|
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: 913.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 1 GIIRIHGLADVMQGEMIELPGGNYALALNLERDSVGAVVMGPYANLKEGMKVTGTGRILEVPVGPELLGRVVNTLGEPID 80
Cdd:PRK09281 37 GIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 81 GKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGKTALAIDSIINQRDSGIFSIYV 160
Cdd:PRK09281 117 GKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 161 AIGQKASTIANVVRKLEEHGALANTIVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:PRK09281 197 AIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 241 LKRPPGREAYPGDVFYLHSRLLERAARVSEayveaftngevKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:PRK09281 277 LRRPPGREAYPGDVFYLHSRLLERAAKLSD-----------ELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 321 TELFNAGVRPAVDPGISVSRVGGSAQTKIVKKLSGGIRTALAQYRELAAFAQFSSDLDETTKKQLDHGQKVTELMKQKQY 400
Cdd:PRK09281 346 SDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERGQRLVELLKQPQY 425
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 157285301 401 APFSVFDQALVIFAAERGYLQDIELNKLADFEAALLSFAH 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: 903.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 1 GIIRIHGLADVMQGEMIELPGGNYALALNLERDSVGAVVMGPYANLKEGMKVTGTGRILEVPVGPELLGRVVNTLGEPID 80
Cdd:COG0056 37 GIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 81 GKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGKTALAIDSIINQRDSGIFSIYV 160
Cdd:COG0056 117 GKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 161 AIGQKASTIANVVRKLEEHGALANTIVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:COG0056 197 AIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 241 LKRPPGREAYPGDVFYLHSRLLERAARVSEAYveaftngevkgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:COG0056 277 LRRPPGREAYPGDVFYLHSRLLERAAKLSDEL-----------GGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 321 TELFNAGVRPAVDPGISVSRVGGSAQTKIVKKLSGGIRTALAQYRELAAFAQFSSDLDETTKKQLDHGQKVTELMKQKQY 400
Cdd:COG0056 346 SDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERGERLVELLKQPQY 425
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 157285301 401 APFSVFDQALVIFAAERGYLQDIELNKLADFEAALLSFAH 440
Cdd:COG0056 426 SPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLR 465
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
1-438 |
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: 782.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 1 GIIRIHGLADVMQGEMIELPGGNYALALNLERDSVGAVVMGPYANLKEGMKVTGTGRILEVPVGPELLGRVVNTLGEPID 80
Cdd:TIGR00962 36 GIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 81 GKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGKTALAIDSIINQRDSGIFSIYV 160
Cdd:TIGR00962 116 GKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 161 AIGQKASTIANVVRKLEEHGALANTIVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:TIGR00962 196 AIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 241 LKRPPGREAYPGDVFYLHSRLLERAARVSEAyveaftngevKGKtGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:TIGR00962 276 LRRPPGREAFPGDVFYLHSRLLERAAKLNDE----------KGG-GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 321 TELFNAGVRPAVDPGISVSRVGGSAQTKIVKKLSGGIRTALAQYRELAAFAQFSSDLDETTKKQLDHGQKVTELMKQKQY 400
Cdd:TIGR00962 345 SDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASDLDEATKKQLERGQRVVELLKQPQY 424
|
410 420 430
....*....|....*....|....*....|....*...
gi 157285301 401 APFSVFDQALVIFAAERGYLQDIELNKLADFEAALLSF 438
Cdd:TIGR00962 425 KPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAY 462
|
|
| 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: 728.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 1 GIIRIHGLADVMQGEMIELPGGNYALALNLERDSVGAVVMGPYANLKEGMKVTGTGRILEVPVGPELLGRVVNTLGEPID 80
Cdd:PRK13343 37 GIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 81 GKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGKTALAIDSIINQRDSGIFSIYV 160
Cdd:PRK13343 117 GGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 161 AIGQKASTIANVVRKLEEHGALANTIVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:PRK13343 197 AIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 241 LKRPPGREAYPGDVFYLHSRLLERAARVSEAYveaftngevkgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:PRK13343 277 LRRPPGREAYPGDIFYLHSRLLERAAKLSPEL-----------GGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 321 TELFNAGVRPAVDPGISVSRVGGSAQTKIVKKLSGGIRTALAQYRELAAFAQFSSDLDETTKKQLDHGQKVTELMKQKQY 400
Cdd:PRK13343 346 SDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLLDAGTQKQITRGRRLRELLKQPRF 425
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 157285301 401 APFSVFDQALVIFAAERGYLQDIELNKLADFEAALLSFAHG 441
Cdd:PRK13343 426 SPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDA 466
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
1-438 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 646.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 1 GIIRIHGLADVMQGEMIELPGGNYALALNLERDSVGAVVMGPYANLKEGMKVTGTGRILEVPVGPELLGRVVNTLGEPID 80
Cdd:CHL00059 16 GIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPID 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 81 GKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGKTALAIDSIINQRDSGIFSIYV 160
Cdd:CHL00059 96 GKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQNVICVYV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 161 AIGQKASTIANVVRKLEEHGALANTIVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:CHL00059 176 AIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 241 LKRPPGREAYPGDVFYLHSRLLERAARVSEAYveaftnGEvkgktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:CHL00059 256 LRRPPGREAYPGDVFYLHSRLLERAAKLSSQL------GE-----GSMTALPIVETQAGDVSAYIPTNVISITDGQIFLS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 321 TELFNAGVRPAVDPGISVSRVGGSAQTKIVKKLSGGIRTALAQYRELAAFAQFSSDLDETTKKQLDHGQKVTELMKQKQY 400
Cdd:CHL00059 325 ADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQS 404
|
410 420 430
....*....|....*....|....*....|....*...
