|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
49-531 |
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: 947.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 49 AEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEG 128
Cdd:COG0056 6 EEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEGIKEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 129 DIVKRTGAIVD----------------------GPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRE 186
Cdd:COG0056 86 DTVKRTGRILSvpvgeallgrvvdplgrpidgkGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 187 LIIGDRQTGKTSIAIDTIINQKrfndgsdeKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYL 266
Cdd:COG0056 166 LIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 267 APYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALP 346
Cdd:COG0056 238 APYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 347 VIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQ 426
Cdd:COG0056 318 IIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 427 FGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVVSQHQALLGTIRA 506
Cdd:COG0056 398 FGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRE 477
|
490 500
....*....|....*....|....*
gi 382546007 507 DGKISEQSDAKLKEIVTNFLAGFEA 531
Cdd:COG0056 478 TGKLDDEIEEKLKAAIEEFKKTFAA 502
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
49-531 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 946.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 49 AEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEG 128
Cdd:PRK09281 6 EEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIKEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 129 DIVKRTGAIVD----------------------GPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRE 186
Cdd:PRK09281 86 DTVKRTGRILEvpvgeallgrvvnplgqpidgkGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 187 LIIGDRQTGKTSIAIDTIINQKrfndgsdeKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYL 266
Cdd:PRK09281 166 LIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 267 APYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALP 346
Cdd:PRK09281 238 APYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 347 VIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQ 426
Cdd:PRK09281 318 IIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 427 FGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVVSQHQALLGTIRA 506
Cdd:PRK09281 398 FGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRE 477
|
490 500
....*....|....*....|....*
gi 382546007 507 DGKISEQSDAKLKEIVTNFLAGFEA 531
Cdd:PRK09281 478 TKDLSDEIEAKLKAAIEEFKKTFAA 502
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
50-529 |
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: 778.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 50 EMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGD 129
Cdd:TIGR00962 6 EISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIREGS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 130 IVKRTGAIVD----------------------GPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQREL 187
Cdd:TIGR00962 86 TVKRTGRILEvpvgdgllgrvvnalgepidgkGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQREL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 188 IIGDRQTGKTSIAIDTIINQKrfndgsdeKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLA 267
Cdd:TIGR00962 166 IIGDRQTGKTAVAIDTIINQK--------DSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 268 PYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPV 347
Cdd:TIGR00962 238 PYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 348 IETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQF 427
Cdd:TIGR00962 318 IETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 428 GSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVVSQHQALLGTIRAD 507
Cdd:TIGR00962 398 ASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTT 477
|
490 500
....*....|....*....|..
gi 382546007 508 GKISEQSDAKLKEIVTNFLAGF 529
Cdd:TIGR00962 478 KKLTEELEAKLKEALKNFKKTF 499
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
66-529 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 711.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 66 VDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAI-------- 137
Cdd:CHL00059 2 VKIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIaqipvsea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 138 ------------VDGP--IGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDT 203
Cdd:CHL00059 82 ylgrvvnalakpIDGKgeISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 204 IINQKrfndGSDekkkLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGK 283
Cdd:CHL00059 162 ILNQK----GQN----VICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 284 HALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNV 363
Cdd:CHL00059 234 HTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 364 ISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGV 443
Cdd:CHL00059 314 ISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 444 RLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVVSQHQALLGTIRADGKISEQSDAKLKEIVT 523
Cdd:CHL00059 394 RLRELLKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQ 473
|
....*.
gi 382546007 524 NFLAGF 529
Cdd:CHL00059 474 EQLELF 479
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
45-531 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 695.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 45 KTGTAEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKL 124
Cdd:PRK13343 2 KSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 125 IKEGDIVKRTGAIVD----------------------GPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGR 182
Cdd:PRK13343 82 ILAGTEVRRTGRVLEvpvgdgllgrvidplgrpldggGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 183 GQRELIIGDRQTGKTSIAIDTIINQKrfndGSDekkkLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAP 262
Cdd:PRK13343 162 GQRELIIGDRQTGKTAIAIDAIINQK----DSD----VICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 263 LQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSL 342
Cdd:PRK13343 234 LQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 343 TALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVA 422
Cdd:PRK13343 314 TALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 423 AFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVVSQHQALLG 502
Cdd:PRK13343 394 AFTRFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSL 473
|
490 500
....*....|....*....|....*....
