|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-559 |
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: 1012.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 1 MQLRAEEISQIIKKQIQNIDKAALVSETGTVLTVGDGIARVHGLSRAMAGELIEFTGqggeTLAGLVLNLEQDNVGSAIF 80
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPG----GVYGMALNLEEDNVGVVLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 81 GDTSVIREGDSVKRTGRIMDVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAM 160
Cdd:COG0056 77 GDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 161 IPIGRGQRELIIGDRQTGKTAVAIDAILNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQY 240
Cdd:COG0056 157 IPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 241 IAPYTGVTIGEYFRDTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKMAEifyvvkkgtt 320
Cdd:COG0056 237 IAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSD---------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 321 ikggeidkgvdgkahvgAHGmseakksleetkksqggdleivkepwsGGSLTALPVIETQAGDVSAYIPTNVISITDGQI 400
Cdd:COG0056 307 -----------------ELG---------------------------GGSLTALPIIETQAGDVSAYIPTNVISITDGQI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 401 FLESDLFFSGVRPAINVGISVSRVGGNAQIKAMKSIAGTLRLDLAQYRAMAAFAQFASDLDARTRQQLERGARLVEILKQ 480
Cdd:COG0056 343 FLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERGERLVELLKQ 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1127363094 481 GQYVPLPVEKQILIIFAGTQGLLDDLPVGELRRFEEELFKFVESKHSTILPDIINKKALDDDLKARMKAAIEAFKKKFV 559
Cdd:COG0056 423 PQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGKLDDEIEEKLKAAIEEFKKTFA 501
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-559 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 1010.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 1 MQLRAEEISQIIKKQIQNIDKAALVSETGTVLTVGDGIARVHGLSRAMAGELIEFtgQGGetLAGLVLNLEQDNVGSAIF 80
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEF--PGG--VYGIALNLEEDNVGAVIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 81 GDTSVIREGDSVKRTGRIMDVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAM 160
Cdd:PRK09281 77 GDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 161 IPIGRGQRELIIGDRQTGKTAVAIDAILNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQY 240
Cdd:PRK09281 157 IPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 241 IAPYTGVTIGEYFRDTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKMAEifyvvkkgtt 320
Cdd:PRK09281 237 LAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSD---------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 321 ikggeiDKGvdgkahvgahgmseakksleetkksqggdleivkepwsGGSLTALPVIETQAGDVSAYIPTNVISITDGQI 400
Cdd:PRK09281 307 ------ELG--------------------------------------GGSLTALPIIETQAGDVSAYIPTNVISITDGQI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 401 FLESDLFFSGVRPAINVGISVSRVGGNAQIKAMKSIAGTLRLDLAQYRAMAAFAQFASDLDARTRQQLERGARLVEILKQ 480
Cdd:PRK09281 343 FLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERGQRLVELLKQ 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1127363094 481 GQYVPLPVEKQILIIFAGTQGLLDDLPVGELRRFEEELFKFVESKHSTILPDIINKKALDDDLKARMKAAIEAFKKKFV 559
Cdd:PRK09281 423 PQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKDLSDEIEAKLKAAIEEFKKTFA 501
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
2-559 |
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: 841.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 2 QLRAEEISQIIKKQIQNIDKAALVSETGTVLTVGDGIARVHGLSRAMAGELIEFTGqggeTLAGLVLNLEQDNVGSAIFG 81
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEG----GVQGIALNLEEDSVGAVIMG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 82 DTSVIREGDSVKRTGRIMDVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMI 161
Cdd:TIGR00962 77 DYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 162 PIGRGQRELIIGDRQTGKTAVAIDAILNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYI 241
Cdd:TIGR00962 157 PIGRGQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 242 APYTGVTIGEYFRDTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKMAEifyvvkkgtti 321
Cdd:TIGR00962 237 APYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLND----------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 322 kggeiDKGvdgkahvgahgmseakksleetkksqggdleivkepwsGGSLTALPVIETQAGDVSAYIPTNVISITDGQIF 401
Cdd:TIGR00962 306 -----EKG--------------------------------------GGSLTALPIIETQAGDVSAYIPTNVISITDGQIF 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 402 LESDLFFSGVRPAINVGISVSRVGGNAQIKAMKSIAGTLRLDLAQYRAMAAFAQFASDLDARTRQQLERGARLVEILKQG 481
Cdd:TIGR00962 343 LESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASDLDEATKKQLERGQRVVELLKQP 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1127363094 482 QYVPLPVEKQILIIFAGTQGLLDDLPVGELRRFEEELFKFVESKHSTILPDIINKKALDDDLKARMKAAIEAFKKKFV 559
Cdd:TIGR00962 423 QYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKLTEELEAKLKEALKNFKKTFA 500
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-558 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 749.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 1 MQLRAEEISQIIKKQIQNIDKAALVSETGTVLTVGDGIARVHGLSRAMAGELIEFtgQGGETlaGLVLNLEQDNVGSAIF 80
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRF--EGGSR--GFAFNLEEELVGAVLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 81 GDTSVIREGDSVKRTGRIMDVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAM 160
Cdd:PRK13343 77 DDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 161 IPIGRGQRELIIGDRQTGKTAVAIDAILNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQY 240
Cdd:PRK13343 157 IPIGRGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 241 IAPYTGVTIGEYFRDTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKMAEifyvvkkgtt 320
Cdd:PRK13343 237 LAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSP---------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 321 ikggeidkgvdgkahvgAHGmseakksleetkksqggdleivkepwsGGSLTALPVIETQAGDVSAYIPTNVISITDGQI 400
Cdd:PRK13343 307 -----------------ELG---------------------------GGSLTALPIIETLAGELSAYIPTNLISITDGQI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 401 FLESDLFFSGVRPAINVGISVSRVGGNAQIKAMKSIAGTLRLDLAQYRAMAAFAQFASDLDARTRQQLERGARLVEILKQ 480
Cdd:PRK13343 343 YLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLLDAGTQKQITRGRRLRELLKQ 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1127363094 481 GQYVPLPVEKQILIIFAGTQGLLDDLPVGELRRFEEELFKFVESKHSTILPDIINKKALDDDLKARMKAAIEAFKKKF 558
Cdd:PRK13343 423 PRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRELDEAWLAALEEILREAGERF 500
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
25-559 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 742.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 25 VSETGTVLTVGDGIARVHGLSRAMAGELIEFtgqgGETLAGLVLNLEQDNVGSAIFGDTSVIREGDSVKRTGRIMDVPVG 104
Cdd:CHL00059 4 IVNTGTVLQVGDGIARIYGLDEVMAGELVEF----EDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 105 EAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGKTAVAI 184
Cdd:CHL00059 80 EAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 185 DAILNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGVTIGEYFRDTGRHALCVY 264
