|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
44-551 |
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: 998.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 44 TQRSAEISNILEERILGVAPKADLEETGRVLSIGDGIARVYGLNNIQADEMVEFSSGLKGMALNLEPDNVGVVVFGNDKL 123
Cdd:COG0056 2 QIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 124 IKQGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGR 203
Cdd:COG0056 82 IKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 204 GQRELIIGDRQTGKTALAIDTIINQKrfneaqdeSKKLYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAAP 283
Cdd:COG0056 162 GQRELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 284 LQYLAPYSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPAMGGGSL 363
Cdd:COG0056 234 LQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 364 TALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVA 443
Cdd:COG0056 314 TALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 444 AFAQFGSDLDAATQQLLNRGVRLTELLKQGQYVPMAIEDQVAVIYCGVRGHLDKMDPAKITKFEKEFLQHIKTSEQALLD 523
Cdd:COG0056 394 AFAQFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLK 473
|
490 500
....*....|....*....|....*...
gi 24658560 524 TIAKDGAISEASDAKLKDIVAKFMSTFQ 551
Cdd:COG0056 474 EIRETGKLDDEIEEKLKAAIEEFKKTFA 501
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
46-552 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 996.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 46 RSAEISNILEERILGVAPKADLEETGRVLSIGDGIARVYGLNNIQADEMVEFSSGLKGMALNLEPDNVGVVVFGNDKLIK 125
Cdd:PRK09281 4 NPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 126 QGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQ 205
Cdd:PRK09281 84 EGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 206 RELIIGDRQTGKTALAIDTIINQKrfneaqdeSKKLYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAAPLQ 285
Cdd:PRK09281 164 RELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 286 YLAPYSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPAMGGGSLTA 365
Cdd:PRK09281 236 YLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 366 LPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAF 445
Cdd:PRK09281 316 LPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 446 AQFGSDLDAATQQLLNRGVRLTELLKQGQYVPMAIEDQVAVIYCGVRGHLDKMDPAKITKFEKEFLQHIKTSEQALLDTI 525
Cdd:PRK09281 396 AQFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEI 475
|
490 500
....*....|....*....|....*..
gi 24658560 526 AKDGAISEASDAKLKDIVAKFMSTFQG 552
Cdd:PRK09281 476 RETKDLSDEIEAKLKAAIEEFKKTFAA 502
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
46-550 |
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: 810.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 46 RSAEISNILEERILGVAPKADLEETGRVLSIGDGIARVYGLNNIQADEMVEFSSGLKGMALNLEPDNVGVVVFGNDKLIK 125
Cdd:TIGR00962 3 KLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 126 QGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQ 205
Cdd:TIGR00962 83 EGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 206 RELIIGDRQTGKTALAIDTIINQKrfneaqdeSKKLYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAAPLQ 285
Cdd:TIGR00962 163 RELIIGDRQTGKTAVAIDTIINQK--------DSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 286 YLAPYSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPAMGGGSLTA 365
Cdd:TIGR00962 235 YLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 366 LPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAF 445
Cdd:TIGR00962 315 LPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 446 AQFGSDLDAATQQLLNRGVRLTELLKQGQYVPMAIEDQVAVIYCGVRGHLDKMDPAKITKFEKEFLQHIKTSEQALLDTI 525
Cdd:TIGR00962 395 SQFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEI 474
|
490 500
....*....|....*....|....*
gi 24658560 526 AKDGAISEASDAKLKDIVAKFMSTF 550
Cdd:TIGR00962 475 NTTKKLTEELEAKLKEALKNFKKTF 499
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
70-550 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 755.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 70 TGRVLSIGDGIARVYGLNNIQADEMVEFSSGLKGMALNLEPDNVGVVVFGNDKLIKQGDIVKRTGAIVDVPVGDELLGRV 149
Cdd:CHL00059 7 TGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 150 VDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTALAIDTIINQK 229
Cdd:CHL00059 87 VNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 230 rfneaqdeSKKLYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAAPLQYLAPYSGCAMGEYFRDKGKHALII 309
Cdd:CHL00059 167 --------GQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLII 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 310 YDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPAMGGGSLTALPVIETQAGDVSAYIPTNVISITD 389
Cdd:CHL00059 239 YDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 390 GQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDAATQQLLNRGVRLTEL 469
Cdd:CHL00059 319 GQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLREL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 470 LKQGQYVPMAIEDQVAVIYCGVRGHLDKMDPAKITKFEKEFLQHIKTSEQALLDTIAKDGAISEASDAKLKDIVAKFMST 549
Cdd:CHL00059 399 LKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQLEL 478
|
.
