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Conserved domains on  [gi|1252061573|emb|SOE87622|]
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ATP synthase F0 subcomplex A subunit [Burkholderia sp. YR290]

Protein Classification

FoF1 ATP synthase subunit a; ATP synthase F0 subunit 6( domain architecture ID 10014231)

FoF1 ATP synthase subunit a is part of the membrane proton channel (Fo complex) of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane; it plays a direct role in the translocation of protons across the membrane; ATP synthase F0 subunit 6 is part of the mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V), which produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
 1-223 1.51e-133

F0F1 ATP synthase subunit A; Provisional


:

Pssm-ID: 237383  Cd Length: 223  Bit Score: 374.80  E-value: 1.51e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573   1 MMHSPLTTEPLMHVGPIAITAPVIVTWGIIASLAVVSALLTRRLSLEPSRMQTVLELLVETIDAQIRDTMQTGPAPYRAL 80
Cdd:PRK13421    1 MTASPLSTVPLFSLGPVPISAPVVVTWAIMAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  81 VGTLFVFVLVANWSSLVPGIEPPTAHLETDAALALVVFFATIVHGVRTRGVRGYLATFAEPTWVMVPLNVVEQITRTFSL 160
Cdd:PRK13421   81 IGTLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVRARGVRGYLATFAEPTWVMIPLNLVEQLTRTFSL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1252061573 161 VVRLFGNVMSGVFVVGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVGEAPLP 223
Cdd:PRK13421  161 IVRLFGNVMSGVFVIGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVSDDEAS 223
 
Name Accession Description Interval E-value
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
 1-223 1.51e-133

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 374.80  E-value: 1.51e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573   1 MMHSPLTTEPLMHVGPIAITAPVIVTWGIIASLAVVSALLTRRLSLEPSRMQTVLELLVETIDAQIRDTMQTGPAPYRAL 80
Cdd:PRK13421    1 MTASPLSTVPLFSLGPVPISAPVVVTWAIMAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  81 VGTLFVFVLVANWSSLVPGIEPPTAHLETDAALALVVFFATIVHGVRTRGVRGYLATFAEPTWVMVPLNVVEQITRTFSL 160
Cdd:PRK13421   81 IGTLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVRARGVRGYLATFAEPTWVMIPLNLVEQLTRTFSL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1252061573 161 VVRLFGNVMSGVFVVGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVGEAPLP 223
Cdd:PRK13421  161 IVRLFGNVMSGVFVIGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVSDDEAS 223
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 22-219 7.73e-63

FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 194.91  E-value: 7.73e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  22 PVIVTWGIIASLAVVSALLTRRLSLEPSRMQTVLELLVETIDAQIRDTMQTGPAPYRALVGTLFVFVLVANWSSLVPGIE 101
Cdd:COG0356     2 TVLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573 102 PPTAHLETDAALALVVFFATIVHGVRTRGVRGYLAT-FAEPTW----VMVPLNVVEQITRTFSLVVRLFGNVMSGVFVVG 176
Cdd:COG0356    82 PPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHlFFPPFPwlapLMLPIEIISELARPLSLSLRLFGNMFAGHIILL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1252061573 177 IVLSLAG--------LLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVGE 219
Cdd:COG0356   162 LLAGLAPflllgvlsLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVEE 212
altF1_A TIGR03306
alternate F1F0 ATPase, F0 subunit A; A small number of taxonomically diverse prokaryotic ...
 15-216 3.93e-59

alternate F1F0 ATPase, F0 subunit A; A small number of taxonomically diverse prokaryotic species 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 F0 subunit A of this apparent second ATP synthase.


