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Conserved domains on  [gi|91694525|gb|ABE41918|]
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ATP synthase subunit 6, partial (mitochondrion) [Amazona ochrocephala nattereri]

Protein Classification

FoF1 ATP synthase subunit a( domain architecture ID 116)

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

Gene Ontology:  GO:0045263|GO:0015078|GO:0015986
PubMed:  11533110|12370007|30901262

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP-synt_Fo_a_6 super family cl00413
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 1-205 2.52e-89

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.


The actual alignment was detected with superfamily member MTH00132:

Pssm-ID: 469762  Cd Length: 227  Bit Score: 261.73  E-value: 2.52e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525    1 MILTFFDQFSSPYLLGIPLIFLSMLLPPLLLPTPNNRWITNRLSTLQLWLTNMITKQLMTPLNKPGHKWAIILTSLMMLL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   81 LTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 91694525  161 LTANLTAGHLLIQLISTAAITLLPIMPAVSALTVTILFLLTMLEL 205
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEV 205
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-205 2.52e-89

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 261.73  E-value: 2.52e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525    1 MILTFFDQFSSPYLLGIPLIFLSMLLPPLLLPTPNNRWITNRLSTLQLWLTNMITKQLMTPLNKPGHKWAIILTSLMMLL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   81 LTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 91694525  161 LTANLTAGHLLIQLISTAAITLLPIMPAVSALTVTILFLLTMLEL 205
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEV 205
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 6-205 2.10e-35

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: 124.24  E-value: 2.10e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525     6 FDQFSSP--YLLGIPLIFLSMLLPPLLLPTP---NNRWITNRLSTLQLWLTNMITKQLMTPLNKPGHKWAIILTSLMMLL 80
Cdd:TIGR01131   2 FSQFDISpiTLFSLTLLSLILLLSLLIFLISsslSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525    81 LTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVR 160
Cdd:TIGR01131  82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 91694525   161 LTANLTAGHLLIQLISTAAITLlpIMPAVSALTVTILFLLTMLEL 205
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLLFSL--MSSAIFALLLLILVALIILEI 204
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 90-205 3.28e-26

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: 98.24  E-value: 3.28e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525  90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVRLTANLTAGH 169
Cdd:cd00310  25 PYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGH 104

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 91694525 170 LLIQLISTAAITLLPImpaVSALTVTILFLLTMLEL 205
Cdd:cd00310 105 LLLALLSGLVPSLLSS---VGLLPLLLPVALTLLEL 137
ATP-synt_A pfam00119
ATP synthase A chain;
90-205 1.36e-22

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 90.63  E-value: 1.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525    90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTS-LGHLLPEGTPTPLIPALILIETISLFIRPLALGVRLTANLTAG 168
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 91694525   169 HLLIQLISTAAITLLPIMPAVSALTVTILFLLTMLEL 205
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFEL 197
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 90-205 9.20e-13

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: 64.32  E-value: 9.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525  90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTS-LGHLLPEGTPtPLIPALILIETISLFIRPLALGVRLTANLTAG 168
Cdd:COG0356  78 PGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAG 156

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 91694525 169 HLLIqlistAAITLLPIMPAVSALTVTILFLLTMLEL 205
Cdd:COG0356 157 HIIL-----LLLAGLAPFLLLGVLSLLLPVAWTAFEL 188
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-205 2.52e-89

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 261.73  E-value: 2.52e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525    1 MILTFFDQFSSPYLLGIPLIFLSMLLPPLLLPTPNNRWITNRLSTLQLWLTNMITKQLMTPLNKPGHKWAIILTSLMMLL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   81 LTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 91694525  161 LTANLTAGHLLIQLISTAAITLLPIMPAVSALTVTILFLLTMLEL 205
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEV 205
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-205 3.23e-88

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 258.99  E-value: 3.23e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525    1 MILTFFDQFSSPYLLGIPLIFLSMLLPPLLLPTPNNRWITNRLSTLQLWLTNMITKQLMTPLNKPGHKWAIILTSLMMLL 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   81 LTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 91694525  161 LTANLTAGHLLIQLISTAAITLLPIMPAVSALTVTILFLLTMLEL 205
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILEL 205
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-205 6.35e-86

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 252.97  E-value: 6.35e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525    1 MILTFFDQFSSPYLLGIPLIFLSMLLPPLLLPTPNNRWITNRLSTLQLWLTNMITKQLMTPLNKPGHKWAIILTSLMMLL 80
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   81 LTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVR 160
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 91694525  161 LTANLTAGHLLIQLISTAAITLLPIMPAVSALTVTILFLLTMLEL 205
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEI 205
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-205 5.81e-68

