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Conserved domains on  [gi|1846474250|ref|WP_171913726|]
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F0F1 ATP synthase subunit A [Paraburkholderia xenovorans]

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
 1-222 4.52e-134

F0F1 ATP synthase subunit A; Provisional


:

Pssm-ID: 237383  Cd Length: 223  Bit Score: 375.96  E-value: 4.52e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250   1 MTESPLTIAPLLQLGPVPITGPVLITWGIMAIVTAGAVVLSRRLSLAPGKTQTALELLVDTIDQQIRDTMQTEAATYRAL 80
Cdd:PRK13421    1 MTASPLSTVPLFSLGPVPISAPVVVTWAIMAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  81 IGTLFVFVLVANWCALVPGVTPPTAHLETDAALALIVLGATIFYGVRSRGATGYLASFAEPSWVMIPLNVVEQITRTFSL 160
Cdd:PRK13421   81 IGTLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVRARGVRGYLATFAEPTWVMIPLNLVEQLTRTFSL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1846474250 161 VVRLFGNVMSGVFVIGILLSLAGLLVPIPLMALDLLTGAVQAYIFAVLSMVFIGAAIGDPHH 222
Cdd:PRK13421  161 IVRLFGNVMSGVFVIGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVSDDEA 222
 
Name Accession Description Interval E-value
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
 1-222 4.52e-134

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 375.96  E-value: 4.52e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250   1 MTESPLTIAPLLQLGPVPITGPVLITWGIMAIVTAGAVVLSRRLSLAPGKTQTALELLVDTIDQQIRDTMQTEAATYRAL 80
Cdd:PRK13421    1 MTASPLSTVPLFSLGPVPISAPVVVTWAIMAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  81 IGTLFVFVLVANWCALVPGVTPPTAHLETDAALALIVLGATIFYGVRSRGATGYLASFAEPSWVMIPLNVVEQITRTFSL 160
Cdd:PRK13421   81 IGTLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVRARGVRGYLATFAEPTWVMIPLNLVEQLTRTFSL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1846474250 161 VVRLFGNVMSGVFVIGILLSLAGLLVPIPLMALDLLTGAVQAYIFAVLSMVFIGAAIGDPHH 222
Cdd:PRK13421  161 IVRLFGNVMSGVFVIGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVSDDEA 222
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 22-219 2.43e-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: 196.06  E-value: 2.43e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  22 PVLITWGIMAIVTAGAVVLSRRLSLAPGKTQTALELLVDTIDQQIRDTMQTEAATYRALIGTLFVFVLVANWCALVPGVT 101
Cdd:COG0356     2 TVLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250 102 PPTAHLETDAALALIVLGATIFYGVRSRGATGYLAS-FAEPSW----VMIPLNVVEQITRTFSLVVRLFGNVMSGVFVIG 176
Cdd:COG0356    82 PPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHlFFPPFPwlapLMLPIEIISELARPLSLSLRLFGNMFAGHIILL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1846474250 177 ILLSLAG--------LLVPIPLMALDLLTGAVQAYIFAVLSMVFIGAAIGD 219
Cdd:COG0356   162 LLAGLAPflllgvlsLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVEE 212
altF1_A TIGR03306
alternate F1F0 ATPase, F0 subunit A; A small number of taxonomically diverse prokaryotic ...
 11-216 1.24e-54

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: 174.16  E-value: 1.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  11 LLQLGPVPITGPVLITWGIMAIVTAGAVVLSRRLS--LAPGKTQTALELLVDTIDQQIRDTMQTEAATYRALIGTLFVFV 88
Cdd:TIGR03306   8 YWQYGFVKINATIAFTWLLMLLLVIGSWLITRRLStgLERSRWQNLLEVLVTGIQEQISDVGLAKPRKYLPFLGTLFLFI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  89 LVANWCALVPGVTPPTAHLETDAALALIVLGATIFYGVRSRGATGYLASFAEPSWVMIPLNVVEQITRTFSLVVRLFGNV 168
Cdd:TIGR03306  88 AVANLLSVIPGYEPPTGSLSTTAALALCVFVAVPLFGIAERGLSGYLKSYLKPTPFMLPFNIIGELSRTLALAVRLFGNM 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1846474250 169 MSGVFVIGILLSLAGLLVPIPLMALDLLTGAVQAYIFAVLSMVFIGAA 216
Cdd:TIGR03306 168 MSGSMILAILLSISPLIFPVLMQVLGLLTGMVQAYIFSVLATVYIAAA 215
ATP-synt_A pfam00119
ATP synthase A chain;
23-214 4.24e-42