gi 24658560 550 F 550
Cdd:CHL00059 479 F 479
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
47-550 |
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 24658560 47 SAEISNILEERILGVAPKADLEETGRVLSIGDGIARVYGLNNIQADEMVEFSSGLKGMALNLEPDNVGVVVFGNDKLIKQ 126
Cdd:PRK13343 5 ADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 127 GDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQR 206
Cdd:PRK13343 85 GTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 207 ELIIGDRQTGKTALAIDTIINQKrfneaqdeSKKLYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAAPLQY 286
Cdd:PRK13343 165 ELIIGDRQTGKTAIAIDAIINQK--------DSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 287 LAPYSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPAMGGGSLTAL 366
Cdd:PRK13343 237 LAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 367 PVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFA 446
Cdd:PRK13343 317 PIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 447 QFGSDLDAATQQLLNRGVRLTELLKQGQYVPMAIEDQVAVIYCGVRGHLDKMDPAKITKFEKEFLQHIKTSEQALLDTIA 526
Cdd:PRK13343 397 RFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALE 476
|
490 500
....*....|....*....|....
gi 24658560 527 KDGAISEASDAKLKDIVAKFMSTF 550
Cdd:PRK13343 477 SPRELDEAWLAALEEILREAGERF 500
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
136-417 |
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: 605.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 136 IVDVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQT 215
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 216 GKTALAIDTIINQKRfneaqdesKKLYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAAPLQYLAPYSGCAM 295
Cdd:cd01132 81 GKTAIAIDTIINQKG--------KKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 296 GEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPAMGGGSLTALPVIETQAGD 375
Cdd:cd01132 153 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 24658560 376 VSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVG 417
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
54-545 |
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: 533.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 54 LEERILGVAPKADLEETGRVLSIGDGIARVYGLNNIQADEMVEFSSGLKGMALNLEPDNVGVVVFGNDKLIKQGDIVKRT 133
Cdd:TIGR03324 12 LDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 134 GAIVDVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQRELIIGDR 213
Cdd:TIGR03324 92 GRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 214 QTGKTALAIDTIINQKRFNeaqdeskkLYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAAPLQYLAPYSGC 293
Cdd:TIGR03324 172 QTGKTAIAIDTILNQKGRN--------VLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 294 AMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPAMGGGSLTALPVIETQA 373
Cdd:TIGR03324 244 SIGEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 374 GDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDLD 453
Cdd:TIGR03324 324 QNISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 454 AATQQLLNRGVRLTELLKQGQYVPMAIEDQVAVIYCGVRGHLDKMDPAKITKFEKEFLQHIKTSEQALLDTIAKDGAISE 533
Cdd:TIGR03324 404 ENTRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSD 483
|
490
....*....|..
gi 24658560 534 ASDAKLKDIVAK 545
Cdd:TIGR03324 484 EDREQILDIARG 495
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
138-416 |
1.28e-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: 374.10 E-value: 1.28e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 138 DVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGK 217
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 218 TALAIDTIINQKrfneaqdESKKLYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAAPLQYLAPYSGCAMGE 297
Cdd:cd19476 81 TVLAMQLARNQA-------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 298 YFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPamGGGSLTALPVIETQAGDVS 377
Cdd:cd19476 154 YFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLT 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 24658560 378 AYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 416
Cdd:cd19476 232 DPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
103-496 |
1.28e-124 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 377.46 E-value: 1.28e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 103 GMALNLEPDN-VGVVVFGNDKLIKQGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDgKGAINTKDRF--------RVGI 173
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVP-VGLLTRSRALleseqtlgKVDA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 174 KAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTALAIDTIINQKRFNEAQDESKKLYCIYVAIGQKRS 253
Cdd:PTZ00185 159 GAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVISIYVSIGQRCS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 254 TVAQIVKRLTDSGAMGYSVIVSATASDAAPLQYLAPYSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGR 333
Cdd:PTZ00185 239 NVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 334 EAYPGDVFYLHSRLLERAAKMSPAMGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSV 413
Cdd:PTZ00185 319 EAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSV 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 414 SRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDAATqqlLNRGVRLTELLKQGQyvPMAIEDQVAVIYCGVRG 493
Cdd:PTZ00185 399 SRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNALVSLYACLNG 473
|
...
gi 24658560 494 HLD 496
Cdd:PTZ00185 474 YLD 476
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
191-414 |
1.40e-115 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 340.87 E-value: 1.40e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 191 GIKAVDSLVPIGRGQRELIIGDRQTGKTALAiDTIINQkrfneaqdeSKKLYCIYVAIGQKRSTVAQIVKRLTDSGAMGY 270
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQ---------ASADVVVYALIGERGREVREFIEELLGSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 271 SVIVSATASDAAPLQYLAPYSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLER 350
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24658560 351 AAKMSPamGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVS 414
Cdd:pfam00006 151 AGRVKG--KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
72-472 |
3.75e-99 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 309.60 E-value: 3.75e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 72 RVLSIGDGIARVYGLNNIQADEMVEFSS--GLKGMALNLEPDNVGVVVFGNDKLIKQGDIVKRTGAIVDVPVGDELLGRV 149
Cdd:PRK07165 4 KIKSIFDYIVEVKGEYDYQQNQFFTLKNnpNVKAFVISATEDKAYLLINNEKGKIKINDELIELNNTNKVKTSKEYFGKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 150 VDALGNAIDGKGAINTKDRFRVGI-----KAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTALAIDT 224
Cdd:PRK07165 84 IDIDGNIIYPEAQNPLSKKFLPNTssifnLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 225 IINQKRFNeaqdeskkLYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSAtASDAAPLQYLAPYSGCAMGE---YFRD 301
Cdd:PRK07165 164 IINQKNTN--------VKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAEnisYNDD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 302 kgkhALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMspaMGGGSLTALPVIETQAGDVSAYIP 381
Cdd:PRK07165 235 ----VLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKF---KNRKTITALPILQTVDNDITSLIS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 382 TNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDAATQQLLN 461
Cdd:PRK07165 308 SNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLF 387
|
410
....*....|.