gi 157285301 401 APFSVFDQALVIFAAERGYLQDIELNKLADFEAALLSF 438
Cdd:CHL00059 405 APLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTY 442
|
|
| 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: 547.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 58 ILEVPVGPELLGRVVNTLGEPIDGKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQI 137
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 138 GKTALAIDSIINQRDSGIFSIYVAIGQKASTIANVVRKLEEHGALANTIVVVASASESAALQYLAPYAGCAMGEYFRDRG 217
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 218 EDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAARVSEAYveaftngevkgKTGSLTALPIIETQ 297
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDEL-----------GGGSLTALPIIETQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 157285301 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 |
9.24e-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: 508.54 E-value: 9.24e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 1 GIIRIHGLADVMQGEMIELPGGNYALALNLERDSVGAVVMGPYANLKEGMKVTGTGRILEVPVGPELLGRVVNTLGEPID 80
Cdd:TIGR03324 37 GIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERTGRVMDVPVGDGLLGRVVDPLGRPLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 81 GKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGKTALAIDSIINQRDSGIFSIYV 160
Cdd:TIGR03324 117 GGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDRQTGKTAIAIDTILNQKGRNVLCIYC 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 161 AIGQKASTIANVVRKLEEHGALANTIVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLL 240
Cdd:TIGR03324 197 AIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSIGEHFMEQGRDVLIVYDDLTQHARAYRELSLL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 241 LKRPPGREAYPGDVFYLHSRLLERAARVSEayveaftngEVKGktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQ 320
Cdd:TIGR03324 277 LRRPPGREAFPGDIFYVHSRLLERSTHLNE---------ELGG--GSLTALPIIETEAQNISAYIPTNLISITDGQIYLS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 321 TELFNAGVRPAVDPGISVSRVGGSAQTKIVKKLSGGIRTALAQYRELAAFAQFSSDLDETTKKQLDHGQKVTELMKQKQY 400
Cdd:TIGR03324 346 PTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDENTRKTIEHGRRIRACLKQTQS 425
|
410 420 430
....*....|....*....|....*....|....*
gi 157285301 401 APFSVFDQALVIFAAERGYLQDIELNKLADFEAAL 435
Cdd:TIGR03324 426 SPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAI 460
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
25-436 |
9.24e-116 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 350.49 E-value: 9.24e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 25 ALALNLERDS-VGAVVMGPYANLKEGMKVTGTGRILEVPVGPELLGRVVNTLGE--PIDGKGPIEAKLSSP-----IEVI 96
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHevPVGLLTRSRALLESEqtlgkVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 97 APGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGKTALAIDSIINQ--------RDSGIFSIYVAIGQKAST 168
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 169 IANVVRKLEEHGALANTIVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGRE 248
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGRE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 249 AYPGDVFYLHSRLLERAARVSEAyveaftngevKGKtGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGV 328
Cdd:PTZ00185 320 AYPGDVFYLHSRLLERAAMLSPG----------KGG-GSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQ 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 329 RPAVDPGISVSRVGGSAQTKIVKKLSGGIRTALAQYRELAAFAQFSSDLDETTkkqLDHGQKVTELMKQKQYapfSVFDQ 408
Cdd:PTZ00185 389 RPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKNP---SFFMN 462
|
410 420
....*....|....*....|....*....