Pssm-ID: 132349  Cd Length: 217  Bit Score: 185.71  E-value: 3.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  15 GPIAITAPVIVTWGIIASLAVVSALLTRRLS--LEPSRMQTVLELLVETIDAQIRDTMQTGPAPYRALVGTLFVFVLVAN 92
Cdd:TIGR03306  12 GFVKINATIAFTWLLMLLLVIGSWLITRRLStgLERSRWQNLLEVLVTGIQEQISDVGLAKPRKYLPFLGTLFLFIAVAN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  93 WSSLVPGIEPPTAHLETDAALALVVFFATIVHGVRTRGVRGYLATFAEPTWVMVPLNVVEQITRTFSLVVRLFGNVMSGV 172
Cdd:TIGR03306  92 LLSVIPGYEPPTGSLSTTAALALCVFVAVPLFGIAERGLSGYLKSYLKPTPFMLPFNIIGELSRTLALAVRLFGNMMSGS 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1252061573 173 FVVGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAA 216
Cdd:TIGR03306 172 MILAILLSISPLIFPVLMQVLGLLTGMVQAYIFSVLATVYIAAA 215
ATP-synt_A pfam00119
ATP synthase A chain;
23-214 1.57e-40

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 138.01  E-value: 1.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  23 VIVTWGIIASLAVVSALLTRRLS-LEPSRMQTVLELLVETIDAQIRDTM-QTGPAPYRALVGTLFVFVLVANWSSLV--- 97
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKTKkLVPGRLQNFVEMLVEFVDNIVKDNIgKKKGRKFFPLLLTLFFFILVSNLLGLIpks 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  98 PGIEPPTAHLETDAALALVVFFATIVHGVRTRGVRGYLATFAEP------TWVMVPLNVVEQITRTFSLVVRLFGNVMSG 171
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKLFVPpvplplVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1252061573 172 VFVVGIVLSLAG-------------LLVPIPLMALDLLTGAVQAYIFAVLAMVFIG 214
Cdd:pfam00119 161 HLLLLLLAGLIFallsagfllgvipPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 76-214 2.77e-38

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases 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.


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 130.21  E-value: 2.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  76 PYRALVGTLFVFVLVANWSSLVPGIEPPTAHLETDAALALVVFFATIVHGVRTRGVRGYLA-----TFAEPTWVMVPLNV 150
Cdd:cd00310     3 KYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHflppgTPLPLAPLMVPIEL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1252061573 151 VEQITRTFSLVVRLFGNVMSGVFVVGIVLSLA----------GLLVPIPLMALDLLTGAVQAYIFAVLAMVFIG 214
Cdd:cd00310    83 ISELIRPLSLSVRLFANMFAGHLLLALLSGLVpsllssvgllPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
 
Name Accession Description Interval E-value
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
 1-223 1.51e-133

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 374.80  E-value: 1.51e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573   1 MMHSPLTTEPLMHVGPIAITAPVIVTWGIIASLAVVSALLTRRLSLEPSRMQTVLELLVETIDAQIRDTMQTGPAPYRAL 80
Cdd:PRK13421    1 MTASPLSTVPLFSLGPVPISAPVVVTWAIMAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  81 VGTLFVFVLVANWSSLVPGIEPPTAHLETDAALALVVFFATIVHGVRTRGVRGYLATFAEPTWVMVPLNVVEQITRTFSL 160
Cdd:PRK13421   81 IGTLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVRARGVRGYLATFAEPTWVMIPLNLVEQLTRTFSL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1252061573 161 VVRLFGNVMSGVFVVGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVGEAPLP 223
Cdd:PRK13421  161 IVRLFGNVMSGVFVIGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVSDDEAS 223
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 22-219 7.73e-63

FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 194.91  E-value: 7.73e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  22 PVIVTWGIIASLAVVSALLTRRLSLEPSRMQTVLELLVETIDAQIRDTMQTGPAPYRALVGTLFVFVLVANWSSLVPGIE 101
Cdd:COG0356     2 TVLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573 102 PPTAHLETDAALALVVFFATIVHGVRTRGVRGYLAT-FAEPTW----VMVPLNVVEQITRTFSLVVRLFGNVMSGVFVVG 176
Cdd:COG0356    82 PPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHlFFPPFPwlapLMLPIEIISELARPLSLSLRLFGNMFAGHIILL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1252061573 177 IVLSLAG--------LLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVGE 219
Cdd:COG0356   162 LLAGLAPflllgvlsLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVEE 212
altF1_A TIGR03306
alternate F1F0 ATPase, F0 subunit A; A small number of taxonomically diverse prokaryotic ...
 15-216 3.93e-59

alternate F1F0 ATPase, F0 subunit A; A small number of taxonomically diverse prokaryotic species 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 F0 subunit A of this apparent second ATP synthase.


