRK04192 272 --LEEFPELidpktgrplmERTVLiantsnmpVAArEAS---------IYTGITIAEYYRDMGYDVLLMADSTSRWAEAL 340
|
170 180 190
....*....|....*....|....*....|....
gi 552765665 282 RAISLLLRRPPGREAYPGdvfYLHSRL---LERA 312
Cdd:PRK04192 341 REISGRLEEMPGEEGYPA---YLASRLaefYERA 371
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
117-376 |
5.95e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 42.38 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 117 PIDGLGPIESEEERVLELQAPSVLQRqpveepmqtgikAIDAMTPIGRGQRQLIIGDRKTGKTavtidTILNQKANWESG 196
Cdd:PRK12608 97 HFDDLTPLHPRERLRLETGSDDLSMR------------VVDLVAPIGKGQRGLIVAPPRAGKT-----VLLQQIAAAVAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 197 DKdKQVRCIYVAIGQKGSTIASVRRTLEehgaldytTIVAAPASDSAGYKWLApFSGAAL--GQQWMYQGNHVLVIYDDL 274
Cdd:PRK12608 160 NH-PEVHLMVLLIDERPEEVTDMRRSVK--------GEVYASTFDRPPDEHIR-VAELVLerAKRLVEQGKDVVILLDSL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765665 275 TKQAEAYRAISlllrRPPGREAYPGdvfyLHSRLLER------AAKLSDdmGAGSMT--ALPIIET--KANDVsafIPTN 344
Cdd:PRK12608 230 TRLARAYNNEV----ESSGRTLSGG----VDARALQRpkrlfgAARNIE--EGGSLTiiATALVDTgsRMDEV---IFEE 296
|
250 260 270
....*....|....*....|....*....|..
gi 552765665 345 VISITDGQVFLESDLFNQGVRPAINVGVSVSR 376
Cdd:PRK12608 297 FKGTGNMEIVLDRELADKRVFPAIDIAKSGTR 328
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
154-192 |
1.29e-03 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 40.65 E-value: 1.29e-03
10 20 30
....*....|....*....|....*....|....*....
gi 552765665 154 KAIDAMTPIGRGQRQLIIGDRKTGKTavtidTILNQKAN 192
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKT-----TLLQNIAN 38
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
156-192 |
1.44e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 41.28 E-value: 1.44e-03
10 20 30
....*....|....*....|....*....|....*..
gi 552765665 156 IDAMTPIGRGQRQLIIGDRKTGKTavtidTILNQKAN 192
Cdd:PRK09376 160 IDLIAPIGKGQRGLIVAPPKAGKT-----VLLQNIAN 191
|
|
| Rho |
COG1158 |
Transcription termination factor Rho [Transcription]; |
155-192 |
1.66e-03 |
|
Transcription termination factor Rho [Transcription];
Pssm-ID: 440772 [Multi-domain] Cd Length: 373 Bit Score: 40.78 E-value: 1.66e-03
10 20 30
....*....|....*....|....*....|....*...
gi 552765665 155 AIDAMTPIGRGQRQLIIGDRKTGKTavtidTILNQKAN 192
Cdd:COG1158 114 VIDLVAPIGKGQRGLIVAPPKAGKT-----TLLQDIAN 146
|
|
| COG2516 |
COG2516 |
Biotin synthase-related protein, radical SAM superfamily [General function prediction only]; |
475-509 |
3.01e-03 |
|
Biotin synthase-related protein, radical SAM superfamily [General function prediction only];
Pssm-ID: 442006 [Multi-domain] Cd Length: 322 Bit Score: 39.96 E-value: 3.01e-03
10 20 30
....*....|....*....|....*....|....*..
gi 552765665 475 LNANTPEVFEQIAGGKALS--DESKEALEAAAKEFAP 509
Cdd:COG2516 164 LDAATPEVFERIRGGKARVswERYWEAIEEAVEVFGP 200
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
156-192 |
5.46e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 39.50 E-value: 5.46e-03
10 20 30
....*....|....*....|....*....|....*..
gi 552765665 156 IDAMTPIGRGQRQLIIGDRKTGKTavtidTILNQKAN 192
Cdd:PRK12678 407 IDLIMPIGKGQRGLIVSPPKAGKT-----TILQNIAN 438
|
|
| |
