|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-440 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 922.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 1 GIIRIHGLADVMQGEMIELPSGRYALALNLERDSVGAVVMGPYADLKEGMKVTGSGRILEVPVGPELLGRVVNTLGQPID 80
Cdd:PRK09281 37 GIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 81 GKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGKTAMAIDAIINQKDSGIYSIYV 160
Cdd:PRK09281 117 GKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 161 AIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:PRK09281 197 AIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 241 LKRPPGREAFPGDVFYLHSRLLERAARVSEEyverftkgevkGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:PRK09281 277 LRRPPGREAYPGDVFYLHSRLLERAAKLSDE-----------LGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 321 TELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAAFAQFSSDLDEATKRQLNHGQKVTELMKQKQY 400
Cdd:PRK09281 346 SDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERGQRLVELLKQPQY 425
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 289498363 401 APMSVFDQALVIFAAERGYLNDVALNKLADFESALLSYAR 440
Cdd:PRK09281 426 SPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLR 465
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-440 |
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: 909.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 1 GIIRIHGLADVMQGEMIELPSGRYALALNLERDSVGAVVMGPYADLKEGMKVTGSGRILEVPVGPELLGRVVNTLGQPID 80
Cdd:COG0056 37 GIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 81 GKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGKTAMAIDAIINQKDSGIYSIYV 160
Cdd:COG0056 117 GKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 161 AIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:COG0056 197 AIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 241 LKRPPGREAFPGDVFYLHSRLLERAARVSEEYverftkgevkgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:COG0056 277 LRRPPGREAYPGDVFYLHSRLLERAAKLSDEL-----------GGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 321 TELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAAFAQFSSDLDEATKRQLNHGQKVTELMKQKQY 400
Cdd:COG0056 346 SDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERGERLVELLKQPQY 425
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 289498363 401 APMSVFDQALVIFAAERGYLNDVALNKLADFESALLSYAR 440
Cdd:COG0056 426 SPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLR 465
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
1-441 |
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: 795.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 1 GIIRIHGLADVMQGEMIELPSGRYALALNLERDSVGAVVMGPYADLKEGMKVTGSGRILEVPVGPELLGRVVNTLGQPID 80
Cdd:TIGR00962 36 GIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 81 GKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGKTAMAIDAIINQKDSGIYSIYV 160
Cdd:TIGR00962 116 GKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 161 AIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:TIGR00962 196 AIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 241 LKRPPGREAFPGDVFYLHSRLLERAARVSEEyverftkgevKGKtGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:TIGR00962 276 LRRPPGREAFPGDVFYLHSRLLERAAKLNDE----------KGG-GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 321 TELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAAFAQFSSDLDEATKRQLNHGQKVTELMKQKQY 400
Cdd:TIGR00962 345 SDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASDLDEATKKQLERGQRVVELLKQPQY 424
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 289498363 401 APMSVFDQALVIFAAERGYLNDVALNKLADFESALLSYARG 441
Cdd:TIGR00962 425 KPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDA 465
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-441 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 738.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 1 GIIRIHGLADVMQGEMIELPSGRYALALNLERDSVGAVVMGPYADLKEGMKVTGSGRILEVPVGPELLGRVVNTLGQPID 80
Cdd:PRK13343 37 GIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 81 GKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGKTAMAIDAIINQKDSGIYSIYV 160
Cdd:PRK13343 117 GGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 161 AIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:PRK13343 197 AIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 241 LKRPPGREAFPGDVFYLHSRLLERAARVSEEYverftkgevkgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:PRK13343 277 LRRPPGREAYPGDIFYLHSRLLERAAKLSPEL-----------GGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 321 TELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAAFAQFSSDLDEATKRQLNHGQKVTELMKQKQY 400
Cdd:PRK13343 346 SDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLLDAGTQKQITRGRRLRELLKQPRF 425
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 289498363 401 APMSVFDQALVIFAAERGYLNDVALNKLADFESALLSYARG 441
Cdd:PRK13343 426 SPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDA 466
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
1-440 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 646.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 1 GIIRIHGLADVMQGEMIELPSGRYALALNLERDSVGAVVMGPYADLKEGMKVTGSGRILEVPVGPELLGRVVNTLGQPID 80
Cdd:CHL00059 16 GIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPID 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 81 GKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGKTAMAIDAIINQKDSGIYSIYV 160
Cdd:CHL00059 96 GKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQNVICVYV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 161 AIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:CHL00059 176 AIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 241 LKRPPGREAFPGDVFYLHSRLLERAARVSEEYverftkGEvkgktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:CHL00059 256 LRRPPGREAYPGDVFYLHSRLLERAAKLSSQL------GE-----GSMTALPIVETQAGDVSAYIPTNVISITDGQIFLS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 321 TELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAAFAQFSSDLDEATKRQLNHGQKVTELMKQKQY 400
Cdd:CHL00059 325 ADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQS 404
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 289498363 401 APMSVFDQALVIFAAERGYLNDVALNKLADFESALLSYAR 440
Cdd:CHL00059 405 APLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLK 444
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
58-342 |
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: 552.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 58 ILEVPVGPELLGRVVNTLGQPIDGKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQT 137