Pssm-ID: 132349  Cd Length: 217  Bit Score: 185.71  E-value: 3.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  15 GPIAITAPVIVTWGIIASLAVVSALLTRRLS--LEPSRMQTVLELLVETIDAQIRDTMQTGPAPYRALVGTLFVFVLVAN 92
Cdd:TIGR03306  12 GFVKINATIAFTWLLMLLLVIGSWLITRRLStgLERSRWQNLLEVLVTGIQEQISDVGLAKPRKYLPFLGTLFLFIAVAN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  93 WSSLVPGIEPPTAHLETDAALALVVFFATIVHGVRTRGVRGYLATFAEPTWVMVPLNVVEQITRTFSLVVRLFGNVMSGV 172
Cdd:TIGR03306  92 LLSVIPGYEPPTGSLSTTAALALCVFVAVPLFGIAERGLSGYLKSYLKPTPFMLPFNIIGELSRTLALAVRLFGNMMSGS 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1252061573 173 FVVGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAA 216
Cdd:TIGR03306 172 MILAILLSISPLIFPVLMQVLGLLTGMVQAYIFSVLATVYIAAA 215
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 12-220 2.24e-57

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 181.53  E-value: 2.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  12 MHVGPIAITAPVIVTWGIIASLAVVSALLTRRLSLEPSRMQTVLELLVETIDAQIRDTMQTGPAPYRALVGTLFVFVLVA 91
Cdd:PRK05815    7 IGFGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  92 NWSSLVP-GIEPPTAHLETDAALALVVFFATIVHGVRTRGVRGYLA-TFAEPTWVMVPLNVVEQITRTFSLVVRLFGNVM 169
Cdd:PRK05815   87 NLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKeFYLQPHPLLLPIEIISEFSRPISLSLRLFGNML 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573 170 SG---------VFVVGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVGEA 220
Cdd:PRK05815  167 AGelilalialLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEEE 226
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 7-217 1.31e-54

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 174.55  E-value: 1.31e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573   7 TTEPLMHVGPIAITAPVIVTWGIIASLAVVSALLTRRLSLEPSRMQTVLELLVETIDAQIRDTMQTGPAPYRALVGTLFV 86
Cdd:PRK13420    4 LAHVLFHIGPLPITESVLTTWGIMIVLVLASWLTTRRLSLDPGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFVGTLWI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  87 FVLVANWSSLVPGIEPPTAHLETDAALALVVFFATIVHGVRTRGVRGYLATFAEPTWVMVPLNVVEQITRTFSLVVRLFG 166
Cdd:PRK13420   84 FILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEGLREYLKHYLSPSPFLLPFHLISEITRTLALAVRLFG 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1252061573 167 NVMSGVFVVGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAV 217
Cdd:PRK13420  164 NIMSLELAALLVLLVAGFLVPVPILMLHIIEALVQAYIFGMLALIYIAGGI 214
ATP-synt_A pfam00119
ATP synthase A chain;
23-214 1.57e-40

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 138.01  E-value: 1.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  23 VIVTWGIIASLAVVSALLTRRLS-LEPSRMQTVLELLVETIDAQIRDTM-QTGPAPYRALVGTLFVFVLVANWSSLV--- 97
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKTKkLVPGRLQNFVEMLVEFVDNIVKDNIgKKKGRKFFPLLLTLFFFILVSNLLGLIpks 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  98 PGIEPPTAHLETDAALALVVFFATIVHGVRTRGVRGYLATFAEP------TWVMVPLNVVEQITRTFSLVVRLFGNVMSG 171
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKLFVPpvplplVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1252061573 172 VFVVGIVLSLAG-------------LLVPIPLMALDLLTGAVQAYIFAVLAMVFIG 214
Cdd:pfam00119 161 HLLLLLLAGLIFallsagfllgvipPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 76-214 2.77e-38

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases 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.


