|
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: 914.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 1 GILSIHGLADVMQGEMIELPGGRYALALNLNRDSVGAVVMGPYADLQEGMKVTGTGRILEVPVGPEMLGRVVNTLGEPID 80
Cdd:PRK09281 37 GIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 81 GKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGKTAMAIDAIINQKDSGIFSIYV 160
Cdd:PRK09281 117 GKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 161 AIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:PRK09281 197 AIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 241 LKRPPGREAFPGDVFYLHSRLLERAARVSEAyvekftngevtGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:PRK09281 277 LRRPPGREAYPGDVFYLHSRLLERAAKLSDE-----------LGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 321 TELFNAGVRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTALAQYRELAAFAQFSSDLDEATKKQLDHGQKVTELMKQKQY 400
Cdd:PRK09281 346 SDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERGQRLVELLKQPQY 425
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 157285153 401 APMSVFDQALVIFAAERGYLQDVELSKVLDFEAALLSFAR 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: 902.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 1 GILSIHGLADVMQGEMIELPGGRYALALNLNRDSVGAVVMGPYADLQEGMKVTGTGRILEVPVGPEMLGRVVNTLGEPID 80
Cdd:COG0056 37 GIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 81 GKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGKTAMAIDAIINQKDSGIFSIYV 160
Cdd:COG0056 117 GKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 161 AIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:COG0056 197 AIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 241 LKRPPGREAFPGDVFYLHSRLLERAARVSEAYvekftngevtgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:COG0056 277 LRRPPGREAYPGDVFYLHSRLLERAAKLSDEL-----------GGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 321 TELFNAGVRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTALAQYRELAAFAQFSSDLDEATKKQLDHGQKVTELMKQKQY 400
Cdd:COG0056 346 SDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERGERLVELLKQPQY 425
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 157285153 401 APMSVFDQALVIFAAERGYLQDVELSKVLDFEAALLSFAR 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: 784.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 1 GILSIHGLADVMQGEMIELPGGRYALALNLNRDSVGAVVMGPYADLQEGMKVTGTGRILEVPVGPEMLGRVVNTLGEPID 80
Cdd:TIGR00962 36 GIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 81 GKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGKTAMAIDAIINQKDSGIFSIYV 160
Cdd:TIGR00962 116 GKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 161 AIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:TIGR00962 196 AIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 241 LKRPPGREAFPGDVFYLHSRLLERAARVSEAyvekftngevTGKtGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:TIGR00962 276 LRRPPGREAFPGDVFYLHSRLLERAAKLNDE----------KGG-GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 321 TELFNAGVRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTALAQYRELAAFAQFSSDLDEATKKQLDHGQKVTELMKQKQY 400
Cdd:TIGR00962 345 SDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASDLDEATKKQLERGQRVVELLKQPQY 424
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 157285153 401 APMSVFDQALVIFAAERGYLQDVELSKVLDFEAALLSFARG 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: 729.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 1 GILSIHGLADVMQGEMIELPGGRYALALNLNRDSVGAVVMGPYADLQEGMKVTGTGRILEVPVGPEMLGRVVNTLGEPID 80
Cdd:PRK13343 37 GIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 81 GKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGKTAMAIDAIINQKDSGIFSIYV 160
Cdd:PRK13343 117 GGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 161 AIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:PRK13343 197 AIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 241 LKRPPGREAFPGDVFYLHSRLLERAARVSEAYvekftngevtgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:PRK13343 277 LRRPPGREAYPGDIFYLHSRLLERAAKLSPEL-----------GGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 321 TELFNAGVRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTALAQYRELAAFAQFSSDLDEATKKQLDHGQKVTELMKQKQY 400
Cdd:PRK13343 346 SDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLLDAGTQKQITRGRRLRELLKQPRF 425
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 157285153 401 APMSVFDQALVIFAAERGYLQDVELSKVLDFEAALLSFARG 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: 639.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 1 GILSIHGLADVMQGEMIELPGGRYALALNLNRDSVGAVVMGPYADLQEGMKVTGTGRILEVPVGPEMLGRVVNTLGEPID 80
Cdd:CHL00059 16 GIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPID 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 81 GKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGKTAMAIDAIINQKDSGIFSIYV 160
Cdd:CHL00059 96 GKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQNVICVYV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 161 AIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:CHL00059 176 AIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 241 LKRPPGREAFPGDVFYLHSRLLERAARVSEAYvekftnGEvtgktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:CHL00059 256 LRRPPGREAYPGDVFYLHSRLLERAAKLSSQL------GE-----GSMTALPIVETQAGDVSAYIPTNVISITDGQIFLS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 321 TELFNAGVRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTALAQYRELAAFAQFSSDLDEATKKQLDHGQKVTELMKQKQY 400
Cdd:CHL00059 325 ADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQS 404
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 157285153 401 APMSVFDQALVIFAAERGYLQDVELSKVLDFEAALLSFAR 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: 548.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 58 ILEVPVGPEMLGRVVNTLGEPIDGKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQT 137
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 138 GKTAMAIDAIINQKDSGIFSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRG 217
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 218 EDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAARVSEAYvekftngevtgKTGSLTALPIIETQ 297
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEL-----------GGGSLTALPIIETQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 157285153 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 |
