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Conserved domains on  [gi|182635574|gb|ACB96348|]
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ATP synthase F0, A subunit [Beijerinckia indica subsp. indica ATCC 9039]

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 3.06e-134

F0F1 ATP synthase subunit A; Provisional


:

Pssm-ID: 237383  Cd Length: 223  Bit Score: 376.34  E-value: 3.06e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574   1 MDSPLTLAPLFHLGPVPITAPVLVTWAIMLILGIGARLVTRHLSIPPSRSQAALETVTGAIDSQIKDTMQVDPAPYRALI 80
Cdd:PRK13421   2 TASPLSTVPLFSLGPVPISAPVVVTWAIMAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRALI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  81 GTIVLYVLTANWSSLVPGVEPPTAHLETDAALALIVFCATIVYGVRAQGLAGYLKTFADPSWVMIPLNVVEQITRTFSLI 160
Cdd:PRK13421  82 GTLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVRARGVRGYLATFAEPTWVMIPLNLVEQLTRTFSLI 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 182635574 161 IRLFGNIMSGVFIIGIILSLAGLLVPIPLMALDLLTGAIQAYIFAILACVFIGAAVSERPAP 222
Cdd:PRK13421 162 VRLFGNVMSGVFVIGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVSDDEAS 223
 
Name Accession Description Interval E-value
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
 1-222 3.06e-134

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 376.34  E-value: 3.06e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574   1 MDSPLTLAPLFHLGPVPITAPVLVTWAIMLILGIGARLVTRHLSIPPSRSQAALETVTGAIDSQIKDTMQVDPAPYRALI 80
Cdd:PRK13421   2 TASPLSTVPLFSLGPVPISAPVVVTWAIMAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRALI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  81 GTIVLYVLTANWSSLVPGVEPPTAHLETDAALALIVFCATIVYGVRAQGLAGYLKTFADPSWVMIPLNVVEQITRTFSLI 160
Cdd:PRK13421  82 GTLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVRARGVRGYLATFAEPTWVMIPLNLVEQLTRTFSLI 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 182635574 161 IRLFGNIMSGVFIIGIILSLAGLLVPIPLMALDLLTGAIQAYIFAILACVFIGAAVSERPAP 222
Cdd:PRK13421 162 VRLFGNVMSGVFVIGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVSDDEAS 223
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 21-218 1.43e-65

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: 201.84  E-value: 1.43e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  21 PVLVTWAIMLILGIGARLVTRHLSIPPSRSQAALETVTGAIDSQIKDTMQVDPAPYRALIGTIVLYVLTANWSSLVPGVE 100
Cdd:COG0356    2 TVLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574 101 PPTAHLETDAALALIVFCATIVYGVRAQGLAGYLKT-FADPSW----VMIPLNVVEQITRTFSLIIRLFGNIMSGVFIIG 175
Cdd:COG0356   82 PPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHlFFPPFPwlapLMLPIEIISELARPLSLSLRLFGNMFAGHIILL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 182635574 176 IILSLAG--------LLVPIPLMALDLLTGAIQAYIFAILACVFIGAAVSE 218
Cdd:COG0356  162 LLAGLAPflllgvlsLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVEE 212
altF1_A TIGR03306
alternate F1F0 ATPase, F0 subunit A; A small number of taxonomically diverse prokaryotic ...
 10-217 3.02e-55

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: 175.70  E-value: 3.02e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574   10 LFHLGPVPITAPVLVTWAIMLILGIGARLVTRHLS--IPPSRSQAALETVTGAIDSQIKDTMQVDPAPYRALIGTIVLYV 87
Cdd:TIGR03306   8 YWQYGFVKINATIAFTWLLMLLLVIGSWLITRRLStgLERSRWQNLLEVLVTGIQEQISDVGLAKPRKYLPFLGTLFLFI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574   88 LTANWSSLVPGVEPPTAHLETDAALALIVFCATIVYGVRAQGLAGYLKTFADPSWVMIPLNVVEQITRTFSLIIRLFGNI 167
Cdd:TIGR03306  88 AVANLLSVIPGYEPPTGSLSTTAALALCVFVAVPLFGIAERGLSGYLKSYLKPTPFMLPFNIIGELSRTLALAVRLFGNM 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 182635574  168 MSGVFIIGIILSLAGLLVPIPLMALDLLTGAIQAYIFAILACVFIGAAVS 217
Cdd:TIGR03306 168 MSGSMILAILLSISPLIFPVLMQVLGLLTGMVQAYIFSVLATVYIAAATR 217
ATP-synt_A pfam00119
ATP synthase A chain;
22-213 1.11e-42