Cdd:CHL00059 160 DTILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 265 DDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKMAeifyvvkkgttikggeidkgvdgkahvgahgmsea 344
Cdd:CHL00059 240 DDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLS----------------------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 345 kksleetkkSQGGdleivkepwsGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLFFSGVRPAINVGISVSRV 424
Cdd:CHL00059 285 ---------SQLG----------EGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRV 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 425 GGNAQIKAMKSIAGTLRLDLAQYRAMAAFAQFASDLDARTRQQLERGARLVEILKQGQYVPLPVEKQILIIFAGTQGLLD 504
Cdd:CHL00059 346 GSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQSAPLTVEEQVATIYTGTNGYLD 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1127363094 505 DLPVGELRRFEEELFKFVESKHSTILPDIINKKALDDDLKARMKAAIEAFKKKFV 559
Cdd:CHL00059 426 SLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQLELFL 480
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
98-425 |
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: 566.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 98 IMDVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQT 177
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 178 GKTAVAIDAILNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGVTIGEYFRDTG 257
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 258 RHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKMAEifyvvKKGttikggeidkgvdgkahvg 337
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSD-----ELG------------------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 338 ahgmseakksleetkksqggdleivkepwsGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLFFSGVRPAINV 417
Cdd:cd01132 217 ------------------------------GGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINV 266
|
....*...
gi 1127363094 418 GISVSRVG 425
Cdd:cd01132 267 GLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
8-547 |
0e+00 |
|
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic species, including Methanosarcina barkeri, have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 alpha subunit of this apparent second ATP synthase.
Pssm-ID: 132367 [Multi-domain] Cd Length: 497 Bit Score: 543.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 8 ISQIIKKQIQNIDKAA-------LVSETGTVLTVGDGIARVHGLSRAMAGELIEFTGQggetLAGLVLNLEQDNVGSAIF 80
Cdd:TIGR03324 1 LTEVLDKAFQQLDQAResfqpqlTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGG----LLGIAFNVDEDEVGVVLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 81 GDTSVIREGDSVKRTGRIMDVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAM 160
Cdd:TIGR03324 77 GEYSHLQAGDEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 161 IPIGRGQRELIIGDRQTGKTAVAIDAILNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQY 240
Cdd:TIGR03324 157 IPIGRGQRELILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 241 IAPYTGVTIGEYFRDTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKMaeifyvvkkgtt 320
Cdd:TIGR03324 237 IAPYAATSIGEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHL------------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 321 ikggeidkgvdgkahvgahgmseakksleetkksqggdleivKEPWSGGSLTALPVIETQAGDVSAYIPTNVISITDGQI 400
Cdd:TIGR03324 305 ------------------------------------------NEELGGGSLTALPIIETEAQNISAYIPTNLISITDGQI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 401 FLESDLFFSGVRPAINVGISVSRVGGNAQIKAMKSIAGTLRLDLAQYRAMAAFAQFASDLDARTRQQLERGARLVEILKQ 480
Cdd:TIGR03324 343 YLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDENTRKTIEHGRRIRACLKQ 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1127363094 481 GQYVPLPVEKQILIIFAGTQGLLDDLPVGELRRFEEELFKFVESKHSTILPDIINKKALDDDLKARM 547
Cdd:TIGR03324 423 TQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSDEDREQI 489
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
64-515 |
4.64e-117 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 359.74 E-value: 4.64e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 64 AGLVLNLEQDN-VGSAIFGDTSVIREGDSVKRTGRIMDVPVGEAVVGRVVNALG--MPID----GKGPIESPHRR-RVEV 135
Cdd:PTZ00185 79 AGLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGheVPVGlltrSRALLESEQTLgKVDA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 136 KAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGKTAVAIDAILNQ--------KGKGVYCVYVAIGQKLS 207
Cdd:PTZ00185 159 GAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 208 TVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGVTIGEYFRDTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGR 287
Cdd:PTZ00185 239 NVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 288 EAYPGDVFYLHSRLLERAAKMAEifyvvkkgttikggeidkgvdGKAhvgahgmseakksleetkksqggdleivkepws 367
Cdd:PTZ00185 319 EAYPGDVFYLHSRLLERAAMLSP---------------------GKG--------------------------------- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 368 GGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLFFSGVRPAINVGISVSRVGGNAQIKAMKSIAGTLRLDLAQY 447
Cdd:PTZ00185 345 GGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAMKAVAGKLKGILAEY 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1127363094 448 RAMAAfaqfasdlDARTRQQLE-----RGARLVEILKQGQyvPLPVEKQILIIFAGTQGLLDDLPVGELRRFE 515
Cdd:PTZ00185 425 RKLAA--------DSVGGSQVQtvpmiRGARFVALFNQKN--PSFFMNALVSLYACLNGYLDDVKVNYAKLYE 487
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
153-422 |
1.37e-104 |
|
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: 314.29 E-value: 1.37e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 153 GLKAVDAMIPIGRGQRELIIGDRQTGKTAVAiDAILNQKGKGVyCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATA 232
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 233 SETAPIQYIAPYTGVTIGEYFRDTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKMAEif 312
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKG-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 313 yvvkkgttikggeidkgvdgkahvgahgmseakksleetkksqggdleivkepwSGGSLTALPVIETQAGDVSAYIPTNV 392
Cdd:pfam00006 157 ------------------------------------------------------KGGSITALPTVLVPGDDITDPIPDNT 182
|
250 260 270
....*....|....*....|....*....|
gi 1127363094 393 ISITDGQIFLESDLFFSGVRPAINVGISVS 422
Cdd:pfam00006 183 RSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
100-424 |
2.06e-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: 310.93 E-value: 2.06e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 100 DVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGK 179
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 180 TAVAIDAILNQ-KGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGVTIGEYFRDTGR 258
Cdd:cd19476 81 TVLAMQLARNQaKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 259 HALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKMaeifyvvkkgttiKGGeidkgvdgkahvga 338
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKV-------------KDG-------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 339 hgmseakksleetkksqggdleivkepwsGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLFFSGVRPAINVG 418
Cdd:cd19476 214 -----------------------------GGSITAIPAVSTPGDDLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVL 264
|
....*.