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 142.24  E-value: 4.24e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  23 VLITWGIMAIVTAGAVVLSRRLS-LAPGKTQTALELLVDTIDQQIRDTM-QTEAATYRALIGTLFVFVLVANWCALV--- 97
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKTKkLVPGRLQNFVEMLVEFVDNIVKDNIgKKKGRKFFPLLLTLFFFILVSNLLGLIpks 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  98 PGVTPPTAHLETDAALALIVLGATIFYGVRSRGATGYLASFAEPS------WVMIPLNVVEQITRTFSLVVRLFGNVMSG 171
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKLFVPPvplplvPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1846474250 172 VFVIGILLSLAG-------------LLVPIPLMALDLLTGAVQAYIFAVLSMVFIG 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 ...
 80-214 3.12e-36

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: 125.20  E-value: 3.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  80 LIGTLFVFVLVANWCALVPGVTPPTAHLETDAALALIVLGATIFYGVRSRGATGYLASF-----AEPSWVMIPLNVVEQI 154
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLppgtpLPLAPLMVPIELISEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250 155 TRTFSLVVRLFGNVMSGVFVIGILLSLA----------GLLVPIPLMALDLLTGAVQAYIFAVLSMVFIG 214
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVpsllssvgllPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
 
Name Accession Description Interval E-value
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
 1-222 4.52e-134

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 375.96  E-value: 4.52e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250   1 MTESPLTIAPLLQLGPVPITGPVLITWGIMAIVTAGAVVLSRRLSLAPGKTQTALELLVDTIDQQIRDTMQTEAATYRAL 80
Cdd:PRK13421    1 MTASPLSTVPLFSLGPVPISAPVVVTWAIMAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  81 IGTLFVFVLVANWCALVPGVTPPTAHLETDAALALIVLGATIFYGVRSRGATGYLASFAEPSWVMIPLNVVEQITRTFSL 160
Cdd:PRK13421   81 IGTLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVRARGVRGYLATFAEPTWVMIPLNLVEQLTRTFSL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1846474250 161 VVRLFGNVMSGVFVIGILLSLAGLLVPIPLMALDLLTGAVQAYIFAVLSMVFIGAAIGDPHH 222
Cdd:PRK13421  161 IVRLFGNVMSGVFVIGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVSDDEA 222
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 22-219 2.43e-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: 196.06  E-value: 2.43e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  22 PVLITWGIMAIVTAGAVVLSRRLSLAPGKTQTALELLVDTIDQQIRDTMQTEAATYRALIGTLFVFVLVANWCALVPGVT 101
Cdd:COG0356     2 TVLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250 102 PPTAHLETDAALALIVLGATIFYGVRSRGATGYLAS-FAEPSW----VMIPLNVVEQITRTFSLVVRLFGNVMSGVFVIG 176
Cdd:COG0356    82 PPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHlFFPPFPwlapLMLPIEIISELARPLSLSLRLFGNMFAGHIILL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1846474250 177 ILLSLAG--------LLVPIPLMALDLLTGAVQAYIFAVLSMVFIGAAIGD 219
Cdd:COG0356   162 LLAGLAPflllgvlsLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVEE 212
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 13-221 2.90e-55

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 176.14  E-value: 2.90e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  13 QLGPVPITGPVLITWGIMAIVTAGAVVLSRRLSLAPGKTQTALELLVDTIDQQIRDTMQTEAATYRALIGTLFVFVLVAN 92
Cdd:PRK05815    8 GFGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  93 WCALVP-GVTPPTAHLETDAALALIVLGATIFYGVRSRGATGYLASF-AEPSWVMIPLNVVEQITRTFSLVVRLFGNVMS 170
Cdd:PRK05815   88 LLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFyLQPHPLLLPIEIISEFSRPISLSLRLFGNMLA 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250 171 G---------VFVIGILLSLAGLLVPIPLMALDLLTGAVQAYIFAVLSMVFIGAAIGDPH 221
Cdd:PRK05815  168 GelilalialLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEEEH 227
altF1_A TIGR03306
alternate F1F0 ATPase, F0 subunit A; A small number of taxonomically diverse prokaryotic ...
 11-216 1.24e-54