2.29e-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: 510.08 E-value: 2.29e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 1 GILSIHGLADVMQGEMIELPGGRYALALNLNRDSVGAVVMGPYADLQEGMKVTGTGRILEVPVGPEMLGRVVNTLGEPID 80
Cdd:TIGR03324 37 GIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERTGRVMDVPVGDGLLGRVVDPLGRPLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 81 GKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGKTAMAIDAIINQKDSGIFSIYV 160
Cdd:TIGR03324 117 GGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDRQTGKTAIAIDTILNQKGRNVLCIYC 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 161 AIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:TIGR03324 197 AIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSIGEHFMEQGRDVLIVYDDLTQHARAYRELSLL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 241 LKRPPGREAFPGDVFYLHSRLLERAARVSEayvekftngEVTGktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:TIGR03324 277 LRRPPGREAFPGDIFYVHSRLLERSTHLNE---------ELGG--GSLTALPIIETEAQNISAYIPTNLISITDGQIYLS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 321 TELFNAGVRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTALAQYRELAAFAQFSSDLDEATKKQLDHGQKVTELMKQKQY 400
Cdd:TIGR03324 346 PTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDENTRKTIEHGRRIRACLKQTQS 425
|
410 420 430
....*....|....*....|....*....|....*
gi 157285153 401 APMSVFDQALVIFAAERGYLQDVELSKVLDFEAAL 435
Cdd:TIGR03324 426 SPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAI 460
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
25-436 |
3.30e-115 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 349.34 E-value: 3.30e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 25 ALALNLNRDS-VGAVVMGPYADLQEGMKVTGTGRILEVPVGPEMLGRVVNTLGEPID------GKGPIEAKLT-SPVEII 96
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQTlGKVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 97 APGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGKTAMAIDAIINQ--------KDSGIFSIYVAIGQKAST 168
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 169 IANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGRE 248
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGRE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 249 AFPGDVFYLHSRLLERAARVSeayvekftngevTGK-TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAG 327
Cdd:PTZ00185 320 AYPGDVFYLHSRLLERAAMLS------------PGKgGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 328 VRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTALAQYRELAAFAQFSSDLDEATkkqLDHGQKVTELMKQKQyapMSVFD 407
Cdd:PTZ00185 388 QRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN---PSFFM 461
|
410 420 430
....*....|....*....|....*....|
gi 157285153 408 QALV-IFAAERGYLQDVELSKVLDFEAALL 436
Cdd:PTZ00185 462 NALVsLYACLNGYLDDVKVNYAKLYEYLLV 491
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
113-339 |
3.78e-109 |
|
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: 320.84 E-value: 3.78e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 113 GYKSVDSMIPIGRGQRELVIGDRQTGKTAMAiDAIINQKDSGIfSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASA 192
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 193 SESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAARVSeay 272
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVK--- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157285153 273 vekftngevtGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVS 339
Cdd:pfam00006 156 ----------GKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
66-431 |
7.19e-108 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 328.09 E-value: 7.19e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 66 EMLGRVVNTLGEPIDgkgPIEAK--------LTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQT 137
Cdd:PRK07165 78 EYFGKIIDIDGNIIY---PEAQNplskkflpNTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 138 GKTAMAIDAIINQKDSGIFSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASaSESAALQYLAPYAGCAMGE---YFr 214
Cdd:PRK07165 155 GKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAP-STSPYEQYLAPYVAMAHAEnisYN- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 215 drgEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAArvseayveKFTNGEvtgktgSLTALPII 294
Cdd:PRK07165 233 ---DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAG--------KFKNRK------TITALPIL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 295 ETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTALAQYRELAAFAQFS 374
Cdd:PRK07165 296 QTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLD 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 157285153 375 SDLDEATKKQLDHGQKVTELMKQKQYAPMSVFDQALVIFAAERGYLQDV-ELSKVLDF 431
Cdd:PRK07165 376 YDLNKETSDLLFKGKMIEKMFNQKGFSLYSYRFVLLISKLISWGLLKDVkDEQKALDF 433
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
61-341 |
2.42e-102 |
|
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: 305.53 E-value: 2.42e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 61 VPVGPEMLGRVVNTLGEPIDGKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGKT 140
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 141 AMAIDAIINQ-KDSGIFSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGED 219
Cdd:cd19476 82 VLAMQLARNQaKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 220 ALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAARVseayvekftngeVTGKtGSLTALPIIETQAG 299
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKV------------KDGG-GSITAIPAVSTPGD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 157285153 300 DVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 341
Cdd:cd19476 229 DLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
346-440 |
2.75e-51 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 169.16 E-value: 2.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 346 QTKIIKKLSGGIRTALAQYRELAAFAQFSSDLDEATKKQLDHGQKVTELMKQKQYAPMSVFDQALVIFAAERGYLQDVEL 425
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90
....*....|....*
gi 157285153 426 SKVLDFEAALLSFAR 440
Cdd:pfam00306 81 EKVKEFEKELLEYLR 95
|
|
| 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 |
5.14e-50 |
|
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: 165.62 E-value: 5.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 350 IKKLSGGIRTALAQYRELAAFAQFSSDLDEATKKQLDHGQKVTELMKQKQYAPMSVFDQALVIFAAERGYLQDVELSKVL 429
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90
....*....|.