gi 24658560 462 RGVRLTELLKQ 472
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 ... |
425-550 |
9.36e-65 |
|
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349748 [Multi-domain] Cd Length: 126 Bit Score: 206.83 E-value: 9.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 425 MKQVAGSMKLELAQYREVAAFAQFGSDLDAATQQLLNRGVRLTELLKQGQYVPMAIEDQVAVIYCGVRGHLDKMDPAKIT 504
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24658560 505 KFEKEFLQHIKTSEQALLDTIAKDGAISEASDAKLKDIVAKFMSTF 550
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
421-546 |
1.03e-63 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 204.21 E-value: 1.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 421 QTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDAATQQLLNRGVRLTELLKQGQYVPMAIEDQVAVIYCGVRGHLDKMDP 500
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24658560 501 AKITKFEKEFLQHIKTSEQALLDTIAKDGAISEASDAKLKDIVAKF 546
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
139-416 |
3.13e-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: 165.81 E-value: 3.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 139 VPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 218
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 219 ALaIDTIINqkrfNEAQDeskklycIYVA--IGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAAPLQYLAPYSGCAMG 296
Cdd:cd01136 82 TL-LGMIAR----NTDAD-------VNVIalIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 297 EYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPamggGSLTALPVIETQAGDV 376
Cdd:cd01136 150 EYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----GSITAFYTVLVEGDDF 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 24658560 377 SAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 416
Cdd:cd01136 226 NDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
130-488 |
1.80e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 163.00 E-value: 1.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 130 VKRTGAIVDVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQRELI 209
Cdd:PRK06936 88 VSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 210 IGDRQTGKTALaIDTIInqkRFNEAQdeskklYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAAPLQYLAP 289
Cdd:PRK06936 168 FAAAGGGKSTL-LASLI---RSAEVD------VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 290 YSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPamggGSLTALPVI 369
Cdd:PRK06936 238 FVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDK----GSITALYTV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 370 ETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFG 449
Cdd:PRK06936 314 LVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIG 393
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 24658560 450 S---DLDAATQQLLNRGVRLTELLKQGQYVPMAIEDQVAVIY 488
Cdd:PRK06936 394 EyqkGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLE 435
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
48-472 |
2.13e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 163.06 E-value: 2.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 48 AEISNILEERI-LGVAPKADLEETGRVLSIGDGIARVyGLNNIQADEMVEFS-SGLKGMALNLEPDNVGVVVFGNDKLIK 125
Cdd:PRK06820 7 ARLTPRLQQQLtRPSAPPEGLRYRGPIVEIGPTLLRA-SLPGVAQGELCRIEpQGMLAEVVSIEQEMALLSPFASSDGLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 126 QGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGiKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQ 205
Cdd:PRK06820 86 CGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWRELDC-PPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 206 RELIIGDRQTGKTALaidtiinqkrFNEAQDESKKLYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATaSDAAPLQ 285
Cdd:PRK06820 165 RIGIFAAAGVGKSTL----------LGMLCADSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVAT-SDRPALE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 286 YL-APYSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmsPAmGGGSLT 364
Cdd:PRK06820 234 RLkGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG---NS-DRGSIT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 365 ALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAA 444
Cdd:PRK06820 310 AFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIEL 389
|
410 420 430
....*....|....*....|....*....|.
gi 24658560 445 FAQFG---SDLDAATQQLLNRGVRLTELLKQ 472
Cdd:PRK06820 390 LVRVGeyqAGEDLQADEALQRYPAICAFLQQ 420
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
115-482 |
2.73e-44 |
|
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: 162.51 E-value: 2.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 115 VVVFGNDKL----------IKQGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSV 184
Cdd:COG1157 58 VVGFRGDRVllmplgdlegISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 185 REPMQTGIKAVDSLVPIGRGQReliIGdr---qtGKTALaIDTIInqkRFNEAQdeskklycIYVA--IGQKRSTVAQIV 259
Cdd:COG1157 138 TEPLDTGVRAIDGLLTVGRGQR---IGifagsgvGKSTL-LGMIA---RNTEAD--------VNVIalIGERGREVREFI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 260 KRLTDSGAMGYSVIVSATASDAAPLQYLAPYSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGD 339
Cdd:COG1157 203 EDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 340 VFYLHSRLLERAAKmspaMGGGSLTAL------------PVIETqagdvsayiptnVISITDGQIFLETELFYKGIRPAI 407
Cdd:COG1157 283 VFALLPRLLERAGN----GGKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 408 NVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVA------AFAQfGSD--LDAAtqqlLNRGVRLTELLKQGQYVPMA 479
Cdd:COG1157 347 DVLASISRVMPDIVSPEHRALARRLRRLLARYEENEdlirigAYQP-GSDpeLDEA----IALIPAIEAFLRQGMDERVS 421
|
...