gi 157285301 409 ALV-IFAAERGYLQDIELNKLADFEAALL 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 |
5.78e-111 |
|
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: 325.47 E-value: 5.78e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 113 GYKAVDSMIPIGRGQRELIIGDRQIGKTALAiDSIINQRDSGIfSIYVAIGQKASTIANVVRKLEEHGALANTIVVVASA 192
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 193 SESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAARvseay 272
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGR----- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157285301 273 veaftngeVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVS 339
Cdd:pfam00006 154 --------VKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
61-341 |
2.15e-105 |
|
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: 313.62 E-value: 2.15e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 61 VPVGPELLGRVVNTLGEPIDGKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGKT 140
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 141 ALAIDSIINQ-RDSGIFSIYVAIGQKASTIANVVRKLEEHGALANTIVVVASASESAALQYLAPYAGCAMGEYFRDRGED 219
Cdd:cd19476 82 VLAMQLARNQaKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 220 ALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAARvseayveaftngeVKGKTGSLTALPIIETQAG 299
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGK-------------VKDGGGSITAIPAVSTPGD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 157285301 300 DVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 341
Cdd:cd19476 229 DLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
66-424 |
4.77e-104 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 318.46 E-value: 4.77e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 66 ELLGRVVNTLGEPIDgkgPIEAK--------LSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQI 137
Cdd:PRK07165 78 EYFGKIIDIDGNIIY---PEAQNplskkflpNTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 138 GKTALAIDSIINQRDSGIFSIYVAIGQKASTIANVVRKLEEHGALANTIVVVASaSESAALQYLAPYAGCAMGE---YFr 214
Cdd:PRK07165 155 GKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAP-STSPYEQYLAPYVAMAHAEnisYN- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 215 drgEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAarvseayveaftnGEVKGKTgSLTALPII 294
Cdd:PRK07165 233 ---DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERA-------------GKFKNRK-TITALPIL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 295 ETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIVKKLSGGIRTALAQYRELAAFAQFS 374
Cdd:PRK07165 296 QTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLD 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 157285301 375 SDLDETTKKQLDHGQKVTELMKQKQYAPFSVFDQALVIFAAERGYLQDIE 424
Cdd:PRK07165 376 YDLNKETSDLLFKGKMIEKMFNQKGFSLYSYRFVLLISKLISWGLLKDVK 425
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
60-341 |
1.83e-51 |
|
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: 174.29 E-value: 1.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 60 EVPVGPELLGRVVNTLGEPIDGKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGK 139
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 140 TALaIDSIINQRDSGIfSIYVAIGQKASTIANVVRKLEEHGALANTIVVVASASESAALQYLAPYAGCAMGEYFRDRGED 219
Cdd:cd01136 81 STL-LGMIARNTDADV-NVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 220 ALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAArvseayveaftngevKGKTGSLTALPIIETQAG 299
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAG---------------NGEKGSITAFYTVLVEGD 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 157285301 300 DVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 341
Cdd:cd01136 224 DFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
2-372 |
5.76e-50 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 175.34 E-value: 5.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 2 IIRIHGLaDVMQGEMIELPGGNYALalnLERDSV-----GAVVMGPYA---NLKEGMKVTGTGRILEVPVGPELLGRVVN 73
Cdd:PRK09099 35 LLRVSGL-DVTLGELCELRQRDGTL---LQRAEVvgfsrDVALLSPFGelgGLSRGTRVIGLGRPLSVPVGPALLGRVID 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 74 TLGEPIDGKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGKTALAidsiinqrds 153
Cdd:PRK09099 111 GLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLM---------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 154 GIF--------SIYVAIGQKASTIANVVRKLEEHGALANTIVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYD 225
Cdd:PRK09099 181 GMFargtqcdvNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 226 DLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAARvseayveaftngevkGKTGSLTALPIIETQAGDVSAFV 305
Cdd:PRK09099 261 SLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM---------------GETGSITALYTVLAEDESGSDPI 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157285301 306 PTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIVKKLSGGIRTALAQYRELAAFAQ 372
Cdd:PRK09099 326 AEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQ 392
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
346-440 |
2.97e-49 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 163.77 E-value: 2.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 346 QTKIVKKLSGGIRTALAQYRELAAFAQFSSDLDETTKKQLDHGQKVTELMKQKQYAPFSVFDQALVIFAAERGYLQDIEL 425
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90
....*....|....*
gi 157285301 426 NKLADFEAALLSFAH 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 ... |
351-440 |
1.91e-47 |
|
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: 159.07 E-value: 1.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 351 KKLSGGIRTALAQYRELAAFAQFSSDLDETTKKQLDHGQKVTELMKQKQYAPFSVFDQALVIFAAERGYLQDIELNKLAD 430
Cdd:cd18113 2 KKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIKE 81
|
90
....*....|
gi 157285301 431 FEAALLSFAH 440
Cdd:cd18113 82 FEKELLEYLR 91
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
2-366 |
3.32e-47 |
|
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: 167.90 E-value: 3.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 2 IIRIHGLaDVMQGE--MIELPGGNYALA--LNLERDSVgaVVMgPYANLKE---GMKVTGTGRILEVPVGPELLGRVVNT 74
Cdd:COG1157 30 LIEAVGP-DASIGElcEIETADGRPVLAevVGFRGDRV--LLM-PLGDLEGispGARVVPTGRPLSVPVGDGLLGRVLDG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 75 LGEPIDGKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQReliIGdrqI------GKTALaIDSII 148
Cdd:COG1157 106 LGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR---IG---IfagsgvGKSTL-LGMIA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 149 NQRDSGIfsiyvaigqkastiaNVV---------------RKLEEHGaLANTIVVVASASESAALQYLAPYAGCAMGEYF 213