gi 157285153 430 DFEAALLSFAR 440
Cdd:cd18113 81 EFEKELLEYLR 91
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
2-372 |
8.92e-49 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 172.26 E-value: 8.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 2 ILSIHGLaDVMQGEMIELPGGRYALalnLNRDSV-----GAVVMGPYADLQE---GMKVTGTGRILEVPVGPEMLGRVVN 73
Cdd:PRK09099 35 LLRVSGL-DVTLGELCELRQRDGTL---LQRAEVvgfsrDVALLSPFGELGGlsrGTRVIGLGRPLSVPVGPALLGRVID 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 74 TLGEPIDGKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGK-TAMAIDAIINQKD 152
Cdd:PRK09099 111 GLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKsTLMGMFARGTQCD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 153 sgiFSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAV 232
Cdd:PRK09099 191 ---VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFAR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 233 AYRQISLLLKRPPGREAFPGDVFYLHSRLLERAARvseayvekftngevtGKTGSLTALPIIETQAGDVSAFVPTNVISI 312
Cdd:PRK09099 268 AQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM---------------GETGSITALYTVLAEDESGSDPIAEEVRGI 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 313 TDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTALAQYRELAAFAQ 372
Cdd:PRK09099 333 LDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQ 392
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
60-341 |
6.51e-48 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 165.04 E-value: 6.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 60 EVPVGPEMLGRVVNTLGEPIDGKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGK 139
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 140 TAMaIDAIINQKDSGIfSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGED 219
Cdd:cd01136 81 STL-LGMIARNTDADV-NVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 220 ALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAARvseayvekftngevtGKTGSLTALPIIETQAG 299
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN---------------GEKGSITAFYTVLVEGD 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 157285153 300 DVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 341
Cdd:cd01136 224 DFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
16-410 |
7.76e-46 |
|
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: 164.05 E-value: 7.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 16 MIELPGGRYALA--LNLNRDSVgaVVMgPYADLQE---GMKVTGTGRILEVPVGPEMLGRVVNTLGEPIDGKGPIEAKLT 90
Cdd:COG1157 45 EIETADGRPVLAevVGFRGDRV--LLM-PLGDLEGispGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEER 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 91 SPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRelvigdrqtgktaMaidaiinqkdsGIFsiyvaigqkA---- 166
Cdd:COG1157 122 RPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR-------------I-----------GIF---------Agsgv 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 167 --ST----IA-------NVV---------------RKLEEHGaLANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGE 218
Cdd:COG1157 169 gkSTllgmIArnteadvNVIaligergrevrefieDDLGEEG-LARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 219 DALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAarvseayvekftnGevTGKTGSLTAL------- 291
Cdd:COG1157 248 NVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERA-------------G--NGGKGSITAFytvlveg 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 292 -----PIIETqagdvsafvptnVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTALAQYRE 366
Cdd:COG1157 313 ddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEE 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 157285153 367 ------LAAFAQFSS-DLDEATKKQldhgQKVTELMKQKQYAPMSvFDQAL 410
Cdd:COG1157 381 nedlirIGAYQPGSDpELDEAIALI----PAIEAFLRQGMDERVS-FEESL 426
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
51-410 |
1.96e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 160.69 E-value: 1.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 51 KVTGTGRILEVPVGPEMLGRVVNTLGEPIDGKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQREL 130
Cdd:PRK06936 87 EVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 131 VIGDRQTGKTAMaIDAIINQKDSGIfSIYVAIGQKASTianvVRKLEEHG----ALANTVVVVASASESAALQYLAPYAG 206
Cdd:PRK06936 167 IFAAAGGGKSTL-LASLIRSAEVDV-TVLALIGERGRE----VREFIESDlgeeGLRKAVLVVATSDRPSMERAKAGFVA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 207 CAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAARvseayvekftngevtGKTG 286
Cdd:PRK06936 241 TSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ---------------SDKG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 287 SLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTALAQYRE 366
Cdd:PRK06936 306 SITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEE 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 157285153 367 ---LAAFAQFSSDLDEATKKQLDHGQKVTELMKQKQYAPmSVFDQAL 410
Cdd:PRK06936 386 velLLQIGEYQKGQDKEADQAIERIGAIRGFLRQGTHEL-SHFNETL 431
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
38-398 |
9.56e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 156.04 E-value: 9.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 38 VVMGPYADLQE---GMKVTGTGRILEVPVGPEMLGRVVNTLGEPIDGKgPIEAKLTS-PVEIIAPGVIDRKSVDQPVQTG 113
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGS-ALPKGLAPvSTDQDPPNPLKRPPIREPMEVG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 114 YKSVDSMIPIGRGQRELVIGDRQTGK-TAMAIDAIINQKDSGIFSIyvaIGQKASTIANVV-RKLEEHGaLANTVVVVAS 191
Cdd:PRK07721 146 VRAIDSLLTVGKGQRVGIFAGSGVGKsTLMGMIARNTSADLNVIAL---IGERGREVREFIeRDLGPEG-LKRSIVVVAT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 192 ASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAArvsea 271
Cdd:PRK07721 222 SDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG----- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 272 yvekftngevTGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIIK 351