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 138 GKTAMAIDAIINQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRG 217
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 218 EDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAARVSEEYverftkgevkgKTGSLTALPIIETQ 297
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEL-----------GGGSLTALPIIETQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 289498363 298 AGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVG 342
Cdd:cd01132 230 AGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
1-435 |
5.29e-179 |
|
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: 509.31 E-value: 5.29e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 1 GIIRIHGLADVMQGEMIELPSGRYALALNLERDSVGAVVMGPYADLKEGMKVTGSGRILEVPVGPELLGRVVNTLGQPID 80
Cdd:TIGR03324 37 GIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERTGRVMDVPVGDGLLGRVVDPLGRPLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 81 GKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGKTAMAIDAIINQKDSGIYSIYV 160
Cdd:TIGR03324 117 GGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDRQTGKTAIAIDTILNQKGRNVLCIYC 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 161 AIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:TIGR03324 197 AIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSIGEHFMEQGRDVLIVYDDLTQHARAYRELSLL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 241 LKRPPGREAFPGDVFYLHSRLLERAARVSEEYverftkgevkgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:TIGR03324 277 LRRPPGREAFPGDIFYVHSRLLERSTHLNEEL-----------GGGSLTALPIIETEAQNISAYIPTNLISITDGQIYLS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 321 TELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAAFAQFSSDLDEATKRQLNHGQKVTELMKQKQY 400
Cdd:TIGR03324 346 PTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDENTRKTIEHGRRIRACLKQTQS 425
|
410 420 430
....*....|....*....|....*....|....*
gi 289498363 401 APMSVFDQALVIFAAERGYLNDVALNKLADFESAL 435
Cdd:TIGR03324 426 SPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAI 460
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
25-436 |
1.56e-114 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 347.41 E-value: 1.56e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 25 ALALNLERDS-VGAVVMGPYADLKEGMKVTGSGRILEVPVGPELLGRVVNTLGQ--PIDGKGPIEAKLSSP-----VEMI 96
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHevPVGLLTRSRALLESEqtlgkVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 97 APGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGKTAMAIDAIINQ--------KDSGIYSIYVAIGQKAST 168
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 169 IANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGRE 248
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGRE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 249 AFPGDVFYLHSRLLERAARVSEeyverfTKGevkgkTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGV 328
Cdd:PTZ00185 320 AYPGDVFYLHSRLLERAAMLSP------GKG-----GGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQ 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 329 RPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAAFAQFSSDLDEATkrqLNHGQKVTELMKQKQyapMSVFDQ 408
Cdd:PTZ00185 389 RPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN---PSFFMN 462
|
410 420
....*....|....*....|....*....
gi 289498363 409 ALV-IFAAERGYLNDVALNKLADFESALL 436
Cdd:PTZ00185 463 ALVsLYACLNGYLDDVKVNYAKLYEYLLV 491
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
113-339 |
5.50e-110 |
|
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: 322.77 E-value: 5.50e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 113 GYKSVDSMIPIGRGQRELIIGDRQTGKTAMAiDAIINQKDSGIySIYVAIGQKASTIANVVRKLEEHGALANTVVVVASA 192
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 193 SESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAARvseey 272
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGR----- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 289498363 273 verftkgeVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVS 339
Cdd:pfam00006 154 --------VKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
66-404 |
2.46e-105 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 321.54 E-value: 2.46e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 66 ELLGRVVNTLGQPIDgkgPIEAK--------LSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQT 137
Cdd:PRK07165 78 EYFGKIIDIDGNIIY---PEAQNplskkflpNTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 138 GKTAMAIDAIINQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASaSESAALQYLAPYAGCAMGE---YFr 214
Cdd:PRK07165 155 GKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAP-STSPYEQYLAPYVAMAHAEnisYN- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 215 drgEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAarvseeyverftkGEVKGKTgSLTALPII 294
Cdd:PRK07165 233 ---DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERA-------------GKFKNRK-TITALPIL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 295 ETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAAFAQFS 374
Cdd:PRK07165 296 QTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLD 375
|
330 340 350
....*....|....*....|....*....|
gi 289498363 375 SDLDEATKRQLNHGQKVTELMKQKQYAPMS 404
Cdd:PRK07165 376 YDLNKETSDLLFKGKMIEKMFNQKGFSLYS 405
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
61-341 |
1.69e-103 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 308.62 E-value: 1.69e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 61 VPVGPELLGRVVNTLGQPIDGKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGKT 140
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 141 AMAIDAIINQ-KDSGIYSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGED 219
Cdd:cd19476 82 VLAMQLARNQaKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 220 ALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAARvseeyverftkgeVKGKTGSLTALPIIETQAG 299
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGK-------------VKDGGGSITAIPAVSTPGD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 289498363 300 DVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 341
Cdd:cd19476 229 DLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
346-440 |
2.15e-50 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 166.85 E-value: 2.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 346 QTKIIKKLSGGIRTALAQYRELAAFAQFSSDLDEATKRQLNHGQKVTELMKQKQYAPMSVFDQALVIFAAERGYLNDVAL 425
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90
....*....|....*
gi 289498363 426 NKLADFESALLSYAR 440
Cdd:pfam00306 81 EKVKEFEKELLEYLR 95
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
2-372 |