gi 24658560 480 IED 482
Cdd:COG1157 422 FEE 424
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
124-487 |
8.71e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 161.04 E-value: 8.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 124 IKQGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGR 203
Cdd:PRK07721 78 IAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 204 GQRELIIGDRQTGKTALaIDTIinqkrfneAQDESKKLYCIYVaIGQKRSTVAQIVKRltDSGAMGY--SVIVSATASDA 281
Cdd:PRK07721 158 GQRVGIFAGSGVGKSTL-MGMI--------ARNTSADLNVIAL-IGERGREVREFIER--DLGPEGLkrSIVVVATSDQP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 282 APLQYLAPYSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmspAMGGG 361
Cdd:PRK07721 226 ALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG----TNASG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 362 SLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYRE 441
Cdd:PRK07721 302 SITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQN 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 24658560 442 VAAFAQFGS-------DLDAATQqllnRGVRLTELLKQGQYVPMAIEDQVAVI 487
Cdd:PRK07721 382 SEDLINIGAykrgssrEIDEAIQ----FYPQIISFLKQGTDEKATFEESIQAL 430
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
50-449 |
4.90e-43 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 159.16 E-value: 4.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 50 ISNILEERILGVApkaDLEETGRVLSIGDGIARVYGLNN---------------IQADEMVEFSsglKGMALnLEPdnvg 114
Cdd:PRK09099 8 LADALERELAALP---AVRRTGKVVEVIGTLLRVSGLDVtlgelcelrqrdgtlLQRAEVVGFS---RDVAL-LSP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 115 vvvFGNDKLIKQGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKA 194
Cdd:PRK09099 77 ---FGELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 195 VDSLVPIGRGQRELIIGDRQTGKTalaidTIINQKRFNEAQDESkklycIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIV 274
Cdd:PRK09099 154 VDGLMTLGEGQRMGIFAPAGVGKS-----TLMGMFARGTQCDVN-----VIALIGERGREVREFIELILGEDGMARSVVV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 275 SATASDAAPLQYLAPYSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkM 354
Cdd:PRK09099 224 CATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-M 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 355 SPAmggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKL 434
Cdd:PRK09099 303 GET---GSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQ 379
|
410
....*....|....*
gi 24658560 435 ELAQYREVAAFAQFG 449
Cdd:PRK09099 380 LLAKHREVETLLQVG 394
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
67-473 |
7.00e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 158.70 E-value: 7.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 67 LEETGRVLSIGDgIARVyglnnIQADEMvefSSGLkGMALNLEPDNVGVVVFGNDKLIKQGDIVKRTGAIVDVPVGDELL 146
Cdd:PRK08472 30 IEADGLNPSVGD-IVKI-----ESSDNG---KECL-GMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 147 GRVVDALGNAIDGKGAINTkDRFRVGIKAPgIIP--RVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTALaIDT 224
Cdd:PRK08472 100 GRVVDPLGRPIDGKGAIDY-ERYAPIMKAP-IAAmkRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTL-MGM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 225 IInqkRFNEAQdeskklycIYVA--IGQKRSTVAQ-IVKRLtdSGAMGYSVIVSATASDAAPLQYLAPYSGCAMGEYFRD 301
Cdd:PRK08472 177 IV---KGCLAP--------IKVValIGERGREIPEfIEKNL--GGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 302 KGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSpamGGGSLTALPVIETQAGDVSAYIP 381
Cdd:PRK08472 244 QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEE---GKGSITAFFTVLVEGDDMSDPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 382 TNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYRE------VAAFaQFGSD--LD 453
Cdd:PRK08472 321 DQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKEnevlirIGAY-QKGNDkeLD 399
|
410 420
....*....|....*....|
gi 24658560 454 AAtqqlLNRGVRLTELLKQG 473
Cdd:PRK08472 400 EA----ISKKEFMEQFLKQN 415
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
139-479 |
1.57e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 149.88 E-value: 1.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 139 VPVGDELLGRVVDALGNAIDGKGAINTKDRfrVGIKAPGIIP--RVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTG 216
Cdd:PRK05688 103 LPMGMSMLGRVLDGAGRALDGKGPMKAEDW--VPMDGPTINPlnRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 217 KTALaidtIINQKRFNEAQdeskklycIYVA--IGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAaPLQYLAPYSGCA 294
Cdd:PRK05688 181 KSVL----LGMMTRFTEAD--------IIVVglIGERGREVKEFIEHILGEEGLKRSVVVASPADDA-PLMRLRAAMYCT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 295 -MGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPamGGGSLTALPVIETQA 373
Cdd:PRK05688 248 rIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEP--GGGSITAFYTVLSEG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 374 GDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYRE------VAAFAQ 447
Cdd:PRK05688 326 DDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQsrdlisVGAYVA 405
|
330 340 350
....*....|....*....|....*....|....
