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Conserved domains on  [gi|1693290044|ref|YP_009651531|]
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ATP synthase F0 subunit 6 (mitochondrion) [Megalonyx jeffersonii]

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 9.61e-137

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 382.38  E-value: 9.61e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044   1 MNENLFASFITPTMMGIPIVLFIVMLPALLFPSPTRLIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  81 LTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693290044 161 TANITAGHLLMHLIGSATLALMSINPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHDNS 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 9.61e-137

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 382.38  E-value: 9.61e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044   1 MNENLFASFITPTMMGIPIVLFIVMLPALLFPSPTRLIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  81 LTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693290044 161 TANITAGHLLMHLIGSATLALMSINPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHDNS 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 ...
 19-225 2.70e-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: 165.84  E-value: 2.70e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  19 IVLFIVMLPALLFPSPTR-LIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFIGLTNLLGLLPHSFTPTTQ 97
Cdd:TIGR01131  20 LILLLSLLIFLISSSLSRwLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  98 LSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGSA 177
Cdd:TIGR01131 100 LSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1693290044 178 TLALMSINPTTafITFIVLILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 180 LFSLMSSAIFA--LLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 5.93e-41

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: 137.15  E-value: 5.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  65 GRTWSLMLISLIMFIGLTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1693290044 145 ETISLFIQPMALAVRLTANITAGHLLMHLIGSATLALMSInptTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
14-223 1.72e-39

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 135.31  E-value: 1.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  14 MMGIPIVLFIVMLPaLLFPSPTRLIANRLISMQQWLISLILKQMM-IIHSPKGRTWSLMLISLIMFIGLTNLLGLL---P 89
Cdd:pfam00119   3 MSLIVALILLLFLL-LATRKTKKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  90 HSFTPTTQLSMNLGMAIPLWAGAVITGFR-HKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGH 168
Cdd:pfam00119  82 GGFTVTADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGH 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1693290044 169 LLMHLIGSATLALMSINPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 162 LLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 19-224 4.17e-26

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: 100.53  E-value: 4.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  19 IVLFIVMLPALLFPSPTRLIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFIGLTNLLGLLPHSFTPTTQL 98
Cdd:COG0356     8 LAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  99 SMNLGMAIPLWAGAVITGFRHK-TKTSLAHFLPQGTPiPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGSA 177
Cdd:COG0356    88 NVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGL 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1693290044 178 TLALMSinpttAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:COG0356   167 APFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 9.61e-137

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 382.38  E-value: 9.61e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044   1 MNENLFASFITPTMMGIPIVLFIVMLPALLFPSPTRLIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  81 LTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693290044 161 TANITAGHLLMHLIGSATLALMSINPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHDNS 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-226 4.21e-88

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 259.37  E-value: 4.21e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044   1 MNENLFASFITPTMMGIPIVLFIVMLPALLFPSPT-RLIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFI 79
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKnRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  80 GLTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1693290044 160 LTANITAGHLLMHLIGSATLALMSINPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHDNS 226
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-225 4.82e-83

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 246.80  E-value: 4.82e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044   1 MNENLFASFITPTMMGIPIVLFIVMLPALLFPSPT-RLIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFI 79
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTnKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  80 GLTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693290044 160 LTANITAGHLLMHLIGSATLALMSINPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-225 2.01e-82

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 245.17  E-value: 2.01e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044   1 MNENLFASFITPTMMGIPIVLFIVMLPALLFPSPT-RLIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFI 79
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTsRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  80 GLTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693290044 160 LTANITAGHLLMHLIGSATLALMSINPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-225 8.44e-71

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 215.58  E-value: 8.44e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044   1 MNENLFASFITPTMMGIPIVLFIVMLPALLFPSPT-RLIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFI 79
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTnRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  80 GLTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693290044 160 LTANITAGHLLMHLIGSATLALMSINPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00179  161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 19-225 2.70e-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: 165.84  E-value: 2.70e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  19 IVLFIVMLPALLFPSPTR-LIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFIGLTNLLGLLPHSFTPTTQ 97
Cdd:TIGR01131  20 LILLLSLLIFLISSSLSRwLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  98 LSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGSA 177
Cdd:TIGR01131 100 LSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1693290044 178 TLALMSINPTTafITFIVLILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 180 LFSLMSSAIFA--LLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-221 1.52e-50