4.05e-50 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 175.73 E-value: 4.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 2 IIRIHGLaDVMQGEMIELPSGRYALalnLERDSV-----GAVVMGPYADLKE---GMKVTGSGRILEVPVGPELLGRVVN 73
Cdd:PRK09099 35 LLRVSGL-DVTLGELCELRQRDGTL---LQRAEVvgfsrDVALLSPFGELGGlsrGTRVIGLGRPLSVPVGPALLGRVID 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 74 TLGQPIDGKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGK-TAMAIDAIINQKD 152
Cdd:PRK09099 111 GLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKsTLMGMFARGTQCD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 153 sgiYSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAV 232
Cdd:PRK09099 191 ---VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFAR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 233 AYRQISLLLKRPPGREAFPGDVFYLHSRLLERAARvseeyverftkgevkGKTGSLTALPIIETQAGDVSAFVPTNVISI 312
Cdd:PRK09099 268 AQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM---------------GETGSITALYTVLAEDESGSDPIAEEVRGI 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 313 TDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAAFAQ 372
Cdd:PRK09099 333 LDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQ 392
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
60-341 |
1.69e-49 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 169.28 E-value: 1.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 60 EVPVGPELLGRVVNTLGQPIDGKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGK 139
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 140 TAMaIDAIINQKDSGIYSIyVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGED 219
Cdd:cd01136 81 STL-LGMIARNTDADVNVI-ALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 220 ALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAArvseeyverftkgevKGKTGSLTALPIIETQAG 299
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAG---------------NGEKGSITAFYTVLVEGD 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 289498363 300 DVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 341
Cdd:cd01136 224 DFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
350-440 |
6.25e-49 |
|
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: 162.92 E-value: 6.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 350 IKKLSGGIRTALAQYRELAAFAQFSSDLDEATKRQLNHGQKVTELMKQKQYAPMSVFDQALVIFAAERGYLNDVALNKLA 429
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90
....*....|.
gi 289498363 430 DFESALLSYAR 440
Cdd:cd18113 81 EFEKELLEYLR 91
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
2-410 |
2.18e-45 |
|
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: 162.89 E-value: 2.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 2 IIRIHGLaDVMQGE--MIELPSGRYALA--LNLERDSVgaVVMgPYADLKE---GMKVTGSGRILEVPVGPELLGRVVNT 74
Cdd:COG1157 30 LIEAVGP-DASIGElcEIETADGRPVLAevVGFRGDRV--LLM-PLGDLEGispGARVVPTGRPLSVPVGDGLLGRVLDG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 75 LGQPIDGKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQReliigdrqtgktaMAIDAiinqkDSG 154
Cdd:COG1157 106 LGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR-------------IGIFA-----GSG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 155 iysiyvaIGqKaST----IA-------NVV---------------RKLEEHGaLANTVVVVASASESAALQYLAPYAGCA 208
Cdd:COG1157 168 -------VG-K-STllgmIArnteadvNVIaligergrevrefieDDLGEEG-LARSVVVVATSDEPPLMRLRAAYTATA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 209 MGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAarvseeyverftkGevKGKTGSL 288
Cdd:COG1157 238 IAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERA-------------G--NGGKGSI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 289 TAL------------PIIETqagdvsafvptnVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGG 356
Cdd:COG1157 303 TAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARR 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 289498363 357 IRTALAQYRE------LAAFAQFSS-DLDEATKRQlnhgQKVTELMKQKQYAPMSvFDQAL 410
Cdd:COG1157 371 LRRLLARYEEnedlirIGAYQPGSDpELDEAIALI----PAIEAFLRQGMDERVS-FEESL 426
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
51-410 |
1.10e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 161.07 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 51 KVTGSGRILEVPVGPELLGRVVNTLGQPIDGKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQREL 130
Cdd:PRK06936 87 EVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 131 IIGDRQTGKTAMaIDAIINQKDSGIySIYVAIGQKASTianvVRKLEEHG----ALANTVVVVASASESAALQYLAPYAG 206
Cdd:PRK06936 167 IFAAAGGGKSTL-LASLIRSAEVDV-TVLALIGERGRE----VREFIESDlgeeGLRKAVLVVATSDRPSMERAKAGFVA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 207 CAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAArvseeyverftkgevKGKTG 286
Cdd:PRK06936 241 TSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG---------------QSDKG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 287 SLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAQYRE 366
Cdd:PRK06936 306 SITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEE 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 289498363 367 ---LAAFAQFSSDLDEATKRQLNHGQKVTELMKQKQYAPmSVFDQAL 410
Cdd:PRK06936 386 velLLQIGEYQKGQDKEADQAIERIGAIRGFLRQGTHEL-SHFNETL 431
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
8-398 |
5.36e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 156.90 E-value: 5.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 8 LADVMQGEMIEL-PSGRYALALNLERDSVgavVMGPYAD---LKEGMKVTGSGRILEVPVGPELLGRVVNTLGQPIDGKG 83
Cdd:PRK06820 45 LPGVAQGELCRIePQGMLAEVVSIEQEMA---LLSPFASsdgLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 84 PIEAKLSsPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGK-TAMAIDAIINQKDSGIYSIyvaI 162
Cdd:PRK06820 122 PLTGQWR-ELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKsTLLGMLCADSAADVMVLAL---I 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 163 GQKASTianvVRKLEEHG----ALANTVVVVASaSESAALQYL-APYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQI 237
Cdd:PRK06820 198 GERGRE----VREFLEQVltpeARARTVVVVAT-SDRPALERLkGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 238 SLLLKRPPGREAFPGDVFYLHSRLLERAArvseeyverftkgevKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQI 317
Cdd:PRK06820 273 GLAAGEPPAAGSFPPSVFANLPRLLERTG---------------NSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHI 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 318 FLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAAFAQF-----SSDL--DEATKRQlnhgQK 390
Cdd:PRK06820 338 VLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVgeyqaGEDLqaDEALQRY----PA 413
|
....*...