gi 1127363094 419 ISVSRV 424
Cdd:cd19476 265 DSTSRV 270
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
136-480 |
3.50e-83 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 269.15 E-value: 3.50e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 136 KAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGKTAVAIDAILNQKGKGVYCVYVAIGQKLSTVRQVVDK 215
Cdd:PRK07165 113 LAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYET 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 216 LESHGAMEYTTVVAAtASETAPIQYIAPYTGVTIGE---YFRDtgrhALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPG 292
Cdd:PRK07165 193 LKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAEnisYNDD----VLIVFDDLTKHANIYREIALLTNKPVGKEAFPG 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 293 DVFYLHSRLLERAAKmaeifYVVKKgttikggeidkgvdgkahvgahgmseakksleetkksqggdleivkepwsggSLT 372
Cdd:PRK07165 268 DMFFAHSKLLERAGK-----FKNRK----------------------------------------------------TIT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 373 ALPVIETQAGDVSAYIPTNVISITDGQIFLESDLFFSGVRPAINVGISVSRVGGNAQIKAMKSIAGTLRLDLAQYRAMAA 452
Cdd:PRK07165 291 ALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLK 370
|
330 340
....*....|....*....|....*...
gi 1127363094 453 FAQFASDLDARTRQQLERGARLVEILKQ 480
Cdd:PRK07165 371 LSMLDYDLNKETSDLLFKGKMIEKMFNQ 398
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
433-558 |
3.30e-68 |
|
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: 216.85 E-value: 3.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 433 MKSIAGTLRLDLAQYRAMAAFAQFASDLDARTRQQLERGARLVEILKQGQYVPLPVEKQILIIFAGTQGLLDDLPVGELR 512
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1127363094 513 RFEEELFKFVESKHSTILPDIINKKALDDDLKARMKAAIEAFKKKF 558
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
429-554 |
2.17e-66 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 212.30 E-value: 2.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 429 QIKAMKSIAGTLRLDLAQYRAMAAFAQFASDLDARTRQQLERGARLVEILKQGQYVPLPVEKQILIIFAGTQGLLDDLPV 508
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1127363094 509 GELRRFEEELFKFVESKHSTILPDIINKKALDDDLKARMKAAIEAF 554
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
11-481 |
8.47e-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: 167.52 E-value: 8.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 11 IIKKQIQNIDKAALVSETGTVLTVGDGIARVHGLsRAMAGELIEFTGQGGETLAGLVLNLEQDNVGSAIFGDTSVIREGD 90
Cdd:COG1157 3 RLARLLARLEELPPVRVSGRVTRVVGLLIEAVGP-DASIGELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGISPGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 91 SVKRTGRIMDVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRel 170
Cdd:COG1157 82 RVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 171 iigdrqtgktaVAIDAilnqkGKGV-----------YC----VYVA-IGQKLSTVRQVVDK-LESHGaMEYTTVVAATAS 233
Cdd:COG1157 160 -----------IGIFA-----GSGVgkstllgmiarNTeadvNVIAlIGERGREVREFIEDdLGEEG-LARSVVVVATSD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 234 ETAPIQYIAPYTGVTIGEYFRDTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAakmaeify 313
Cdd:COG1157 223 EPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERA-------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 314 vvkkgttikggeidkgvdgkahvgahGMSEakksleetkksqggdleivkepwsGGSLTAL------------PVIETqa 381
Cdd:COG1157 295 --------------------------GNGG------------------------KGSITAFytvlvegddmndPIADA-- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 382 gdvsayiptnVISITDGQIFLESDLFFSGVRPAINVGISVSRVggnaqikaMKSIAGTLRLDLAQY--RAMAAFAQfASD 459
Cdd:COG1157 323 ----------VRGILDGHIVLSRKLAERGHYPAIDVLASISRV--------MPDIVSPEHRALARRlrRLLARYEE-NED 383
|
490 500 510
....*....|....*....|....*....|..
gi 1127363094 460 L----------DARTRQQLERGARLVEILKQG 481
Cdd:COG1157 384 LirigayqpgsDPELDEAIALIPAIEAFLRQG 415
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
101-424 |
3.51e-43 |
|
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: 155.41 E-value: 3.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 101 VPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGKT 180
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 181 aVAIDAILNQKGKGVYcVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGVTIGEYFRDTGRHA 260
Cdd:cd01136 82 -TLLGMIARNTDADVN-VIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 261 LCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAakmaeifyvvkkgttikggeidkgvdgkahvgahG 340
Cdd:cd01136 160 LLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERA----------------------------------G 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 341 MSEAkksleetkksqggdleivkepwsgGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLFFSGVRPAINVGIS 420
Cdd:cd01136 206 NGEK------------------------GSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLAS 261
|
....