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 130.21  E-value: 2.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  76 PYRALVGTLFVFVLVANWSSLVPGIEPPTAHLETDAALALVVFFATIVHGVRTRGVRGYLA-----TFAEPTWVMVPLNV 150
Cdd:cd00310     3 KYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHflppgTPLPLAPLMVPIEL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1252061573 151 VEQITRTFSLVVRLFGNVMSGVFVVGIVLSLA----------GLLVPIPLMALDLLTGAVQAYIFAVLAMVFIG 214
Cdd:cd00310    83 ISELIRPLSLSVRLFANMFAGHLLLALLSGLVpsllssvgllPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
atpI CHL00046
ATP synthase CF0 A subunit
 24-214 6.05e-35

ATP synthase CF0 A subunit


Pssm-ID: 176987  Cd Length: 228  Bit Score: 123.89  E-value: 6.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  24 IVTWGIIASLAVVSALLTRRLSLEPSRMQTVLELLVETIDAQIRDtmQTGPAPYRALV---GTLFVFVLVANWS------ 94
Cdd:CHL00046   27 ITSWVVIAILLGSALLATRNLQTIPTGGQNFFEYVLEFIRDLAKT--QIGEEEYRPWVpfiGTMFLFIFVSNWSgallpw 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  95 --SLVPGIE--PPTAHLETDAALALVVFFATIVHGVRTRGVrGYLATFAEPTWVMVPLNVVEQITRTFSLVVRLFGNVMS 170
Cdd:CHL00046  105 klIELPHGElaAPTNDINTTVALALLTSVAYFYAGLSKKGL-GYFGKYIQPTPILLPINILEDFTKPLSLSFRLFGNILA 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1252061573 171 GVFVVGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIG 214
Cdd:CHL00046  184 DELVVAVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIG 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 26-213 8.08e-28

ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be designated ATP synthase, F0 subunit A; eukaryotic (chloroplast and mitochondrial) forms should be designated ATP synthase, F0 subunit 6. The F1/F0 ATP synthase is a multisubunit, membrane associated enzyme found in bacteria and mitochondria and chloroplast. This enzyme is principally involved in the synthesis of ATP from ADP and inorganic phosphate by coupling the energy derived from the proton electrochemical gradient across the biological membrane. A brief description of this multisubunit enzyme complex: F1 and F0 represent two major clusters of subunits. Individual subunits in each of these clusters are named differently in prokaryotes and in organelles e.g., mitochondria and chloroplast. The bacterial equivalent of subunit 6 is named subunit 'A'. It has been shown that proton is conducted though this subunit. Typically, deprotonation and reprotonation of the acidic amino acid side-chains are implicated in the process. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273458  Cd Length: 226  Bit Score: 105.37  E-value: 8.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  26 TWGIIASLAVVSALLTRRLSLEPSRMQTVLELLVETIDAQIRDTMQTGPAPYRALVGTLFVFVLVANWSSLVPGIEPPTA 105
Cdd:TIGR01131  19 SLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573 106 HLETDAALALVVFFATIVHGVRTR--GVRGYLATFAEPTW---VMVPLNVVEQITRTFSLVVRLFGNVMSGVFVVGIVLS 180
Cdd:TIGR01131  99 HLSFTLGLALPLWLGLTISGFRKHpkGFLAHLVPSGTPLPlipFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSG 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1252061573 181 LA-----------GLLVPIPLMALDLLTGAVQAYIFAVLAMVFI 213
Cdd:TIGR01131 179 LLfslmssaifalLLLILVALIILEIFVAFIQAYVFTLLTCLYL 222
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 17-217 4.74e-19