Cdd:COG1157 179 RNTEADV---------------NVIaligergrevrefieDDLGEEG-LARSVVVVATSDEPPLMRLRAAYTATAIAEYF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 214 RDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAarvseayveaftnGevKGKTGSLTAL-- 291
Cdd:COG1157 243 RDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERA-------------G--NGGKGSITAFyt 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 292 ----------PIIETqagdvsafvptnVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIVKKLSGGIRTAL 361
Cdd:COG1157 308 vlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLL 375
|
....*
gi 157285301 362 AQYRE 366
Cdd:COG1157 376 ARYEE 380
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
51-410 |
4.33e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 164.93 E-value: 4.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 51 KVTGTGRILEVPVGPELLGRVVNTLGEPIDGKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQREL 130
Cdd:PRK06936 87 EVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 131 IIGDRQIGKTALaIDSIINQRDSGIfSIYVAIGQKASTianvVRKLEEHG----ALANTIVVVASASESAALQYLAPYAG 206
Cdd:PRK06936 167 IFAAAGGGKSTL-LASLIRSAEVDV-TVLALIGERGRE----VREFIESDlgeeGLRKAVLVVATSDRPSMERAKAGFVA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 207 CAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAArvseayveaftngevKGKTG 286
Cdd:PRK06936 241 TSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG---------------QSDKG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 287 SLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIVKKLSGGIRTALAQYRE 366
Cdd:PRK06936 306 SITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEE 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 157285301 367 ---LAAFAQFSSDLDETTKKQLDHGQKVTELMKQKQYAPfSVFDQAL 410
Cdd:PRK06936 386 velLLQIGEYQKGQDKEADQAIERIGAIRGFLRQGTHEL-SHFNETL 431
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
38-398 |
2.84e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 160.27 E-value: 2.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 38 VVMGPYANLKE---GMKVTGTGRILEVPVGPELLGRVVNTLGEPIDGKgPIEAKLSS-PIEVIAPGVIARKSVDQPVQTG 113
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGS-ALPKGLAPvSTDQDPPNPLKRPPIREPMEVG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 114 YKAVDSMIPIGRGQRELIIGDRQIGKTALAidSIINQRDSGIFSIYVAIGQKASTIANVV-RKLEEHGaLANTIVVVASA 192
Cdd:PRK07721 146 VRAIDSLLTVGKGQRVGIFAGSGVGKSTLM--GMIARNTSADLNVIALIGERGREVREFIeRDLGPEG-LKRSIVVVATS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 193 SESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAArvseay 272
Cdd:PRK07721 223 DQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG------ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 273 veafTNGEvkgktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIVKK 352
Cdd:PRK07721 297 ----TNAS-----GSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKE 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 157285301 353 LSGGIRTALAQYRE------LAAFAQFSS-DLDETTKKQldhgQKVTELMKQK 398
Cdd:PRK07721 368 AANRFRELLSTYQNsedlinIGAYKRGSSrEIDEAIQFY----PQIISFLKQG 416
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
8-410 |
5.02e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 159.59 E-value: 5.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 8 LADVMQGEMIEL-PGGNYALALNLERDSVgavVMGPYAN---LKEGMKVTGTGRILEVPVGPELLGRVVNTLGEPIDGKG 83
Cdd:PRK06820 45 LPGVAQGELCRIePQGMLAEVVSIEQEMA---LLSPFASsdgLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 84 PIEAKLSsPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGKTALaIDSIINQRDSGIFsIYVAIG 163
Cdd:PRK06820 122 PLTGQWR-ELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTL-LGMLCADSAADVM-VLALIG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 164 QKASTianvVRKLEEHG----ALANTIVVVASaSESAALQYL-APYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQIS 238
Cdd:PRK06820 199 ERGRE----VREFLEQVltpeARARTVVVVAT-SDRPALERLkGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 239 LLLKRPPGREAYPGDVFYLHSRLLERAArvseayveaftngevKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIF 318
Cdd:PRK06820 274 LAAGEPPAAGSFPPSVFANLPRLLERTG---------------NSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 319 LQTELFNAGVRPAVDPGISVSRVGGSAQTKIVKKLSGGIRTALAQYRE---LAAFAQFSSDLDETTKKQLDHGQKVTELM 395
Cdd:PRK06820 339 LSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEielLVRVGEYQAGEDLQADEALQRYPAICAFL 418
|
410
....*....|....*..
gi 157285301 396 KQK--QYAPFSVFDQAL 410
Cdd:PRK06820 419 QQDhsETAHLETTLEHL 435
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
59-348 |
7.49e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 156.00 E-value: 7.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 59 LEVPVGPELLGRVVNTLGEPIDGKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIG 138
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 139 KTALAidSIINQRDSGIFSIYVAIGQKASTIANVVRKlEEHGALANTIVVVASASESAALQYLAPYAGCAMGEYFRDRGE 218
Cdd:PRK08472 170 KSTLM--GMIVKGCLAPIKVVALIGERGREIPEFIEK-NLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 219 DALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAarvseayveaftnGEVKGKtGSLTALPIIETQA 298
Cdd:PRK08472 247 DVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERA-------------GKEEGK-GSITAFFTVLVEG 312
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 157285301 299 GDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTK 348
Cdd:PRK08472 313 DDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
1-366 |
3.70e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 143.60 E-value: 3.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 1 GIIRIHGLA-DVMQGEMIELPGGNyalalnleRDSVGAVV----MGPYANLKEGMKVTGTGRI------LEVPVGPELLG 69
Cdd:PRK06002 36 SHYRVRGLSrFVRLGDFVAIRADG--------GTHLGEVVrvdpDGVTVKPFEPRIEIGLGDAvfrkgpLRIRPDPSWKG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 70 RVVNTLGEPIDGKGPI-EAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGK-TALAIDSi 147
Cdd:PRK06002 108 RVINALGEPIDGLGPLaPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKsTLLAMLA- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 148 inqRDSGIFSIYVA-IGQKASTianvVRK-LEEH--GALANTIVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIV 223
Cdd:PRK06002 187 ---RADAFDTVVIAlVGERGRE----VREfLEDTlaDNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 224 YDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAARVSEAyveaftngevkgkTGSLTALPIIETQAGDVSA 303
Cdd:PRK06002 260 VDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEG-------------GGSITGIFSVLVDGDDHND 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157285301 304 FVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIVKKLSGGIRTALAQYRE 366
Cdd:PRK06002 327 PVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEE 389
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
8-402 |
5.95e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 142.78 E-value: 5.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 8 LADVMQGEMIEL-PGGNYALALNLERDSVGAVVMGPYANLKEGMKVTGTGRILEVPVGPELLGRVVNTLGEPIDGKgPIE 86
Cdd:PRK07594 37 LPGVFMGELCCIkPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 87 AKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGKTALaIDSIINQRDSGIfSIYVAIGQKA 166
Cdd:PRK07594 116 DVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLCNAPDADS-NVLVLIGERG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 167 STIANVVRKLEEHGALANTIVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPG 246
Cdd:PRK07594 194 REVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 247 REAYPGDVFYLHSRLLERAArvseayveaftngevKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNA 326
Cdd:PRK07594 274 SGEYPPGVFSALPRLLERTG---------------MGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAER 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157285301 327 GVRPAVDPGISVSRVGGSAQTKIVKKLSGGIRTALAQYRE---LAAFAQFSSDLDETTKKQLDHGQKVTELMKQKQYAP 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 |
1.13e-37 |
|
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: 138.51 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 58 ILEVPVGPELLGRVVNTLGEPIDGKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDR-- 135
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 136 -------QIGKTAlaidSIINQRDSGIFsIYVAIGQKASTIANVVRKLEEHGALANTIVVVASASESAALQYLAPYAGCA 208
Cdd:cd01135 81 phnelaaQIARQA----GVVGSEENFAI-VFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 209 MGEYFR-DRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGdvfYLHSRL---LERAarvseayveaftnGEVKGK 284
Cdd:cd01135 156 TAEYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERA-------------GRVEGR 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157285301 285 TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSA 345
Cdd:cd01135 220 KGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSG 280
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
27-367 |
1.29e-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: 142.55 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 27 ALNLERDSVGAVVMGPYANLKEGMKVTGTGRILEVPVGPELLGRVVNTLGEPIDGKGPIEAKLSSPIEVIAPGVIARKSV 106
Cdd:TIGR01039 44 AQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 107 DQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGKTALAIDSIIN-QRDSGIFSIYVAIGQKASTIANVVRKLEEHGALANT 185
Cdd:TIGR01039 124 VEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 186 IVVVASASESAALQYLAPYAGCAMGEYFRD-RGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLER 264
Cdd:TIGR01039 204 ALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQER 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 265 AARVseayveaftngevkgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVggs 344
Cdd:TIGR01039 284 ITST---------------KTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRL--- 345
|
330 340
....*....|....*....|....*..
gi 157285301 345 AQTKIVK----KLSGGIRTALAQYREL 367
Cdd:TIGR01039 346 LDPSVVGeehyDVARGVQQILQRYKEL 372
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
49-341 |
1.02e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 139.84 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 49 GMKVTGTGRILEVPVGPELLGRVVNTLGEPIDGKGPI--EAKLSSPIEVIAPgvIARKSVDQPVQTGYKAVDSMIPIGRG 126
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIytDQRASRHSPPINP--LSRRPITEPLDVGVRAINAMLTVGKG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 127 QRELIIGDRQIGKTALAIdsiINQRDSGIFSIYVA-IGQKASTIANVVRK-LEEHGaLANTIVVVASASESAALQYLAPY 204
Cdd:PRK08972 163 QRMGLFAGSGVGKSVLLG---MMTRGTTADVIVVGlVGERGREVKEFIEEiLGEEG-RARSVVVAAPADTSPLMRLKGCE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 205 AGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAArvseayveaftNGevKGK 284
Cdd:PRK08972 239 TATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAG-----------NG--GPG 305
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 157285301 285 TGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 341
Cdd:PRK08972 306 QGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRV 362
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
49-404 |
1.56e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 138.87 E-value: 1.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 49 GMKVTGTGRILEVPVGPELLGRVVNTLGEPIDGKGPI--EAKLSSPIEVIAPgvIARKSVDQPVQTGYKAVDSMIPIGRG 126
Cdd:PRK07196 78 GARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLggSTPLQQQLPQIHP--LQRRAVDTPLDVGVNAINGLLTIGKG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 127 QRELIIGDRQIGKTALAidSIINQRDSGIFSIYVAIGQKASTIANVVRKLEEHGALANTIVVVASASESAALQYLAPYAG 206
Cdd:PRK07196 156 QRVGLMAGSGVGKSVLL--GMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELC 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 207 CAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAArvseayveaftNGEvkgKTG 286
Cdd:PRK07196 234 HAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG-----------NSS---GNG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 287 SLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSR----VGGSAQTKIVKKLSGGIrTALA 362
Cdd:PRK07196 300 TMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCY-ADYM 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 157285301 363 QYRELAAFAQFSSDLDETTKKQLDHGQKVTELMKQK--QYAPFS 404
Cdd:PRK07196 379 AIKPLIPLGGYVAGADPMADQAVHYYPAITQFLRQEvgHPALFS 422
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
55-370 |
3.70e-35 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 135.12 E-value: 3.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 55 TGRILEVPVGPELLGRVVNTLGEpIDGK--GPIEAK---LSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRE 129
Cdd:PRK08149 76 TGKPLSVWVGEALLGAVLDPTGK-IVERfdAPPTVGpisEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 130 LIIGDRQIGKTALaIDSIINQRDSGIFSIYVaIGQKASTIANVVRKLEEHGALANTIVVVASASESAALQYLAPYAGCAM 209
Cdd:PRK08149 155 GIFASAGCGKTSL-MNMLIEHSEADVFVIGL-IGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTV 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 210 GEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAARVseayveaftngevkgKTGSLT 289
Cdd:PRK08149 233 AEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT---------------LAGSIT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 290 ALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIVKKLSGGIRTALAQYRELAA 369
Cdd:PRK08149 298 AFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQL 377
|
.