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 143.40  E-value: 1.11e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574   22 VLVTWAIMLILGIGARLVTR-HLSIPPSRSQAALETVTGAIDSQIKDTM-QVDPAPYRALIGTIVLYVLTANWSSLV--- 96
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRkTKKLVPGRLQNFVEMLVEFVDNIVKDNIgKKKGRKFFPLLLTLFFFILVSNLLGLIpks 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574   97 PGVEPPTAHLETDAALALIVFCATIVYGVRAQGLAGYLKTFADPS------WVMIPLNVVEQITRTFSLIIRLFGNIMSG 170
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKLFVPPvplplvPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 182635574  171 VFIIGIILSLAG-------------LLVPIPLMALDLLTGAIQAYIFAILACVFIG 213
Cdd:pfam00119 161 HLLLLLLAGLIFallsagfllgvipPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 75-213 5.56e-39

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: 132.14  E-value: 5.56e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  75 PYRALIGTIVLYVLTANWSSLVPGVEPPTAHLETDAALALIVFCATIVYGVRAQGLAGYLK-----TFADPSWVMIPLNV 149
Cdd:cd00310    3 KYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHflppgTPLPLAPLMVPIEL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 182635574 150 VEQITRTFSLIIRLFGNIMSGVFIIGIILSLA----------GLLVPIPLMALDLLTGAIQAYIFAILACVFIG 213
Cdd:cd00310   83 ISELIRPLSLSVRLFANMFAGHLLLALLSGLVpsllssvgllPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
 
Name Accession Description Interval E-value
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
 1-222 3.06e-134

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 376.34  E-value: 3.06e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574   1 MDSPLTLAPLFHLGPVPITAPVLVTWAIMLILGIGARLVTRHLSIPPSRSQAALETVTGAIDSQIKDTMQVDPAPYRALI 80
Cdd:PRK13421   2 TASPLSTVPLFSLGPVPISAPVVVTWAIMAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRALI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  81 GTIVLYVLTANWSSLVPGVEPPTAHLETDAALALIVFCATIVYGVRAQGLAGYLKTFADPSWVMIPLNVVEQITRTFSLI 160
Cdd:PRK13421  82 GTLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVRARGVRGYLATFAEPTWVMIPLNLVEQLTRTFSLI 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 182635574 161 IRLFGNIMSGVFIIGIILSLAGLLVPIPLMALDLLTGAIQAYIFAILACVFIGAAVSERPAP 222
Cdd:PRK13421 162 VRLFGNVMSGVFVIGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVSDDEAS 223
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 21-218 1.43e-65

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: 201.84  E-value: 1.43e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  21 PVLVTWAIMLILGIGARLVTRHLSIPPSRSQAALETVTGAIDSQIKDTMQVDPAPYRALIGTIVLYVLTANWSSLVPGVE 100
Cdd:COG0356    2 TVLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574 101 PPTAHLETDAALALIVFCATIVYGVRAQGLAGYLKT-FADPSW----VMIPLNVVEQITRTFSLIIRLFGNIMSGVFIIG 175
Cdd:COG0356   82 PPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHlFFPPFPwlapLMLPIEIISELARPLSLSLRLFGNMFAGHIILL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 182635574 176 IILSLAG--------LLVPIPLMALDLLTGAIQAYIFAILACVFIGAAVSE 218
Cdd:COG0356  162 LLAGLAPflllgvlsLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVEE 212
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 11-218 2.96e-58

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 183.84  E-value: 2.96e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  11 FHLGPVPITAPVLVTWAIMLILGIGARLVTRHLSIPPSRSQAALETVTGAIDSQIKDTMQVDPAPYRALIGTIVLYVLTA 90
Cdd:PRK05815   7 IGFGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  91 NWSSLVP-GVEPPTAHLETDAALALIVFCATIVYGVRAQGLAGYLK-TFADPSWVMIPLNVVEQITRTFSLIIRLFGNIM 168
Cdd:PRK05815  87 NLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKeFYLQPHPLLLPIEIISEFSRPISLSLRLFGNML 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 182635574 169 SGVFIIGII---------LSLAGLLVPIPLMALDLLTGAIQAYIFAILACVFIGAAVSE 218
Cdd:PRK05815 167 AGELILALIallggagllLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEE 225
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 10-227 5.43e-56