gi 1127363094 421 VSRV 424
Cdd:cd01136 262 ISRV 265
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
17-455 |
1.52e-42 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 158.78 E-value: 1.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 17 QNIDKAALVSETGTVLTVGDGIARVHGLSRAMaGELIEFTGQGGETL-AGLVLNLEQDNVGSAIFGDTSVIREGDSVKRT 95
Cdd:PRK09099 14 RELAALPAVRRTGKVVEVIGTLLRVSGLDVTL-GELCELRQRDGTLLqRAEVVGFSRDVALLSPFGELGGLSRGTRVIGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 96 GRIMDVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDR 175
Cdd:PRK09099 93 GRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 176 QTGKTavaidAILNQKGKGVYC---VYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGVTIGEY 252
Cdd:PRK09099 173 GVGKS-----TLMGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 253 FRDTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAakmaeifyvvkkgttikggeidkgvdg 332
Cdd:PRK09099 248 FRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERA--------------------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 333 kahvgahGMSEAkksleetkksqggdleivkepwsgGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLFFSGVR 412
Cdd:PRK09099 301 -------GMGET------------------------GSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQY 349
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1127363094 413 PAINVGISVSRVGGNAQIKAMKSIAGTLRLDLAQYRAMAAFAQ 455
Cdd:PRK09099 350 PAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQ 392
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-493 |
2.24e-39 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 149.58 E-value: 2.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 29 GTVLTVGDGIARVhGLSRAMAGELIEFTGQGgetLAGLVLNLEQDNVGSAIFGDTSVIREGDSVKRTGRIMDVPVGEAVV 108
Cdd:PRK06820 31 GPIVEIGPTLLRA-SLPGVAQGELCRIEPQG---MLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 109 GRVVNALGMPIDGkGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGKTAVAidAIL 188
Cdd:PRK06820 107 GRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLL--GML 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 189 NQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGVTIGEYFRDTGRHALCVYDDLS 268
Cdd:PRK06820 184 CADSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 269 KQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAkmaeifyvvkkgttikggeidkgvdgkahvgahgmseakksl 348
Cdd:PRK06820 264 RYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG------------------------------------------ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 349 eetkksqggdleivkePWSGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLFFSGVRPAINVGISVSRVGGNA 428
Cdd:PRK06820 302 ----------------NSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQI 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 429 QIKAMKSIAGTLRLDLAQYRAMAAFAQ---FASDLDARTRQQLERGARLVEILKQ--GQYVPLPVEKQIL 493
Cdd:PRK06820 366 VSAGQLAMAQKLRRMLACYQEIELLVRvgeYQAGEDLQADEALQRYPAICAFLQQdhSETAHLETTLEHL 435
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
24-480 |
7.45e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 145.53 E-value: 7.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 24 LVSETGTVLTVGDGIARVHGLSR-AMAGELIEFTGQGGETLaGLVLNLEQDNVGSAIFGDTSVIREGDSVKRTGRIMDVP 102
Cdd:PRK06002 23 LVRIGGTVSEVTASHYRVRGLSRfVRLGDFVAIRADGGTHL-GEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGPLRIRP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 103 vGEAVVGRVVNALGMPIDGKGPI-ESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGK-T 180
Cdd:PRK06002 102 -DPSWKGRVINALGEPIDGLGPLaPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKsT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 181 AVAIDAilnqKGKGVYCVYVA-IGQKLSTVRQVV-DKLESHgaMEYTTVVAATASETAPIQYIAPYTGVTIGEYFRDTGR 258
Cdd:PRK06002 181 LLAMLA----RADAFDTVVIAlVGERGREVREFLeDTLADN--LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 259 HALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAkmaeifyvvkkgttikggeidKGVDGkahvga 338
Cdd:PRK06002 255 NVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAG---------------------PGAEG------ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 339 hgmseakksleetkksqggdleivkepwsGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLFFSGVRPAINVG 418
Cdd:PRK06002 308 -----------------------------GGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPL 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1127363094 419 ISVSRVGGNAQIKAMKSIAGTLRLDLAQY------RAMAAFAQFA-SDLDARTRQQlergARLVEILKQ 480
Cdd:PRK06002 359 ASISRLARHAWTPEQRKLVSRLKSMIARFeetrdlRLIGGYRAGSdPDLDQAVDLV----PRIYEALRQ 423
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
81-481 |
3.55e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 137.96 E-value: 3.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 81 GDTSVIREGDSVKRTGRIMDVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAM 160
Cdd:PRK06936 77 GEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 161 IPIGRGQRELIIGDRQTGKTAVAIDAIlnqKGKGV-YCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQ 239
Cdd:PRK06936 157 LTCGEGQRMGIFAAAGGGKSTLLASLI---RSAEVdVTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMER 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 240 YIAPYTGVTIGEYFRDTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAakmaeifyvvkkgt 319
Cdd:PRK06936 234 AKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERA-------------- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 320 tikgGEIDKgvdgkahvgahgmseakksleetkksqggdleivkepwsgGSLTALPVIETQAGDVSAYIPTNVISITDGQ 399
Cdd:PRK06936 300 ----GQSDK----------------------------------------GSITALYTVLVEGDDMTEPVADETRSILDGH 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 400 IFLESDLFFSGVRPAINVGISVSRVGGNAQIKAMKSIAGTLRLDLAQYRAMAAFAQ---FASDLDARTRQQLERGARLVE 476
Cdd:PRK06936 336 IILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQigeYQKGQDKEADQAIERIGAIRG 415
|
....*
gi 1127363094 477 ILKQG 481
Cdd:PRK06936 416 FLRQG 420
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
38-447 |
9.38e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 133.69 E-value: 9.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 38 IARVHGLS------RAMAGEL--IEFTGQGGETLAGLVLNLEQDNVGSAIFGDTSVIREGDSVKRTGRIMDVPVGEAVVG 109
Cdd:PRK07721 22 VSRVIGLMieskgpESSIGDVcyIHTKGGGDKAIKAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSGLIG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 110 RVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGKT------AVA 183
Cdd:PRK07721 102 QVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKStlmgmiARN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 184 IDAILNqkgkgvycVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGVTIGEYFRDTGRHALCV 263
Cdd:PRK07721 182 TSADLN--------VIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLM 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 264 YDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAakmaeifyvvkkGTTIKggeidkgvdgkahvgahgmse 343
Cdd:PRK07721 254 MDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERT------------GTNAS--------------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 344 akksleetkksqggdleivkepwsgGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLFFSGVRPAINVGISVSR 423
Cdd:PRK07721 301 -------------------------GSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSR 355
|
410 420
....*....|....*....|....