gi 24658560 448 FGsdlDAATQQLLNRGVRLTELLKQG--QYVPMA 479
Cdd:PRK05688 406 GG---DPETDLAIARFPHLVQFLRQGlrENVSLA 436
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
139-473 |
1.37e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 144.07 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 139 VPVGDELLGRVVDALGNAIDGKGAINTKDRfrVGIKAPGIIP--RVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTG 216
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIYTDQR--ASRHSPPINPlsRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 217 KTA-LAIDTiinqkRFNEAQdeskklyCIYVA-IGQKRSTVAQIVKRLTDSGAMGYSVIVSATAsDAAPLQYLapySGC- 293
Cdd:PRK08972 175 KSVlLGMMT-----RGTTAD-------VIVVGlVGERGREVKEFIEEILGEEGRARSVVVAAPA-DTSPLMRL---KGCe 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 294 ---AMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPamGGGSLTALPVIE 370
Cdd:PRK08972 239 tatTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 371 TQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYRE------VAA 444
Cdd:PRK08972 317 TEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQnrdlisIGA 396
|
330 340
....*....|....*....|....*....
gi 24658560 445 FAQfGSdlDAATQQLLNRGVRLTELLKQG 473
Cdd:PRK08972 397 YKQ-GS--DPRIDNAIRLQPAMNAFLQQT 422
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
115-482 |
3.31e-37 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 142.83 E-value: 3.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 115 VVVFGNDKLI------KQG----DIVKRTGAIVDVPVGDELLGRVVDALGNAI---DGKGAINTKDRFR-VGIKAPGIIP 180
Cdd:PRK08149 48 VVGFQRERTIlslignAQGlsrqVVLKPTGKPLSVWVGEALLGAVLDPTGKIVerfDAPPTVGPISEERvIDVAPPSYAE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 181 RVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTALaIDTIINQkrfNEAQdeskklycIYVA--IGQKRSTVAQI 258
Cdd:PRK08149 128 RRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSL-MNMLIEH---SEAD--------VFVIglIGERGREVTEF 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 259 VKRLTDSGAMGYSVIVSATaSDAAPLQYL-APYSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYP 337
Cdd:PRK08149 196 VESLRASSRREKCVLVYAT-SDFSSVDRCnAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 338 GDVFYLHSRLLERAAkmspAMGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVG 417
Cdd:PRK08149 275 ASVFDSLPRLLERPG----ATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVF 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24658560 418 SAAQTKAMKQVAGSMKLELAQYREVAAFAQFG-------SDLDAAtqqlLNRGVRLTELLKQGQYVPMAIED 482
Cdd:PRK08149 351 GQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGeyrrgenADNDRA----MDKRPALEAFLKQDVAEKSSFSD 418
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
71-472 |
4.74e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 139.75 E-value: 4.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 71 GRVLSIGDGIARVYGLNN-IQADEMVEFSSGLK---GMALNLEPDNVGVVVFGNDKLIKQGDIVKRTGAIVDVPvGDELL 146
Cdd:PRK06002 28 GTVSEVTASHYRVRGLSRfVRLGDFVAIRADGGthlGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGPLRIRP-DPSWK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 147 GRVVDALGNAIDGKGAINTKDRFR-VGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTAL----- 220
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLlamla 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 221 ---AIDTIInqkrfneaqdeskklyciyVA-IGQKRSTVAQIVKRlTDSGAMGYSVIVSATASDAAPLQYLAPYSGCAMG 296
Cdd:PRK06002 187 radAFDTVV-------------------IAlVGERGREVREFLED-TLADNLKKAVAVVATSDESPMMRRLAPLTATAIA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 297 EYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmsP-AMGGGSLTALPVIETQAGD 375
Cdd:PRK06002 247 EYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAG---PgAEGGGSITGIFSVLVDGDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 376 VSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYRE------VAAFaQFG 449
Cdd:PRK06002 324 HNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdlrlIGGY-RAG 402
|
410 420
....*....|....*....|....*
gi 24658560 450 SD--LDAATQQLlnrgVRLTELLKQ 472
Cdd:PRK06002 403 SDpdLDQAVDLV----PRIYEALRQ 423
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
69-135 |
6.84e-36 |
|
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: 128.34 E-value: 6.84e-36
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24658560 69 ETGRVLSIGDGIARVYGLNNIQADEMVEFSSGLKGMALNLEPDNVGVVVFGNDKLIKQGDIVKRTGA 135
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
139-415 |
1.04e-34 |
|
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: 131.96 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 139 VPVGDELLGRVVDALGNAIDGKGAINTKDRfrVGIKAPGIIP--RVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTG 216
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDGGPPILPEDY--LDINGPPINPvaRIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 217 KTALAIdTIINQKRFneaQDESKKLYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAAPLQYLAPYSGCAMG 296
Cdd:cd01135 82 HNELAA-QIARQAGV---VGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 297 EYFR-DKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMSPAmgGGSLTALPVIETQ 372
Cdd:cd01135 158 EYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTMP 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 24658560 373 AGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSR 415
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
141-472 |
1.63e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 135.40 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 141 VGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTAL 220
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 221 aIDTIinqKRFNEAQdeskklYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATAsDAAPLQYLAPYSGC-AMGEYF 299
Cdd:PRK07196 172 -LGMI---TRYTQAD------VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPA-DESPLMRIKATELChAIATYY 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 300 RDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmspAMGGGSLTALPVIETQAGDVSAY 379
Cdd:PRK07196 241 RDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGN---SSGNGTMTAIYTVLAEGDDQQDP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 380 IPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDL---DAAT 456
Cdd:PRK07196 318 IVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVagaDPMA 397
|
330
....*....|....*.
