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Conserved domains on  [gi|164519171|ref|YP_001648882|]
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ATP synthase F0 subunit 6 (mitochondrion) [Xyrauchen texanus]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009577)

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
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-228 2.63e-118

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177190  Cd Length: 227  Bit Score: 336.08  E-value: 2.63e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171   1 MAMSFFDQFREPILPGsTPDCYRNRPTLSTLPPHHPHDELTNRLITIQGWLINRFTSQLMLPLNVGGHKWALLLASLMVF 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLG-IPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  81 LITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGV 160
Cdd:MTH00132  80 LITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164519171 161 RLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 228
Cdd:MTH00132 160 RLTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-228 2.63e-118

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 336.08  E-value: 2.63e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171   1 MAMSFFDQFREPILPGsTPDCYRNRPTLSTLPPHHPHDELTNRLITIQGWLINRFTSQLMLPLNVGGHKWALLLASLMVF 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLG-IPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  81 LITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGV 160
Cdd:MTH00132  80 LITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164519171 161 RLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 228
Cdd:MTH00132 160 RLTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 42-228 7.18e-48

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: 156.98  E-value: 7.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171   42 NRLITIQGWLINRFTSQLMLPLNVGGHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRN 121
Cdd:TIGR01131  42 SRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRK 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  122 QPTIALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLlpMMPTVAILTAAVLFLL 201
Cdd:TIGR01131 122 HPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSL--MSSAIFALLLLILVAL 199

                         170       180
                  ....*....|....*....|....*..
gi 164519171  202 TLLEVAVAMIQAYVFVLLLSLYLQENV 228
Cdd:TIGR01131 200 IILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 67-225 2.72e-40

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: 135.22  E-value: 2.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  67 GHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIALGHLLPEGTPIPLIPVLIII 146
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164519171 147 ETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMmptVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQ 225
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
66-225 1.69e-34

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 122.21  E-value: 1.69e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171   66 GGHKWALLLASLMVFLITINMLGLL---PYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIA-LGHLLPEGTPIPLIP 141
Cdd:pfam00119  53 KGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  142 VLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLS 221
Cdd:pfam00119 133 LLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTA 212


                  ....
gi 164519171  222 LYLQ 225
Cdd:pfam00119 213 VYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 67-226 7.56e-24

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: 94.37  E-value: 7.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  67 GHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIA-LGHLLPEGTPIPLIPVLII 145
Cdd:COG0356   54 GRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFPWLAPLMLPI 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171 146 iETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLpmmptVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQ 225
Cdd:COG0356  134 -EIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLL-----LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYIS 207


                 .
gi 164519171 226 E 226
Cdd:COG0356  208 L 208
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-228 2.63e-118

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 336.08  E-value: 2.63e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171   1 MAMSFFDQFREPILPGsTPDCYRNRPTLSTLPPHHPHDELTNRLITIQGWLINRFTSQLMLPLNVGGHKWALLLASLMVF 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLG-IPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  81 LITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGV 160
Cdd:MTH00132  80 LITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164519171 161 RLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 228
Cdd:MTH00132 160 RLTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-228 9.59e-104

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 299.19  E-value: 9.59e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171   1 MAMSFFDQFREPILPGsTPDCYRNRPTLSTLPPHHPHDELTNRLITIQGWLINRFTSQLMLPLNVGGHKWALLLASLMVF 80
Cdd:MTH00073   1 MNLSFFDQFLSPTLLG-IPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  81 LITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGV 160
Cdd:MTH00073  80 LITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164519171 161 RLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 228
Cdd:MTH00073 160 RLTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-228 1.10e-95

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 278.63  E-value: 1.10e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171   1 MAMSFFDQFREPILPGsTPDCYRNRPTLSTLPPHHPHDELTNRLITIQGWLINRFTSQLMLPLNVGGHKWALLLASLMVF 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLG-IPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  81 LITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGV 160
Cdd:MTH00120  80 LLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164519171 161 RLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 228
Cdd:MTH00120 160 RLTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-228 7.39e-83

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 246.40  E-value: 7.39e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171   1 MAMSFFDQFREPILPGsTPDCYRNRPTLSTLPPHHPHDELTNRLITIQGWLINRFTSQLMLPLNVGGHKWALLLASLMVF 80
Cdd:MTH00179   1 MMLSMFDQFESPSLLG-IPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  81 LITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGV 160
Cdd:MTH00179  80 LLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164519171 161 RLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 228
Cdd:MTH00179 160 RLTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 40-227 3.20e-69