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 163.80  E-value: 1.52e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044   1 MNENLFASFITPTMMGIPIVLFIVMLPALLFPSPTRLIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFIG 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  81 LTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1693290044 161 TANITAGHLLMHLIGSatlALMSINPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLY 221
Cdd:MTH00157  161 AANMIAGHLLLTLLGN---TGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLY 218
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-225 6.16e-49

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 159.75  E-value: 6.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044   1 MNENLFASFITPTMMGIPIVLF--IVMLPALLFPSPTRLIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMF 78
Cdd:MTH00035    3 INNSIFGQFSPDTILFIPLTLLssVIALSWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  79 IGLTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAV 158
Cdd:MTH00035   83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1693290044 159 RLTANITAGHLLMHLIGSATLALMSiNPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00035  163 RLAANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 5.93e-41

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: 137.15  E-value: 5.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  65 GRTWSLMLISLIMFIGLTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1693290044 145 ETISLFIQPMALAVRLTANITAGHLLMHLIGSATLALMSInptTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 5.04e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 137.09  E-value: 5.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044   1 MNENLFASFITPTMMGIPIVLFI---VMLPALLFPSPTRLIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIM 77
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFSMISLSwitLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  78 FIGLTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALA 157
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693290044 158 VRLTANITAGHLLMHLIGSATLALMSINPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHDNS 226
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP-synt_A pfam00119
ATP synthase A chain;
14-223 1.72e-39

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 135.31  E-value: 1.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  14 MMGIPIVLFIVMLPaLLFPSPTRLIANRLISMQQWLISLILKQMM-IIHSPKGRTWSLMLISLIMFIGLTNLLGLL---P 89
Cdd:pfam00119   3 MSLIVALILLLFLL-LATRKTKKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  90 HSFTPTTQLSMNLGMAIPLWAGAVITGFR-HKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGH 168
Cdd:pfam00119  82 GGFTVTADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGH 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1693290044 169 LLMHLIGSATLALMSINPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 162 LLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 25-224 2.81e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 134.99  E-value: 2.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  25 MLPALLFPSPTRLIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFIGLTNLLGLLPHSFTPTTQLSMNLGM 104
Cdd:MTH00173   28 LMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044 105 AIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGSATLA-LMS 183
Cdd:MTH00173  108 ALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYLSSsLFS 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1693290044 184 INPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00173  188 SSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 4-226 1.02e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 118.30  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044   4 NLFASFITPTMMGIPIVLFIVMLPALLFPSPtrliaNRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFIGLTN 83
Cdd:MTH00005   14 NSLFNNLSSTAFWAFNFSIILLLSSSFWITP-----NRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  84 LLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTAN 163
Cdd:MTH00005   89 LSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAAN 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693290044 164 ITAGHLLMHLIGSATLALMSINPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHDNS 226
Cdd:MTH00005  169 MSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 19-224 3.01e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 114.37  E-value: 3.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  19 IVLFIVMLPALLFPSPTRLIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFIGLTNLLGLLPHSFTPTTQL 98
Cdd:MTH00172   22 IMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHI 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  99 SMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGSAT 178
Cdd:MTH00172  102 VVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFG 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1693290044 179 LALMSINPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00172  182 FNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 10-224 1.61e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 105.09  E-value: 1.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  10 ITPTMMGIPIVLFIVMLpaLLFPSPTRLIANRLISMQQwLISLILKQMMIIH-SPKGRTWSLMLISLIMFIGLTNLLGLL 88
Cdd:MTH00175   26 VTFTNSSMMMVLAVIIF--WLLLKGDKLIPNRWQSIME-LIYLNIRSVVHDNlGKSGQKYFPFILSLFLFIAILNILGLF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  89 PHSFTPTTQLSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGH 168
Cdd:MTH00175  103 PYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGH 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1693290044 169 LLMHLI-GSATLALMSINPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00175  183 LLFAILsGFAFNMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 19-224 4.17e-26