gi 24658560 457 QQLLNRGVRLTELLKQ 472
Cdd:PRK07196 398 DQAVHYYPAITQFLRQ 413
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
139-482 |
6.99e-34 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 133.54 E-value: 6.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 139 VPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIpRVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 218
Cdd:PRK07594 91 VPVGEALLGRVIDGFGRPLDGRELPDVCWKDYDAMPPPAMV-RQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 219 AL------AIDTIINqkrfneaqdeskklycIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAAPLQYLAPYSG 292
Cdd:PRK07594 170 TLlamlcnAPDADSN----------------VLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 293 CAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmspaMGG-GSLTALPVIET 371
Cdd:PRK07594 234 TTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTVLV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 372 QAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGS- 450
Cdd:PRK07594 309 EGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEy 388
|
330 340 350
....*....|....*....|....*....|....
gi 24658560 451 --DLDAATQQLLNRGVRLTELLKQGQYVPMAIED 482
Cdd:PRK07594 389 qrGVDTDTDKAIDTYPDICTFLRQSKDEVCGPEL 422
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
139-482 |
1.40e-32 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 130.29 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 139 VPVGDELLGRVVDALGNAIDGKGAINTKdrFRVGIKAPGIIP--RVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTG 216
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTG--ETGALITPPFNPlqRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 217 KTALaidtIINQKRFNEAQdeskklyCIYVA-IGQKRSTVAQIVKRLTDSGAMGYSVIVSATAsDAAPLQYL--APYSgC 293
Cdd:PRK07960 188 KSVL----LGMMARYTQAD-------VIVVGlIGERGREVKDFIENILGAEGRARSVVIAAPA-DVSPLLRMqgAAYA-T 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 294 AMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmSPAMGGGSLTALPVIETQA 373
Cdd:PRK07960 255 RIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG--NGISGGGSITAFYTVLTEG 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 374 GDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYRE------VAAFAQ 447
Cdd:PRK07960 333 DDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFQRnrdlvsVGAYAK 412
|
330 340 350
....*....|....*....|....*....|....*....
gi 24658560 448 fGSDldaatqQLLNRGVRL----TELLKQGQYVPMAIED 482
Cdd:PRK07960 413 -GSD------PMLDKAIALwpqlEAFLQQGIFERADWED 444
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
106-488 |
6.49e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 119.31 E-value: 6.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 106 LNLEPDNVGVVVFGNDKLIKQGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDgKGAINTKDRfRVGIKAPGI--IPRVS 183
Cdd:PRK06793 58 IAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLN-EEAENIPLQ-KIKLDAPPIhaFEREE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 184 VREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTALaIDTIinqkrfneAQDESKKLYCIYVaIGQKRSTVAQIVKRLT 263
Cdd:PRK06793 136 ITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTL-LGMI--------AKNAKADINVISL-VGERGREVKDFIRKEL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 264 DSGAMGYSVIVSATASDAAPLQYLAPYSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPgreaYPGDVFYL 343
Cdd:PRK06793 206 GEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 344 HS---RLLERAAKMSpamgGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAA 420
Cdd:PRK06793 282 ESymkKLLERSGKTQ----KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEI 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24658560 421 QTKAMKQVAGSMKLELAQYREVAAFAQFGS----DLDAATQQLLNRGVRLTELLKQGQYVPMAIEDQVAVIY 488
Cdd:PRK06793 358 VSPNHWQLANEMRKILSIYKENELYFKLGTiqenAENAYIFECKNKVEGINTFLKQGRSDSFQFDDIVEAMH 429
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
83-415 |
2.17e-28 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 118.00 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 83 VYGLNNIQADEMVEFSSG----LKGMALNLEPDNVGVVVF-GNDKLIKQGDIVKRTGAIVDVPVGDELLGRVVDALGNAI 157
Cdd:PRK04196 17 VEGVEGVAYGEIVEIELPngekRRGQVLEVSEDKAVVQVFeGTTGLDLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 158 DGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQReliigdrqtgktaLAIdtiinqkrF------ 231
Cdd:PRK04196 97 DGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQK-------------LPI--------Fsgsglp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 232 -NE--AQ--------DESKKLYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAAPLQYLAPYSGCAMGEYFR 300
Cdd:PRK04196 156 hNElaAQiarqakvlGEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 301 -DKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMSpamgG--GSLTALPVIETQAG 374
Cdd:PRK04196 236 fEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIK----GkkGSITQIPILTMPDD 308
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 24658560 375 DVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSR 415
Cdd:PRK04196 309 DITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
139-472 |
1.01e-27 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 115.77 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 139 VPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 218
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 219 ALaIDTIINQkrfneaqdeSKKLYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAAPLQYLAPYSGCAMGEY 298
Cdd:PRK05922 172 SL-LSTIAKG---------SKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 299 FRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPamggGSLTALPVIETQAGDVSA 378
Cdd:PRK05922 242 FRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDK----GSITALYAILHYPNHPDI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 379 YIPTnVISITDGQIFL---ETELFykgiRPAINVGLSVSRvgSAAQTKAMKQVAGSMKLE--LAQYREVAAFAQFGSDLD 453
Cdd:PRK05922 318 FTDY-LKSLLDGHFFLtpqGKALA----SPPIDILTSLSR--SARQLALPHHYAAAEELRslLKAYHEALDIIQLGAYVP 390
|
330
....*....|....*....
