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Conserved domains on  [gi|44921849|gb|AAS49295|]
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ATPase 6, partial (mitochondrion) [Rhadinocentrus ornatus]

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 ...
 2-113 5.29e-46

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: 147.71  E-value: 5.29e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44921849    2 MTLGLFDQFMSPMLLGIPLILIALSLPWILFPQPTAHWLDDRLLALQGHFVNNFTHQILQSVSPKGHKWAVLFMTLMLLL 81
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 44921849   82 VTLNTLGLLPYTFTPTTQLSLNMALAAPLWLA 113
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLA 112
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 2-113 5.29e-46

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 147.71  E-value: 5.29e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44921849    2 MTLGLFDQFMSPMLLGIPLILIALSLPWILFPQPTAHWLDDRLLALQGHFVNNFTHQILQSVSPKGHKWAVLFMTLMLLL 81
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 44921849   82 VTLNTLGLLPYTFTPTTQLSLNMALAAPLWLA 113
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLA 112
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 6-113 1.87e-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: 44.50  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44921849     6 LFDQFMSP----MLLGIPLILIALSLPWILFPQ-PTAHWLDDRLLALQGHFVNNFTHQILQSVSPKGHKWAVLFMTLMLL 80
Cdd:TIGR01131   1 LFSQFDISpitlFSLTLLSLILLLSLLIFLISSsLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 44921849    81 LVTLNTLGLLPYTFTPTTQLSLNMALAAPLWLA 113
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLG 113
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 2-113 5.29e-46

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 147.71  E-value: 5.29e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44921849    2 MTLGLFDQFMSPMLLGIPLILIALSLPWILFPQPTAHWLDDRLLALQGHFVNNFTHQILQSVSPKGHKWAVLFMTLMLLL 81
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 44921849   82 VTLNTLGLLPYTFTPTTQLSLNMALAAPLWLA 113
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLA 112
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 2-113 3.38e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 127.78  E-value: 3.38e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44921849    2 MTLGLFDQFMSPMLLGIPLILIALSLPWILFPQPTAHWLDDRLLALQGHFVNNFTHQILQSVSPKGHKWAVLFMTLMLLL 81
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 44921849   82 VTLNTLGLLPYTFTPTTQLSLNMALAAPLWLA 113
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLA 112
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 2-113 4.13e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 112.23  E-value: 4.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44921849    2 MTLGLFDQFMSPMLLGIPLILIALSLPWILFPQPTAHWLDDRLLALQGHFVNNFTHQILQSVSPKGHKWAVLFMTLMLLL 81
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 44921849   82 VTLNTLGLLPYTFTPTTQLSLNMALAAPLWLA 113
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLA 112
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 2-113 4.14e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 99.25  E-value: 4.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44921849    2 MTLGLFDQFMSPMLLGIPLILIALSLPWILFPQPTAHWLDDRLLALQGHFVNNFTHQILQSVSPKGHKWAVLFMTLMLLL 81
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 44921849   82 VTLNTLGLLPYTFTPTTQLSLNMALAAPLWLA 113
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLG 112
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 2-113 6.08e-18

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 75.37  E-value: 6.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44921849    2 MTLGLFDQFMSPMLLGIPLILIALSLPWILFPQPTaHWLDDRLLALQGHFVNNFTHQILQSVSPKGHKWAVLFMTLMLLL 81
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPN-RLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 44921849   82 VTLNTLGLLPYTFTPTTQLSLNMALAAPLWLA 113
Cdd:MTH00101  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAG 111
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-113 8.07e-11

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 56.52  E-value: 8.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44921849    1 MMTLGLFDQFMSPMLLGIPLILIALS--LPWILFPQPTaHWLDDRLLALQGHFVNNFTHQILQSVSPKGHKWAVLFMTLM 78
Cdd:MTH00035   2 IINNSIFGQFSPDTILFIPLTLLSSViaLSWLFFINPT-NWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVF 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 44921849   79 LLLVTLNTLGLLPYTFTPTTQLSLNMALAAPLWLA 113
Cdd:MTH00035  81 ILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMS 115
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 6-113 1.87e-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: 44.50  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44921849     6 LFDQFMSP----MLLGIPLILIALSLPWILFPQ-PTAHWLDDRLLALQGHFVNNFTHQILQSVSPKGHKWAVLFMTLMLL 80
Cdd:TIGR01131   1 LFSQFDISpitlFSLTLLSLILLLSLLIFLISSsLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 44921849    81 LVTLNTLGLLPYTFTPTTQLSLNMALAAPLWLA 113
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLG 113
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 2-113 4.10e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 40.79  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44921849    2 MTLGLFDQFMSPMLLGIPLILIALSLPWI-LFPQPTAHWL-DDRLLALQGHFVNNFTHQILQSVSPKGHKWAVLFMTLML 79
Cdd:MTH00176   1 MLVDLFSSFDPPNKNIFSMISLSWITLLLfLLLMPSSVWFcPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 44921849   80 LLVTLNTLGLLPYTFTPTTQLSLNMALAAPLWLA 113
Cdd:MTH00176  81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLG 114
 
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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