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Conserved domains on  [gi|1929135872|gb|QOY44665|]
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ATP synthase F0 subunit 6 [Ellobius talpinus]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009564)

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 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 2.59e-127

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 358.88  E-value: 2.59e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872   1 MNENLFTSFITPTMMGLPIVILIIMLPSMLMTSSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  81 STNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAIRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1929135872 161 TANITAGHLLIHLIGGATLILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 2.59e-127

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 358.88  E-value: 2.59e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872   1 MNENLFTSFITPTMMGLPIVILIIMLPSMLMTSSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  81 STNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAIRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1929135872 161 TANITAGHLLIHLIGGATLILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
3-225 4.50e-51

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: 165.07  E-value: 4.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872   3 ENLFTSFITPTMMGLPIVILIIMLPSMLMTSS--KRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFIG 80
Cdd:TIGR01131   3 SQFDISPITLFSLTLLSLILLLSLLIFLISSSlsRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  81 STNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAIRL 160
Cdd:TIGR01131  83 ISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRL 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929135872 161 TANITAGHLLIHLIGGatLILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 163 FANISAGHLLLTLLSG--LLFSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
65-222 1.61e-40

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: 135.99  E-value: 1.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  65 GRTWTLMLVSLIMFIGSTNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1929135872 145 ETISLFIQPMALAIRLTANITAGHLLIHLIGGATLILTSMSPPtatITFIILALLTVLEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGL---LPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
14-223 5.87e-40

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 136.47  E-value: 5.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  14 MMGLPIVILIIMLpSMLMTSSKRLLPNRLHSFQQWLIKLIIKQMM-LIQTPKGRTWTLMLVSLIMFIGSTNLLGLL---P 89
Cdd:pfam00119   3 MSLIVALILLLFL-LLATRKTKKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  90 HTFTPTTQLSTNLSMAIPLWAGAVILGFR-HKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAIRLTANITAGH 168
Cdd:pfam00119  82 GGFTVTADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGH 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1929135872 169 LLIHLIGGATLILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 162 LLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
19-224 2.41e-29

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: 108.62  E-value: 2.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  19 IVILIIMLPSMLMTSSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFIGSTNLLGLLPHTFTPTTQL 98
Cdd:COG0356     8 LAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  99 STNLSMAIPLWAGAVILGFRHK-LKPSLAHFLPQGTPiYLIPMLIIIETISLFIQPMALAIRLTANITAGHLLIHLIGGA 177
Cdd:COG0356    88 NVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGL 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1929135872 178 TLILTSmspptATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHD 224
Cdd:COG0356   167 APFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 2.59e-127

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 358.88  E-value: 2.59e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872   1 MNENLFTSFITPTMMGLPIVILIIMLPSMLMTSSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  81 STNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAIRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1929135872 161 TANITAGHLLIHLIGGATLILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
1-226 6.02e-81

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 241.27  E-value: 6.02e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872   1 MNENLFTSFITPTMMGLPIVILIIMLPSMLMTSSK-RLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFI 79
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKnRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  80 GSTNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAIR 159
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929135872 160 LTANITAGHLLIHLIGGATLILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
1-226 1.92e-78

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 234.86  E-value: 1.92e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872   1 MNENLFTSFITPTMMGLPIVILIIMLPSMLM-TSSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFI 79
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFpTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  80 GSTNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAIR 159
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929135872 160 LTANITAGHLLIHLIGGATLILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-225 5.78e-78

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 233.61  E-value: 5.78e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872   1 MNENLFTSFITPTMMGLPIVILIIMLPSMLM-TSSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFI 79
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFpTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  80 GSTNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAIR 159
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1929135872 160 LTANITAGHLLIHLIGGATLILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
1-226 2.64e-66

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 204.03  E-value: 2.64e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872   1 MNENLFTSFITPTMMGLPIVILIIMLPSMLM-TSSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFI 79
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFpSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  80 GSTNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAIR 159
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929135872 160 LTANITAGHLLIHLIGGATLILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00179  161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
1-225 5.95e-52

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 167.46  E-value: 5.95e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872   1 MNENLFTSFITPTMMGLPIVIL--IIMLPSMLMTSSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMF 78
Cdd:MTH00035    3 INNSIFGQFSPDTILFIPLTLLssVIALSWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  79 IGSTNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAI 158
Cdd:MTH00035   83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1929135872 159 RLTANITAGHLLIHLIGGATLILTSmSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00035  163 RLAANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
3-225 4.50e-51

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: 165.07  E-value: 4.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872   3 ENLFTSFITPTMMGLPIVILIIMLPSMLMTSS--KRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFIG 80
Cdd:TIGR01131   3 SQFDISPITLFSLTLLSLILLLSLLIFLISSSlsRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  81 STNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAIRL 160
Cdd:TIGR01131  83 ISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRL 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929135872 161 TANITAGHLLIHLIGGatLILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 163 FANISAGHLLLTLLSG--LLFSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-221 1.10e-47