gi 1127363094 424 VGGNAQIKAMKSIAGTLRLDLAQY 447
Cdd:PRK07721 356 VMNHIVSPEHKEAANRFRELLSTY 379
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
28-448 |
1.89e-33 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 132.77 E-value: 1.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 28 TGTVLTVGDGIARVHgLSRAMAGELIEFTGQGGetLAGLVlNLEQDNVGSAIFGDTSVIREGDSVKRTGRIMDVPVGEAV 107
Cdd:PRK07594 22 WGRIQDVSATLLNAW-LPGVFMGELCCIKPGEE--LAEVV-GINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 108 VGRVVNALGMPIDGKGPIESPHrRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGKTAVAidAI 187
Cdd:PRK07594 98 LGRVIDGFGRPLDGRELPDVCW-KDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLL--AM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 188 LNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGVTIGEYFRDTGRHALCVYDDL 267
Cdd:PRK07594 175 LCNAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 268 SKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAakmaeifyvvkkgttikggeidkgvdgkahvgahGMSEAkks 347
Cdd:PRK07594 255 TRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERT----------------------------------GMGEK--- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 348 leetkksqggdleivkepwsgGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLFFSGVRPAINVGISVSRVGGN 427
Cdd:PRK07594 298 ---------------------GSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPV 356
|
410 420
....*....|....*....|.
gi 1127363094 428 AQIKAMKSIAGTLRLDLAQYR 448
Cdd:PRK07594 357 VTSHEHRQLAAILRRCLALYQ 377
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
12-427 |
1.15e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 127.49 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 12 IKKQIQNIDKAALVSETGTVLTVGDGIARVHGLSRAMaGELIEF-TGQGGETLAGLVLNLEQDNVGSAIFGDTSVIREGD 90
Cdd:PRK08472 3 LESLKNKLQKFNLSPRFGSITKISPTIIEADGLNPSV-GDIVKIeSSDNGKECLGMVVVIEKEQFGISPFSFIEGFKIGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 91 SVKRTGRIMDVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVeVKAP-GIIQRQPVTEPMQTGLKAVDAMIPIGRGQRE 169
Cdd:PRK08472 82 KVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPI-MKAPiAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 170 LIIGDRQTGKTAVaIDAILnqKGKGVYCVYVA-IGQKLSTVRQVVDKlESHGAMEYTTVVAATASETAPIQYIAPYTGVT 248
Cdd:PRK08472 161 GIFAGSGVGKSTL-MGMIV--KGCLAPIKVVAlIGERGREIPEFIEK-NLGGDLENTVIVVATSDDSPLMRKYGAFCAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 249 IGEYFRDTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKmaeifyvvkkgttikggeidk 328
Cdd:PRK08472 237 VAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK--------------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 329 gvdgkahvgahgmseakkslEETKksqggdleivkepwsgGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLFF 408
Cdd:PRK08472 296 --------------------EEGK----------------GSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTD 339
|
410
....*....|....*....
gi 1127363094 409 SGVRPAINVGISVSRVGGN 427
Cdd:PRK08472 340 FGIYPPINILNSASRVMND 358
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
41-423 |
1.09e-29 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 122.24 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 41 VHGLSRAMAGELIEFTGQGGETLAGLVLNLEQDNVGSAIFGDTSVI-REGDSVKRTGRIMDVPVGEAVVGRVVNALGMPI 119
Cdd:PRK04196 17 VEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 120 DGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQR------------ELiigdrqtgktAVAI--D 185
Cdd:PRK04196 97 DGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnEL----------AAQIarQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 186 AILNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGVTIGEYFR-DTGRHALCVY 264
Cdd:PRK04196 167 AKVLGEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMHVLVIL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 265 DDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL---LERAAKmaeifyvvkkgttIKGgeidkgvdgkahvgahgm 341
Cdd:PRK04196 247 TDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGR-------------IKG------------------ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 342 seaKKsleetkksqggdleivkepwsgGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLFFSGVRPAINVGISV 421
Cdd:PRK04196 293 ---KK----------------------GSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSL 347
|
..
gi 1127363094 422 SR 423
Cdd:PRK04196 348 SR 349
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
89-424 |
1.43e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 121.73 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 89 GDSVKRTGRIMDVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQR 168
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 169 -----------ELIIGDRQTGKTAVAIdailnqkgkgvycVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAP 237
Cdd:PRK08972 165 mglfagsgvgkSVLLGMMTRGTTADVI-------------VVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 238 IQYIAPYTGVTIGEYFRDTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAkmaeifyvvkk 317
Cdd:PRK08972 232 MRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAG----------- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 318 gttikggeidkgvdgkahvgahgmseakksleetkksQGGDLEivkepwsgGSLTALPVIETQAGDVSAYIPTNVISITD 397
Cdd:PRK08972 301 -------------------------------------NGGPGQ--------GSITAFYTVLTEGDDLQDPIADASRAILD 335
|
330 340
....*....|....*....|....*..