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: 174.16  E-value: 1.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  11 LLQLGPVPITGPVLITWGIMAIVTAGAVVLSRRLS--LAPGKTQTALELLVDTIDQQIRDTMQTEAATYRALIGTLFVFV 88
Cdd:TIGR03306   8 YWQYGFVKINATIAFTWLLMLLLVIGSWLITRRLStgLERSRWQNLLEVLVTGIQEQISDVGLAKPRKYLPFLGTLFLFI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  89 LVANWCALVPGVTPPTAHLETDAALALIVLGATIFYGVRSRGATGYLASFAEPSWVMIPLNVVEQITRTFSLVVRLFGNV 168
Cdd:TIGR03306  88 AVANLLSVIPGYEPPTGSLSTTAALALCVFVAVPLFGIAERGLSGYLKSYLKPTPFMLPFNIIGELSRTLALAVRLFGNM 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1846474250 169 MSGVFVIGILLSLAGLLVPIPLMALDLLTGAVQAYIFAVLSMVFIGAA 216
Cdd:TIGR03306 168 MSGSMILAILLSISPLIFPVLMQVLGLLTGMVQAYIFSVLATVYIAAA 215
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 11-217 2.83e-52

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 168.38  E-value: 2.83e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  11 LLQLGPVPITGPVLITWGIMAIVTAGAVVLSRRLSLAPGKTQTALELLVDTIDQQIRDTMQTEAATYRALIGTLFVFVLV 90
Cdd:PRK13420    8 LFHIGPLPITESVLTTWGIMIVLVLASWLTTRRLSLDPGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFVGTLWIFILV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  91 ANWCALVPGVTPPTAHLETDAALALIVLGATIFYGVRSRGATGYLASFAEPSWVMIPLNVVEQITRTFSLVVRLFGNVMS 170
Cdd:PRK13420   88 ANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEGLREYLKHYLSPSPFLLPFHLISEITRTLALAVRLFGNIMS 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1846474250 171 GVFVIGILLSLAGLLVPIPLMALDLLTGAVQAYIFAVLSMVFIGAAI 217
Cdd:PRK13420  168 LELAALLVLLVAGFLVPVPILMLHIIEALVQAYIFGMLALIYIAGGI 214
ATP-synt_A pfam00119
ATP synthase A chain;
23-214 4.24e-42

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 142.24  E-value: 4.24e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  23 VLITWGIMAIVTAGAVVLSRRLS-LAPGKTQTALELLVDTIDQQIRDTM-QTEAATYRALIGTLFVFVLVANWCALV--- 97
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKTKkLVPGRLQNFVEMLVEFVDNIVKDNIgKKKGRKFFPLLLTLFFFILVSNLLGLIpks 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  98 PGVTPPTAHLETDAALALIVLGATIFYGVRSRGATGYLASFAEPS------WVMIPLNVVEQITRTFSLVVRLFGNVMSG 171
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKLFVPPvplplvPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1846474250 172 VFVIGILLSLAG-------------LLVPIPLMALDLLTGAVQAYIFAVLSMVFIG 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 ...
 80-214 3.12e-36

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: 125.20  E-value: 3.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  80 LIGTLFVFVLVANWCALVPGVTPPTAHLETDAALALIVLGATIFYGVRSRGATGYLASF-----AEPSWVMIPLNVVEQI 154
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLppgtpLPLAPLMVPIELISEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250 155 TRTFSLVVRLFGNVMSGVFVIGILLSLA----------GLLVPIPLMALDLLTGAVQAYIFAVLSMVFIG 214
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVpsllssvgllPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
atpI CHL00046
ATP synthase CF0 A subunit
 13-214 3.63e-34

ATP synthase CF0 A subunit


Pssm-ID: 176987  Cd Length: 228  Bit Score: 121.96  E-value: 3.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  13 QLGPVPITGPVLIT-WGIMAIVTAGAVVLSRRLSLAPGKTQTALELLVDTIDQQIRDTM-QTEAATYRALIGTLFVFVLV 90
Cdd:CHL00046   15 QIGGFQVHGQVLITsWVVIAILLGSALLATRNLQTIPTGGQNFFEYVLEFIRDLAKTQIgEEEYRPWVPFIGTMFLFIFV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  91 ANWC-ALVP---------GVTPPTAHLETDAALALIVLGATIFYGVRSRGaTGYLASFAEPSWVMIPLNVVEQITRTFSL 160
Cdd:CHL00046   95 SNWSgALLPwklielphgELAAPTNDINTTVALALLTSVAYFYAGLSKKG-LGYFGKYIQPTPILLPINILEDFTKPLSL 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1846474250 161 VVRLFGNVMSGVFVIGILLSLAGLLVPIPLMALDLLTGAVQAYIFAVLSMVFIG 214
Cdd:CHL00046  174 SFRLFGNILADELVVAVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIG 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 24-217 1.20e-25