Cdd:PRK07721 297 ----------TNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHK 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 157285153 352 KLSGGIRTALAQYRE------LAAFAQFSS-DLDEATKKQldhgQKVTELMKQK 398
Cdd:PRK07721 367 EAANRFRELLSTYQNsedlinIGAYKRGSSrEIDEAIQFY----PQIISFLKQG 416
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
8-398 |
2.85e-41 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 151.89 E-value: 2.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 8 LADVMQGEMIEL-PGGRYALALNLNRDSVgavVMGPYAD---LQEGMKVTGTGRILEVPVGPEMLGRVVNTLGEPIDGKG 83
Cdd:PRK06820 45 LPGVAQGELCRIePQGMLAEVVSIEQEMA---LLSPFASsdgLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 84 PIEAKLtSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGK-TAMAIDAIINQKDSGIFSIyvaI 162
Cdd:PRK06820 122 PLTGQW-RELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKsTLLGMLCADSAADVMVLAL---I 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 163 GQKASTianvVRKLEEHG----ALANTVVVVASaSESAALQYL-APYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQI 237
Cdd:PRK06820 198 GERGRE----VREFLEQVltpeARARTVVVVAT-SDRPALERLkGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 238 SLLLKRPPGREAFPGDVFYLHSRLLERAArvseayvekftngevTGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQI 317
Cdd:PRK06820 273 GLAAGEPPAAGSFPPSVFANLPRLLERTG---------------NSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHI 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 318 FLQTELFNAGVRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTALAQYRE---LAAFAQFSSDLDEATKKQLDHGQKVTEL 394
Cdd:PRK06820 338 VLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEielLVRVGEYQAGEDLQADEALQRYPAICAF 417
|
....
gi 157285153 395 MKQK 398
Cdd:PRK06820 418 LQQD 421
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
59-348 |
1.78e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 147.14 E-value: 1.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 59 LEVPVGPEMLGRVVNTLGEPIDGKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTG 138
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 139 K-TAMAIdaIINQKDSGIfSIYVAIGQKASTIANVVRKlEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRG 217
Cdd:PRK08472 170 KsTLMGM--IVKGCLAPI-KVVALIGERGREIPEFIEK-NLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 218 EDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAarvseayvekftnGEVTGKtGSLTALPIIETQ 297
Cdd:PRK08472 246 LDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERA-------------GKEEGK-GSITAFFTVLVE 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 157285153 298 AGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTK 348
Cdd:PRK08472 312 GDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
27-341 |
8.09e-37 |
|
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: 140.24 E-value: 8.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 27 ALNLNRDSVGAVVMGPYADLQEGMKVTGTGRILEVPVGPEMLGRVVNTLGEPIDGKGPIEAKLTSPVEIIAPGVIDRKSV 106
Cdd:TIGR01039 44 AQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 107 DQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGKTAMAIDAIIN-QKDSGIFSIYVAIGQKASTIANVVRKLEEHGALANT 185
Cdd:TIGR01039 124 VEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 186 VVVVASASESAALQYLAPYAGCAMGEYFRD-RGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLER 264
Cdd:TIGR01039 204 ALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQER 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157285153 265 AArvseayvekftngevTGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 341
Cdd:TIGR01039 284 IT---------------STKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRL 345
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
8-402 |
7.21e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 137.01 E-value: 7.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 8 LADVMQGEMIEL-PGGRYALALNLNRDSVGAVVMGPYADLQEGMKVTGTGRILEVPVGPEMLGRVVNTLGEPIDGKgPIE 86
Cdd:PRK07594 37 LPGVFMGELCCIkPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 87 AKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGKTAMaIDAIINQKDSGIfSIYVAIGQKA 166
Cdd:PRK07594 116 DVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLCNAPDADS-NVLVLIGERG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 167 STIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPG 246
Cdd:PRK07594 194 REVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 247 REAFPGDVFYLHSRLLERAArvseayvekftngevTGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNA 326
Cdd:PRK07594 274 SGEYPPGVFSALPRLLERTG---------------MGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAER 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157285153 327 GVRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTALAQYRE---LAAFAQFSSDLDEATKKQLDHGQKVTELMKQKQYAP 402
Cdd:PRK07594 339 GHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEvelLIRIGEYQRGVDTDTDKAIDTYPDICTFLRQSKDEV 417
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
58-345 |
8.22e-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: 8.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 58 ILEVPVGPEMLGRVVNTLGEPIDGKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGD--- 134
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGsgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 135 ----------RQTGktamaidaIINQKDSGIFsIYVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPY 204
Cdd:cd01135 81 phnelaaqiaRQAG--------VVGSEENFAI-VFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 205 AGCAMGEYFR-DRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGdvfYLHSRL---LERAarvseayvekftnGE 280
Cdd:cd01135 152 MALTTAEYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERA-------------GR 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157285153 281 VTGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSA 345