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 178.01  E-value: 5.43e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  10 LFHLGPVPITAPVLVTWAIMLILGIGARLVTRHLSIPPSRSQAALETVTGAIDSQIKDTMQVDPAPYRALIGTIVLYVLT 89
Cdd:PRK13420   8 LFHIGPLPITESVLTTWGIMIVLVLASWLTTRRLSLDPGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFVGTLWIFILV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  90 ANWSSLVPGVEPPTAHLETDAALALIVFCATIVYGVRAQGLAGYLKTFADPSWVMIPLNVVEQITRTFSLIIRLFGNIMS 169
Cdd:PRK13420  88 ANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEGLREYLKHYLSPSPFLLPFHLISEITRTLALAVRLFGNIMS 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 182635574 170 GVFIIGIILSLAGLLVPIPLMALDLLTGAIQAYIFAILACVFIGAAVSERPAPSQQEP 227
Cdd:PRK13420 168 LELAALLVLLVAGFLVPVPILMLHIIEALVQAYIFGMLALIYIAGGIQAHELKSQGES 225
altF1_A TIGR03306
alternate F1F0 ATPase, F0 subunit A; A small number of taxonomically diverse prokaryotic ...
 10-217 3.02e-55

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: 175.70  E-value: 3.02e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574   10 LFHLGPVPITAPVLVTWAIMLILGIGARLVTRHLS--IPPSRSQAALETVTGAIDSQIKDTMQVDPAPYRALIGTIVLYV 87
Cdd:TIGR03306   8 YWQYGFVKINATIAFTWLLMLLLVIGSWLITRRLStgLERSRWQNLLEVLVTGIQEQISDVGLAKPRKYLPFLGTLFLFI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574   88 LTANWSSLVPGVEPPTAHLETDAALALIVFCATIVYGVRAQGLAGYLKTFADPSWVMIPLNVVEQITRTFSLIIRLFGNI 167
Cdd:TIGR03306  88 AVANLLSVIPGYEPPTGSLSTTAALALCVFVAVPLFGIAERGLSGYLKSYLKPTPFMLPFNIIGELSRTLALAVRLFGNM 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 182635574  168 MSGVFIIGIILSLAGLLVPIPLMALDLLTGAIQAYIFAILACVFIGAAVS 217
Cdd:TIGR03306 168 MSGSMILAILLSISPLIFPVLMQVLGLLTGMVQAYIFSVLATVYIAAATR 217
ATP-synt_A pfam00119
ATP synthase A chain;
22-213 1.11e-42

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 143.40  E-value: 1.11e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574   22 VLVTWAIMLILGIGARLVTR-HLSIPPSRSQAALETVTGAIDSQIKDTM-QVDPAPYRALIGTIVLYVLTANWSSLV--- 96
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRkTKKLVPGRLQNFVEMLVEFVDNIVKDNIgKKKGRKFFPLLLTLFFFILVSNLLGLIpks 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574   97 PGVEPPTAHLETDAALALIVFCATIVYGVRAQGLAGYLKTFADPS------WVMIPLNVVEQITRTFSLIIRLFGNIMSG 170
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKLFVPPvplplvPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 182635574  171 VFIIGIILSLAG-------------LLVPIPLMALDLLTGAIQAYIFAILACVFIG 213
Cdd:pfam00119 161 HLLLLLLAGLIFallsagfllgvipPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 75-213 5.56e-39

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: 132.14  E-value: 5.56e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  75 PYRALIGTIVLYVLTANWSSLVPGVEPPTAHLETDAALALIVFCATIVYGVRAQGLAGYLK-----TFADPSWVMIPLNV 149
Cdd:cd00310    3 KYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHflppgTPLPLAPLMVPIEL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 182635574 150 VEQITRTFSLIIRLFGNIMSGVFIIGIILSLA----------GLLVPIPLMALDLLTGAIQAYIFAILACVFIG 213
Cdd:cd00310   83 ISELIRPLSLSVRLFANMFAGHLLLALLSGLVpsllssvgllPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
atpI CHL00046
ATP synthase CF0 A subunit
 23-213 1.48e-30