gi 382546007 503 TIRADGKISEQSDAKLKEIVTNFLAGFEA 531
Cdd:PRK13343 474 ALESPRELDEAWLAALEEILREAGERFAA 502
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
128-396 |
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: 567.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 128 GDIVKRTGAIVDG--PIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTII 205
Cdd:cd01132 12 GRVVDALGNPIDGkgPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTAIAIDTII 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 206 NQKRfndgsdekKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHA 285
Cdd:cd01132 92 NQKG--------KKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 286 LIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVIS 365
Cdd:cd01132 164 LIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTNVIS 243
|
250 260 270
....*....|....*....|....*....|.
gi 382546007 366 ITDGQIFLETELFYKGIRPAINVGLSVSRVG 396
Cdd:cd01132 244 ITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
65-513 |
1.02e-175 |
|
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: 504.69 E-value: 1.02e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 65 SVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDGPIG- 143
Cdd:TIGR03324 22 QLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERTGRVMDVPVGd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 144 ---------------------SKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAID 202
Cdd:TIGR03324 102 gllgrvvdplgrpldgggplaSSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDRQTGKTAIAID 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 203 TIINQKRFNdgsdekkkLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNG 282
Cdd:TIGR03324 182 TILNQKGRN--------VLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSIGEHFMEQG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 283 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTN 362
Cdd:TIGR03324 254 RDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQNISAYIPTN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 363 VISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRG 442
Cdd:TIGR03324 334 LISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDENTRKTIEHG 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 382546007 443 VRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVVSQHQALLGTIRADGKISEQ 513
Cdd:TIGR03324 414 RRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSDE 484
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
128-395 |
8.15e-122 |
|
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: 358.69 E-value: 8.15e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 128 GDIVKRTGAIVDG--PIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTII 205
Cdd:cd19476 10 GRILDGLGEPLDGlpPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLAR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 206 NQKrfndgsdEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHA 285
Cdd:cd19476 90 NQA-------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 286 LIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDafGGGSLTALPVIETQAGDVSAYIPTNVIS 365
Cdd:cd19476 163 LLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNTFA 240
|
250 260 270
....*....|....*....|....*....|
gi 382546007 366 ITDGQIFLETELFYKGIRPAINVGLSVSRV 395
Cdd:cd19476 241 ILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
104-486 |
1.59e-117 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 358.58 E-value: 1.59e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 104 GMSLNLEPDN-VGVVVFGNDKLIKEGDIVKRTGAIVDGPIG--------------------SKTRR---------RVGLK 153
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGagvlgkvvnplghevpvgllTRSRAlleseqtlgKVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 154 APGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGSDEKKKLYCIYVAIGQKRST 233
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 234 VAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGRE 313
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGRE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 314 AYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVS 393
Cdd:PTZ00185 320 AYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVS 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 394 RVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATqqlLSRGVRLTELLKQGQysPMAIEEQVAVIYAGVRGY 473
Cdd:PTZ00185 400 RVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNALVSLYACLNGY 474
|
410
....*....|...
gi 382546007 474 LDKLEPSKITKFE 486
Cdd:PTZ00185 475 LDDVKVNYAKLYE 487
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
170-393 |
4.33e-116 |
|
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: 341.64 E-value: 4.33e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 170 GIKAVDSLVPIGRGQRELIIGDRQTGKTSIAiDTIINQKRFNdgsdekkklYCIYVAIGQKRSTVAQLVKRLTDADAMKY 249
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD---------VVVYALIGERGREVREFIEELLGSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 250 TIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLER 329
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 382546007 330 AAKMNDafGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVS 393
Cdd:pfam00006 151 AGRVKG--KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
153-456 |
3.95e-100 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 311.52 E-value: 3.95e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 153 KAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKrfndgsdeKKKLYCIYVAIGQKRS 232
Cdd:PRK07165 113 LAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQK--------NTNVKCIYVAIGQKRE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 233 TVAQLVKRLTDADAMKYTIVVSAtASDAAPLQYLAPYSGCSMGE---YFRDngkhALIIYDDLSKQAVAYRQMSLLLRRP 309
Cdd:PRK07165 185 NLSRIYETLKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAEnisYNDD----VLIVFDDLTKHANIYREIALLTNKP 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 310 PGREAYPGDVFYLHSRLLERAAKMNdafGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVG 389
Cdd:PRK07165 260 VGKEAFPGDMFFAHSKLLERAGKFK---NRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDID 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 382546007 390 LSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSP 456
Cdd:PRK07165 337 LSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKGKMIEKMFNQKGFSL 403
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
404-529 |
6.18e-67 |
|
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: 211.84 E-value: 6.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 404 MKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKIT 483
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 382546007 484 KFENAFLSHVVSQHQALLGTIRADGKISEQSDAKLKEIVTNFLAGF 529
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
400-525 |
1.86e-65 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 208.06 E-value: 1.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 400 QTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEP 479
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 382546007 480 SKITKFENAFLSHVVSQHQALLGTIRADGKISEQSDAKLKEIVTNF 525
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
128-395 |
3.54e-37 |
|
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: 138.08 E-value: 3.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 128 GDIVKRTGAIVDGPIGSKTRRRVGLKAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTsiaidTII 205
Cdd:cd01136 10 GRVIDALGEPLDGKGLPDEPERRPLIAAPPNPlkRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS-----TLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 206 NQKRFNDGSDekkklycIYVA--IGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGK 283
Cdd:cd01136 85 GMIARNTDAD-------VNVIalIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 284 HALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmndaFGGGSLTALPVIETQAGDVSAYIPTNV 363
Cdd:cd01136 158 KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN----GEKGSITAFYTVLVEGDDFNDPIADEV 233
|
250 260 270
....*....|....*....|....*....|..