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 84.02  E-value: 4.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  17 IAITAPVIVTWGIIASLAVVSALLTRRL-----SLEPSRMQTVLELLVETIDAQI-RDTMQTGPAPYRALVGTLFVFVLV 90
Cdd:PRK13419  104 ISITKHVVMMWIASAILLVVFLAAGRKYkkmtkSQAPKGLANAMEALVEFIRLDVaKSNIGHGYEKFLPYLLTVFFFILV 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  91 ANWSSLVPGIEPPTAHLETDAALALVVFFATIVHGVRTRGVRGYLATFAEPT----W-VMVPLNVVEQITRTFSLVVRLF 165
Cdd:PRK13419  184 CNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGThwslWiIMIPIEFIGLFTKPFALTVRLF 263

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1252061573 166 GNVMSGVFVV----GIVLSL------AGLLVP--IPLMALDLLTGAVQAYIFAVLAMVFIGAAV 217
Cdd:PRK13419  264 ANMTAGHIVIlsliFISFILksyivaVAVSVPfaIFIYLLELFVAFLQAYIFTMLSALFIGLAT 327
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 23-209 1.25e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 53.50  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  23 VIVTWGiiaSLAVVSALLTRRLSLEPSRMQTVLELLVETIDAQIRDTMQTGPAPYRALVGTLFVFVLVANWSSLVPGIEP 102
Cdd:MTH00176   20 ISLSWI---TLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFILVMSLNLSGLIPYVFT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573 103 PTAHLETDAALALVVFFATIVHGVRtRGVRGYLATF---AEPTW---VMVPLNVVEQITRTFSLVVR------------- 163
Cdd:MTH00176   97 STSHLVITLSLALPLWLGVILSGFI-NNFYSRLSHLvpqGTPPLlnpFLVLIELVSLLIRPLTLAVRlaanlsaghlllg 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1252061573 164 LFGNVMSGVFVVGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLA 209
Cdd:MTH00176  176 LLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLL 221
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 39-217 3.88e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 49.23  E-value: 3.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  39 LLTRRLSLEPSRMQTVLELLVETIDAQIRDTMQTGPAPYRALVGTLFVFVLVANWSSLVPGIEPPTAHLETDAALALVVF 118
Cdd:MTH00175   44 LLLKGDKLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSII 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573 119 FATIVHGVRT-----------RGVRGYLATFaeptwvMVPLNVVEQITRTFSLVVRLFGNVMSGVFVVGI---------- 177
Cdd:MTH00175  124 IAVTLLGFLTfkwnflsilmpGGAPLVLAPF------LVLIETLSYLIRAISLGVRLAANISAGHLLFAIlsgfafnmls 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1252061573 178 ----VLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAV 217
Cdd:MTH00175  198 ngliILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGDTI 241
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 45-213 5.23e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 49.17  E-value: 5.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  45 SLEPSRMQTVLELLVETIDAQIRDTMQTGPAPYRALVGTLFVFVLVANWSSLVPGIEPPTAHLETDAALALVVFFATIVH 124
Cdd:MTH00174   58 TLVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573 125 GVRTRGVRGY--LATFAEPTWVMVPLNVVEQ---ITRTFSLVVRLFGNVMSGVFVVGIVLSLA----------GLLVPIP 189
Cdd:MTH00174  138 GLITFRFNFFsiLMPQGAPLALAPLLTIIETlsyISRAISLGVRLAANISSGHLLFSIIASFAwkmintgiliGSFVPFA 217