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 156.48  E-value: 1.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872   1 MNENLFTSFITPTMMGLPIVILIIMLPSMLMTSSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFIG 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  81 STNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAIRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929135872 161 TANITAGHLLIHLIGGatlILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLY 221
Cdd:MTH00157  161 AANMIAGHLLLTLLGN---TGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLY 218
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
65-222 1.61e-40

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: 135.99  E-value: 1.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  65 GRTWTLMLVSLIMFIGSTNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1929135872 145 ETISLFIQPMALAIRLTANITAGHLLIHLIGGATLILTSMSPPtatITFIILALLTVLEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGL---LPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
1-226 1.61e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 138.24  E-value: 1.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872   1 MNENLFTSFITPTMMGLPIVILI---IMLPSMLMTSSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIM 77
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFSMISLSwitLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  78 FIGSTNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALA 157
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1929135872 158 IRLTANITAGHLLIHLIGGATLILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP-synt_A pfam00119
ATP synthase A chain;
14-223 5.87e-40

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 136.47  E-value: 5.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  14 MMGLPIVILIIMLpSMLMTSSKRLLPNRLHSFQQWLIKLIIKQMM-LIQTPKGRTWTLMLVSLIMFIGSTNLLGLL---P 89
Cdd:pfam00119   3 MSLIVALILLLFL-LLATRKTKKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  90 HTFTPTTQLSTNLSMAIPLWAGAVILGFR-HKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAIRLTANITAGH 168
Cdd:pfam00119  82 GGFTVTADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGH 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1929135872 169 LLIHLIGGATLILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 162 LLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
5-224 2.21e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 124.98  E-value: 2.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872   5 LFTSFITPTMMGLPIVILIIMLPSMLMT---SSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFIGS 81
Cdd:MTH00173    5 LFSSFDDHNSSFSSLSFLMWLLSLMSLFffsSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLIS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  82 TNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAIRLT 161
Cdd:MTH00173   85 LNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLL 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1929135872 162 ANITAGHLLIHLIGGATLI-LTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00173  165 ANISAGHIVLTLIGNYLSSsLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
4-226 1.15e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 112.90  E-value: 1.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872   4 NLFTSFITPTMMGLPIVILIIMLPSMLMTsskrlLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFIGSTN 83
Cdd:MTH00005   14 NSLFNNLSSTAFWAFNFSIILLLSSSFWI-----TPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  84 LLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAIRLTAN 163
Cdd:MTH00005   89 LSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAAN 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929135872 164 ITAGHLLIHLIGGATLILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00005  169 MSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
19-224 2.27e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 112.06  E-value: 2.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  19 IVILIIMLPSMLMTSSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFIGSTNLLGLLPHTFTPTTQL 98
Cdd:MTH00172   22 IMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHI 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  99 STNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAIRLTANITAGHLLIHLIGGAT 178
Cdd:MTH00172  102 VVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFG 181
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1929135872 179 LILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00172  182 FNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
19-224 2.41e-29

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: 108.62  E-value: 2.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  19 IVILIIMLPSMLMTSSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFIGSTNLLGLLPHTFTPTTQL 98
Cdd:COG0356     8 LAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  99 STNLSMAIPLWAGAVILGFRHK-LKPSLAHFLPQGTPiYLIPMLIIIETISLFIQPMALAIRLTANITAGHLLIHLIGGA 177
Cdd:COG0356    88 NVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGL 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1929135872 178 TLILTSmspptATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHD 224
Cdd:COG0356   167 APFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
14-224 2.31e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 104.70  E-value: 2.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  14 MMGLPIVILIIMLpsmlmtSSKRLLPNRLHSFQQwLIKLIIKQMMLIQTPK-GRTWTLMLVSLIMFIGSTNLLGLLPHTF 92
Cdd:MTH00175   34 MMVLAVIIFWLLL------KGDKLIPNRWQSIME-LIYLNIRSVVHDNLGKsGQKYFPFILSLFLFIAILNILGLFPYVF 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  93 TPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETISLFIQPMALAIRLTANITAGHLLIH 172
Cdd:MTH00175  107 TPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFA 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1929135872 173 LIGGATL-ILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00175  187 ILSGFAFnMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
4-224 1.98e-25

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 99.10  E-value: 1.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872   4 NLFTSFITPTMMGLPIVILIIMLPSMLMTSSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFIGSTN 83
Cdd:PRK05815    8 GFGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  84 LLGLLP-HTFTPTTQLSTNLSMAIPLWAGAVILGFR-HKLKPSLAHFLPQGTPIylipmLIIIETISLFIQPMALAIRLT 161
Cdd:PRK05815   88 LLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKkKGLGGYLKEFYLQPHPL-----LLPIEIISEFSRPISLSLRLF 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929135872 162 ANITAGHLLIHLIGGatliLTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYLHD 224
Cdd:PRK05815  163 GNMLAGELILALIAL----LGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
10-222 9.42e-19