gi 382546007 364 ISITDGQIFLETELFYKGIRPAINVGLSVSRV 395
Cdd:cd01136 234 RSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
70-136 |
2.01e-35 |
|
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: 126.80 E-value: 2.01e-35
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 382546007 70 ETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGA 136
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
155-466 |
1.12e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 132.54 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 155 PGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTS----IAIDTiinQKRFNdgsdekkklycIYVAIGQK 230
Cdd:PRK07721 130 PNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTlmgmIARNT---SADLN-----------VIALIGER 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 231 RSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPP 310
Cdd:PRK07721 196 GREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPP 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 311 GREAYPGDVFYLHSRLLERAAkmndAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGL 390
Cdd:PRK07721 276 TTKGYTPSVFAILPKLLERTG----TNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLK 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 391 SVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGS-------DLDAATQqllsRGVRLTELLKQGQYSPMAIEEQV 463
Cdd:PRK07721 352 SVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAykrgssrEIDEAIQ----FYPQIISFLKQGTDEKATFEESI 427
|
...
gi 382546007 464 AVI 466
Cdd:PRK07721 428 QAL 430
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
128-457 |
1.01e-32 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 129.93 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 128 GDIVKRTGAIVDG--PIGSKTRRRVGlKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAidtii 205
Cdd:PRK06820 107 GRILDGLGAPIDGgpPLTGQWRELDC-PPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLL----- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 206 nqKRFNDGSDEKkklyCIYVA-IGQKRSTVAQLVKRLTDADAMKYTIVVSATaSDAAPLQYL-APYSGCSMGEYFRDNGK 283
Cdd:PRK06820 181 --GMLCADSAAD----VMVLAlIGERGREVREFLEQVLTPEARARTVVVVAT-SDRPALERLkGLSTATTIAEYFRDRGK 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 284 HALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDafggGSLTALPVIETQAGDVSAYIPTNV 363
Cdd:PRK06820 254 KVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDR----GSITAFYTVLVEGDDMNEPVADEV 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 364 ISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFG---SDLDAATQQLLS 440
Cdd:PRK06820 330 RSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGeyqAGEDLQADEALQ 409
|
330
....*....|....*....
gi 382546007 441 RGVRLTELLKQ--GQYSPM 457
Cdd:PRK06820 410 RYPAICAFLQQdhSETAHL 428
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
128-471 |
1.80e-32 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 129.10 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 128 GDIVKRTGAIVDG--PIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIaIDTII 205
Cdd:PRK06936 105 GRVLDGLGQPFDGghPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTL-LASLI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 206 NQKRFNdgsdekkklYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHA 285
Cdd:PRK06936 184 RSAEVD---------VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 286 LIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNDAfggGSLTALPVIETQAGDVSAYIPTNVIS 365
Cdd:PRK06936 255 LLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG-QSDK---GSITALYTVLVEGDDMTEPVADETRS 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 366 ITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGS---DLDAATQQLLSRG 442
Cdd:PRK06936 331 ILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEyqkGQDKEADQAIERI 410
|
330 340
....*....|....*....|....*....