                         170       180
                  ....*....|....*....|....*...
gi 1252061573 190 LM----ALDLLTGAVQAYIFAVLAMVFI 213
Cdd:MTH00174  218 ILifvtILEMAVAIIQAYVFTLLTIVYL 245
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 48-208 3.06e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 46.78  E-value: 3.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  48 PSRMQTVLELLVETIDAQIRDTMQTGPAPYRALVGTLFVFVLVANWSSLVPGIEPPTAHLETDAALALVVFFATIVHGV- 126
Cdd:MTH00173   42 SSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLf 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573 127 -RTRGVRGYLATFAEPTWVMVPLNVVEQIT---RTFSLVVRLFGNV--------------MSGVFVVGIVLSLAGLLVPI 188
Cdd:MTH00173  122 yNPSKSLAGLVPAGAPAGLNPFLVLIETVSiliRPLTLTVRLLANIsaghivltlignylSSSLFSSSVVSLLLVLLIQV 201

                         170       180
                  ....*....|....*....|
gi 1252061573 189 PLMALDLLTGAVQAYIFAVL 208
Cdd:MTH00173  202 GYFIFEVAVMLIQAYIFTLL 221
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 33-214 2.48e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 43.88  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  33 LAVVSALLTRRLSLEPSRMQTVLELLVETIDAQIRDTMQTGPAPYRALVGTLFVFVLVANWSSLVPGIEPPTAHLETDAA 112
Cdd:MTH00172   27 VIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHIVVTLG 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573 113 LALvvffaTIVHGVRTRGVRGYLATFAE---PT---WVMVPLNV----VEQITRTFSLVVRLFGNVMSG----------- 171
Cdd:MTH00172  107 LSF-----SIIIGVTLAGFWRFKWDFFSilmPSgapLGLAPLLVlietVSYISRAISLGVRLAANLSAGhllfailagfg 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1252061573 172 --VFVVGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIG 214
Cdd:MTH00172  182 fnMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLA 226
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 48-208 9.85e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 39.33  E-value: 9.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  48 PSRMQTVLELLVETIDAQIRDTMQTGPAPYRALVGTLFVFVLVANWSSLVPGIEPPTAHLETDAALALVVFFATIVHGVR 127
Cdd:MTH00005   44 PNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVT 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573 128 ---TRGVRGYLATFAePTWVMVPLNVVEQIT---RTFSLVVRLFGNVMSGvfvvGIVLSLAG------LLVPIPLMALDL 195
Cdd:MTH00005  124 fspKKFAAHLLPGGA-PDWLNPFLVLIETISilvRPITLSFRLAANMSAG----HIVLSLIGiyaasaLFSSISSTILLI 198

                         170       180
                  ....*....|....*....|....
gi 1252061573 196 LTGA-----------VQAYIFAVL 208
Cdd:MTH00005  199 LTQMgyilfevgiclIQAYIFCLL 222
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 49-208 3.44e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 37.64  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573  49 SRMQTVLELLVETIDAQIRDTMQTGPAPYRALVGTLFVFVLVANWSSLVPGIEPPTAHLETDAALALVVFFATIVHGVRT 128
Cdd:MTH00073   41 NRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRN 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573 129 RGVR--GYLATFAEPTWVMVPLNVVEQIT---RTFSLVVRLFGNVMSG----------VFVVGIVLSLAGLLVPIPLMAL 193
Cdd:MTH00073  121 QPTAslGHLLPEGTPTLLIPILIIIETISlfiRPLALGVRLTANLTAGhlliqlistaTLVLLPLMPTVSILTMIVLFLL 200

                         170
                  ....*....|....*...
gi 1252061573 194 DLLTGAV---QAYIFAVL 208
Cdd:MTH00073  201 TLLEIAVamiQAYVFVLL 218
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 144-214 3.66e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 37.95  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252061573 144 VMVPLN-VVEQITRTFSLVVRLFGNVMSGVFVV-----GIVLSLAGLLVPIPLMA------LDLLTGAVQAYIFAVLAMV 211
Cdd:PRK13417  264 IMWPLEfIVSPMAKTFALTVRLLANMTAGHVIIlalmgFIFQFQSWGIVPVSVIGsgliyvLEIFVAFLQAYIFVLLTSL 343


                  ...
gi 1252061573 212 FIG 214
Cdd:PRK13417  344 FVG 346
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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