gi 1127363094 398 GQIFLESDLFFSGVRPAINVGISVSRV 424
Cdd:PRK08972 336 GHIVLSRELADSGHYPAIDIEASISRV 362
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
97-305 |
4.68e-29 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 120.01 E-value: 4.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 97 RIMDVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQ 176
Cdd:PRK05922 88 RPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 177 TGKTAVAidAILNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGVTIGEYFRDT 256
Cdd:PRK05922 168 SGKSSLL--STIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQ 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1127363094 257 GRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERA 305
Cdd:PRK05922 246 GHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERA 294
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
14-451 |
2.10e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 118.16 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 14 KQIQNIDKaalVSETGTVLTVGDGIARVHGLSRAMA-GELIEFTGQGGETLAGLVLNLEQDNVGSAIFGDTSVIREGDSV 92
Cdd:PRK08927 7 AAIGDIDT---LVIYGRVVAVRGLLVEVAGPIHALSvGARIVVETRGGRPVPCEVVGFRGDRALLMPFGPLEGVRRGCRA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 93 KRTGRIMDVPVGEAVVGRVVNALGMPIDGKGPI-ESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELI 171
Cdd:PRK08927 84 VIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 172 IGDRQTGKTAVaidaiLNQKGKGVYC---VYVAIGQKLSTVRQVV-DKLESHGaMEYTTVVAATASETAPIQYIAPYTGV 247
Cdd:PRK08927 164 FAGSGVGKSVL-----LSMLARNADAdvsVIGLIGERGREVQEFLqDDLGPEG-LARSVVVVATSDEPALMRRQAAYLTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 248 TIGEYFRDTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAakmaeifyvvkkgttikggeid 327
Cdd:PRK08927 238 AIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERA---------------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 328 kgvdGKAHVGAhgmseakksleetkksqggdleivkepwsgGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLF 407
Cdd:PRK08927 296 ----GPGPIGE------------------------------GTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIA 341
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1127363094 408 FSGVRPAINVGISVSRVGGNAQIKAMKSIAGTLRLDLAQYRAMA 451
Cdd:PRK08927 342 ERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADME 385
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
98-423 |
2.58e-28 |
|
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: 114.63 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 98 IMDVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDrqT 177
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSG--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 178 GKTA------VAIDAILNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGVTIGE 251
Cdd:cd01135 79 GLPHnelaaqIARQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 252 YFR-DTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL---LERAAKmaeifyvvkkgttIKGgeid 327
Cdd:cd01135 159 YLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGR-------------VEG---- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 328 kgvdgkahvgahgmseakksleetkksqggdleivkepwSGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLF 407
Cdd:cd01135 219 ---------------------------------------RKGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLH 259
|
330
....*....|....*.
gi 1127363094 408 FSGVRPAINVGISVSR 423
Cdd:cd01135 260 NKGIYPPIDVLPSLSR 275
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
95-501 |
4.59e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 117.14 E-value: 4.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 95 TGRImdvPVGEAVVGRVVNALGMPIDGKGPIESPHrrRVEVKAPGI--IQRQPVTEPMQTGLKAVDAMIPIGRGQRELII 172
Cdd:PRK05688 100 TGRL---PMGMSMLGRVLDGAGRALDGKGPMKAED--WVPMDGPTInpLNRHPISEPLDVGIRSINGLLTVGRGQRLGLF 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 173 GDRQTGKTAVAidAILNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGVTIGEY 252
Cdd:PRK05688 175 AGTGVGKSVLL--GMMTRFTEADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEY 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 253 FRDTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAakmaeifyvvkkgttikgGEIDKGvdg 332
Cdd:PRK05688 253 FRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERA------------------GNAEPG--- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 333 kahvgahgmseakksleetkksqggdleivkepwsGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLFFSGVR 412
Cdd:PRK05688 312 -----------------------------------GGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHY 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 413 PAINVGISVSRVggnaqikaMKSIAGTLRLDLAQY-RAMAAFAQFASDL----------DARTRQQLERGARLVEILKQG 481
Cdd:PRK05688 357 PAIDIEASISRV--------MPQVVDPEHLRRAQRfKQLWSRYQQSRDLisvgayvaggDPETDLAIARFPHLVQFLRQG 428
|
410 420
....*....|....*....|...
gi 1127363094 482 --QYVPL-PVEKQILIIFAGTQG 501
Cdd:PRK05688 429 lrENVSLaQSREQLAAIFAPAAG 451
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
92-448 |
1.62e-26 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 112.40 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 92 VKRTGRIMDVPVGEAVVGRVVNALGMpIDGK--GPIESPHR---RRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRG 166
Cdd:PRK08149 73 LKPTGKPLSVWVGEALLGAVLDPTGK-IVERfdAPPTVGPIseeRVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 167 QRELIIGDRQTGKTAVaIDAILNQKGKGVYcVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTG 246
Cdd:PRK08149 152 QRMGIFASAGCGKTSL-MNMLIEHSEADVF-VIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 247 VTIGEYFRDTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAakmaeifyvvkkGTTIKggei 326
Cdd:PRK08149 230 TTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERP------------GATLA---- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 327 dkgvdgkahvgahgmseakksleetkksqggdleivkepwsgGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDL 406
Cdd:PRK08149 294 ------------------------------------------GSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKL 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1127363094 407 FFSGVRPAINVGISVSRVGGN-------AQIKAMKSIAGTLR-----LDLAQYR 448
Cdd:PRK08149 332 AAKGHYPAIDVLKSVSRVFGQvtdpkhrQLAAAFRKLLTRLEelqlfIDLGEYR 385
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
27-97 |
3.53e-26 |
|
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: 101.38 E-value: 3.53e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1127363094 27 ETGTVLTVGDGIARVHGLSRAMAGELIEFTGQggetLAGLVLNLEQDNVGSAIFGDTSVIREGDSVKRTGR 97