gi 157285301 370 F 370
Cdd:PRK08149 378 F 378
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
48-340 |
7.09e-33 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 129.18 E-value: 7.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 48 EGMKVTGTGRILEVPVGPELLGRVVNTLGEPIDGKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQ 127
Cdd:PRK04196 65 KDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 128 R------------ELIIgdrQIGKTALAIDSiinqrDSGIFSIYVAIGQKASTIANVVRKLEEHGALANTIVVVASASES 195
Cdd:PRK04196 145 KlpifsgsglphnELAA---QIARQAKVLGE-----EENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 196 AALQYLAPYAGCAMGEYFR-DRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGdvfYLHSRL---LERAarvsea 271
Cdd:PRK04196 217 AIERILTPRMALTAAEYLAfEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERA------ 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157285301 272 yveaftnGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSR 340
Cdd:PRK04196 288 -------GRIKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
40-341 |
1.51e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 125.23 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 40 MGPYANLKEGMKV---TGTGRIlevPVGPELLGRVVNTLGEPIDGKGPIEAKLSSPIE--VIAPgvIARKSVDQPVQTGY 114
Cdd:PRK05688 82 VGSVAGIAPGARVvplADTGRL---PMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDgpTINP--LNRHPISEPLDVGI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 115 KAVDSMIPIGRGQRELIIGDRQIGKTALaIDSIINQRDSGIfsIYVA-IGQKASTIANVVRKLEEHGALANTiVVVASAS 193
Cdd:PRK05688 157 RSINGLLTVGRGQRLGLFAGTGVGKSVL-LGMMTRFTEADI--IVVGlIGERGREVKEFIEHILGEEGLKRS-VVVASPA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 194 ESAALQYLAPYAGCA-MGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAArvseay 272
Cdd:PRK05688 233 DDAPLMRLRAAMYCTrIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG------ 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157285301 273 veaftNGEVKGktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 341
Cdd:PRK05688 307 -----NAEPGG--GSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV 368
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
4-368 |
6.88e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 117.77 E-value: 6.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 4 RIHGLADVM--------QGEMIELPGGNYALAL----NLER--------DSVG-----AVVMgPYANLkEGMKVTGTGRI 58
Cdd:PRK08927 8 AIGDIDTLViygrvvavRGLLVEVAGPIHALSVgariVVETrggrpvpcEVVGfrgdrALLM-PFGPL-EGVRRGCRAVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 59 LE----VPVGPELLGRVVNTLGEPIDGKGPI-EAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIG 133
Cdd:PRK08927 86 ANaaaaVRPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 134 DRQIGKTALAidSIINQRDSGIFSIYVAIGQKASTIANVVRK-LEEHGaLANTIVVVASASESAALQYLAPYAGCAMGEY 212
Cdd:PRK08927 166 GSGVGKSVLL--SMLARNADADVSVIGLIGERGREVQEFLQDdLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAIAEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 213 FRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAarvseayveaftnGEVKGKTGSLTALP 292
Cdd:PRK08927 243 FRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERA-------------GPGPIGEGTITGLF 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157285301 293 IIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIVKKLSGGIRTALAQYRELA 368
Cdd:PRK08927 310 TVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADME 385
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
60-421 |
3.46e-28 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 116.04 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 60 EVPVGPELLGRVVNTLGEPIDGKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGK 139
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 140 TAL-AIDSIINQRDSGIFSIyvaIGQKASTIANVVRKLEEHGALANTIVVVASASESAALQYL-APYAgCAMGEYFRDRG 217
Cdd:PRK07960 189 SVLlGMMARYTQADVIVVGL---IGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQgAAYA-TRIAEDFRDRG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 218 EDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAArvseayveaftNGEVKGktGSLTALPIIETQ 297
Cdd:PRK07960 265 QHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG-----------NGISGG--GSITAFYTVLTE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 298 AGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRvggsAQTKIVKKlsggirtalAQYRELAAFAQFSSDL 377
Cdd:PRK07960 332 GDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISR----AMTALIDE---------QHYARVRQFKQLLSSF 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 157285301 378 dettkkqldhgQKVTELMKQKQYAPFS--VFDQALVIFAAERGYLQ 421
Cdd:PRK07960 399 -----------QRNRDLVSVGAYAKGSdpMLDKAIALWPQLEAFLQ 433
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
49-366 |
1.87e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 113.53 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 49 GMKVTGTGRILEVPVGPELLGRVVNTLGEPIDGkgPIEAKLSSPIEVIAPGVIA--RKSVDQPVQTGYKAVDSMIPIGRG 126
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIHAfeREEITDVFETGIKSIDSMLTIGIG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 127 QRELIIGDRQIGKTALAidSIINQRDSGIFSIYVAIGQKASTIANVVRK-LEEHGaLANTIVVVASASESAALQYLAPYA 205
Cdd:PRK06793 157 QKIGIFAGSGVGKSTLL--GMIAKNAKADINVISLVGERGREVKDFIRKeLGEEG-MRKSVVVVATSDESHLMQLRAAKL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 206 GCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPgreaYPGDVFYLHS---RLLERAArvseayveaftngevK 282
Cdd:PRK06793 234 ATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSG---------------K 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 283 GKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSAQTKIVKKLSGGIRTALA 362
Cdd:PRK06793 295 TQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILS 374
|
....