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: 99.59  E-value: 1.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  24 LITWGIMAIVTAGAVVLSRRLSLAPGKTQTALELLVDTIDQQIRDTMQTEAATYRALIGTLFVFVLVANWCALVPGVTPP 103
Cdd:TIGR01131  17 LLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250 104 TAHLETDAALALIVLGATIFYGVRSR--GATGYLASFAEPSW---VMIPLNVVEQITRTFSLVVRLFGNVMSGVFVIGIL 178
Cdd:TIGR01131  97 TSHLSFTLGLALPLWLGLTISGFRKHpkGFLAHLVPSGTPLPlipFLVIIETISYLARPISLSVRLFANISAGHLLLTLL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1846474250 179 LSLA-----------GLLVPIPLMALDLLTGAVQAYIFAVLSMVFIGAAI 217
Cdd:TIGR01131 177 SGLLfslmssaifalLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 19-222 4.56e-18

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 81.33  E-value: 4.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  19 ITGPVLITWGIMAIV-----TAGAVVLSRRLSLAPGKTQTALELLVDTIDQQI-RDTMQTEAATYRALIGTLFVFVLVAN 92
Cdd:PRK13419  106 ITKHVVMMWIASAILlvvflAAGRKYKKMTKSQAPKGLANAMEALVEFIRLDVaKSNIGHGYEKFLPYLLTVFFFILVCN 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  93 WCALVPGVTPPTAHLETDAALALIVLGATIFYGVRSRGATGYLASFA---EPS-W-VMIPLNVVEQITRTFSLVVRLFGN 167
Cdd:PRK13419  186 LLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTggtHWSlWiIMIPIEFIGLFTKPFALTVRLFAN 265

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1846474250 168 VMSGVFVIGILLSL----------AGLLVP--IPLMALDLLTGAVQAYIFAVLSMVFIGAAIGDPHH 222
Cdd:PRK13419  266 MTAGHIVILSLIFIsfilksyivaVAVSVPfaIFIYLLELFVAFLQAYIFTMLSALFIGLATAHEGH 332
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 19-209 6.68e-09

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 54.27  E-value: 6.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  19 ITGPVLITWGIMAIvtaGAVVLSRRLSLAPGKTQTALELLVDTIDQQIRDTMQTEAATYRALIGTLFVFVLVANWCALVP 98
Cdd:MTH00176   16 IFSMISLSWITLLL---FLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFILVMSLNLSGLIP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  99 GVTPPTAHLETDAALALIVLGATIFYGVR--SRGATGYLASFAEPSWVMIPLNVVEQIT---RTFSLVVRLFGNVMSGVF 173
Cdd:MTH00176   93 YVFTSTSHLVITLSLALPLWLGVILSGFInnFYSRLSHLVPQGTPPLLNPFLVLIELVSlliRPLTLAVRLAANLSAGHL 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1846474250 174 VIGIL------------LSLAGLLVP-IPLMALDLLTGAVQAYIFAVLS 209
Cdd:MTH00176  173 LLGLLgaamwgllpvspLIGFLLLIVqILYFMFEIAVCMIQAYVFTLLL 221
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 29-217 8.95e-09