gi 289498363 391 VTELMKQK 398
Cdd:PRK06820 414 ICAFLQQD 421
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
47-348 |
1.92e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 152.53 E-value: 1.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 47 KEGMKVTGSGRILEVPVGPELLGRVVNTLGQPIDGKGPIEAKLSSPVeMIAP-GVIDRKSVDQPVQTGYKSVDSMIPIGR 125
Cdd:PRK08472 78 KIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPI-MKAPiAAMKRGLIDEVFSVGVKSIDGLLTCGK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 126 GQRELIIGDRQTGK-TAMAIdaIINQKDSGIYSIYVaIGQKASTIANVVRKlEEHGALANTVVVVASASESAALQYLAPY 204
Cdd:PRK08472 157 GQKLGIFAGSGVGKsTLMGM--IVKGCLAPIKVVAL-IGERGREIPEFIEK-NLGGDLENTVIVVATSDDSPLMRKYGAF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 205 AGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAarvseeyverftkGEVKGK 284
Cdd:PRK08472 233 CAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERA-------------GKEEGK 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 289498363 285 tGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTK 348
Cdd:PRK08472 300 -GSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
38-398 |
2.21e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 152.18 E-value: 2.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 38 VVMGPYADLKE---GMKVTGSGRILEVPVGPELLGRVVNTLGQPIDGKgPIEAKLSS-PVEMIAPGVIDRKSVDQPVQTG 113
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGS-ALPKGLAPvSTDQDPPNPLKRPPIREPMEVG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 114 YKSVDSMIPIGRGQRELIIGDRQTGK-TAMAIDAIINQKDSGIYSIyvaIGQKASTIANVV-RKLEEHGaLANTVVVVAS 191
Cdd:PRK07721 146 VRAIDSLLTVGKGQRVGIFAGSGVGKsTLMGMIARNTSADLNVIAL---IGERGREVREFIeRDLGPEG-LKRSIVVVAT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 192 ASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAArvsee 271
Cdd:PRK07721 222 SDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG----- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 272 yverftkgevKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIK 351
Cdd:PRK07721 297 ----------TNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHK 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 289498363 352 KLSGGIRTALAQYRE------LAAFAQFSS-DLDEATKRQlnhgQKVTELMKQK 398
Cdd:PRK07721 367 EAANRFRELLSTYQNsedlinIGAYKRGSSrEIDEAIQFY----PQIISFLKQG 416
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
27-341 |
4.67e-36 |
|
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: 138.31 E-value: 4.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 27 ALNLERDSVGAVVMGPYADLKEGMKVTGSGRILEVPVGPELLGRVVNTLGQPIDGKGPIEAKLSSPVEMIAPGVIDRKSV 106
Cdd:TIGR01039 44 AQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 107 DQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGKTAMAIDAIIN-QKDSGIYSIYVAIGQKASTIANVVRKLEEHGALANT 185
Cdd:TIGR01039 124 VEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 186 VVVVASASESAALQYLAPYAGCAMGEYFRD-RGEDALIVYDDLSKQAVAYRQISLLLKRppgreaFPGDVFYLHSRLLER 264
Cdd:TIGR01039 204 ALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGR------MPSAVGYQPTLATEM 277
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 289498363 265 AarvseEYVERFTkgevKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 341
Cdd:TIGR01039 278 G-----ELQERIT----STKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRL 345
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
58-340 |
6.30e-35 |
|
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: 130.81 E-value: 6.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 58 ILEVPVGPELLGRVVNTLGQPIDGKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQT 137
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 138 GKTAMAI----DAIINQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYF 213
Cdd:cd01135 81 PHNELAAqiarQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 214 R-DRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGdvfYLHSRL---LERAarvseeyverftkGEVKGKTGSLT 289
Cdd:cd01135 161 AyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERA-------------GRVEGRKGSIT 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 289498363 290 ALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSR 340
Cdd:cd01135 225 QIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
49-397 |
1.24e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 133.86 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 49 GMKVTGSGRILEVPVGPELLGRVVNTLGQPIDGKGPI--EAKLSSPVEMIAPgvIDRKSVDQPVQTGYKSVDSMIPIGRG 126
Cdd:PRK07196 78 GARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLggSTPLQQQLPQIHP--LQRRAVDTPLDVGVNAINGLLTIGKG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 127 QRELIIGDRQTGKTAMAidAIINQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAG 206
Cdd:PRK07196 156 QRVGLMAGSGVGKSVLL--GMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELC 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 207 CAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAArvseeyverftKGEvkgKTG 286
Cdd:PRK07196 234 HAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG-----------NSS---GNG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 287 SLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSR----VGGAAQTKIIKKLSGGIrTALA 362