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: 100.53  E-value: 4.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  19 IVLFIVMLPALLFPSPTRLIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFIGLTNLLGLLPHSFTPTTQL 98
Cdd:COG0356     8 LAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  99 SMNLGMAIPLWAGAVITGFRHK-TKTSLAHFLPQGTPiPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGSA 177
Cdd:COG0356    88 NVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGL 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1693290044 178 TLALMSinpttAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:COG0356   167 APFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 10-224 8.23e-24

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 94.86  E-value: 8.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  10 ITPTMMGIPIVLFIVMLPALLFPSPTRLIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFIGLTNLLGLLP 89
Cdd:PRK05815   14 FDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  90 -HSFTPTTQLSMNLGMAIPLWAGAVITGFRHKtktSLAHFLPQGTPIPlIPMLVIIETISLFIQPMALAVRLTANITAGH 168
Cdd:PRK05815   94 yLLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGE 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1693290044 169 LLMHLIGSatlaLMSINPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:PRK05815  170 LILALIAL----LGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 37-224 6.35e-22

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 90.38  E-value: 6.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  37 LIANRLISMQQWLISLILKQMMIIHSPKGRTWSLMLISLIMFIGLTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITG 116
Cdd:MTH00174   59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAG 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044 117 FRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGSATLALMSINPTT-AFITFIV 195
Cdd:MTH00174  139 LITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPFAI 218

                         170       180
                  ....*....|....*....|....*....
gi 1693290044 196 LILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00174  219 LIFVTILEMAVAIIQAYVFTLLTIVYLRD 247
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 72-222 4.71e-17

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 78.25  E-value: 4.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  72 LISLIMFIGLTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFR-HKTKTSLAHfLPQGTPIPLIPMLVIIETISLF 150
Cdd:PRK13419  174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAH-LTGGTHWSLWIIMIPIEFIGLF 252

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693290044 151 IQPMALAVRLTANITAGHL----LMHLIGSATLALMSINPTTAFITFIVLilltiLEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13419  253 TKPFALTVRLFANMTAGHIvilsLIFISFILKSYIVAVAVSVPFAIFIYL-----LELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 74-222 9.16e-11

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 58.84  E-value: 9.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  74 SLIMFIGLTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRHKTKTSlaHFLPQGTPIPLIPM-LVIIETISLFIQ 152
Cdd:MTH00087   57 FTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTFsMLFVEIVSELSR 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044 153 PMALAVRLTANITAGHLLMHLIGSATlalmsinpttaFITFIVLILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00087  135 PLALTLRLTVNLMVGHLISSLLNFLG-----------EKYVWLSILAIMMECFVAFIQSYIFSRLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 93-222 2.67e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 56.05  E-value: 2.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  93 TPTTQLSMNLGMAIPLWAGAVITGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETI-SLFIQPMALAVRLTANITAGH-LL 170
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHvII 296

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1693290044 171 MHLIGsatLALMSINPTTAFITFIVLILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13417  297 LALMG---FIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 74-222 1.54e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 38.57  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044  74 SLIMFIGLTNLLGLLPHSFTPTTQLSMNLGMAIPL-----WAGAVITGFRHKTKTSLAHFlpqgtpipliPMLVIIETIS 148
Cdd:PRK13420   80 TLWIFILVANLIGLIPGFHSPTADLSVTAALALLVffsvhWFGIRAEGLREYLKHYLSPS----------PFLLPFHLIS 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1693290044 149 LFIQPMALAVRLTANItaghllMHLIGSATLALMsinpttaFITFIVLILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13420  150 EITRTLALAVRLFGNI------MSLELAALLVLL-------VAGFLVPVPILMLHIIEALVQAYIFGMLALIYI 210
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 126-215 2.09e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 37.56  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693290044 126 AHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGSatlaLMSINpttaFITFIVLILLTILEFA 205
Cdd:MTH00050   80 SSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGCFGGVALGN----LCFIS----YWWFLVLFFLFFYEVF 151

                          90
                  ....*....|
gi 1693290044 206 VALIQAYVFT 215
Cdd:MTH00050  152 VALVHWFIVS 161
 
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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