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 207.49  E-value: 5.81e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525    1 MILTFFDQFSSPYLLGIPLIFLSMLLPPLLLPTPNNRWITNRLSTLQLWLTNMITKQLMTPLNKPGHKWAIILTSLMMLL 80
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   81 LTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVR 160
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 91694525  161 LTANLTAGHLLIQLISTAAITLLPIMPAVSALTVTILFLLTMLEL 205
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEV 205
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 6-205 4.02e-60

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 187.47  E-value: 4.02e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525    6 FDQFSSPYLLGIPLIFLSMLLPPLLLPTPNnRWITNRLSTLQLWLTNMITKQLMTPLNKPGHKWAIILTSLMMLLLTINL 85
Cdd:MTH00101   6 FASFITPTILGLPIVTLIIMFPSLLFPTPN-RLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIGSTNL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   86 LGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVRLTANL 165
Cdd:MTH00101  85 LGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANI 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 91694525  166 TAGHLLIQLISTAAITLLPIMPAVSALTVTILFLLTMLEL 205
Cdd:MTH00101 165 TAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEF 204
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 6-205 2.10e-35

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: 124.24  E-value: 2.10e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525     6 FDQFSSP--YLLGIPLIFLSMLLPPLLLPTP---NNRWITNRLSTLQLWLTNMITKQLMTPLNKPGHKWAIILTSLMMLL 80
Cdd:TIGR01131   2 FSQFDISpiTLFSLTLLSLILLLSLLIFLISsslSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525    81 LTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVR 160
Cdd:TIGR01131  82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 91694525   161 LTANLTAGHLLIQLISTAAITLlpIMPAVSALTVTILFLLTMLEL 205
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLLFSL--MSSAIFALLLLILVALIILEI 204
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 6-204 1.13e-34

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 122.39  E-value: 1.13e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525    6 FDQFSSPYLLGIPLIFLSMLLPPL-LLPTPNNRWITNRLSTLQLWLTNMITKQLMTPLNKPGHKWAIILTSLMMLLLTIN 84
Cdd:MTH00035   8 FGQFSPDTILFIPLTLLSSVIALSwLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILILSIN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   85 LLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVRLTAN 164
Cdd:MTH00035  88 VLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRLAAN 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 91694525  165 LTAGHLLIQLISTaAITLLPIMPAVSALTVTILFLLTMLE 204
Cdd:MTH00035 168 LTAGHLLIFLLST-AIWELSNSPLISIITLIIFFLLFILE 206
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 90-200 1.52e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 106.41  E-value: 1.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVRLTANLTAGH 169
Cdd:MTH00157  89 PYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGH 168

                         90       100       110
                 ....*....|....*....|....*....|.
gi 91694525  170 LLIQLISTAAITLLPIMPAVSALTVTILFLL 200
Cdd:MTH00157 169 LLLTLLGNTGPSLSSMILSILILIQILLLIL 199
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-205 1.57e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 101.26  E-value: 1.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525    1 MILTFFDQFSSPYLLGIPLIFLS-MLLPPLLLPTPNNRWIT-NRLSTLQLWLTNMITKQLMTPLNKPGHKWAIILTSLMM 78
Cdd:MTH00176   1 MLVDLFSSFDPPNKNIFSMISLSwITLLLFLLLMPSSVWFCpSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   79 LLLTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALG 158
Cdd:MTH00176  81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 91694525  159 VRLTANLTAGHLLIQLISTAAITLLPIMPAVSALTVTILFLLTMLEL 205
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEI 207
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 90-205 3.28e-26

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: 98.24  E-value: 3.28e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525  90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVRLTANLTAGH 169
Cdd:cd00310  25 PYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGH 104

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 91694525 170 LLIQLISTAAITLLPImpaVSALTVTILFLLTMLEL 205
Cdd:cd00310 105 LLLALLSGLVPSLLSS---VGLLPLLLPVALTLLEL 137
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 2-205 2.99e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 95.32  E-value: 2.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525    2 ILTFFDQFSSPYLLGIPLIFLSMLLPPLLLPTPNnRWITNRLSTLQLWLTNMITKQLMTPLNKPGHKWAIILTSLMMLLL 81
Cdd:MTH00173   5 LFSSFDDHNSSFSSLSFLMWLLSLMSLFFFSSSV-WVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   82 TINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVRL 161
Cdd:MTH00173  84 SLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRL 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 91694525  162 TANLTAGHLLIQLISTAAITLLPIMPAVSALTVTILFLL-TMLEL 205
Cdd:MTH00173 164 LANISAGHIVLTLIGNYLSSSLFSSSVVSLLLVLLIQVGyFIFEV 208
ATP-synt_A pfam00119
ATP synthase A chain;
90-205 1.36e-22