gi 382546007 443 VRLTELLKQGQYSPMAIEEQVAVIYAGVR 471
Cdd:PRK06936 411 GAIRGFLRQGTHELSHFNETLNLLETLTQ 439
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
140-428 |
3.19e-31 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 125.65 E-value: 3.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 140 GPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIaidtiinQKRFNDGSDekkk 219
Cdd:PRK09099 120 GPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTL-------MGMFARGTQ---- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 220 lyC---IYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQA 296
Cdd:PRK09099 189 --CdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 297 VAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNDAfggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETE 376
Cdd:PRK09099 267 RAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-MGET---GSITALYTVLAEDESGSDPIAEEVRGILDGHMILSRE 342
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 382546007 377 LFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFG 428
Cdd:PRK09099 343 IAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVG 394
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
128-468 |
5.96e-31 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 124.72 E-value: 5.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 128 GDIVKRTGAIV---DGPIGSKTR---RRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIaI 201
Cdd:PRK08149 90 GAVLDPTGKIVerfDAPPTVGPIseeRVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSL-M 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 202 DTIINQKRFNdgsdekkklycIYVA--IGQKRSTVAQLVKRLTDADAMKYTIVVSATaSDAAPLQYL-APYSGCSMGEYF 278
Cdd:PRK08149 169 NMLIEHSEAD-----------VFVIglIGERGREVTEFVESLRASSRREKCVLVYAT-SDFSSVDRCnAALVATTVAEYF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 279 RDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmndAFGGGSLTALPVIETQAGDVSAY 358
Cdd:PRK08149 237 RDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPG----ATLAGSITAFYTVLLESEEEPDP 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 359 IPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFG-------SDL 431
Cdd:PRK08149 313 IGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGeyrrgenADN 392
|
330 340 350
....*....|....*....|....*....|....*..
gi 382546007 432 DAATQQllsRGVrLTELLKQGQYSPMAIEEQVAVIYA 468
Cdd:PRK08149 393 DRAMDK---RPA-LEAFLKQDVAEKSSFSDTLERLNE 425
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
128-472 |
8.62e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 124.46 E-value: 8.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 128 GDIVKRTGAIVDGPIGSKTRRRVGLKAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKtSIAIDTIi 205
Cdd:PRK05688 111 GRVLDGAGRALDGKGPMKAEDWVPMDGPTINPlnRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK-SVLLGMM- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 206 nqKRFNDGSdekkklycIYVA--IGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAaPLQYLAPYSGCS-MGEYFRDNG 282
Cdd:PRK05688 189 --TRFTEAD--------IIVVglIGERGREVKEFIEHILGEEGLKRSVVVASPADDA-PLMRLRAAMYCTrIAEYFRDKG 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 283 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNDAFGGGSLTALPVIETQAGDVSAYIPTN 362
Cdd:PRK05688 258 KNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEGDDQQDPIADS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 363 VISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYRE------VAAFAQFGsdlDAATQ 436
Cdd:PRK05688 336 ARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQsrdlisVGAYVAGG---DPETD 412
|
330 340 350
....*....|....*....|....*....|....*....
gi 382546007 437 QLLSRGVRLTELLKQG--QYSPMA-IEEQVAVIYAGVRG 472
Cdd:PRK05688 413 LAIARFPHLVQFLRQGlrENVSLAqSREQLAAIFAPAAG 451
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
155-460 |
1.04e-27 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 115.44 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 155 PGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTsiaidTIINQKRFNDGSDEKkklycIYVAIGQKRSTV 234
Cdd:PRK07594 127 PPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKS-----TLLAMLCNAPDADSN-----VLVLIGERGREV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 235 AQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREA 314
Cdd:PRK07594 197 REFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 315 YPGDVFYLHSRLLERAAkMNDAfggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSR 394
Cdd:PRK07594 277 YPPGVFSALPRLLERTG-MGEK---GSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSR 352
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 382546007 395 VGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGS---DLDAATQQLLSRGVRLTELLKQGQYSPMAIE 460
Cdd:PRK07594 353 VFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEyqrGVDTDTDKAIDTYPDICTFLRQSKDEVCGPE 421
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
135-461 |
1.54e-27 |
|
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: 114.74 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 135 GAIVDG---PIGSK----TRRRVGLKAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQReliIGdr---qtGKTS---- 198
Cdd:COG1157 100 GRVLDGlgrPLDGKgplpGEERRPLDAPPPNPleRARITEPLDTGVRAIDGLLTVGRGQR---IGifagsgvGKSTllgm 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 199 IAidtiinqkRFNDgSDekkklycIYVA--IGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGE 276
Cdd:COG1157 177 IA--------RNTE-AD-------VNVIalIGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 277 YFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmndaFGGGSLTAL----------- 345
Cdd:COG1157 241 YFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN----GGKGSITAFytvlvegddmn 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 346 -PVIETqagdvsayiptnVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVA-- 422
Cdd:COG1157 317 dPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEdl 384
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 382546007 423 ----AFAQfGSD--LDAAtqqlLSRGVRLTELLKQGQYSPMAIEE 461
Cdd:COG1157 385 irigAYQP-GSDpeLDEA----IALIPAIEAFLRQGMDERVSFEE 424
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
72-451 |
1.36e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 112.40 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 72 GRVLSIGDGIARVHGL-RNVQAEEMVEFSSGlKGMSL----NLEPDNVGVVVFGNDKLIKEGDIVKRTGAI--------- 137
Cdd:PRK06002 28 GTVSEVTASHYRVRGLsRFVRLGDFVAIRAD-GGTHLgevvRVDPDGVTVKPFEPRIEIGLGDAVFRKGPLrirpdpswk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 138 ----------VDG--PIGSKTRRR-VGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSI----- 199
Cdd:PRK06002 107 grvinalgepIDGlgPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLlamla 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 200 ---AIDTIInqkrfndgsdekkklyciyVA-IGQKRSTVAQLVKRlTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMG 275
Cdd:PRK06002 187 radAFDTVV-------------------IAlVGERGREVREFLED-TLADNLKKAVAVVATSDESPMMRRLAPLTATAIA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 276 EYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDafGGGSLTALPVIETQAGDV 355
Cdd:PRK06002 247 EYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLVDGDDH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 356 SAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYRE------VAAFaQFGS 429
Cdd:PRK06002 325 NDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdlrlIGGY-RAGS 403
|
410 420
....*....|....*....|....
gi 382546007 430 D--LDAATQQLlsrgVRLTELLKQ 451
Cdd:PRK06002 404 DpdLDQAVDLV----PRIYEALRQ 423
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
128-451 |
1.97e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 111.91 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 128 GDIVKRTGAIVDG--PIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKtSIAIDTII 205
Cdd:PRK07196 98 GRVINGLGEPLDGkgQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGK-SVLLGMIT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 206 NQKRFNdgsdekkklYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATAsDAAPLQYLAPYSGC-SMGEYFRDNGKH 284
Cdd:PRK07196 177 RYTQAD---------VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPA-DESPLMRIKATELChAIATYYRDKGHD 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 285 ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmnDAFGGGSLTALPVIETQAGDVSAYIPTNVI 364
Cdd:PRK07196 247 VLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQDPIVDCAR 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 365 SITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDL---DAATQQLLSR 441
Cdd:PRK07196 324 AVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVagaDPMADQAVHY 403
|
330
....*....|
gi 382546007 442 GVRLTELLKQ 451
Cdd:PRK07196 404 YPAITQFLRQ 413
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
64-452 |
5.11e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 110.55 E-value: 5.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 64 TSVDLEETGRVLSIGDgIARVHGLRNvQAEEMvefssglkGMSLNLEPDNVGVVVFG-------NDK--LIKEGDIVKRT 134
Cdd:PRK08472 26 SPTIIEADGLNPSVGD-IVKIESSDN-GKECL--------GMVVVIEKEQFGISPFSfiegfkiGDKvfISKEGLNIPVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 135 ----GAIVDG---PIGSKTRRRVGLKAPGIIPRIS------VREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKtSIAI 201
Cdd:PRK08472 96 rnllGRVVDPlgrPIDGKGAIDYERYAPIMKAPIAamkrglIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGK-STLM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 202 DTIINqkrfndGSDEKKKLyciyVA-IGQKRSTVAQLVKRLTDADaMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRD 280
Cdd:PRK08472 175 GMIVK------GCLAPIKV----VAlIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 281 NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNdafGGGSLTALPVIETQAGDVSAYIP 360
Cdd:PRK08472 244 QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEE---GKGSITAFFTVLVEGDDMSDPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 361 TNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYRE------VAAFaQFGSD--LD 432
Cdd:PRK08472 321 DQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKEnevlirIGAY-QKGNDkeLD 399
|
410 420
....*....|....*....|
gi 382546007 433 AAtqqlLSRGVRLTELLKQG 452
Cdd:PRK08472 400 EA----ISKKEFMEQFLKQN 415
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
128-467 |
5.68e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 110.45 E-value: 5.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 128 GDIVKRTGAIVDGPIGSKTRRRVGLKAPGI--IPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTsiaidTII 205
Cdd:PRK06793 99 GKVLSANGEVLNEEAENIPLQKIKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKS-----TLL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 206 NQKRFNDGSDEKkklycIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHA 285
Cdd:PRK06793 174 GMIAKNAKADIN-----VISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 286 LIIYDDLSKQAVAYRQMSLLLRRPPgreaYPGDVFYLHS---RLLERAAKMNDafggGSLTALPVIETQAGDVSAYIPTN 362
Cdd:PRK06793 249 LLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK----GSITGIYTVLVDGDDLNGPVPDL 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 363 VISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGS----DLDAATQQL 438
Cdd:PRK06793 321 ARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTiqenAENAYIFEC 400
|
330 340
....*....|....*....|....*....