gi 24658560 454 AATQQlLNRGVRLTELLKQ 472
Cdd:PRK05922 391 GQDAH-LDRAVKLLPSIKQ 408
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
105-479 |
2.82e-26 |
|
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 211621 [Multi-domain] Cd Length: 461 Bit Score: 111.73 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 105 ALNLEPDNVGVVVFGNDKLIKQGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSV 184
Cdd:TIGR01039 44 AQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 185 REPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTALAIDTIINQKRFNEAqdeskklYCIYVAIGQKRSTVAQIVKRLTD 264
Cdd:TIGR01039 124 VEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGG-------YSVFAGVGERTREGNDLYHEMKE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 265 SGAMGYSVIVSATASDAAPLQYLAPYSGCAMGEYFRD-KGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYL 343
Cdd:TIGR01039 197 SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 344 HSRLLERAAkmspAMGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQT- 422
Cdd:TIGR01039 277 MGELQERIT----STKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVg 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24658560 423 KAMKQVAGSMKLELAQYREVA-AFAQFGSD-LDAATQQLLNRGVRLTELLKQ------------GQYVPMA 479
Cdd:TIGR01039 353 EEHYDVARGVQQILQRYKELQdIIAILGMDeLSEEDKLTVERARRIQRFLSQpffvaevftgqpGKYVPLK 423
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
146-482 |
3.02e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 111.61 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 146 LGRVVDALGNAIDGKGAInTKDRFRVGIKA--PGIIPRVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTALaid 223
Cdd:PRK08927 99 LGRVVNALGEPIDGKGPL-PQGPVPYPLRAppPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVL--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 224 tiINQKRFNEAQDESkklycIYVAIGQKRSTVAQIVKrlTDSGAMGY--SVIVSATASDAAPLQYLAPYSGCAMGEYFRD 301
Cdd:PRK08927 175 --LSMLARNADADVS-----VIGLIGERGREVQEFLQ--DDLGPEGLarSVVVVATSDEPALMRRQAAYLTLAIAEYFRD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 302 KGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmsP-AMGGGSLTALPVIETQAGDVSAYI 380
Cdd:PRK08927 246 QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG---PgPIGEGTITGLFTVLVDGDDHNEPV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 381 PTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSdLDAATQQLL 460
Cdd:PRK08927 323 ADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGA-YRAGSDPEV 401
|
330 340
....*....|....*....|....*.
gi 24658560 461 NRGVR----LTELLKQGQYVPMAIED 482
Cdd:PRK08927 402 DEAIRlnpaLEAFLRQGKDEATSLAE 427
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
133-425 |
1.70e-24 |
|
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: 106.73 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 133 TGAIVDVPVGDELLGRVVDALGNAIDGKGAINTKDRfrVGIKAPGIIP--RVSVREPMQTGIKAVDSLVPIGRGQRELII 210
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDY--LDINGQPINPyaRIYPEEMIQTGISAIDVMNSIARGQKIPIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 211 GD-------------RQTGKTALAIDTIINQKRFNEAqdeskklyCIYVAIGQKRSTvAQIVKR-LTDSGAMGYSVIVSA 276
Cdd:TIGR01040 148 SAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFA--------IVFAAMGVNMET-ARFFKQdFEENGSMERVCLFLN 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 277 TASDAAPLQYLAPYSGCAMGEYFR-DKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMS 355
Cdd:TIGR01040 219 LANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVE 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 356 PAmgGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAM 425
Cdd:TIGR01040 299 GR--NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
106-394 |
1.21e-21 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 97.80 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 106 LNLEPDNVGVVVFGNDKLIKQGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGAINTKdrfRVGIKAPGIIP--RVS 183
Cdd:PRK02118 43 IRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGE---PIEIGGPSVNPvkRIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 184 VREPMQTGIKAVD---SLVpigRGQReliigdrqtgktaLAIDTIINQKrFNE------AQDESKKLycIYVAIGQKRST 254
Cdd:PRK02118 120 PREMIRTGIPMIDvfnTLV---ESQK-------------IPIFSVSGEP-YNAllariaLQAEADII--ILGGMGLTFDD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 255 VAQIVKRLTDSGAMGYSVIVSATASDAAPLQYLAPYSGCAMGEYFR-DKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGR 333
Cdd:PRK02118 181 YLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSN 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24658560 334 EAYPGDvfyLHSRLLERAAKMSPAMGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFL 394
Cdd:PRK02118 261 RGYPGS---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, ... |
425-492 |
6.00e-21 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 86.73 E-value: 6.00e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 425 MKQVAGSMKLELAQYREVAAFAQFGSD--LDAATQQLLNRGVRLTELLKQGQYVPMAIEDQVAVIYCGVR 492
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
139-416 |
1.98e-18 |
|
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: 85.35 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 139 VPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 218
Cdd:cd01133 2 VPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 219 ALAIDTIINQKRFNEAqdeskklYCIYVAIGQKRSTVAQIVKRLTDSGamgysVIVSATASDAApLQY-----------L 287
Cdd:cd01133 82 VLIMELINNIAKAHGG-------YSVFAGVGERTREGNDLYHEMKESG-----VINLDGLSKVA-LVYgqmneppgaraR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 288 APYSGCAMGEYFRD-KGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmspAMGGGSLTAL 366
Cdd:cd01133 149 VALTGLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERIT----STKKGSITSV 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 24658560 367 PVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 416
Cdd:cd01133 225 QAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
68-134 |
4.30e-18 |
|
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: 78.36 E-value: 4.30e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24658560 68 EETGRVLSIGDGIARVYGLNNIQADEMVEFSSGLKGMALNLEPDNVGVVVFGNDKLIKQGDIVKRTG 134
Cdd:pfam02874 3 QVIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
124-220 |
2.08e-17 |
|
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: 84.76 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 124 IKQGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGR 203
Cdd:COG0055 66 LVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAK 145
|
90
....*....|....*..