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 90.63  E-value: 1.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525    90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTS-LGHLLPEGTPTPLIPALILIETISLFIRPLALGVRLTANLTAG 168
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 91694525   169 HLLIQLISTAAITLLPIMPAVSALTVTILFLLTMLEL 205
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFEL 197
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 2-204 5.84e-20

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 84.01  E-value: 5.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525    2 ILTFFDQFSSPYLLGIPLIFLSMLLPPLLLPTPNNRWIT-NRLSTLQLWLTNMITKQLMTPLNKPGHKWAIILTSLMMLL 80
Cdd:MTH00005   5 IFSSFDPATNSLFNNLSSTAFWAFNFSIILLLSSSFWITpNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   81 LTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVR 160
Cdd:MTH00005  85 ILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFR 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 91694525  161 LTANLTAGHLLIQLISTAAITLLPIMPAVSALTVTILFLLTMLE 204
Cdd:MTH00005 165 LAANMSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFE 208
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 1-205 2.87e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 76.97  E-value: 2.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525    1 MILTFFDQFSSPYLLGIPL-------------IFLSMLLPPLLLPTPNNRWITNRLSTLQLWLTNMITKQLMTPLNKPGH 67
Cdd:MTH00175   1 MLAAYFDQFNIIRLITIQAflgdwlvtftnssMMMVLAVIIFWLLLKGDKLIPNRWQSIMELIYLNIRSVVHDNLGKSGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   68 KWAIILTSLMMLLLTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIET 147
Cdd:MTH00175  81 KYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIET 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 91694525  148 ISLFIRPLALGVRLTANLTAGHLLIQLISTAAITLLPI-MPAVSALTVTILFLLTMLEL 205
Cdd:MTH00175 161 LSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNgLIILSLFPMLIMIFITLLEM 219
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 90-205 2.91e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 77.00  E-value: 2.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVRLTANLTAGH 169
Cdd:MTH00172  92 PYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGH 171

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 91694525  170 LLIQLISTAAITLLPIMPAVSALTVTILFLLTMLEL 205
Cdd:MTH00172 172 LLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEI 207
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 90-205 9.20e-13

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: 64.32  E-value: 9.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525  90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTS-LGHLLPEGTPtPLIPALILIETISLFIRPLALGVRLTANLTAG 168
Cdd:COG0356  78 PGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAG 156

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 91694525 169 HLLIqlistAAITLLPIMPAVSALTVTILFLLTMLEL 205
Cdd:COG0356 157 HIIL-----LLLAGLAPFLLLGVLSLLLPVAWTAFEL 188
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 90-205 1.67e-11

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 61.49  E-value: 1.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVRLTANLTAGH 169
Cdd:MTH00174 111 PYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGH 190

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 91694525  170 LLIQLISTAAITLLPIMPAV-SALTVTILFLLTMLEL 205
Cdd:MTH00174 191 LLFSIIASFAWKMINTGILIgSFVPFAILIFVTILEM 227
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 91-199 5.57e-11

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 59.42  E-value: 5.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   91 YTFTPTTQLSMNMALAFPLWLATLLTGLRNQpttSLGHLLPEGTPTPlIPALILIETISLFIRPLALGVRLTANLTAGHL 170
Cdd:PRK05815  95 LLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGEL 170

                         90       100
                 ....*....|....*....|....*....
gi 91694525  171 LIQLISTAAITLLPIMPAVSALTVTILFL 199
Cdd:PRK05815 171 ILALIALLGGAGLLLALAPLILPVAWTIF 199
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 90-177 1.57e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 49.59  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSlgHLLPEGTPTPLIP-ALILIETISLFIRPLALGVRLTANLTAG 168
Cdd:MTH00087  72 PYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTfSMLFVEIVSELSRPLALTLRLTVNLMVG 149


                 ....*....
gi 91694525  169 HLLIQLIST 177
Cdd:MTH00087 150 HLISSLLNF 158
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 90-172 3.85e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 49.36  E-value: 3.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVRLTANLTAGH 169
Cdd:PRK13419 191 PYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAGH 270


                 ...
gi 91694525  170 LLI 172
Cdd:PRK13419 271 IVI 273
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 94-172 8.85e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 45.27  E-value: 8.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91694525   94 TPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETI-SLFIRPLALGVRLTANLTAGHLLI 172
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 90-168 4.70e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 36.40  E-value: 4.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91694525   90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTTSLGHLLPEGTPTPLIPALILIETISLFIRPLALGVRLTANLTAG 168
Cdd:MTH00050  43 PYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLG 121
 
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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