ATP synthase CF0 A subunit


Pssm-ID: 176987  Cd Length: 228  Bit Score: 112.72  E-value: 1.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  23 LVTWAIMLILGIGARLVTRHLSIPPSRSQAALETVTGAIDSQIKDTM-QVDPAPYRALIGTIVLYVLTANWS-------- 93
Cdd:CHL00046  27 ITSWVVIAILLGSALLATRNLQTIPTGGQNFFEYVLEFIRDLAKTQIgEEEYRPWVPFIGTMFLFIFVSNWSgallpwkl 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  94 SLVPGVE--PPTAHLETDAALALIVFCATIVYGVRAQGLaGYLKTFADPSWVMIPLNVVEQITRTFSLIIRLFGNIMSGV 171
Cdd:CHL00046 107 IELPHGElaAPTNDINTTVALALLTSVAYFYAGLSKKGL-GYFGKYIQPTPILLPINILEDFTKPLSLSFRLFGNILADE 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 182635574 172 FIIGIILSLAGLLVPIPLMALDLLTGAIQAYIFAILACVFIG 213
Cdd:CHL00046 186 LVVAVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIG 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 21-212 3.08e-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: 98.43  E-value: 3.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574   21 PVLVTWAIMLILGIGARLVTRHLSipPSRSQAALETVTGAIDSQIKDTMQVDPAPYRALIGTIVLYVLTANWSSLVPGVE 100
Cdd:TIGR01131  17 LLSLILLLSLLIFLISSSLSRWLI--PSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  101 PPTAHLETDAALALIVFCATIVYGVRA--QGLAGYLKTFADPSW---VMIPLNVVEQITRTFSLIIRLFGNIMSGVFIIG 175
Cdd:TIGR01131  95 TPTSHLSFTLGLALPLWLGLTISGFRKhpKGFLAHLVPSGTPLPlipFLVIIETISYLARPISLSVRLFANISAGHLLLT 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 182635574  176 IILSLA-----------GLLVPIPLMALDLLTGAIQAYIFAILACVFI 212
Cdd:TIGR01131 175 LLSGLLfslmssaifalLLLILVALIILEIFVAFIQAYVFTLLTCLYL 222
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 18-216 2.59e-14

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 70.93  E-value: 2.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  18 ITAPVLVTW---AIMLIL--GIGARLVTRHLSIPPSRSQAALETVTGAIDSQI-KDTMQVDPAPYRALIGTIVLYVLTAN 91
Cdd:PRK13419 106 ITKHVVMMWiasAILLVVflAAGRKYKKMTKSQAPKGLANAMEALVEFIRLDVaKSNIGHGYEKFLPYLLTVFFFILVCN 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  92 WSSLVPGVEPPTAHLETDAALALIVFCATIVYGVRAQGLAGYLKTF-ADPSW----VMIPLNVVEQITRTFSLIIRLFGN 166
Cdd:PRK13419 186 LLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLtGGTHWslwiIMIPIEFIGLFTKPFALTVRLFAN 265

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 182635574 167 IMSGVFII----GIILSL------AGLLVP--IPLMALDLLTGAIQAYIFAILACVFIGAAV 216
Cdd:PRK13419 266 MTAGHIVIlsliFISFILksyivaVAVSVPfaIFIYLLELFVAFLQAYIFTMLSALFIGLAT 327
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 22-208 2.66e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 46.56  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  22 VLVTWAIMLIlgiGARLVTRHLSIPPSRSQAALETVTGAIDSQIKDTMQVDPAPYRALIGTIVLYVLTANWSSLVPGVEP 101
Cdd:MTH00176  20 ISLSWITLLL---FLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFILVMSLNLSGLIPYVFT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574 102 PTAHLETDAALALIVFCATIVYGVRaQGLAGYLKTFADPS------WVMIPLNVVEQITRTFSLIIRLFGNIMSGVFIIG 175
Cdd:MTH00176  97 STSHLVITLSLALPLWLGVILSGFI-NNFYSRLSHLVPQGtppllnPFLVLIELVSLLIRPLTLAVRLAANLSAGHLLLG 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 182635574 176 I------------ILSLAGLLVP-IPLMALDLLTGAIQAYIFAILA 208
Cdd:MTH00176 176 LlgaamwgllpvsPLIGFLLLIVqILYFMFEIAVCMIQAYVFTLLL 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 23-212 3.44e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 43.77  E-value: 3.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  23 LVTWAIMLILGIGARLVTRhlSIPPSRSQAALETVTGAIDSQIKDTMQVDPAPYRALIGTIVLYVLTANWSSLVPGVEPP 102
Cdd:MTH00174  39 MMSFAVFLFYTIGAKGNNN--TLVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTP 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574 103 TAHLETDAALALIVFCATIVYGVRAQGLAGY--LKTFADPSWVMIPLNVVEQ---ITRTFSLIIRLFGNIMSGVFIIGII 177
Cdd:MTH00174 117 TVHMVITLGLSFAIIVGTTLAGLITFRFNFFsiLMPQGAPLALAPLLTIIETlsyISRAISLGVRLAANISSGHLLFSII 196