gi 157285301 363 QYRE 366
Cdd:PRK06793 375 IYKE 378
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
40-340 |
3.10e-27 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 113.08 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 40 MGPYANLKEGMKVTGTGRILEVPVGPELLGRVVNTLGEPIDGKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDS 119
Cdd:PRK05922 71 LSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 120 MIPIGRGQRELIIGDRQIGKTALAidSIINQRDSGIFSIYVAIGQKASTIANVVRKLEEHGALANTIVVVASASESAALQ 199
Cdd:PRK05922 151 FLTLGKGQRIGVFSEPGSGKSSLL--STIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 200 YLAPYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAArvseayveaftng 279
Cdd:PRK05922 229 VIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG------------- 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157285301 280 evKGKTGSLTALPIIETQAGDVSAFVPTnVISITDGQIFLqTELFNAGVRPAVDPGISVSR 340
Cdd:PRK05922 296 --NNDKGSITALYAILHYPNHPDIFTDY-LKSLLDGHFFL-TPQGKALASPPIDILTSLSR 352
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
55-345 |
1.26e-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: 111.35 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 55 TGRILEVPVGPELLGRVVNTLGEPIDGKGPI--EAKLSSPIEVIAPgvIARKSVDQPVQTGYKAVDSMIPIGRGQRELII 132
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVlaEDYLDINGQPINP--YARIYPEEMIQTGISAIDVMNSIARGQKIPIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 133 GD-------------RQIGKTALAIDSIINQRDSGIFSIYVAIGQKASTIANVVRKLEEHGALANTIVVVASASESAALQ 199
Cdd:TIGR01040 148 SAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIER 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 200 YLAPYAGCAMGEYFR-DRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAARVseayveaftn 278
Cdd:TIGR01040 228 IITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV---------- 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157285301 279 gevKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVGGSA 345
Cdd:TIGR01040 298 ---EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 361
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
60-341 |
1.02e-24 |
|
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: 102.68 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 60 EVPVGPELLGRVVNTLGEPIDGKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGK 139
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 140 TALaIDSIINQ--RDSGIFSIYVAIGQKASTIANVVRKLEEHG-----ALANTIVVVASASESAALQYLAPYAGCAMGEY 212
Cdd:cd01133 81 TVL-IMELINNiaKAHGGYSVFAGVGERTREGNDLYHEMKESGvinldGLSKVALVYGQMNEPPGARARVALTGLTMAEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 213 FRD-RGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSRLLERAARVseayveaftngevkgKTGSLTAL 291
Cdd:cd01133 160 FRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST---------------KKGSITSV 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 157285301 292 PIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRV 341
Cdd:cd01133 225 QAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
33-367 |
2.94e-24 |
|
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: 104.40 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 33 DSVGAVVMGPYANLKEGMKVTGTGRILEVPVGPELLGRVVNTLGEPIDGKGPIEAKLSSPIEVIAPGVIARKSVDQPVQT 112
Cdd:COG0055 53 NTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILET 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 113 GYKAVDSMIPIGRGQRELIIGDRQIGKTALaIDSIIN---QRDSGIfSIYVAIGQKASTIANVVRKLEEHGALANTIVVV 189
Cdd:COG0055 133 GIKVIDLLAPYAKGGKIGLFGGAGVGKTVL-IMELIHniaKEHGGV-SVFAGVGERTREGNDLYREMKESGVLDKTALVF 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 190 ASASESAALQYLAPYAGCAMGEYFRD-RGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAY-P---GDVfylhSRLLER 264
Cdd:COG0055 211 GQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYqPtlaTEM----GALQER 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 265 AARVseayveaftngevkgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSRVggs 344
Cdd:COG0055 287 ITST---------------KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRI--- 348
|
330 340
....*....|....*....|....*..