Cdd:cd01135 216 VEGRKGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSG 280
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
49-397 |
8.99e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 134.25 E-value: 8.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 49 GMKVTGTGRILEVPVGPEMLGRVVNTLGEPIDGKGPI--EAKLTSPVEIIAPgvIDRKSVDQPVQTGYKSVDSMIPIGRG 126
Cdd:PRK07196 78 GARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLggSTPLQQQLPQIHP--LQRRAVDTPLDVGVNAINGLLTIGKG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 127 QRELVIGDRQTGKTAMAidAIINQKDSGIFSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAG 206
Cdd:PRK07196 156 QRVGLMAGSGVGKSVLL--GMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELC 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 207 CAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAArvseayvekftNGEvtgKTG 286
Cdd:PRK07196 234 HAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG-----------NSS---GNG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 287 SLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSR----VGGSAQTKIIKKLSGGIrTALA 362
Cdd:PRK07196 300 TMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCY-ADYM 378
|
330 340 350
....*....|....*....|....*....|....*
gi 157285153 363 QYRELAAFAQFSSDLDEATKKQLDHGQKVTELMKQ 397
Cdd:PRK07196 379 AIKPLIPLGGYVAGADPMADQAVHYYPAITQFLRQ 413
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
65-366 |
1.34e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 131.27 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 65 PEMLGRVVNTLGEPIDGKGPIEAKLTS-PVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGKT--- 140
Cdd:PRK06002 103 PSWKGRVINALGEPIDGLGPLAPGTRPmSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKStll 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 141 AMAIDAiinqkdSGIFSIYVA-IGQKASTianvVRK-LEEH--GALANTVVVVASASESAALQYLAPYAGCAMGEYFRDR 216
Cdd:PRK06002 183 AMLARA------DAFDTVVIAlVGERGRE----VREfLEDTlaDNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDR 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 217 GEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAARVSEAyvekftngevtgkTGSLTALPIIET 296
Cdd:PRK06002 253 GENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEG-------------GGSITGIFSVLV 319
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 297 QAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTALAQYRE 366
Cdd:PRK06002 320 DGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEE 389
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
49-341 |
2.25e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 130.21 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 49 GMKVTGTGRILEVPVGPEMLGRVVNTLGEPIDGKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQR 128
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 129 -----------ELVIGDRQTGKTAmaiDAIInqkdSGIfsiyvaIGQKASTIANVVRK-LEEHGaLANTVVVVASASESA 196
Cdd:PRK08972 165 mglfagsgvgkSVLLGMMTRGTTA---DVIV----VGL------VGERGREVKEFIEEiLGEEG-RARSVVVAAPADTSP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 197 ALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAArvseayvekf 276
Cdd:PRK08972 231 LMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAG---------- 300
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157285153 277 tNGevTGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 341
Cdd:PRK08972 301 -NG--GPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRV 362
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
55-410 |
4.80e-32 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 126.26 E-value: 4.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 55 TGRILEVPVGPEMLGRVVNTLGEpIDGK--GPIEAK---LTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRE 129
Cdd:PRK08149 76 TGKPLSVWVGEALLGAVLDPTGK-IVERfdAPPTVGpisEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 130 LVIGDRQTGKTaMAIDAIINQKDSGIFSIYVaIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAM 209
Cdd:PRK08149 155 GIFASAGCGKT-SLMNMLIEHSEADVFVIGL-IGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTV 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 210 GEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAARVseayvekftngevtgKTGSLT 289
Cdd:PRK08149 233 AEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT---------------LAGSIT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 290 ALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTALAQYRELAA 369
Cdd:PRK08149 298 AFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQL 377
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 157285153 370 FAQF-------SSDLDEATKKQldhgQKVTELMKQKQYAPMSvFDQAL 410
Cdd:PRK08149 378 FIDLgeyrrgeNADNDRAMDKR----PALEAFLKQDVAEKSS-FSDTL 420
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
16-341 |
2.54e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 124.84 E-value: 2.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 16 MIELPGGRY-----ALALNLNRDSVGAVVMGPYADLQEGMKVT---GTGRIlevPVGPEMLGRVVNTLGEPIDGKGPIEA 87
Cdd:PRK05688 53 LVINDDSYHpvqveAEVMGFSGDKVFLMPVGSVAGIAPGARVVplaDTGRL---PMGMSMLGRVLDGAGRALDGKGPMKA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 88 KLTSPVE--IIAPgvIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGKTaMAIDAIINQKDSGIfsIYVA-IGQ 164
Cdd:PRK05688 130 EDWVPMDgpTINP--LNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKS-VLLGMMTRFTEADI--IVVGlIGE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 165 KASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRP 244
Cdd:PRK05688 205 RGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 245 PGREAFPGDVFYLHSRLLERAArvseayvekftNGEVTGktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELF 324
Cdd:PRK05688 285 PATKGYPPSVFAKLPKLVERAG-----------NAEPGG--GSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLA 351
|
330
....*....|....*..
