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Conserved domains on  [gi|1294136449|gb|AUB13408|]
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ATPase 6, partial (mitochondrion) [Drosophila melanogaster]

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 ...
 1-49 8.19e-17

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 MTH00157:

Pssm-ID: 469762  Cd Length: 223  Bit Score: 69.43  E-value: 8.19e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1294136449   1 GNTGPSMSYMLVTFLLMAQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 49
Cdd:MTH00157  175 GNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-49 8.19e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 69.43  E-value: 8.19e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1294136449   1 GNTGPSMSYMLVTFLLMAQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 49
Cdd:MTH00157  175 GNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 6-49 1.62e-06

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: 41.81  E-value: 1.62e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1294136449   6 SMSYMLVTFLLMAQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 49
Cdd:TIGR01131 183 LMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_A pfam00119
ATP synthase A chain;
6-46 2.17e-03

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 33.23  E-value: 2.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1294136449   6 SMSYMLVTFLLMAQIALLVLESAVAMIQSYVFAVLSTLYSS 46
Cdd:pfam00119 176 SAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-49 8.19e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 69.43  E-value: 8.19e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1294136449   1 GNTGPSMSYMLVTFLLMAQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 49
Cdd:MTH00157  175 GNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 6-49 1.62e-06

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: 41.81  E-value: 1.62e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1294136449   6 SMSYMLVTFLLMAQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 49
Cdd:TIGR01131 183 LMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 6-48 1.37e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 39.25  E-value: 1.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1294136449   6 SMSYMLVTFLLMAQIALLVLESAVAMIQSYVFAVLSTLYSSEV 48
Cdd:MTH00176  186 PVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 2-47 1.00e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 37.11  E-value: 1.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1294136449   2 NTGPSMSYMLVTFLLMaqiaLLVLESAVAMIQSYVFAVLSTLYSSE 47
Cdd:MTH00120  184 PTMPTLSLLTLIILLL----LTILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 6-44 1.33e-04

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 36.47  E-value: 1.33e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1294136449   6 SMSYMLVTFLLMaqIALLVLESAVAMIQSYVFAVLSTLY 44
Cdd:MTH00101  185 STTTALITFIIL--ILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 6-47 8.49e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 34.54  E-value: 8.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1294136449   6 SMSYMLVTFLLMAQIALLVLESAVAMIQSYVFAVLSTLYSSE 47
Cdd:MTH00179  184 NFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 5-47 1.05e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 34.08  E-value: 1.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1294136449   5 PSMSYMLVTFLLMaqiaLLVLESAVAMIQSYVFAVLSTLYSSE 47
Cdd:MTH00132  187 PTVAILTATLLFL----LTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 6-47 1.06e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 34.17  E-value: 1.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1294136449   6 SMSYMLVTFLLMAQIALLVLESAVAMIQSYVFAVLSTLYSSE 47
Cdd:MTH00073  184 PLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP-synt_A pfam00119
ATP synthase A chain;
6-46 2.17e-03

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 33.23  E-value: 2.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1294136449   6 SMSYMLVTFLLMAQIALLVLESAVAMIQSYVFAVLSTLYSS 46
Cdd:pfam00119 176 SAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 8-47 8.81e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 31.48  E-value: 8.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1294136449   8 SYMLVTFLLMAQIALLVLESAVAMIQSYVFAVLSTLYSSE 47
Cdd:MTH00035  188 SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
 
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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