gi 157285301 345 AQTKIVKK----LSGGIRTALAQYREL 367
Cdd:COG0055 349 LDPLIVGEehyrVAREVQRILQRYKEL 375
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
21-340 |
4.55e-22 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 97.80 E-value: 4.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 21 GGNYALALNLERDSVGAVVMGPYANLKEGMKVTGTGRILEVPVGPELLGRVVNTLGEPIDGKGPIEAKlssPIEVIAPGV 100
Cdd:PRK02118 36 GSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGE---PIEIGGPSV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 101 --IARKSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQIGKTALAIdSIINQRDSGIFsIYVAIGQKASTIANVVRKLEE 178
Cdd:PRK02118 113 npVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA-RIALQAEADII-ILGGMGLTFDDYLFFKDTFEN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 179 HGALANTIVVVASASESAALQYLAPYAGCAMGEYFR-DRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYL 257
Cdd:PRK02118 191 AGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 258 HSRLLERAARVSEAyveaftngevkgktGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQtelfnagvRPAVDPGIS 337
Cdd:PRK02118 271 LASRYEKAVDFEDG--------------GSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLR--------RGRIDPFGS 328
|
...
gi 157285301 338 VSR 340
Cdd:PRK02118 329 LSR 331
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
35-367 |
3.81e-21 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 95.49 E-value: 3.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 35 VGAVVMGPYANLKEGMKVTGTGRILEVPVGPELLGRVVNTLGEPIDGKGPIEAKLSSPIEVIAPGVIARKSVDQPVQTGY 114
Cdd:CHL00060 70 VRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 115 KAVDSMIPIGRGQRELIIGDRQIGKTALAIDSIIN-QRDSGIFSIYVAIGQKASTIANVVRKLEEHGalantIVVVASAS 193
Cdd:CHL00060 150 KVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGERTREGNDLYMEMKESG-----VINEQNIA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 194 ES-AALQY----LAPYA-------GCAMGEYFRD-RGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGDVFYLHSR 260
Cdd:CHL00060 225 ESkVALVYgqmnEPPGArmrvgltALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 261 LLERAARVseayveaftngevkgKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLQTELFNAGVRPAVDPGISVSR 340
Cdd:CHL00060 305 LQERITST---------------KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTST 369
|
330 340 350
....*....|....*....|....*....|.
gi 157285301 341 VggsAQTKIVK----KLSGGIRTALAQYREL 367
Cdd:CHL00060 370 M---LQPRIVGeehyETAQRVKQTLQRYKEL 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 |
4.71e-21 |
|
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: 86.35 E-value: 4.71e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 157285301 1 GIIRIHGLADVMQGEMIELPGGNYALALNLERDSVGAVVMGPYANLKEGMKVTGTGR 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 |
7.49e-19 |
|
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: 86.47 E-value: 7.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 59 LEVPVGPELLGRVVNTLGEPIDgkgpIEAKLSSPIevIAPGV------------IARK-SVDQPVQTGYKAVDSMIPIGR 125
Cdd:cd01134 2 LSVELGPGLLGSIFDGIQRPLE----VIAETGSIF--IPRGVnvqrwpvrqprpVKEKlPPNVPLLTGQRVLDTLFPVAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 126 GQRELIIGDRQIGKTALaIDSIINQRDSGIFsIYVAIGQKASTIANVVR-----KLEEHGA--------LANTIVVVASA 192
Cdd:cd01134 76 GGTAAIPGPFGCGKTVI-SQSLSKWSNSDVV-IYVGCGERGNEMAEVLEefpelKDPITGEslmertvlIANTSNMPVAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 193 SESAAlqylapYAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGdvfYLHSRL---LERAARVS 269
Cdd:cd01134 154 REASI------YTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYERAGRVR 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157285301 270 eayveafTNGEvKGKTGSLTALPIIETQAGDVSAFVPTNVISITdgQIF--LQTELFNAGVRPAVDPGISVSR 340
Cdd:cd01134 225 -------CLGS-PGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
204-290 |
2.09e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 62.49 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 204 YAGCAMGEYFRDRGEDALIVYDDLSKQAVAYRQISLLLKRPPGREAYPGdvfYLHSRL---LERAARVSeayveafTNGe 280
Cdd:PRK04192 310 YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASRLaefYERAGRVK-------TLG- 378
|
90
....*....|
gi 157285301 281 vkGKTGSLTA 290
Cdd:PRK04192 379 --GEEGSVTI 386
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
158-312 |
2.78e-10 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 62.73 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 158 IYVAIGQKASTIANVvrkLEEHGALAN----------TIVVVASASESAALQYLAPYAGCAMGEYFRDRGEDALIVYDDL 227
Cdd:PRK14698 686 IYIGCGERGNEMTDV---LEEFPKLKDpktgkplmerTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADST 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157285301 228 SKQAVAYRQISLLLKRPPGREAYPGdvfYLHSRL---LERAARVseayveaFTNGEvKGKTGSLTALPIIETQAGDVSAF 304
Cdd:PRK14698 763 SRWAEALREISGRLEEMPGEEGYPA---YLASKLaefYERAGRV-------VTLGS-DYRVGSVSVIGAVSPPGGDFSEP 831
|
....*...
gi 157285301 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, ... |
350-414 |
7.05e-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: 52.06 E-value: 7.05e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157285301 350 VKKLSGGIRTALAQYRELAAFAQFSSD--LDETTKKQLDHGQKVTELMKQKQYAPFSVFDQALVIFA 414
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYP 67
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
1-56 |
2.16e-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: 2.16e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 157285301 1 GIIRIHGLADVMQGEMIELPGGNYALALNLERDSVGAVVMGPYANLKEGMKVTGTG 56
Cdd:pfam02874 14 GIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| |