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 83.25  E-value: 9.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  10 ITPT----MMGLPIVILIIMLP---SMLMTSSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKG-RTWTLMLVSLIMFIGS 81
Cdd:PRK13419  104 ISITkhvvMMWIASAILLVVFLaagRKYKKMTKSQAPKGLANAMEALVEFIRLDVAKSNIGHGyEKFLPYLLTVFFFILV 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  82 TNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFR-HKLKPSLAHfLPQGTPIYLIPMLIIIETISLFIQPMALAIRL 160
Cdd:PRK13419  184 CNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAH-LTGGTHWSLWIIMIPIEFIGLFTKPFALTVRL 262
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929135872 161 TANITAGHLLIHLIGGATLILTS-MSPPTATITFIILALLtvLEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13419  263 FANMTAGHIVILSLIFISFILKSyIVAVAVSVPFAIFIYL--LELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
64-224 3.36e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 80.37  E-value: 3.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  64 KGRTWTLMLVSLIMFIGSTNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLII 143
Cdd:MTH00174   86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872 144 IETISLFIQPMALAIRLTANITAGHLLIHLIGG-ATLILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00174  166 IETLSYISRAISLGVRLAANISSGHLLFSIIASfAWKMINTGILIGSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245

                  ..
gi 1929135872 223 HD 224
Cdd:MTH00174  246 RD 247
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
71-222 7.50e-11

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 59.22  E-value: 7.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  71 MLVSLIMFigstNLLGLLPHTFTPTTQLSTNLSMAIPLWAGAVILGFRHKLKpsLAHFLPQGTPIYLIPM-LIIIETISL 149
Cdd:MTH00087   58 TFIVLLLF----CFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEK--FSVYLSKGSDSFLKTFsMLFVEIVSE 131
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929135872 150 FIQPMALAIRLTANITAGHLLIHLIGGATLILtsmspptatitFIILALLTVLEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00087  132 LSRPLALTLRLTVNLMVGHLISSLLNFLGEKY-----------VWLSILAIMMECFVAFIQSYIFSRLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
93-222 6.96e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 57.98  E-value: 6.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  93 TPTTQLSTNLSMAIPLWAGAVILGFRHKLKPSLAHFLPQGTPIYLIPMLIIIETI-SLFIQPMALAIRLTANITAGHLLI 171
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1929135872 172 HLIGGatLILTSMSPPTATITFIILALLTVLEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13417  297 LALMG--FIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
10-222 4.45e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 45.89  E-value: 4.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  10 ITPTMMGLPIVILIIMLPSMLMTSSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFIGSTNLLGLLP 89
Cdd:PRK13420   16 ITESVLTTWGIMIVLVLASWLTTRRLSLDPGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFVGTLWIFILVANLIGLIP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  90 HTFTPTTQLSTNLSMAIPLWAGAVILGFRHK-LKPSLAHFLPQGtpiyliPMLIIIETISLFIQPMALAIRLTANITA-- 166
Cdd:PRK13420   96 GFHSPTADLSVTAALALLVFFSVHWFGIRAEgLREYLKHYLSPS------PFLLPFHLISEITRTLALAVRLFGNIMSle 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1929135872 167 -GHLLIHLIGGatliltsmspptatitFIILALLTVLEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13420  170 lAALLVLLVAG----------------FLVPVPILMLHIIEALVQAYIFGMLALIYI 210
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
126-215 2.24e-04

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 40.64  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872 126 AHFLPQGTPIYLIPMLIIIETISLFIQPMALAIRLTANITAGHLLIHLIGGATLIltsmspptATITFIILALLTVLEFA 205
Cdd:MTH00050   80 SSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGCFGGVALGNLCFI--------SYWWFLVLFFLFFYEVF 151
                          90
                  ....*....|
gi 1929135872 206 VALIQAYVFT 215
Cdd:MTH00050  152 VALVHWFIVS 161
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
20-217 1.89e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 38.14  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872  20 VILIIMLPSMLMTSSKRLLPNRLHSFQQWLIKLIIKQMMLIQTPKGRTWTLMLVSLIMFIGSTNLLGLLPHTFTPTTQLS 99
Cdd:PRK13421   29 IMAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRALIGTLFLFVLVANWSSLVPGVEPPTAHLE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929135872 100 TNLSMAIPLWAGAVILGFRHK-LKPSLAHFLpqgTPIYLIPMLIIIETISlfiQPMALAIRLTANITAGHLLIhligGAT 178
Cdd:PRK13421  109 TDAALALIVFLATIYYGVRARgVRGYLATFA---EPTWVMIPLNLVEQLT---RTFSLIVRLFGNVMSGVFVI----GIV 178
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1929135872 179 LILTSMSPPtatITFIILALLTvlefavALIQAYVFTLL 217
Cdd:PRK13421  179 LSLAGLLVP---IPLMALDLLT------GAVQAYIFAVL 208
 
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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