Cdd:PRK07196 300 TMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCY-ADYM 378
|
330 340 350
....*....|....*....|....*....|....*
gi 289498363 363 QYRELAAFAQFSSDLDEATKRQLNHGQKVTELMKQ 397
Cdd:PRK07196 379 AIKPLIPLGGYVAGADPMADQAVHYYPAITQFLRQ 413
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
49-341 |
1.61e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 133.67 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 49 GMKVTGSGRILEVPVGPELLGRVVNTLGQPIDGKGPI--EAKLSSPVEMIAPgvIDRKSVDQPVQTGYKSVDSMIPIGRG 126
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIytDQRASRHSPPINP--LSRRPITEPLDVGVRAINAMLTVGKG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 127 QR-----------ELIIGDRQTGKTAmaiDAIInqkdSGIysiyvaIGQKASTIANVVRK-LEEHGaLANTVVVVASASE 194
Cdd:PRK08972 163 QRmglfagsgvgkSVLLGMMTRGTTA---DVIV----VGL------VGERGREVKEFIEEiLGEEG-RARSVVVAAPADT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 195 SAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAarvseeyve 274
Cdd:PRK08972 229 SPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERA--------- 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 289498363 275 rftkGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 341
Cdd:PRK08972 300 ----GNGGPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRV 362
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
8-402 |
1.87e-34 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 133.15 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 8 LADVMQGEMIEL-PSGRYALALNLERDSVGAVVMGPYADLKEGMKVTGSGRILEVPVGPELLGRVVNTLGQPIDGKgPIE 86
Cdd:PRK07594 37 LPGVFMGELCCIkPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 87 AKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGKTAMaIDAIINQKDSGIySIYVAIGQKA 166
Cdd:PRK07594 116 DVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLCNAPDADS-NVLVLIGERG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 167 STIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPG 246
Cdd:PRK07594 194 REVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 247 REAFPGDVFYLHSRLLERAArvseeyverftkgevKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNA 326
Cdd:PRK07594 274 SGEYPPGVFSALPRLLERTG---------------MGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAER 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 289498363 327 GVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAQYRE---LAAFAQFSSDLDEATKRQLNHGQKVTELMKQKQYAP 402
Cdd:PRK07594 339 GHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEvelLIRIGEYQRGVDTDTDKAIDTYPDICTFLRQSKDEV 417
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
1-366 |
2.78e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 132.81 E-value: 2.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 1 GIIRIHGLA-DVMQGEMIELPS-GRYALA--LNLERDSVGAVVMGPYADLKEGMKVTGSGRiLEVPVGPELLGRVVNTLG 76
Cdd:PRK06002 36 SHYRVRGLSrFVRLGDFVAIRAdGGTHLGevVRVDPDGVTVKPFEPRIEIGLGDAVFRKGP-LRIRPDPSWKGRVINALG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 77 QPIDGKGPI-EAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGKT---AMAIDAiinqkd 152
Cdd:PRK06002 115 EPIDGLGPLaPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKStllAMLARA------ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 153 SGIYSIYVA-IGQKASTianvVRK-LEEH--GALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLS 228
Cdd:PRK06002 189 DAFDTVVIAlVGERGRE----VREfLEDTlaDNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDSVT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 229 KQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAARVSEEyverftkgevkgkTGSLTALPIIETQAGDVSAFVPTN 308
Cdd:PRK06002 265 RFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEG-------------GGSITGIFSVLVDGDDHNDPVADS 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 289498363 309 VISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAQYRE 366
Cdd:PRK06002 332 IRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEE 389
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
55-370 |
6.47e-32 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 125.88 E-value: 6.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 55 SGRILEVPVGPELLGRVVNTLGQpIDGK--GPIEAK---LSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRE 129
Cdd:PRK08149 76 TGKPLSVWVGEALLGAVLDPTGK-IVERfdAPPTVGpisEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 130 LIIGDRQTGKTaMAIDAIINQKDSGIYSIYVaIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAM 209
Cdd:PRK08149 155 GIFASAGCGKT-SLMNMLIEHSEADVFVIGL-IGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTV 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 210 GEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAARVseeyverftkgevkgKTGSLT 289
Cdd:PRK08149 233 AEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT---------------LAGSIT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 290 ALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTALAQYRELAA 369
Cdd:PRK08149 298 AFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQL 377
|
.
