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Conserved domains on  [gi|1707765467|gb|QDP18047|]
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ATP synthase F0 subunit 6, partial (mitochondrion) [Poekilocerus bufonius]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009593)

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 MTH00157
ATP synthase F0 subunit 6; Provisional
1-128 2.37e-60

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 184.60  E-value: 2.37e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLG 80
Cdd:MTH00157   96 SHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLG 175
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1707765467  81 NTGPMINLNLITILIISQMLLMMLESAVALIQAYVFSILSTLYSSETY 128
Cdd:MTH00157  176 NTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-128 2.37e-60

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 184.60  E-value: 2.37e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLG 80
Cdd:MTH00157   96 SHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLG 175
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1707765467  81 NTGPMINLNLITILIISQMLLMMLESAVALIQAYVFSILSTLYSSETY 128
Cdd:MTH00157  176 NTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
1-125 1.47e-33

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: 114.42  E-value: 1.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLG 80
Cdd:cd00310    32 SHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGHLLLALLS 111
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1707765467  81 NTGPMINLNLITILIISQMLLMMLESAVALIQAYVFSILSTLYSS 125
Cdd:cd00310   112 GLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
1-126 1.53e-32

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: 113.84  E-value: 1.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLG 80
Cdd:TIGR01131  98 SHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLS 177
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1707765467  81 NTGP-MINLNLITILIISQMLLMMLESAVALIQAYVFSILSTLYSSE 126
Cdd:TIGR01131 178 GLLFsLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP-synt_A pfam00119
ATP synthase A chain;
1-125 1.34e-18

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 77.53  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFGWINN-TKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLL 79
Cdd:pfam00119  88 ADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLL 167
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1707765467  80 GNTGPMINLNLITILIIS---QMLLMMLESAVALIQAYVFSILSTLYSS 125
Cdd:pfam00119 168 AGLIFALLSAGFLLGVIPpllGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
1-123 5.14e-14

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: 65.48  E-value: 5.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFG-WINNTKHMLAHLVPQGTPPMlMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLL 79
Cdd:COG0356    85 ADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFPWL-APLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLL 163
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1707765467  80 GNTGPMINLNLITILIisQMLLMMLESAVALIQAYVFSILSTLY 123
Cdd:COG0356   164 AGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-128 2.37e-60

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 184.60  E-value: 2.37e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLG 80
Cdd:MTH00157   96 SHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLG 175
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1707765467  81 NTGPMINLNLITILIISQMLLMMLESAVALIQAYVFSILSTLYSSETY 128
Cdd:MTH00157  176 NTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
1-125 1.47e-33

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: 114.42  E-value: 1.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLG 80
Cdd:cd00310    32 SHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGHLLLALLS 111
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1707765467  81 NTGPMINLNLITILIISQMLLMMLESAVALIQAYVFSILSTLYSS 125
Cdd:cd00310   112 GLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
1-128 5.27e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 115.13  E-value: 5.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLG 80
Cdd:MTH00176   99 SHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLAVRLAANLSAGHLLLGLLG 178
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1707765467  81 NTGP---MINLNLITILIISQMLLMMLESAVALIQAYVFSILSTLYSSETY 128
Cdd:MTH00176  179 AAMWgllPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
1-126 1.53e-32

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: 113.84  E-value: 1.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLG 80
Cdd:TIGR01131  98 SHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLS 177
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1707765467  81 NTGP-MINLNLITILIISQMLLMMLESAVALIQAYVFSILSTLYSSE 126
Cdd:TIGR01131 178 GLLFsLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
1-126 6.37e-28

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 101.97  E-value: 6.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLG 80
Cdd:MTH00035  100 SHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRLAANLTAGHLLIFLLS 179
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1707765467  81 NT-GPMINLNLI-TILIISQMLLMMLESAVALIQAYVFSILSTLYSSE 126
Cdd:MTH00035  180 TAiWELSNSPLIsIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
1-127 5.02e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 94.55  E-value: 5.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLG 80
Cdd:MTH00173   99 SHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIG 178
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1707765467  81 N--TGPMINLNLITILIIS--QMLLMMLESAVALIQAYVFSILSTLYSSET 127
Cdd:MTH00173  179 NylSSSLFSSSVVSLLLVLliQVGYFIFEVAVMLIQAYIFTLLIKLYSDEH 229
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
1-126 5.32e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 94.80  E-value: 5.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLG 80
Cdd:MTH00005  101 SHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIG 180
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1707765467  81 NTGPMINLNLI---TILIISQMLLMMLESAVALIQAYVFSILSTLYSSE 126
Cdd:MTH00005  181 IYAASALFSSIsstILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
8-123 3.34e-24

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 92.32  E-value: 3.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   8 SIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLGN-TGPMI 86
Cdd:MTH00101  103 GMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGaTLALM 182
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1707765467  87 NLNLITILI--ISQMLLMMLESAVALIQAYVFSILSTLY 123
Cdd:MTH00101  183 SISTTTALItfIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
8-126 9.32e-23

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 88.73  E-value: 9.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   8 SIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLG------- 80
Cdd:MTH00120  104 ALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVRLTANLTAGHLLIQLIStatlnll 183
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1707765467  81 NTGPMINLNLITILiisqMLLMMLESAVALIQAYVFSILSTLYSSE 126
Cdd:MTH00120  184 PTMPTLSLLTLIIL----LLLTILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
1-126 9.73e-23

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 88.47  E-value: 9.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLG 80
Cdd:MTH00179   97 TQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVRLTANITAGHLLMHLIS 176
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1707765467  81 ----NTGPMINLNLITILIISqMLLMMLESAVALIQAYVFSILSTLYSSE 126
Cdd:MTH00179  177 savfVLMNFMGMVALLTLLVL-FLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
5-126 8.06e-22

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 86.08  E-value: 8.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   5 LTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGP 84
Cdd:MTH00132  101 LNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAAF 180
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1707765467  85 MINLNLITILIISQMLLMM---LESAVALIQAYVFSILSTLYSSE 126
Cdd:MTH00132  181 VLLPLMPTVAILTATLLFLltlLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
5-126 1.07e-19

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 80.78  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   5 LTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGP 84
Cdd:MTH00073  101 LNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVRLTANLTAGHLLIQLISTATL 180
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1707765467  85 MINLNLITILIISQM---LLMMLESAVALIQAYVFSILSTLYSSE 126
Cdd:MTH00073  181 VLLPLMPTVSILTMIvlfLLTLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP-synt_A pfam00119
ATP synthase A chain;
1-125 1.34e-18

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 77.53  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFGWINN-TKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLL 79
Cdd:pfam00119  88 ADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLL 167
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1707765467  80 GNTGPMINLNLITILIIS---QMLLMMLESAVALIQAYVFSILSTLYSS 125
Cdd:pfam00119 168 AGLIFALLSAGFLLGVIPpllGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
2-128 5.22e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 76.58  E-value: 5.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   2 HMVLTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLGN 81
Cdd:MTH00175  111 HIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSG 190
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1707765467  82 TGPMINLNLITILIISQMLLMM----LESAVALIQAYVFSILSTLYSSETY 128
Cdd:MTH00175  191 FAFNMLSNGLIILSLFPMLIMIfitlLEMAVAVIQAYVFCLLTTIYLGDTI 241
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
2-127 6.38e-16

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 70.84  E-value: 6.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   2 HMVLTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLGN 81
Cdd:MTH00172  100 HIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAG 179
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1707765467  82 TG-PMIN----LNLITILIISQMLLmmLESAVALIQAYVFSILSTLYSSET 127
Cdd:MTH00172  180 FGfNMLCasgfLSLFPLLIMVFITL--LEIAVAVIQAYVFCLLTTIYLADT 228
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
1-123 5.14e-14

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: 65.48  E-value: 5.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFG-WINNTKHMLAHLVPQGTPPMlMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLL 79
Cdd:COG0356    85 ADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFPWL-APLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLL 163
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1707765467  80 GNTGPMINLNLITILIisQMLLMMLESAVALIQAYVFSILSTLY 123
Cdd:COG0356   164 AGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
1-123 1.29e-12

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 61.73  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   1 SHMVLTFSIALPMWLSFMLFG-WINNTKHMLAHLVPQGTPpmlmsFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLL 79
Cdd:PRK05815  101 ADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQPHP-----LLLPIEIISEFSRPISLSLRLFGNMLAGELILALI 175
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1707765467  80 GNTGPMINLNLITILIISqMLLMMLESAVALIQAYVFSILSTLY 123
Cdd:PRK05815  176 ALLGGAGLLLALAPLILP-VAWTIFEIFVGTLQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
2-127 6.74e-09

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 51.86  E-value: 6.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   2 HMVLTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLGN 81
Cdd:MTH00174  119 HMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIAS 198
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1707765467  82 TG-PMINLNLITILIISQMLLM---MLESAVALIQAYVFSILSTLYSSET 127
Cdd:MTH00174  199 FAwKMINTGILIGSFVPFAILIfvtILEMAVAIIQAYVFTLLTIVYLRDT 248
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
30-123 2.72e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 50.51  E-value: 2.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467  30 LAHLVpQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHllltllgntgpMINLNLITILIISQ----------- 98
Cdd:PRK13419  228 LAHLT-GGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAGH-----------IVILSLIFISFILKsyivavavsvp 295
                          90       100
                  ....*....|....*....|....*..
gi 1707765467  99 --MLLMMLESAVALIQAYVFSILSTLY 123
Cdd:PRK13419  296 faIFIYLLELFVAFLQAYIFTMLSALF 322
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
5-123 8.80e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 49.12  E-value: 8.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   5 LTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETI-SNLIRPGTLAVRLAANMIAGHLLLT-LLGNT 82
Cdd:PRK13417  224 VTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVIILaLMGFI 303
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1707765467  83 GPMINLNLITILIISQMLLMMLESAVALIQAYVFSILSTLY 123
Cdd:PRK13417  304 FQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
6-126 2.55e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 44.20  E-value: 2.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   6 TFSIALPMWLSFMLFGWINNTKhmLAHLVPQGTPPMLMSF-MVLIETISNLIRPGTLAVRLAANMIAGHLLLTllgntgp 84
Cdd:MTH00087   84 TFLYALVAWLSTFLSFLSKSEK--FSVYLSKGSDSFLKTFsMLFVEIVSELSRPLALTLRLTVNLMVGHLISS------- 154
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1707765467  85 MINLNLITILIISQMLLMMlESAVALIQAYVFSILSTLYSSE 126
Cdd:MTH00087  155 LLNFLGEKYVWLSILAIMM-ECFVAFIQSYIFSRLIYLYLNE 195
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
4-120 1.77e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 36.40  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765467   4 VLTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPPMLMSFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLGNTG 83
Cdd:MTH00050   53 VFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGCFGGVALGNLC 132
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1707765467  84 pMINLNLITILIIsqmlLMMLESAVALIQAY-VFSILS 120
Cdd:MTH00050  133 -FISYWWFLVLFF----LFFYEVFVALVHWFiVSSILS 165
 
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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