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGG----VKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
103-480 |
6.47e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 110.75 E-value: 6.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 103 VGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGKTAV 182
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 183 AidAILNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGVTIGEYFRDTGRHALC 262
Cdd:PRK07196 172 L--GMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 263 VYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAakmaeifyvvkkgttikggeidkgvdgkahvgahGMS 342
Cdd:PRK07196 250 LVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESA----------------------------------GNS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 343 EAkksleetkksqggdleivkepwsGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLFFSGVRPAINVGISVS 422
Cdd:PRK07196 296 SG-----------------------NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSIS 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1127363094 423 R----VGGNAQIKAMKSIAGTLRlDLAQYRAMAAFAQFASDLDARTRQQLERGARLVEILKQ 480
Cdd:PRK07196 353 RcmsqVIGSQQAKAASLLKQCYA-DYMAIKPLIPLGGYVAGADPMADQAVHYYPAITQFLRQ 413
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
30-438 |
1.10e-24 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 107.50 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 30 TVLTVGDGIARVHGLSRAMAGELIEFTGQGGETLAGLVLNLEQDNVGSAIFGDTSVIREGDS-VKRTGRIMDVPVGEAVV 108
Cdd:TIGR01040 4 TVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTtCEFTGDILRTPVSEDML 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 109 GRVVNALGMPIDgKGPiesphrrRVEVKAPGIIQRQPVT--------EPMQTGLKAVDAMIPIGRGQRELIIGD------ 174
Cdd:TIGR01040 84 GRVFNGSGKPID-KGP-------PVLAEDYLDINGQPINpyariypeEMIQTGISAIDVMNSIARGQKIPIFSAaglphn 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 175 -------RQTGKTAVAIDAILNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGV 247
Cdd:TIGR01040 156 eiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 248 TIGEYFR-DTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKmaeifyvvkkgttikggei 326
Cdd:TIGR01040 236 TTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGR------------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 327 dkgVDGKahvgahgmseakksleetkksqggdleivkepwsGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDL 406
Cdd:TIGR01040 297 ---VEGR----------------------------------NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQL 339
|
410 420 430
....*....|....*....|....*....|..
gi 1127363094 407 FFSGVRPAINVGISVSRVggnaqikaMKSIAG 438
Cdd:TIGR01040 340 HNRQIYPPINVLPSLSRL--------MKSAIG 363
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
101-472 |
9.36e-24 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 104.48 E-value: 9.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 101 VPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGKT 180
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKS 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 181 AVAidAILNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGVTIGEYFRDTGRHA 260
Cdd:PRK07960 190 VLL--GMMARYTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHV 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 261 LCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAkmaeifyvvkkgttikggeidKGVDGkahvgahg 340
Cdd:PRK07960 268 LLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG---------------------NGISG-------- 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 341 mseakksleetkksqggdleivkepwsGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESDLFFSGVRPAINVGIS 420
Cdd:PRK07960 319 ---------------------------GGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEAS 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1127363094 421 VSRvggnaqikAMKSIagtlrLDLAQYRAMAAFAQFASDLDaRTRQQLERGA 472
Cdd:PRK07960 372 ISR--------AMTAL-----IDEQHYARVRQFKQLLSSFQ-RNRDLVSVGA 409
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
66-290 |
6.18e-23 |
|
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: 102.10 E-value: 6.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 66 LVLNLEQ---DNVGSAI-FGDTSVIREGDSVKRTGRIMDVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGII 141
Cdd:TIGR01039 39 LTLEVAQhlgDDTVRTIaMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 142 QRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGKTAVAIDAILN-QKGKGVYCVYVAIGQKLSTVRQVVDKLESHG 220
Cdd:TIGR01039 119 EQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKESG 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1127363094 221 AMEYTTVVAATASETAPIQYIAPYTGVTIGEYFRDT-GRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAY 290
Cdd:TIGR01039 199 VIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGY 269
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
67-424 |
3.14e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 99.67 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 67 VLNLEQDNVGSAIFGDTSVIREGDSVKRTGRIMDVPVGEAVVGRVVNALGMPIDGkgPIESPHRRRVEVKAPGI--IQRQ 144
Cdd:PRK06793 57 VIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIhaFERE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 145 PVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGKTAVAidAILNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEY 224
Cdd:PRK06793 135 EITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLL--GMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 225 TTVVAATASETAPIQYIAPYTGVTIGEYFRDTGRHALCVYDDLSKQAVAYRQLSLLLRRPPgreaypgdvfylhsrller 304
Cdd:PRK06793 213 SVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP------------------- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 305 aakmaeifyvvkkgttikggeidkgVDGKAHVGAHGMseaKKSLEETKKSQggdleivkepwsGGSLTALPVIETQAGDV 384
Cdd:PRK06793 274 -------------------------IGGKTLLMESYM---KKLLERSGKTQ------------KGSITGIYTVLVDGDDL 313
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1127363094 385 SAYIPTNVISITDGQIFLESDLFFSGVRPAINVGISVSRV 424
Cdd:PRK06793 314 NGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRI 353
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
101-290 |
9.71e-20 |
|
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: 89.59 E-value: 9.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 101 VPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGKT 180
Cdd:cd01133 2 VPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 181 AVAIDAILN-QKGKGVYCVYVAIGQKlstVRQVVD--------KLESHGAMEYTTVVAATASETAPIQYIAPYTGVTIGE 251