gi 24658560 204 GqreliigdrqtGKTAL 220
Cdd:COG0055 146 G-----------GKIGL 151
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
186-415 |
5.83e-16 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 78.39 E-value: 5.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 186 EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTalaidtIINQK--RFNEAQdeskklYCIYVAIGQKRSTVAQIVKRL- 262
Cdd:cd01134 58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKT------VISQSlsKWSNSD------VVIYVGCGERGNEMAEVLEEFp 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 263 ------TDSGAMGYSVIVSATASDAAPLQYLAPYSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY 336
Cdd:cd01134 126 elkdpiTGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGY 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 337 PGdvfYLHSRL---LERAAKMSpAMGG----GSLTALPVIETQAGDVSAYIPTNVISITdgQIF--LETELFYKGIRPAI 407
Cdd:cd01134 206 PA---YLGARLaefYERAGRVR-CLGSpgreGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSI 279
|
....*...
gi 24658560 408 NVGLSVSR 415
Cdd:cd01134 280 NWLISYSK 287
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
124-408 |
2.07e-10 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 63.14 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 124 IKQGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGII---PRVSVREpmqTGIKAVDSLVP 200
Cdd:CHL00060 81 LMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTKLSIFE---TGIKVVDLLAP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 201 IGRGQRELIIGDRQTGKTALAIDTIINQKRFN----------EAQDESKKLYciyvaIGQKRSTVAQiVKRLTDS----- 265
Cdd:CHL00060 158 YRRGGKIGLFGGAGVGKTVLIMELINNIAKAHggvsvfggvgERTREGNDLY-----MEMKESGVIN-EQNIAESkvalv 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 266 -GAM----GYSVIVSATASdaaplqylapysgcAMGEYFRDKGKH-ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGD 339
Cdd:CHL00060 232 yGQMneppGARMRVGLTAL--------------TMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPT 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24658560 340 VFYLHSRLLERAAKMSPamggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAIN 408
Cdd:CHL00060 298 LSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 362
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
181-365 |
5.26e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 62.11 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 181 RVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT----ALAidtiinqkRFNEAQdeskklYCIYVAIGQKRSTVA 256
Cdd:PRK04192 204 KLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTvtqhQLA--------KWADAD------IVIYVGCGERGNEMT 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 257 QIVK---RLTD--SGA--MGYSVIVSAT-----ASDAAPLqylapYSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMS 324
Cdd:PRK04192 270 EVLEefpELIDpkTGRplMERTVLIANTsnmpvAAREASI-----YTGITIAEYYRDMGYDVLLMADSTSRWAEALREIS 344
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24658560 325 LLLRRPPGREAYPGdvfYLHSRL---LERAAKMSpAMGG--GSLTA 365
Cdd:PRK04192 345 GRLEEMPGEEGYPA---YLASRLaefYERAGRVK-TLGGeeGSVTI 386
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
244-408 |
1.31e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 61.19 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 244 IYVAIGQKRSTVAQIVKRL-------TDSGAMGYSVIVSATASDAAPLQYLAPYSGCAMGEYFRDKGKHALIIYDDLSKQ 316
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFpklkdpkTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24658560 317 AVAYRQMSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKMSPAMGGGSLTALPVIETQAGDVSAYIPTNVISITDG 390
Cdd:PRK14698 766 AEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKV 842
|
170
....*....|....*...
gi 24658560 391 QIFLETELFYKGIRPAIN 408
Cdd:PRK14698 843 FWALDADLARRRHFPAIN 860
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
70-135 |
1.10e-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: 1.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24658560 70 TGRVLSIGDGIARVYGLNNIQADEMVEF-------SSGLKGMALNLEPDNVGVVVFGNDKLIKQGDIVKRTGA 135
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIergdgnnETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| |