gi 289498363 370 F 370
Cdd:PRK08149 378 F 378
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
7-340 |
6.20e-30 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 121.09 E-value: 6.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 7 GLADVMQGEM--IELPSG--RYALALNLERDSVGAVVMGPYADLK-EGMKVTGSGRILEVPVGPELLGRVVNTLGQPIDG 81
Cdd:PRK04196 19 GVEGVAYGEIveIELPNGekRRGQVLEVSEDKAVVQVFEGTTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 82 KGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQR------------ELiigdrqtgktAMAI--DAI 147
Cdd:PRK04196 99 GPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnEL----------AAQIarQAK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 148 INQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFR-DRGEDALIVYDD 226
Cdd:PRK04196 169 VLGEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMHVLVILTD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 227 LSKQAVAYRQISLLLKRPPGREAFPGdvfYLHSRL---LERAarvseeyverftkGEVKGKTGSLTALPIIETQAGDVSA 303
Cdd:PRK04196 249 MTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERA-------------GRIKGKKGSITQIPILTMPDDDITH 312
|
330 340 350
....*....|....*....|....*....|....*..
gi 289498363 304 FVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSR 340
Cdd:PRK04196 313 PIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
16-341 |
1.30e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 119.84 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 16 MIELPSGRY-----ALALNLERDSVGAVVMGPYADLKEGMKVT---GSGRIlevPVGPELLGRVVNTLGQPIDGKGPIEA 87
Cdd:PRK05688 53 LVINDDSYHpvqveAEVMGFSGDKVFLMPVGSVAGIAPGARVVplaDTGRL---PMGMSMLGRVLDGAGRALDGKGPMKA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 88 KLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGKTaMAIDAIINQKDSGIysIYVA-IGQKA 166
Cdd:PRK05688 130 EDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKS-VLLGMMTRFTEADI--IVVGlIGERG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 167 STIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPG 246
Cdd:PRK05688 207 REVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 247 REAFPGDVFYLHSRLLERAarvseeyverftkGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNA 326
Cdd:PRK05688 287 TKGYPPSVFAKLPKLVERA-------------GNAEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEE 353
|
330
....*....|....*
gi 289498363 327 GVRPAVDPGISVSRV 341
Cdd:PRK05688 354 GHYPAIDIEASISRV 368
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
54-375 |
2.11e-26 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 110.64 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 54 GSGRILevPVGPELLGRVVNTLGQPIDGKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIG 133
Cdd:PRK07960 105 QSGKQL--PLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 134 DRQTGKTAM-AIDAIINQKDSGIYSIyvaIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEY 212
Cdd:PRK07960 183 GSGVGKSVLlGMMARYTQADVIVVGL---IGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAED 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 213 FRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAarvseeyverftkGEVKGKTGSLTALP 292
Cdd:PRK07960 260 FRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERA-------------GNGISGGGSITAFY 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 293 IIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRvggaAQTKIIKKlsggirtalAQYRELAAFAQ 372
Cdd:PRK07960 327 TVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISR----AMTALIDE---------QHYARVRQFKQ 393
|
...
gi 289498363 373 FSS 375
Cdd:PRK07960 394 LLS 396
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
37-380 |
2.49e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 110.45 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 37 AVVMgPYADLkEGMKVTGSGRILE----VPVGPELLGRVVNTLGQPIDGKGPI-EAKLSSPVEMIAPGVIDRKSVDQPVQ 111
Cdd:PRK08927 66 ALLM-PFGPL-EGVRRGCRAVIANaaaaVRPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 112 TGYKSVDSMIPIGRGQRELIIGDRQTGK-TAMAIDAIINQKDSGIYSIyvaIGQKASTIANVVRK-LEEHGaLANTVVVV 189
Cdd:PRK08927 144 LGVRALNTFLTCCRGQRMGIFAGSGVGKsVLLSMLARNADADVSVIGL---IGERGREVQEFLQDdLGPEG-LARSVVVV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 190 ASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAarvs 269
Cdd:PRK08927 220 ATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERA---- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 270 eeyverftkGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKI 349
Cdd:PRK08927 296 ---------GPGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPE 366
|
330 340 350
....*....|....*....|....*....|....*...
gi 289498363 350 IKKLSGGIRTALAQYRE------LAAFAQFSS-DLDEA 380
Cdd:PRK08927 367 ENPLVRRARQLMATYADmeelirLGAYRAGSDpEVDEA 404
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
49-366 |
3.15e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 110.07 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 49 GMKVTGSGRILEVPVGPELLGRVVNTLGQPIDGkgPIEAKLSSPVEMIAPGV--IDRKSVDQPVQTGYKSVDSMIPIGRG 126
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 127 QRELIIGDRQTGK-TAMAIDAIINQKDSGIYSIyvaIGQKASTIANVVRK-LEEHGaLANTVVVVASASESAALQYLAPY 204
Cdd:PRK06793 157 QKIGIFAGSGVGKsTLLGMIAKNAKADINVISL---VGERGREVKDFIRKeLGEEG-MRKSVVVVATSDESHLMQLRAAK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 205 AGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPgreaFPGDVFYLHS---RLLERAArvseeyverftkgev 281
Cdd:PRK06793 233 LATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSG--------------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 282 KGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGAAQTKIIKKLSGGIRTAL 361
Cdd:PRK06793 294 KTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKIL 373
|
....*
gi 289498363 362 AQYRE 366
Cdd:PRK06793 374 SIYKE 378
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
2-340 |
4.65e-26 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 109.61 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 2 IIRIHGLADVMqGEMIELPSGRY----ALALNLERDSVGAVVMGPYADLKEGMKVTGSGRILEVPVGPELLGRVVNTLGQ 77
Cdd:PRK05922 30 LLEAQGLSACL-GELCQISLSKSppilAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 78 PIDGKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGKTAMaIDAIINQKDSGIYS 157
Cdd:PRK05922 109 PLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSL-LSTIAKGSKSTINV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 158 IYVaIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQI 237
Cdd:PRK05922 188 IAL-IGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 238 SLLLKRPPGREAFPGDVFYLHSRLLERAArvseeyverftkgevKGKTGSLTALPIIETQAGDVSAFVPTnVISITDGQI 317
Cdd:PRK05922 267 ALARGETLSAHHYAASVFHHVSEFTERAG---------------NNDKGSITALYAILHYPNHPDIFTDY-LKSLLDGHF 330
|
330 340
....*....|....*....|...