gi 382546007 439 LSRGVRLTELLKQGQYSPMAIEEQVAVIY 467
Cdd:PRK06793 401 KNKVEGINTFLKQGRSDSFQFDDIVEAMH 429
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
128-438 |
1.30e-25 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 109.49 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 128 GDIVKRTGAIVDGPIGSKTRRRVGLKAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKtSIAIDTIi 205
Cdd:PRK07960 118 GRVLDGSGKPLDGLPAPDTGETGALITPPFNPlqRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK-SVLLGMM- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 206 nqKRFNDGSdekkklyCIYVA-IGQKRSTVAQLVKRLTDADAMKYTIVVSATAsDAAPLQYL--APYSgCSMGEYFRDNG 282
Cdd:PRK07960 196 --ARYTQAD-------VIVVGlIGERGREVKDFIENILGAEGRARSVVIAAPA-DVSPLLRMqgAAYA-TRIAEDFRDRG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 283 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNDAFGGGSLTALPVIETQAGDVSAYIPTN 362
Cdd:PRK07960 265 QHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG--NGISGGGSITAFYTVLTEGDDQQDPIADS 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 363 VISITDGQIFLETELFYKGIRPAINVGLSVSRVGSA-------AQTRAMKQ-----------------VAGTMKL---EL 415
Cdd:PRK07960 343 ARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAlideqhyARVRQFKQllssfqrnrdlvsvgayAKGSDPMldkAI 422
|
330 340
....*....|....*....|....*..
gi 382546007 416 AQYREVAAFAQFG----SDLDAATQQL 438
Cdd:PRK07960 423 ALWPQLEAFLQQGiferADWEDSLQAL 449
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
140-452 |
5.23e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 107.48 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 140 GPIgsKTRRRVGLKAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKtSIAIDTIINqkrfndGSDEK 217
Cdd:PRK08972 119 GPI--YTDQRASRHSPPINPlsRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGK-SVLLGMMTR------GTTAD 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 218 kklyCIYVA-IGQKRSTVAQLVKRLTDADAMKYTIVVSATAsDAAPLQYLapySGC----SMGEYFRDNGKHALIIYDDL 292
Cdd:PRK08972 190 ----VIVVGlVGERGREVKEFIEEILGEEGRARSVVVAAPA-DTSPLMRL---KGCetatTIAEYFRDQGLNVLLLMDSL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 293 SKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIF 372
Cdd:PRK08972 262 TRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAG--NGGPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIV 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 373 LETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYRE------VAAFAQfGSdlDAATQQLLSRGVRLT 446
Cdd:PRK08972 340 LSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQnrdlisIGAYKQ-GS--DPRIDNAIRLQPAMN 416
|
....*.
gi 382546007 447 ELLKQG 452
Cdd:PRK08972 417 AFLQQT 422
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
160-394 |
3.99e-24 |
|
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: 101.92 E-value: 3.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 160 RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIdTIINQKRFNDGSDEKKklyCIYVAIGQKRSTVAQLVK 239
Cdd:cd01135 46 RIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLPHNELAA-QIARQAGVVGSEENFA---IVFAAMGVTMEEARFFKD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 240 RLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR-DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGd 318
Cdd:cd01135 122 DFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG- 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 382546007 319 vfYLHSRL---LERAAKMNDAfgGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSR 394
Cdd:cd01135 201 --YMYTDLatiYERAGRVEGR--KGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
404-471 |
1.30e-22 |
|
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: 91.35 E-value: 1.30e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 404 MKQVAGTMKLELAQYREVAAFAQFGSD--LDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVR 471
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
135-458 |
3.81e-21 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 96.13 E-value: 3.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 135 GAIVDG---PIGS-----KTRRRVGLKAPgiiPRISVREPMQ----TGIKAVDSLVPIGRGQRELIIGDRQTGKTSIaID 202
Cdd:PRK05922 100 GRVLDGfgnPLDGkeqlpKTHLKPLFSSP---PSPMSRQPIQeifpTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSL-LS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 203 TIINqkrfndGSdekKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNG 282
Cdd:PRK05922 176 TIAK------GS---KSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 283 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmNDAfggGSLTALPVIETQAGDVSAYIPTn 362
Cdd:PRK05922 247 HRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-NDK---GSITALYAILHYPNHPDIFTDY- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 363 VISITDGQIFL---ETELFykgiRPAINVGLSVSRvgSAAQTRAMKQVAGTMKLE--LAQYREVAAFAQFGSDLDAATQQ 437
Cdd:PRK05922 322 LKSLLDGHFFLtpqGKALA----SPPIDILTSLSR--SARQLALPHHYAAAEELRslLKAYHEALDIIQLGAYVPGQDAH 395
|
330 340
....*....|....*....|.