gi 157285153 325 NAGVRPAVDPGISVSRV 341
Cdd:PRK05688 352 EEGHYPAIDIEASISRV 368
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
2-340 |
3.68e-31 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 124.55 E-value: 3.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 2 ILSIHGLADVMQGEM--IELPGG--RYALALNLNRDSVGAVVMGPYADL-QEGMKVTGTGRILEVPVGPEMLGRVVNTLG 76
Cdd:PRK04196 14 LLFVEGVEGVAYGEIveIELPNGekRRGQVLEVSEDKAVVQVFEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 77 EPIDGKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQR------------ELvigdrqtgktAMAI 144
Cdd:PRK04196 94 RPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnEL----------AAQI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 145 --DAIINQKDSGIFSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFR-DRGEDAL 221
Cdd:PRK04196 164 arQAKVLGEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMHVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 222 IVYDDLSKQAVAYRQISLLLKRPPGREAFPGdvfYLHSRL---LERAarvseayvekftnGEVTGKTGSLTALPIIETQA 298
Cdd:PRK04196 244 VILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERA-------------GRIKGKKGSITQIPILTMPD 307
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 157285153 299 GDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSR 340
Cdd:PRK04196 308 DDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
3-380 |
8.23e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 111.61 E-value: 8.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 3 LSIHGLADVMQGEMIELPGGRYALALN-----LNRDS-------VG-----AVVMgPYADLqEGMKVTGTGRILE----V 61
Cdd:PRK08927 15 LVIYGRVVAVRGLLVEVAGPIHALSVGarivvETRGGrpvpcevVGfrgdrALLM-PFGPL-EGVRRGCRAVIANaaaaV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 62 PVGPEMLGRVVNTLGEPIDGKGPIeAKLTSPVEIIA--PGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGK 139
Cdd:PRK08927 93 RPSRAWLGRVVNALGEPIDGKGPL-PQGPVPYPLRAppPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 140 -TAMAIDAIINQKDSGIFSIyvaIGQKASTIANVVRK-LEEHGaLANTVVVVASASESAALQYLAPYAGCAMGEYFRDRG 217
Cdd:PRK08927 172 sVLLSMLARNADADVSVIGL---IGERGREVQEFLQDdLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 218 EDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAarvseayvekftnGEVTGKTGSLTALPIIETQ 297
Cdd:PRK08927 248 KDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERA-------------GPGPIGEGTITGLFTVLVD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 298 AGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTALAQYRE------LAAFA 371
Cdd:PRK08927 315 GDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADmeelirLGAYR 394
|
410
....*....|
gi 157285153 372 QFSS-DLDEA 380
Cdd:PRK08927 395 AGSDpEVDEA 404
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
60-421 |
8.72e-27 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 111.80 E-value: 8.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 60 EVPVGPEMLGRVVNTLGEPIDGKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGK 139
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 140 TAM-AIDAIINQKDSGIFSIyvaIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGE 218
Cdd:PRK07960 189 SVLlGMMARYTQADVIVVGL---IGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQ 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 219 DALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAArvseayvekftNGEVTGktGSLTALPIIETQA 298
Cdd:PRK07960 266 HVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG-----------NGISGG--GSITAFYTVLTEG 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 299 GDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRvggsAQTKIIKKlsggirtalAQYRELAAFAQFSSDLd 378
Cdd:PRK07960 333 DDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISR----AMTALIDE---------QHYARVRQFKQLLSSF- 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 157285153 379 eatkkqldhgQKVTELMKQKQYAPMS--VFDQALVIFAAERGYLQ 421
Cdd:PRK07960 399 ----------QRNRDLVSVGAYAKGSdpMLDKAIALWPQLEAFLQ 433
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
49-366 |
1.22e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 111.22 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 49 GMKVTGTGRILEVPVGPEMLGRVVNTLGEPIDGkgPIEAKLTSPVEIIAPGV--IDRKSVDQPVQTGYKSVDSMIPIGRG 126
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 127 QRELVIGDRQTGK-TAMAIDAIINQKDSGIFSIyvaIGQKASTIANVVRK-LEEHGaLANTVVVVASASESAALQYLAPY 204
Cdd:PRK06793 157 QKIGIFAGSGVGKsTLLGMIAKNAKADINVISL---VGERGREVKDFIRKeLGEEG-MRKSVVVVATSDESHLMQLRAAK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 205 AGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPgreaFPGDVFYLHS---RLLERAARVseayvekftngev 281
Cdd:PRK06793 233 LATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKT------------- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 282 tgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIIKKLSGGIRTAL 361
Cdd:PRK06793 296 --QKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKIL 373
|
....*
gi 157285153 362 AQYRE 366
Cdd:PRK06793 374 SIYKE 378
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
55-345 |
2.27e-26 |
|
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: 110.97 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 55 TGRILEVPVGPEMLGRVVNTLGEPIDGKGPI--EAKLTSPVEIIAPgvIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVI 132
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVlaEDYLDINGQPINP--YARIYPEEMIQTGISAIDVMNSIARGQKIPIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 133 GD-------------RQTGKTAMAIDAIINQKDSGIFSIYVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQ 199
Cdd:TIGR01040 148 SAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIER 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 200 YLAPYAGCAMGEYFR-DRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAARVseayvekftn 278
Cdd:TIGR01040 228 IITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV---------- 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157285153 279 gevTGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSA 345
Cdd:TIGR01040 298 ---EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 361
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
2-340 |
1.22e-25 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 108.45 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 2 ILSIHGLADVMqGEMIELPGGRY----ALALNLNRDSVGAVVMGPYADLQEGMKVTGTGRILEVPVGPEMLGRVVNTLGE 77
Cdd:PRK05922 30 LLEAQGLSACL-GELCQISLSKSppilAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 78 PIDGKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGKTAMaIDAIINQKDSGIfS 157
Cdd:PRK05922 109 PLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSL-LSTIAKGSKSTI-N 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 158 IYVAIGQKASTIANVVRKLEEHGALANTVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQI 237
Cdd:PRK05922 187 VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 238 SLLLKRPPGREAFPGDVFYLHSRLLERAArvseayvekftngevTGKTGSLTALPIIETQAGDVSAFVPTnVISITDGQI 317
Cdd:PRK05922 267 ALARGETLSAHHYAASVFHHVSEFTERAG---------------NNDKGSITALYAILHYPNHPDIFTDY-LKSLLDGHF 330
|
330 340
....*....|....*....|...
gi 157285153 318 FLqTELFNAGVRPAVDPGISVSR 340
Cdd:PRK05922 331 FL-TPQGKALASPPIDILTSLSR 352
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
60-341 |
1.21e-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: 99.60 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 60 EVPVGPEMLGRVVNTLGEPIDGKGPIEAKLTSPVEIIAPGVIDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGK 139
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 140 TAMAIDAIIN-QKDSGIFSIYVAIGQKASTIANVVRKLEEHG-----ALANTVVVVASASESAALQYLAPYAGCAMGEYF 213
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGERTREGNDLYHEMKESGvinldGLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 214 RD-RGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFYLHSRLLERAArvseayvekftngevTGKTGSLTALP 292
Cdd:cd01133 161 RDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERIT---------------STKKGSITSVQ 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 157285153 293 IIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 341
Cdd:cd01133 226 AVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
30-367 |
8.35e-23 |
|
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: 100.16 E-value: 8.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 30 LNRDSVGAVVMGPYADLQEGMKVTGTGRILEVPVGPEMLGRVVNTLGEPIDGKGPIEAKLTSPVEIIAPGVIDRKSVDQP 109
Cdd:COG0055 50 LGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 110 VQTGYKSVDSMIPIGRGQRELVIGDRQTGKTAMAIDAIIN--QKDSGIfSIYVAIGQKASTIANVVRKLEEHGALANTVV 187
Cdd:COG0055 130 LETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNiaKEHGGV-SVFAGVGERTREGNDLYREMKESGVLDKTAL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 188 VVASASESAALQYLAPYAGCAMGEYFRD-RGEDALIVYDDLSKQAVAYRQISLLLKRPPGReafpgdVFY---LHS---R 260
Cdd:COG0055 209 VFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSA------VGYqptLATemgA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 261 LLERAARVseayvekftngevtgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSR 340
Cdd:COG0055 283 LQERITST---------------KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSR 347
|
330 340 350
....*....|....*....|....*....|....*..
gi 157285153 341 ------VG----GSAQtkiikklsgGIRTALAQYREL 367
Cdd:COG0055 348 ildpliVGeehyRVAR---------EVQRILQRYKEL 375
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
21-340 |
1.43e-20 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 93.56 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 21 GGRYALALNLNRDSVGAVVMGPYADLQEGMKVTGTGRILEVPVGPEMLGRVVNTLGEPIDGKGPIEAKltsPVEIIAPGV 100
Cdd:PRK02118 36 GSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGE---PIEIGGPSV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 101 --IDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDrqTGKTAMAIDA-IINQKDSGIFsIYVAIGQKASTIANVVRKLE 177
Cdd:PRK02118 113 npVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSV--SGEPYNALLArIALQAEADII-ILGGMGLTFDDYLFFKDTFE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 178 EHGALANTVVVVASASESAALQYLAPYAGCAMGEYFR-DRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGDVFY 256
Cdd:PRK02118 190 NAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYS 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 257 LHSRLLERAARVSEAyvekftngevtgktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQtelfnagvRPAVDPGI 336
Cdd:PRK02118 270 DLASRYEKAVDFEDG--------------GSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLR--------RGRIDPFG 327
|
....