gi 289498363 318 FLqTELFNAGVRPAVDPGISVSR 340
Cdd:PRK05922 331 FL-TPQGKALASPPIDILTSLSR 352
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
55-341 |
3.91e-25 |
|
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: 107.12 E-value: 3.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 55 SGRILEVPVGPELLGRVVNTLGQPIDGKGPI--EAKLSSPVEMIAPgvIDRKSVDQPVQTGYKSVDSMIPIGRGQRELII 132
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVlaEDYLDINGQPINP--YARIYPEEMIQTGISAIDVMNSIARGQKIPIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 133 GD-------------RQTGKTAMAIDAIINQKDSGIYSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQ 199
Cdd:TIGR01040 148 SAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIER 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 200 YLAPYAGCAMGEYFR-DRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAARVseeyverftk 278
Cdd:TIGR01040 228 IITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV---------- 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 289498363 279 gevKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 341
Cdd:TIGR01040 298 ---EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 357
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
60-341 |
2.46e-23 |
|
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: 98.83 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 60 EVPVGPELLGRVVNTLGQPIDGKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGK 139
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 140 TAMAIDAIIN-QKDSGIYSIYVAIGQKASTIANVVRKLEEHG-----ALANTVVVVASASESAALQYLAPYAGCAMGEYF 213
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGERTREGNDLYHEMKESGvinldGLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 214 RD-RGEDALIVYDDLSKQAVAYRQISLLLKRPPGReafpgdVFYlhsrlleRAARVSE--EYVERFTkgevKGKTGSLTA 290
Cdd:cd01133 161 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSA------VGY-------QPTLATEmgSLQERIT----STKKGSITS 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 289498363 291 LPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 341
Cdd:cd01133 224 VQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
33-367 |
1.45e-21 |
|
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: 96.70 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 33 DSVGAVVMGPYADLKEGMKVTGSGRILEVPVGPELLGRVVNTLGQPIDGKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQT 112
Cdd:COG0055 53 NTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILET 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 113 GYKSVDSMIPIGRGQRELIIGDRQTGKTAMaIDAIIN---QKDSGiYSIYVAIGQKASTIANVVRKLEEHGALANTVVVV 189
Cdd:COG0055 133 GIKVIDLLAPYAKGGKIGLFGGAGVGKTVL-IMELIHniaKEHGG-VSVFAGVGERTREGNDLYREMKESGVLDKTALVF 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 190 ASASESAALQYLAPYAGCAMGEYFRD-RGEDALIVYDDLSKQAVAYRQISLLLKRPPGReafpgdVFY---LHS---RLL 262
Cdd:COG0055 211 GQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSA------VGYqptLATemgALQ 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 263 ERAARVseeyverftkgevkgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSR-- 340
Cdd:COG0055 285 ERITST---------------KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRil 349
|
330 340 350
....*....|....*....|....*....|....*
gi 289498363 341 ----VG----GAAQtkiikklsgGIRTALAQYREL 367
Cdd:COG0055 350 dpliVGeehyRVAR---------EVQRILQRYKEL 375
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
1-57 |
1.40e-20 |
|
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: 84.81 E-value: 1.40e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 289498363 1 GIIRIHGLADVMQGEMIELPSGRYALALNLERDSVGAVVMGPYADLKEGMKVTGSGR 57
Cdd:cd18116 11 GIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
22-340 |
3.93e-20 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 92.02 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 22 GRYALALNLERDSVGAVVMGPYADLKEGMKVTGSGRILEVPVGPELLGRVVNTLGQPIDGKGPIEAKlssPVEMIAPGV- 100
Cdd:PRK02118 37 SSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGE---PIEIGGPSVn 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 101 -IDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDrqTGKTAMAIDA-IINQKDSGIYsIYVAIGQKASTIANVVRKLEE 178
Cdd:PRK02118 114 pVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSV--SGEPYNALLArIALQAEADII-ILGGMGLTFDDYLFFKDTFEN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 179 HGALANTVVVVASASESAALQYLAPYAGCAMGEYFR-DRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDvfyL 257
Cdd:PRK02118 191 AGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGS---L 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 258 HSRLleraARVSEEYVErFTKGevkgktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQtelfnagvRPAVDPGIS 337
Cdd:PRK02118 268 YSDL----ASRYEKAVD-FEDG------GSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLR--------RGRIDPFGS 328
|
...