Cdd:cd01133 82 VLIMELINNiAKAHGGYSVFAGVGER---TREGNDlyhemkesGVINLDGLSKVALVYGQMNEPPGARARVALTGLTMAE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1127363094 252 YFRD-TGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAY 290
Cdd:cd01133 159 YFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGY 198
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
66-255 |
1.22e-17 |
|
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439825 [Multi-domain] Cd Length: 468 Bit Score: 85.91 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 66 LVLNLEQ---DNVGSAI-FGDTSVIREGDSVKRTGRIMDVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGII 141
Cdd:COG0055 42 LVLEVAQhlgDNTVRCIaMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 142 QRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGKTAVAIDAILN--QKGKGvYCVYVAIGQKlstVRQVVDKL--- 216
Cdd:COG0055 122 EQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNiaKEHGG-VSVFAGVGER---TREGNDLYrem 197
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1127363094 217 -EShGAMEYTTVVAATASETAPIQYIAPYTGVTIGEYFRD 255
Cdd:COG0055 198 kES-GVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRD 236
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
129-307 |
3.09e-17 |
|
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: 82.24 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 129 HRRRVEVKAPgIIQRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGKTAV--------AIDAIlnqkgkgvycVYV 200
Cdd:cd01134 40 QRWPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVIsqslskwsNSDVV----------IYV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 201 AIGQKLSTVRQVVD-----KLESHGA--MEYTTVVAATASETAPIQYIAPYTGVTIGEYFRDTGRHALCVYDDLSKQAVA 273
Cdd:cd01134 109 GCGERGNEMAEVLEefpelKDPITGEslMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEA 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 1127363094 274 YRQLSLLLRRPPGREAYPGdvfYLHSRL---LERAAK 307
Cdd:cd01134 189 LREISGRLEEMPAEEGYPA---YLGARLaefYERAGR 222
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
10-405 |
6.96e-15 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 77.00 E-value: 6.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 10 QIIKKQIQNIdkaalvseTGTVLTVgdgIARVHGLsramaGELIEFTGQGGETLAGlVLNLEQDNVGSAIFGDTSVIREG 89
Cdd:PRK02118 2 QKIYTKITDI--------TGNVITV---EAEGVGY-----GELATVERKDGSSLAQ-VIRLDGDKVTLQVFGGTRGISTG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 90 DSVKRTGRIMDVPVGEAVVGRVVNALGMPIDGkGPieSPHRRRVEVKAPGI--IQRQPVTEPMQTGLKAVDAMIPIGRGQ 167
Cdd:PRK02118 65 DEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GP--ELEGEPIEIGGPSVnpVKRIVPREMIRTGIPMIDVFNTLVESQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 168 RELIIGDrqTGKTAVAIDAILNQKGKGVYCVYVAIGQKLSTVRQVVDKLESHGAMEYTTVVAATASETAPIQYIAPYTGV 247
Cdd:PRK02118 142 KIPIFSV--SGEPYNALLARIALQAEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 248 TIGEYFR-DTGRHALCVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDvfyLHSRLLERAAKMAEIfyvvkkgttikggei 326
Cdd:PRK02118 220 AVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGS---LYSDLASRYEKAVDF--------------- 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1127363094 327 dkgvdgkahvgahgmseakksleetkksQGgdleivkepwsGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESD 405
Cdd:PRK02118 282 ----------------------------ED-----------GGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLRRG 321
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
433-499 |
3.83e-14 |
|
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: 67.47 E-value: 3.83e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1127363094 433 MKSIAGTLRLDLAQYRAMAAFAQFASD--LDARTRQQLERGARLVEILKQGQYVPLPVEKQILIIFAGT 499
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIK 69
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
25-96 |
1.83e-13 |
|
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: 65.26 E-value: 1.83e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1127363094 25 VSETGTVLTVGDGIARVHGLSRAMAGELIEFtgqgGETLAGLVLNLEQDNVGSAIFGDTSVIREGDSVKRTG 96
Cdd:pfam02874 2 VQVIGPVVDVEFGIGRLPGLLNALEVELVEF----GSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
142-305 |
2.19e-12 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 69.81 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 142 QRQPVTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGKTAV--------AIDAIlnqkgkgvycVYVAIGQklstvR--Q 211
Cdd:PRK04192 203 EKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTqhqlakwaDADIV----------IYVGCGE-----RgnE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 212 VVDKLES----------HGAMEYTTVVAAT-----ASETAPIqyiapYTGVTIGEYFRDTGRHALCVYDDLSKQAVAYRQ 276
Cdd:PRK04192 268 MTEVLEEfpelidpktgRPLMERTVLIANTsnmpvAAREASI-----YTGITIAEYYRDMGYDVLLMADSTSRWAEALRE 342
|
170 180 190
....*....|....*....|....*....|..
gi 1127363094 277 LSLLLRRPPGREAYPGdvfYLHSRL---LERA 305
Cdd:PRK04192 343 ISGRLEEMPGEEGYPA---YLASRLaefYERA 371
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
67-255 |
8.86e-12 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 67.76 E-value: 8.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 67 VLNLEQDNVGSAI-FGDTSVIREGDSVKRTGRIMDVPVGEAVVGRVVNALGMPIDGKGPIESPHRRRVEVKAPGIIQRQP 145
Cdd:CHL00060 61 VQQLLGNNRVRAVaMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 146 VTEPMQTGLKAVDAMIPIGRGQRELIIGDRQTGKTAVAIDAILN-QKGKGVYCVYVAIGQ------------KLSTVRQV 212
Cdd:CHL00060 141 KLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGErtregndlymemKESGVINE 220
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1127363094 213 VDKLESHGAMEYttvvaATASETAPIQYIAPYTGVTIGEYFRD 255
Cdd:CHL00060 221 QNIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRD 258
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
198-303 |
3.88e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 59.65 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1127363094 198 VYVAIGQKLSTVRQVVD---KLESHGA----MEYTTVVAATASETAPIQYIAPYTGVTIGEYFRDTGRHALCVYDDLSKQ 270
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEefpKLKDPKTgkplMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
90 100 110
....*....|....*....|....*....|...
gi 1127363094 271 AVAYRQLSLLLRRPPGREAYPGdvfYLHSRLLE 303
Cdd:PRK14698 766 AEALREISGRLEEMPGEEGYPA---YLASKLAE 795
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
28-97 |
3.44e-06 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 45.00 E-value: 3.44e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1127363094 28 TGTVLTVGDGIARVHGLSRAMAGELIEFTGQGGETLAGL---VLNLEQDNVGSAIFGDTSVIREGDSVKRTGR 97
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDGNNETVLkaeVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| |