gi 157285153 337 SVSR 340
Cdd:PRK02118 328 SLSR 331
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
30-367 |
1.60e-20 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 93.57 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 30 LNRDSVGAVVMGPYADLQEGMKVTGTGRILEVPVGPEMLGRVVNTLGEPIDGKGPIEAKLTSPVEIIAPGVIDRKSVDQP 109
Cdd:CHL00060 65 LGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 110 VQTGYKSVDSMIPIGRGQRELVIGDRQTGKTAMAIDAIIN-QKDSGIFSIYVAIGQKASTIANVVRKLEEHGalantVVV 188
Cdd:CHL00060 145 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGERTREGNDLYMEMKESG-----VIN 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 189 VASASES-AALQY----LAPYA-------GCAMGEYFRD-RGEDALIVYDDLSKQAVAYRQISLLLKRppgreaFPGDVF 255
Cdd:CHL00060 220 EQNIAESkVALVYgqmnEPPGArmrvgltALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGR------MPSAVG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 256 Y---LHSR---LLERAARVseayvekftngevtgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVR 329
Cdd:CHL00060 294 YqptLSTEmgsLQERITST---------------KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIY 358
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 157285153 330 PAVDPGISVS-----RVGGSAQTKIIKKlsggIRTALAQYREL 367
Cdd:CHL00060 359 PAVDPLDSTStmlqpRIVGEEHYETAQR----VKQTLQRYKEL 397
|
|
| 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 |
9.47e-19 |
|
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: 79.80 E-value: 9.47e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 157285153 1 GILSIHGLADVMQGEMIELPGGRYALALNLNRDSVGAVVMGPYADLQEGMKVTGTGR 57
Cdd:cd18116 11 GIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
59-340 |
3.45e-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: 84.55 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 59 LEVPVGPEMLGRVVNTLGEPIDgkgpIEAKLTS------------PVEIIAPgVIDRKSVDQPVQTGYKSVDSMIPIGRG 126
Cdd:cd01134 2 LSVELGPGLLGSIFDGIQRPLE----VIAETGSifiprgvnvqrwPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 127 QRELVIGDRQTGKTAMaIDAIINQKDSGIFsIYVAIGQKASTIANVVR-----KLEEHGA--------LANTVVVVASAS 193
Cdd:cd01134 77 GTAAIPGPFGCGKTVI-SQSLSKWSNSDVV-IYVGCGERGNEMAEVLEefpelKDPITGEslmertvlIANTSNMPVAAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 194 ESAAlqylapYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAFPGdvfYLHSRL---LERAARVSe 270
Cdd:cd01134 155 EASI------YTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYERAGRVR- 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157285153 271 ayvekfTNGEvTGKTGSLTALPIIETQAGDVSAFVPTNVISITdgQIF--LQTELFNAGVRPAVDPGISVSR 340
Cdd:cd01134 225 ------CLGS-PGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
46-290 |
2.17e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 62.49 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 46 LQEGMKVTGTGRILEVP----------VGPEMLGRVVN-------TLGEPI------DGKGpIEAKLTS--PVEIIAPgV 100
Cdd:PRK04192 124 VKVGDKVEAGDILGTVQetpsiehkimVPPGVSGTVKEivsegdyTVDDTIavledeDGEG-VELTMMQkwPVRRPRP-Y 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 101 IDRKSVDQPVQTGYKSVDSMIPIGRGQRELVIGDRQTGKTaMAIDAIINQKDSGIfSIYVAIGQKASTIANVV------- 173
Cdd:PRK04192 202 KEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT-VTQHQLAKWADADI-VIYVGCGERGNEMTEVLeefpeli 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 174 -----RKLEEHGAL-ANTVVVVASASESAAlqylapYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGR 247
Cdd:PRK04192 280 dpktgRPLMERTVLiANTSNMPVAAREASI------YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGE 353
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 157285153 248 EAFPGdvfYLHSRL---LERAARVSeayvekfTNGevtGKTGSLTA 290
Cdd:PRK04192 354 EGYPA---YLASRLaefYERAGRVK-------TLG---GEEGSVTI 386
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|
| 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 |
4.79e-10 |
|
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: 55.53 E-value: 4.79e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157285153 351 KKLSGGIRTALAQYRELAAFAQFSSD--LDEATKKQLDHGQKVTELMKQKQYAPMSVFDQALVIFA 414
Cdd:cd01429 2 KAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYP 67
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
158-312 |
6.59e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 61.58 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 158 IYVAIGQKASTIANVvrkLEEHGALAN----------TVVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDL 227
Cdd:PRK14698 686 IYIGCGERGNEMTDV---LEEFPKLKDpktgkplmerTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADST 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285153 228 SKQAVAYRQISLLLKRPPGREAFPGdvfYLHSRL---LERAARVseayvekFTNGEvTGKTGSLTALPIIETQAGDVSAF 304
Cdd:PRK14698 763 SRWAEALREISGRLEEMPGEEGYPA---YLASKLaefYERAGRV-------VTLGS-DYRVGSVSVIGAVSPPGGDFSEP 831
|
....*...
gi 157285153 305 VPTNVISI 312
Cdd:PRK14698 832 VVQNTLRV 839
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
1-56 |
2.14e-08 |
|
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: 50.62 E-value: 2.14e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 157285153 1 GILSIHGLADVMQGEMIELPGGRYALALNLNRDSVGAVVMGPYADLQEGMKVTGTG 56
Cdd:pfam02874 14 GIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| |