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 53.89  E-value: 8.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  29 IMAIVTAGAVVLSRRLSLAPGKTQTALELLVDTIDQQIRDTMQTEAATYRALIGTLFVFVLVANWCALVPGVTPPTAHLE 108
Cdd:MTH00172   23 MMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHIV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250 109 TDAALAL-IVLGATI--FYGVRSRGATGYLASFA----EPSWVMIPLnvVEQITRTFSLVVRLFGNVMSGVFVIGIL--- 178
Cdd:MTH00172  103 VTLGLSFsIIIGVTLagFWRFKWDFFSILMPSGAplglAPLLVLIET--VSYISRAISLGVRLAANLSAGHLLFAILagf 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1846474250 179 ----------LSLAGLLVPIPLMALDLLTGAVQAYIFAVLSMVFIGAAI 217
Cdd:MTH00172  181 gfnmlcasgfLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTI 229
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 6-217 4.41e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 49.23  E-value: 4.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250   6 LTIAPLLQLGPVPITGPVLITWGIMAIVTagavVLSRRLSLAPGKTQTALELLVDTIDQQIRDTMQTEAATYRALIGTLF 85
Cdd:MTH00175   15 ITIQAFLGDWLVTFTNSSMMMVLAVIIFW----LLLKGDKLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  86 VFVLVANWCALVPGVTPPTAHLETDAALAL-IVLGATIFYGVRSR----------GATGYLASFaepswvMIPLNVVEQI 154
Cdd:MTH00175   91 LFIAILNILGLFPYVFTPTAHIIITFGLSLsIIIAVTLLGFLTFKwnflsilmpgGAPLVLAPF------LVLIETLSYL 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1846474250 155 TRTFSLVVRLFGNVMSGVFVIGIL--------------LSLAGLLVPIPLMALDLLTGAVQAYIFAVLSMVFIGAAI 217
Cdd:MTH00175  165 IRAISLGVRLAANISAGHLLFAILsgfafnmlsngliiLSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGDTI 241
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 45-213 8.19e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 48.40  E-value: 8.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  45 SLAPGKTQTALELLVDTIDQQIRDTMQTEAATYRALIGTLFVFVLVANWCALVPGVTPPTAHLETDAALALIVLGATIFY 124
Cdd:MTH00174   58 TLVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250 125 GVRSRGATGY--LASFAEPSWVMIPLNVVEQ---ITRTFSLVVRLFGNVMSGVFVIGILLSLA----------GLLVPIP 189
Cdd:MTH00174  138 GLITFRFNFFsiLMPQGAPLALAPLLTIIETlsyISRAISLGVRLAANISSGHLLFSIIASFAwkmintgiliGSFVPFA 217

                         170       180
                  ....*....|....*....|....*...
gi 1846474250 190 LM----ALDLLTGAVQAYIFAVLSMVFI 213
Cdd:MTH00174  218 ILifvtILEMAVAIIQAYVFTLLTIVYL 245
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 80-208 4.05e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 43.32  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  80 LIGTLFVFVLVANWCALVPGVTPPTAHLETDAALALIVLGATIFYGV---RSRGATGYLASFAepSWVMIP-LNVVEQIT 155
Cdd:MTH00173   74 LLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLfynPSKSLAGLVPAGA--PAGLNPfLVLIETVS 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250 156 ---RTFSLVVRLFGNV--------------MSGVFVIGILLSLAGLLVPIPLMALDLLTGAVQAYIFAVL 208
Cdd:MTH00173  152 iliRPLTLTVRLLANIsaghivltlignylSSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLL 221
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 144-217 5.12e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 40.26  E-value: 5.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250 144 VMIPLN-VVEQITRTFSLVVRLFGNVMSGVFVIGILL-----SLAGLLVPIPLMA------LDLLTGAVQAYIFAVLSMV 211
Cdd:PRK13417  264 IMWPLEfIVSPMAKTFALTVRLLANMTAGHVIILALMgfifqFQSWGIVPVSVIGsgliyvLEIFVAFLQAYIFVLLTSL 343


                  ....*.
gi 1846474250 212 FIGAAI 217
Cdd:PRK13417  344 FVGLSM 349
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 39-208 1.88e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 38.18  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  39 VLSRRLSLAPGKTQTALELLVDTIDQQIRDTMQTEAATYRALIGTLFVFVLVANWCALVPGVTPPTAHLETDAALALIVL 118
Cdd:MTH00005   35 LLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLW 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250 119 GATIFYGVR---SRGATGYLASFAePSWVMIPLNVVEQIT---RTFSLVVRLFGNVMSGVFVIGIL--LSLAGLLVPIPL 190
Cdd:MTH00005  115 LSLIMSSVTfspKKFAAHLLPGGA-PDWLNPFLVLIETISilvRPITLSFRLAANMSAGHIVLSLIgiYAASALFSSISS 193

                         170       180
                  ....*....|....*....|....*....
gi 1846474250 191 MALDLLTGA-----------VQAYIFAVL 208
Cdd:MTH00005  194 TILLILTQMgyilfevgiclIQAYIFCLL 222
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 83-210 6.64e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 36.68  E-value: 6.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250  83 TLFVFVLVANWCALVPGVTPPTAHLETDAALALIVLGATIFYG------------VRSrGATGYLASFAepswVMIPLnv 150
Cdd:MTH00157   74 SLFSFILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGwinntnhmfahlVPQ-GTPPILMPFM----VLIET-- 146

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1846474250 151 VEQITRTFSLVVRLFGNVMSGVFVIGIL----LSLAGLLVPI---PLMALDLLTGAV---QAYIFAVLSM 210
Cdd:MTH00157  147 ISNLIRPGTLAVRLAANMIAGHLLLTLLgntgPSLSSMILSIlilIQILLLILESAVaiiQSYVFSVLST 216
 
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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