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 182635574 178 LSLA----------GLLVPIPLM----ALDLLTGAIQAYIFAILACVFI 212
Cdd:MTH00174 197 ASFAwkmintgiliGSFVPFAILifvtILEMAVAIIQAYVFTLLTIVYL 245
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 79-209 4.01e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 43.32  E-value: 4.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  79 LIGTIVLYVLTANWSSLVPGVEPPTAHLETDAALALIVFCATIVYGVRA---QGLAGYLKTFAdpSWVMIP-LNVVEQIT 154
Cdd:MTH00173  74 LLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYnpsKSLAGLVPAGA--PAGLNPfLVLIETVS 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 182635574 155 ---RTFSLIIRLFGNI--------------MSGVFIIGIILSLAGLLVPIPLMALDLLTGAIQAYIFAILAC 209
Cdd:MTH00173 152 iliRPLTLTVRLLANIsaghivltlignylSSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIK 223
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 27-213 6.03e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 42.72  E-value: 6.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  27 AIMLILGIGARLV-TRHLSIPPSRSQAALETVTGAIDSQIKDTMQVDPAPYRALIGTIVLYVLTANWSSLVPGVEPPTAH 105
Cdd:MTH00172  21 SIMMILVIIVVLLlFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTH 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574 106 LETDAALALivfcaTIVYGVRAQGLAGYLKTFAD---PS---WVMIPLNV----VEQITRTFSLIIRLFGNIMSGVFIIG 175
Cdd:MTH00172 101 IVVTLGLSF-----SIIIGVTLAGFWRFKWDFFSilmPSgapLGLAPLLVlietVSYISRAISLGVRLAANLSAGHLLFA 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 182635574 176 II-------------LSLAGLLVPIPLMALDLLTGAIQAYIFAILACVFIG 213
Cdd:MTH00172 176 ILagfgfnmlcasgfLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLA 226
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 79-207 1.30e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 41.86  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  79 LIGTIVLYVLTANWSSLVPGVEPPTAHLETDAALALIVFCATIVYGVRAQGLA--GYLKTFADPSWVMIPLNVVEQIT-- 154
Cdd:MTH00179  72 LFLSLMLFLLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIalAHLLPEGTPTPLIPMLVWIETISll 151

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 182635574 155 -RTFSLIIRLFGNIM----------SGVFIIGIILSLAGLLVPIPLMALDLL---TGAIQAYIFAIL 207
Cdd:MTH00179 152 iRPLALGVRLTANITaghllmhlisSAVFVLMNFMGMVALLTLLVLFLLTLLevaVAMIQAYVFVLL 218
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 28-217 2.27e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 41.15  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574  28 IMLILGIGARLVtrhlsipPSRSQAALETVTGAIDSQIKDTMQVDPAPYRALIGTIVLYVLTANWSSLVPGVEPPTAHLE 107
Cdd:MTH00175  41 IFWLLLKGDKLI-------PNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHII 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574 108 TDAALALIVFCATIVYGVRAQGLaGYLKTFAdPSWV-------MIPLNVVEQITRTFSLIIRLFGNIMSGVFIIGII--- 177
Cdd:MTH00175 114 ITFGLSLSIIIAVTLLGFLTFKW-NFLSILM-PGGAplvlapfLVLIETLSYLIRAISLGVRLAANISAGHLLFAILsgf 191

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 182635574 178 -----------LSLAGLLVPIPLMALDLLTGAIQAYIFAILACVFIGAAVS 217
Cdd:MTH00175 192 afnmlsngliiLSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGDTIA 242
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 143-213 2.31e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 41.41  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574 143 VMIPLN-VVEQITRTFSLIIRLFGNIMSGVFII-----GIILSLAGLLVPIPLMA------LDLLTGAIQAYIFAILACV 210
Cdd:PRK13417 264 IMWPLEfIVSPMAKTFALTVRLLANMTAGHVIIlalmgFIFQFQSWGIVPVSVIGsgliyvLEIFVAFLQAYIFVLLTSL 343


                 ...
gi 182635574 211 FIG 213
Cdd:PRK13417 344 FVG 346
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 133-211 3.65e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 40.35  E-value: 3.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182635574 133 YLKTFadpswVMIPLNVVEQITRTFSLIIRLFGNIMSGVFIIGIILSLAGLLVPIPLMAL--DLLTGAIQAYIFAILACV 210
Cdd:MTH00087 117 FLKTF-----SMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLLNFLGEKYVWLSILAImmECFVAFIQSYIFSRLIYL 191


                 .
gi 182635574 211 F 211
Cdd:MTH00087 192 Y 192
 
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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