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 211.73  E-value: 3.20e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  40 LTNRLITIQGWLINRFTSQLMLPLNVGGHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGM 119
Cdd:MTH00101  38 INNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGF 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171 120 RNQPTIALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLF 199
Cdd:MTH00101 118 RNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLALMSISTTTALITFIILI 197

                        170       180
                 ....*....|....*....|....*...
gi 164519171 200 LLTLLEVAVAMIQAYVFVLLLSLYLQEN 227
Cdd:MTH00101 198 LLTILEFAVALIQAYVFTLLVSLYLHDN 225
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 42-228 7.18e-48

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: 156.98  E-value: 7.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171   42 NRLITIQGWLINRFTSQLMLPLNVGGHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRN 121
Cdd:TIGR01131  42 SRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRK 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  122 QPTIALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLlpMMPTVAILTAAVLFLL 201
Cdd:TIGR01131 122 HPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSL--MSSAIFALLLLILVAL 199

                         170       180
                  ....*....|....*....|....*..
gi 164519171  202 TLLEVAVAMIQAYVFVLLLSLYLQENV 228
Cdd:TIGR01131 200 IILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 64-228 4.82e-43

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 144.73  E-value: 4.82e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  64 NVGGHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIALGHLLPEGTPIPLIPVL 143
Cdd:MTH00035  66 NPNTAPWAGLLTTVFILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLM 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171 144 IIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPmMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLY 223
Cdd:MTH00035 146 VWIETLSLFAQPIALGLRLAANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFY 224


                 ....*
gi 164519171 224 LQENV 228
Cdd:MTH00035 225 LEQNI 229
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 67-225 2.72e-40

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: 135.22  E-value: 2.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  67 GHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIALGHLLPEGTPIPLIPVLIII 146
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164519171 147 ETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMmptVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQ 225
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 72-226 3.00e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 137.22  E-value: 3.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  72 LLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIALGHLLPEGTPIPLIPVLIIIETISL 151
Cdd:MTH00157  70 LIFISLFSFILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISN 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164519171 152 FIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTaavLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 226
Cdd:MTH00157 150 LIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSSMILSILILI---QILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 70-227 2.93e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 132.46  E-value: 2.93e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  70 WALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIALGHLLPEGTPIPLIPVLIIIETI 149
Cdd:MTH00176  71 SASIIISLFILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELV 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164519171 150 SLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 227
Cdd:MTH00176 151 SLLIRPLTLAVRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 41-226 1.62e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 125.36  E-value: 1.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  41 TNRLITIQGWLINRFTSQLMLPLNVGGHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMR 120
Cdd:MTH00173  42 SSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLF 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171 121 NQPTIALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAV-FVLLPMMPTVAILTAAVLF 199
Cdd:MTH00173 122 YNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYLsSSLFSSSVVSLLLVLLIQV 201

                        170       180
                 ....*....|....*....|....*..
gi 164519171 200 LLTLLEVAVAMIQAYVFVLLLSLYLQE 226
Cdd:MTH00173 202 GYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_A pfam00119
ATP synthase A chain;
66-225 1.69e-34

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 122.21  E-value: 1.69e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171   66 GGHKWALLLASLMVFLITINMLGLL---PYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIA-LGHLLPEGTPIPLIP 141
Cdd:pfam00119  53 KGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  142 VLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLS 221
Cdd:pfam00119 133 LLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTA 212


                  ....
gi 164519171  222 LYLQ 225
Cdd:pfam00119 213 VYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 42-224 1.34e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 112.83  E-value: 1.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  42 NRLITIQGWLINRFTSQLMLPLNVGGHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRN 121
Cdd:MTH00172  43 KRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWR 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171 122 QPTIALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLL 201
Cdd:MTH00172 123 FKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFI 202

                        170       180
                 ....*....|....*....|...
gi 164519171 202 TLLEVAVAMIQAYVFVLLLSLYL 224
Cdd:MTH00172 203 TLLEIAVAVIQAYVFCLLTTIYL 225
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 42-223 2.46e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 106.74  E-value: 2.46e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  42 NRLITIQGWLINRFTSQLMLPLNVGGHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRN 121
Cdd:MTH00005  45 NRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTF 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171 122 QPTIALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLL 201
Cdd:MTH00005 125 SPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGIYAASALFSSISSTILLILTQMGY 204

