NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|211998747|gb|ACJ15307|]
View 

ATPase subunit 6, partial (mitochondrion) [Moho bishopi]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 6-51 1.40e-23

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 MTH00120:

Pssm-ID: 469762  Cd Length: 227  Bit Score: 87.57  E-value: 1.40e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 211998747   6 LRNQPSTSLGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:MTH00120 118 LRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVRLTA 163
 
Name Accession Description Interval E-value
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 6-51 1.40e-23

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 87.57  E-value: 1.40e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 211998747   6 LRNQPSTSLGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:MTH00120 118 LRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVRLTA 163
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 6-51 3.07e-14

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: 62.99  E-value: 3.07e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 211998747    6 LRNQPSTSLGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:TIGR01131 119 FRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFA 164
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 6-51 3.14e-11

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: 53.94  E-value: 3.14e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 211998747   6 LRNQPSTSLGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:cd00310   53 IKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFA 98
ATP-synt_A pfam00119
ATP synthase A chain;
14-51 3.29e-07

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 44.02  E-value: 3.29e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 211998747   14 LGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:pfam00119 118 FKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFG 155
 
Name Accession Description Interval E-value
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 6-51 1.40e-23

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 87.57  E-value: 1.40e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 211998747   6 LRNQPSTSLGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:MTH00120 118 LRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVRLTA 163
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 6-51 1.67e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 81.94  E-value: 1.67e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 211998747   6 LRNQPSTSLGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:MTH00073 118 LRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVRLTA 163
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 6-51 1.80e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 81.84  E-value: 1.80e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 211998747   6 LRNQPSTSLGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:MTH00132 118 MRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTA 163
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 6-51 2.10e-19

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 76.53  E-value: 2.10e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 211998747   6 LRNQPSTSLGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:MTH00179 118 LFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVRLTA 163
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 6-51 8.74e-17

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 69.60  E-value: 8.74e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 211998747   6 LRNQPSTSLGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:MTH00101 117 FRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTA 162
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 10-51 6.46e-15

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 64.89  E-value: 6.46e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 211998747  10 PSTSLGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:MTH00173 124 PSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLA 165
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 8-51 2.29e-14

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 63.26  E-value: 2.29e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 211998747   8 NQPSTSLGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:MTH00157 119 NNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAA 162
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 6-51 3.07e-14

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: 62.99  E-value: 3.07e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 211998747    6 LRNQPSTSLGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:TIGR01131 119 FRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFA 164
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 14-51 9.08e-12

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 56.52  E-value: 9.08e-12
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 211998747  14 LGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:MTH00035 129 LSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRLAA 166
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 6-51 3.14e-11

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: 53.94  E-value: 3.14e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 211998747   6 LRNQPSTSLGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:cd00310   53 IKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFA 98
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 6-51 5.79e-11

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 54.27  E-value: 5.79e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 211998747   6 LRNQPSTSLGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:MTH00176 120 FINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLAVRLAA 165
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 8-51 1.86e-09

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 50.12  E-value: 1.86e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 211998747   8 NQPSTSLGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:MTH00005 124 FSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAA 167
ATP-synt_A pfam00119
ATP synthase A chain;
14-51 3.29e-07

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 44.02  E-value: 3.29e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 211998747   14 LGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:pfam00119 118 FKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFG 155
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 17-51 1.01e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 42.72  E-value: 1.01e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 211998747  17 LLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:MTH00172 131 LMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAA 165
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 14-51 1.07e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 42.69  E-value: 1.07e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 211998747  14 LGHLLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:MTH00175 139 LSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAA 176
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 17-51 2.84e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 36.07  E-value: 2.84e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 211998747  17 LLPEGTPTPLIPALILIETTSLLIRPVALGVRLTA 51
Cdd:MTH00174 150 LMPQGAPLALAPLLTIIETLSYISRAISLGVRLAA 184
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 14-50 1.34e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 33.80  E-value: 1.34e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 211998747  14 LGHLLPEGTPTPLIP-ALILIETTSLLIRPVALGVRLT 50
Cdd:MTH00087 106 FSVYLSKGSDSFLKTfSMLFVEIVSELSRPLALTLRLT 143
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 17-48 4.58e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 32.16  E-value: 4.58e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 211998747  17 LLPEGTPTPLIPALILIETTSLLIRPVALGVR 48
Cdd:MTH00050  82 FVPVGTPLYICPFVCIAETISYIIRPVVLILR 113
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 14-49 8.14e-03

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 31.69  E-value: 8.14e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 211998747  14 LGHLLPEGTPTPlIPALILIETTSLLIRPVALGVRL 49
Cdd:PRK05815 127 LGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRL 161
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH