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Conserved domains on  [gi|84488642|ref|YP_448834|]
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ATP synthase F0 subunit 6 (mitochondrion) [Indotestudo elongata]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009573)

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 MTH00120
ATP synthase F0 subunit 6; Provisional
1-227 1.76e-92

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177181  Cd Length: 227  Bit Score: 270.54  E-value: 1.76e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642    1 MNLMLFDQFMSPQILGIPLFALALLTPSIMFPTQNSRWLTNRFSTLQLWTINLFTKHLMLPINKTGHKWSIILTSLMTLL 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   81 LMINLLGLLPYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84488642  161 LTANLTAGHLLIQLLSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
 
Name Accession Description Interval E-value
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
1-227 1.76e-92

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 270.54  E-value: 1.76e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642    1 MNLMLFDQFMSPQILGIPLFALALLTPSIMFPTQNSRWLTNRFSTLQLWTINLFTKHLMLPINKTGHKWSIILTSLMTLL 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   81 LMINLLGLLPYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84488642  161 LTANLTAGHLLIQLLSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
5-227 6.07e-37

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: 128.86  E-value: 6.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642     5 LFDQFMSPQ--ILGIPLFALALLTPSIMF---PTQNSRWLTNRFSTLQLWTINLFTKHLMLPINKTGHKWSIILTSLMTL 79
Cdd:TIGR01131   1 LFSQFDISPitLFSLTLLSLILLLSLLIFlisSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642    80 LLMINLLGLLPYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGV 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84488642   160 RLTANLTAGHLLIqlLSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:TIGR01131 161 RLFANISAGHLLL--TLLSGLLFSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
90-224 9.25e-29

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: 105.56  E-value: 9.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642  90 PYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVRLTANLTAGH 169
Cdd:cd00310  25 PYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGH 104
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 84488642 170 LLIqllSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310 105 LLL---ALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
90-224 4.22e-24

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 95.25  E-value: 4.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642    90 PYTFTPTTQLSMNMGLALPMWMATIFTGFRNQ-LTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 84488642   169 HLLIQLLSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
90-225 1.23e-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: 69.72  E-value: 1.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642  90 PYTFTPTTQLSMNMGLALPMWMATIFTGFRNQ-LTTSLGHLLPEGTPtPLTPILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:COG0356  78 PGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAG 156
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 84488642 169 HLLIqllstSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQE 225
Cdd:COG0356 157 HIIL-----LLLAGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
1-227 1.76e-92

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 270.54  E-value: 1.76e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642    1 MNLMLFDQFMSPQILGIPLFALALLTPSIMFPTQNSRWLTNRFSTLQLWTINLFTKHLMLPINKTGHKWSIILTSLMTLL 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   81 LMINLLGLLPYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84488642  161 LTANLTAGHLLIQLLSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-227 2.31e-92

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 270.21  E-value: 2.31e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642    1 MNLMLFDQFMSPQILGIPLFALALLTPSIMFPTQNSRWLTNRFSTLQLWTINLFTKHLMLPINKTGHKWSIILTSLMTLL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   81 LMINLLGLLPYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84488642  161 LTANLTAGHLLIQLLSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
1-227 3.88e-88

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 259.51  E-value: 3.88e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642    1 MNLMLFDQFMSPQILGIPLFALALLTPSIMFPTQNSRWLTNRFSTLQLWTINLFTKHLMLPINKTGHKWSIILTSLMTLL 80
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   81 LMINLLGLLPYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVR 160
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84488642  161 LTANLTAGHLLIQLLSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
1-226 6.02e-70

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 213.27  E-value: 6.02e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642    1 MNLMLFDQFMSPQILGIPLFALALLTPSIMFPTQNSRWLTNRFSTLQLWTINLFTKHLMLPINKTGHKWSIILTSLMTLL 80
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   81 LMINLLGLLPYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVR 160
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84488642  161 LTANLTAGHLLIQLLSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 9.83e-65

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 200.18  E-value: 9.83e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642    1 MNLMLFDQFMSPQILGIPLFALALLTPSIMFPTQNsRWLTNRFSTLQLWTINLFTKHLMLPINKTGHKWSIILTSLMTLL 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPN-RLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   81 LMINLLGLLPYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVR 160
Cdd:MTH00101  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84488642  161 LTANLTAGHLLIQLLSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00101 160 LTANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
5-227 6.07e-37

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: 128.86  E-value: 6.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642     5 LFDQFMSPQ--ILGIPLFALALLTPSIMF---PTQNSRWLTNRFSTLQLWTINLFTKHLMLPINKTGHKWSIILTSLMTL 79
Cdd:TIGR01131   1 LFSQFDISPitLFSLTLLSLILLLSLLIFlisSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642    80 LLMINLLGLLPYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGV 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84488642   160 RLTANLTAGHLLIqlLSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:TIGR01131 161 RLFANISAGHLLL--TLLSGLLFSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
5-227 1.32e-33

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 120.46  E-value: 1.32e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642    5 LFDQFMSPQILGIPL----FALALLTPSIMFPTQnsrWLTNRFSTLQLWTINLFTKHLMLPINKTGHKWSIILTSLMTLL 80
Cdd:MTH00035   7 IFGQFSPDTILFIPLtllsSVIALSWLFFINPTN---WLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   81 LMINLLGLLPYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVR 160
Cdd:MTH00035  84 LSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLR 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84488642  161 LTANLTAGHLLIqLLSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00035 164 LAANLTAGHLLI-FLLSTAIWELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
90-225 1.30e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 112.57  E-value: 1.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   90 PYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVRLTANLTAGH 169
Cdd:MTH00157  89 PYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGH 168
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 84488642  170 LLIQLLSTSVLTLLKTTMTLSiltTMILLLLTILELAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00157 169 LLLTLLGNTGPSLSSMILSIL---ILIQILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
1-226 1.05e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 110.12  E-value: 1.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642    1 MNLMLFDQFMSPQILGIPLFALA---LLTPSIMFPTQNSRWLTNRFSTLQLWTiNLFTKHLMLPINKTGHKWSIILTSLM 77
Cdd:MTH00176   1 MLVDLFSSFDPPNKNIFSMISLSwitLLLFLLLMPSSVWFCPSKLQVFMLMFS-TFLPEMILRSNGSYILGSASIIISLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   78 TLLLMINLLGLLPYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLAL 157
Cdd:MTH00176  80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84488642  158 GVRLTANLTAGHLLIQLLSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00176 160 AVRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
90-224 9.25e-29

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: 105.56  E-value: 9.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642  90 PYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVRLTANLTAGH 169
Cdd:cd00310  25 PYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGH 104
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 84488642 170 LLIqllSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310 105 LLL---ALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
90-225 4.19e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 95.70  E-value: 4.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   90 PYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVRLTANLTAGH 169
Cdd:MTH00173  92 PFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGH 171
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 84488642  170 LLIQLLSTSVLTLLKTTMTLSILTTMILLLLTILE-LAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00173 172 IVLTLIGNYLSSSLFSSSVVSLLLVLLIQVGYFIFeVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_A pfam00119
ATP synthase A chain;
90-224 4.22e-24

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 95.25  E-value: 4.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642    90 PYTFTPTTQLSMNMGLALPMWMATIFTGFRNQ-LTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 84488642   169 HLLIQLLSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
6-222 8.44e-23

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 92.10  E-value: 8.44e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642    6 FDQFMSPQILGIPLFALALLTPSIMFPTQNSRWLT-NRFSTLQLWTINLFTKHLMLPINKTGHKWSIILTSLMTLLLMIN 84
Cdd:MTH00005   9 FDPATNSLFNNLSSTAFWAFNFSIILLLSSSFWITpNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   85 LLGLLPYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVRLTAN 164
Cdd:MTH00005  89 LSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAAN 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 84488642  165 LTAGHLLIQLLSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLY 222
Cdd:MTH00005 169 MSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
90-227 3.29e-22

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 90.87  E-value: 3.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   90 PYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVRLTANLTAGH 169
Cdd:MTH00172  92 PYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGH 171
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 84488642  170 LLIQLLSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00172 172 LLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTI 229
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
90-227 6.05e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 79.67  E-value: 6.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   90 PYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVRLTANLTAGH 169
Cdd:MTH00175 103 PYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGH 182
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 84488642  170 LLIQLLS-TSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00175 183 LLFAILSgFAFNMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGDTI 241
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
90-225 1.23e-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: 69.72  E-value: 1.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642  90 PYTFTPTTQLSMNMGLALPMWMATIFTGFRNQ-LTTSLGHLLPEGTPtPLTPILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:COG0356  78 PGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAG 156
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 84488642 169 HLLIqllstSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQE 225
Cdd:COG0356 157 HIIL-----LLLAGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
91-225 5.76e-14

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 68.28  E-value: 5.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   91 YTFTPTTQLSMNMGLALPMWMATIFTGFRNQlttSLGHLLPEGTPTPlTPILIMIETISLFIRPLALGVRLTANLTAGHL 170
Cdd:PRK05815  95 LLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGEL 170
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 84488642  171 LIqllsTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQE 225
Cdd:PRK05815 171 IL----ALIALLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
90-227 4.76e-13

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 66.12  E-value: 4.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   90 PYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVRLTANLTAGH 169
Cdd:MTH00174 111 PYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGH 190
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 84488642  170 LLIQLLSTSVLTLLKT-TMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00174 191 LLFSIIASFAWKMINTgILIGSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYLRDTV 249
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
90-223 1.81e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 53.59  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   90 PYTFTPTTQLSMNMGLALPMWMATIFTGFRNQ-LTTSLGHLlPEGTPTPLTPILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:PRK13419 191 PYGATATGNINVTLTLAVFTFFITQYAAIKAHgIKGYLAHL-TGGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAG 269
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 84488642  169 HLLIQLLSTSVLTLLKTTMTLSILTTMILLLLTILELaVAMIQAYVFVLLLSLYL 223
Cdd:PRK13419 270 HIVILSLIFISFILKSYIVAVAVSVPFAIFIYLLELF-VAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
90-225 2.41e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 52.29  E-value: 2.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   90 PYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSlgHLLPEGTPTPL-TPILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:MTH00087  72 PYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLkTFSMLFVEIVSELSRPLALTLRLTVNLMVG 149
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 84488642  169 HLLIqllstsvltllKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00087 150 HLIS-----------SLLNFLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
94-223 3.75e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 52.97  E-value: 3.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488642   94 TPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETI-SLFIRPLALGVRLTANLTAGHLLI 172
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 84488642  173 qlLSTSVLTLLKTTMTLSILTTMILLLLTILELAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13417 297 --LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
90-168 1.94e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 37.56  E-value: 1.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84488642   90 PYTFTPTTQLSMNMGLALPMWMATIFTGFRNQLTTSLGHLLPEGTPTPLTPILIMIETISLFIRPLALGVRLTANLTAG 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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