gi 382546007 438 lLSRGVRLTELLKQGQYSPMA 458
Cdd:PRK05922 396 -LDRAVKLLPSIKQFLSQPLS 415
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
146-461 |
6.65e-18 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 86.19 E-value: 6.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 146 TRRRVGlkapgiiprisvrEPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTsiaidTIINQKRFNDGSDekkklyciyV 225
Cdd:PRK08927 134 SRARVG-------------EPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKS-----VLLSMLARNADAD---------V 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 226 A----IGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQ 301
Cdd:PRK08927 187 SviglIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQRE 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 302 MSLLLRRPPGREAYPGDVFYLHSRLLERAAKmnDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKG 381
Cdd:PRK08927 267 IGLSAGEPPTTKGYTPTVFAELPRLLERAGP--GPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERG 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 382 IRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSdLDAATQQLLSRGVR----LTELLKQGQYSPM 457
Cdd:PRK08927 345 RYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGA-YRAGSDPEVDEAIRlnpaLEAFLRQGKDEAT 423
|
....
gi 382546007 458 AIEE 461
Cdd:PRK08927 424 SLAE 427
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
160-404 |
1.08e-17 |
|
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: 85.54 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 160 RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDtIINQ--------KRFNDGSDEKkklYCI-YVAIGQK 230
Cdd:TIGR01040 118 RIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ-ICRQaglvklptKDVHDGHEDN---FAIvFAAMGVN 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 231 RSTvAQLVKR-LTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR-DNGKHALIIYDDLSKQAVAYRQMSLLLRR 308
Cdd:TIGR01040 194 MET-ARFFKQdFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 309 PPGREAYPGDVFYLHSRLLERAAKMNDAfgGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINV 388
Cdd:TIGR01040 273 VPGRRGFPGYMYTDLATIYERAGRVEGR--NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINV 350
|
250
....*....|....*.
gi 382546007 389 GLSVSRVGSAAQTRAM 404
Cdd:TIGR01040 351 LPSLSRLMKSAIGEGM 366
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
71-461 |
1.88e-17 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 84.88 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 71 TGRVLSIGDGIARVhglrnvqaeEMVEFSSGL-----------KGMSLNLEPDNVGVVVFGNDKLIKEGdivkrtgaivd 139
Cdd:PRK04196 40 RGQVLEVSEDKAVV---------QVFEGTTGLdlkdtkvrftgEPLKLPVSEDMLGRIFDGLGRPIDGG----------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 140 GPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDtIINQKRFNdGSDEKkk 219
Cdd:PRK04196 100 PEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQ-IARQAKVL-GEEEN-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 220 LYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR-DNGKHALIIYDDLSKQAVA 298
Cdd:PRK04196 176 FAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMHVLVILTDMTNYCEA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 299 YRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMNDAfgGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLET 375
Cdd:PRK04196 256 LREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 376 ELFYKGIRPAINVGLSVSR-----VGsAAQTRA-MKQVAGTMKLELAQYREVAAFAQF-GSD-LDAATQQLLSRGVRL-T 446
Cdd:PRK04196 331 ELHRKGIYPPIDVLPSLSRlmkdgIG-EGKTREdHKDVANQLYAAYARGKDLRELAAIvGEEaLSERDRKYLKFADAFeR 409
|
410
....*....|....*
gi 382546007 447 ELLKQGQYSPMAIEE 461
Cdd:PRK04196 410 EFVNQGFDENRSIEE 424
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
69-135 |
5.85e-17 |
|
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: 75.27 E-value: 5.85e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 382546007 69 EETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTG 135
Cdd:pfam02874 3 QVIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
165-394 |
2.17e-16 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 79.54 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 165 EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTsiaidtIINQK--RFNDgSDekkklYCIYVAIGQKRSTVA------- 235
Cdd:cd01134 58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKT------VISQSlsKWSN-SD-----VVIYVGCGERGNEMAevleefp 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 236 QLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY 315
Cdd:cd01134 126 ELKDPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGY 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 316 PGdvfYLHSRL---LERAAK---MNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITdgQIF--LETELFYKGIRPAIN 387
Cdd:cd01134 206 PA---YLGARLaefYERAGRvrcLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSIN 280
|
....*..
gi 382546007 388 VGLSVSR 394
Cdd:cd01134 281 WLISYSK 287
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
128-395 |
1.67e-15 |
|
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: 78.99 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 128 GDIVKRTGAIVD--GPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTII 205
Cdd:TIGR01039 86 GRIFNVLGEPIDekGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELIN 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 206 NQKRFNDGsdekkklYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRD-NGKH 284
Cdd:TIGR01039 166 NIAKEHGG-------YSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 285 ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNdafgGGSLTALPVIETQAGDVSAYIPTNVI 364
Cdd:TIGR01039 239 VLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTK----TGSITSVQAVYVPADDLTDPAPATTF 314
|
250 260 270
....*....|....*....|....*....|.
gi 382546007 365 SITDGQIFLETELFYKGIRPAINVGLSVSRV 395
Cdd:TIGR01039 315 AHLDATTVLSRKIAELGIYPAVDPLDSTSRL 345
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
237-373 |
2.91e-11 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 65.44 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 237 LVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR-DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY 315
Cdd:PRK02118 184 FKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGY 263
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 382546007 316 PGDvfyLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFL 373
Cdd:PRK02118 264 PGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
223-407 |
9.41e-11 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 64.66 E-value: 9.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 223 IYVAIGQKRSTVAQLVK---RLTDADA----MKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQ 295
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEefpKLKDPKTgkplMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 296 AVAYRQMSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDG 369
Cdd:PRK14698 766 AEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKV 842
|
170 180 190
....*....|....*....|....*....|....*...
gi 382546007 370 QIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQV 407
Cdd:PRK14698 843 FWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNV 880
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
128-395 |
6.71e-10 |
|
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: 59.93 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 128 GDIVKRTGAIVD--GPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTII 205
Cdd:cd01133 10 GRIFNVLGEPIDerGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELIN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 206 NQKRFNDGsdekkklYCIYVAIGQKRSTVAQLVkrltdaDAMKYTIVVSATASDAAPLQY-----------LAPYSGCSM 274
Cdd:cd01133 90 NIAKAHGG-------YSVFAGVGERTREGNDLY------HEMKESGVINLDGLSKVALVYgqmneppgaraRVALTGLTM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 275 GEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDafggGSLTALPVIETQAG 353
Cdd:cd01133 157 AEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKK----GSITSVQAVYVPAD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 382546007 354 DVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 395
Cdd:cd01133 233 DLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
111-344 |
3.08e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 59.41 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 111 PDNVGVVVfgndKLIKEGDI-VKRTGAIVDGPIGSKTRRRVGLKAPGIIPRISVR-----EPMQTGIKAVDSLVPIGRGQ 184
Cdd:PRK04192 153 PGVSGTVK----EIVSEGDYtVDDTIAVLEDEDGEGVELTMMQKWPVRRPRPYKEklppvEPLITGQRVIDTFFPVAKGG 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 185 RELIIGDRQTGKT----SIAidtiinqkRFNDgSDekkklYCIYVAIGQKRSTVAQLVK---RLTDADA----MKYTIVV 253
Cdd:PRK04192 229 TAAIPGPFGSGKTvtqhQLA--------KWAD-AD-----IVIYVGCGERGNEMTEVLEefpELIDPKTgrplMERTVLI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 382546007 254 SAT-----ASDAAPLqylapYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL-- 326
Cdd:PRK04192 295 ANTsnmpvAAREASI-----YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASRLae 366
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250 260
....*....|....*....|.
gi 382546007 327 -LERAAKMNdAFGG--GSLTA 344
Cdd:PRK04192 367 fYERAGRVK-TLGGeeGSVTI 386
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| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
71-136 |
3.10e-04 |
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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: 39.22 E-value: 3.10e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 382546007 71 TGRVLSIGDGIARVHGLRNVQAEEMVEF-------SSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGA 136
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIergdgnnETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
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