gi 289498363 338 VSR 340
Cdd:PRK02118 329 LSR 331
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
35-367 |
9.47e-20 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 91.26 E-value: 9.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 35 VGAVVMGPYADLKEGMKVTGSGRILEVPVGPELLGRVVNTLGQPIDGKGPIEAKLSSPVEMIAPGVIDRKSVDQPVQTGY 114
Cdd:CHL00060 70 VRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 115 KSVDSMIPIGRGQRELIIGDRQTGKTAMAIDAIIN-QKDSGIYSIYVAIGQKASTIANVVRKLEEHGalantVVVVASAS 193
Cdd:CHL00060 150 KVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGERTREGNDLYMEMKESG-----VINEQNIA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 194 ES-AALQY----LAPYA-------GCAMGEYFRD-RGEDALIVYDDLSKQAVAYRQISLLLKRppgreaFPGDVFYLHSR 260
Cdd:CHL00060 225 ESkVALVYgqmnEPPGArmrvgltALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGR------MPSAVGYQPTL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 261 LLERAArvseeYVERFTkgevKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVS- 339
Cdd:CHL00060 299 STEMGS-----LQERIT----STKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSt 369
|
330 340 350
....*....|....*....|....*....|..
gi 289498363 340 ----RVGGAAQTKIIKKlsggIRTALAQYREL 367
Cdd:CHL00060 370 mlqpRIVGEEHYETAQR----VKQTLQRYKEL 397
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
59-340 |
1.91e-18 |
|
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: 85.32 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 59 LEVPVGPELLGRVVNTLGQPIDGkgpIEAKLSS-----------PVEMIAPgVIDRKSVDQPVQTGYKSVDSMIPIGRGQ 127
Cdd:cd01134 2 LSVELGPGLLGSIFDGIQRPLEV---IAETGSIfiprgvnvqrwPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 128 RELIIGDRQTGKTAMaIDAIINQKDSGIYsIYVAIGQKASTIANVVR-----KLEEHGA--------LANTVVVVASASE 194
Cdd:cd01134 78 TAAIPGPFGCGKTVI-SQSLSKWSNSDVV-IYVGCGERGNEMAEVLEefpelKDPITGEslmertvlIANTSNMPVAARE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 195 SAAlqylapYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGdvfYLHSRL---LERAARVSee 271
Cdd:cd01134 156 ASI------YTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYERAGRVR-- 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 289498363 272 yverfTKGEvKGKTGSLTALPIIETQAGDVSAFVPTNVISITdgQIF--LQTELFNAGVRPAVDPGISVSR 340
Cdd:cd01134 225 -----CLGS-PGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
46-290 |
8.46e-11 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 64.03 E-value: 8.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 46 LKEGMKVTGSGRILEVP----------VGPELLGRVVN-------TLGQPI------DGKGpIEAKLSS--PVEMIAPgV 100
Cdd:PRK04192 124 VKVGDKVEAGDILGTVQetpsiehkimVPPGVSGTVKEivsegdyTVDDTIavledeDGEG-VELTMMQkwPVRRPRP-Y 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 101 IDRKSVDQPVQTGYKSVDSMIPIGRGQRELIIGDRQTGKTaMAIDAIINQKDSGIySIYVAIGQKASTIANVV------- 173
Cdd:PRK04192 202 KEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT-VTQHQLAKWADADI-VIYVGCGERGNEMTEVLeefpeli 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 174 -----RKLEEHGAL-ANTVVVVASASESAAlqylapYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGR 247
Cdd:PRK04192 280 dpktgRPLMERTVLiANTSNMPVAAREASI------YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGE 353
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 289498363 248 EAFPGdvfYLHSRL---LERAARVSeeyverfTKGevkGKTGSLTA 290
Cdd:PRK04192 354 EGYPA---YLASRLaefYERAGRVK-------TLG---GEEGSVTI 386
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
158-312 |
4.90e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 61.96 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 158 IYVAIGQKASTIANVvrkLEEHGALAN----------TVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDL 227
Cdd:PRK14698 686 IYIGCGERGNEMTDV---LEEFPKLKDpktgkplmerTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADST 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289498363 228 SKQAVAYRQISLLLKRPPGREAFPGdvfYLHSRL---LERAARVseeyverFTKGEvKGKTGSLTALPIIETQAGDVSAF 304
Cdd:PRK14698 763 SRWAEALREISGRLEEMPGEEGYPA---YLASKLaefYERAGRV-------VTLGS-DYRVGSVSVIGAVSPPGGDFSEP 831
|
....*...
gi 289498363 305 VPTNVISI 312
Cdd:PRK14698 832 VVQNTLRV 839
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
351-414 |
1.69e-09 |
|
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: 53.99 E-value: 1.69e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 289498363 351 KKLSGGIRTALAQYRELAAFAQFSSD--LDEATKRQLNHGQKVTELMKQKQYAPMSVFDQALVIFA 414
Cdd:cd01429 2 KAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYP 67
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
1-56 |
6.82e-09 |
|
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: 52.16 E-value: 6.82e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 289498363 1 GIIRIHGLADVMQGEMIELPSGRYALALNLERDSVGAVVMGPYADLKEGMKVTGSG 56
Cdd:pfam02874 14 GIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| |