                        170       180
                 ....*....|....*....|..
gi 164519171 202 TLLEVAVAMIQAYVFVLLLSLY 223
Cdd:MTH00005 205 ILFEVGICLIQAYIFCLLLSLY 226
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 63-228 5.81e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 100.85  E-value: 5.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  63 LNVGGHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIALGHLLPEGTPIPLIPV 142
Cdd:MTH00175  75 LGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPF 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171 143 LIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPM-MPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLS 221
Cdd:MTH00175 155 LVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNgLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTT 234


                 ....*..
gi 164519171 222 LYLQENV 228
Cdd:MTH00175 235 IYLGDTI 241
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 67-226 7.56e-24

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: 94.37  E-value: 7.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  67 GHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIA-LGHLLPEGTPIPLIPVLII 145
Cdd:COG0356   54 GRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFPWLAPLMLPI 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171 146 iETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLpmmptVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQ 225
Cdd:COG0356  134 -EIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLL-----LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYIS 207


                 .
gi 164519171 226 E 226
Cdd:COG0356  208 L 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 67-226 3.79e-21

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 87.54  E-value: 3.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  67 GHKWALLLASLMVFLITINMLGLLP-YTFTPTTQLSLNMGFAVPLWLATVIIGMRNQptiALGHLLPEGTPIPLIPVLII 145
Cdd:PRK05815  69 GKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQPHPLLLPI 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171 146 iETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAvlflLTLLEVAVAMIQAYVFVLLLSLYLQ 225
Cdd:PRK05815 146 -EIISEFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILPVA----WTIFEIFVGTLQAYIFMMLTIVYIS 220


                 .
gi 164519171 226 E 226
Cdd:PRK05815 221 M 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 42-228 2.69e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 80.75  E-value: 2.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  42 NRLITIQGWLINRFTSQLMLPLNVGGHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRN 121
Cdd:MTH00174  62 NRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLIT 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171 122 QPTIALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMMPTV-AILTAAVLFL 200
Cdd:MTH00174 142 FRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPFAILIF 221

                        170       180
                 ....*....|....*....|....*...
gi 164519171 201 LTLLEVAVAMIQAYVFVLLLSLYLQENV 228
Cdd:MTH00174 222 VTILEMAVAIIQAYVFTLLTIVYLRDTV 249
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 74-224 2.47e-14

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 70.93  E-value: 2.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  74 LASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIALGHLLPEGTPIPLIPVLIIIETISLFI 153
Cdd:PRK13419 174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGTHWSLWIIMIPIEFIGLFT 253

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164519171 154 RPLALGVRLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLtLLEVAVAMIQAYVFVLLLSLYL 224
Cdd:PRK13419 254 KPFALTVRLFANMTAGHIVILSLIFISFILKSYIVAVAVSVPFAIFIY-LLELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 76-226 1.90e-12

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 63.46  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  76 SLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQptIALGHLLP-EGTPIPLIPVLIIIETISLFIR 154
Cdd:MTH00087  57 FTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKS--EKFSVYLSkGSDSFLKTFSMLFVEIVSELSR 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164519171 155 PLALGVRLTANLTAGHLLIQLIATAVFVLLPMMptvailtaavlFLLTLLEVAVAMIQAYVFVLLLSLYLQE 226
Cdd:MTH00087 135 PLALTLRLTVNLMVGHLISSLLNFLGEKYVWLS-----------ILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 95-224 4.91e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 49.50  E-value: 4.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  95 TPTTQLSLNMGFAVPLWLATVIIGMRNQPTIALGHLLPEGTPIPLIPVLIIIETI-SLFIRPLALGVRLTANLTAGHLLI 173
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 164519171 174 qlIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYL 224
Cdd:PRK13417 297 --LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 73-224 1.08e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 38.96  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164519171  73 LLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTIA-LGHLLpegtpiPLIPVLIIIETISL 151
Cdd:PRK13420  77 FVGTLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEGLREyLKHYL------SPSPFLLPFHLISE 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164519171 152 FIRPLALGVRLTANLTAghllIQLIATAVFVLLPMMPTVAILtaavlflltLLEVAVAMIQAYVFVLLLSLYL 224
Cdd:PRK13420 151 ITRTLALAVRLFGNIMS----LELAALLVLLVAGFLVPVPIL---------MLHIIEALVQAYIFGMLALIYI 210
 
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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