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Conserved domains on  [gi|529217424|ref|YP_008379130|]
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ATP synthase subunit 6 (mitochondrion) [Prolemur simus]

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 1.62e-131

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 369.28  E-value: 1.62e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424   1 MNENLFASFITPTIVGIPIVIFIIMIPSIIFPSPTRLINNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFIG 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFRHKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529217424 161 TANITAGHLLMHLIGGATLVLTSISPATASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.62e-131

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 369.28  E-value: 1.62e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424   1 MNENLFASFITPTIVGIPIVIFIIMIPSIIFPSPTRLINNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFIG 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFRHKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529217424 161 TANITAGHLLMHLIGGATLVLTSISPATASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 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 ...
 36-225 3.78e-54

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: 173.16  E-value: 3.78e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424   36 RLINNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIK 115
Cdd:TIGR01131  38 WLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTIS 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  116 GFRHKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGatLVLTSISPATASITFII 195
Cdd:TIGR01131 118 GFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSG--LLFSLMSSAIFALLLLI 195

                         170       180       190
                  ....*....|....*....|....*....|
gi 529217424  196 LTLLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 196 LVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 3.06e-44

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: 145.23  E-value: 3.06e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  65 GQTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFRHKTKASLAHFLPQGTPIPLIPMLVII 144
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529217424 145 ETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISpatASITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSV---GLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
35-223 7.69e-40

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 136.08  E-value: 7.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424   35 TRLINNRLTSLQQWLVRLILKQLMS-IHSIKGQTWSLMLISLILFIGSTNLLGLL---PHSFTPTTQLSMNLGMAIPLWA 110
Cdd:pfam00119  23 KKLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  111 ATVIKGFR-HKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPATA 189
Cdd:pfam00119 103 LVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLG 182

                         170       180       190
                  ....*....|....*....|....*....|....
gi 529217424  190 SITFIILTLLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 183 VIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 64-224 6.74e-27

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: 102.46  E-value: 6.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  64 KGQTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFRHK-TKASLAHFLPQGTPiPLIPMLV 142
Cdd:COG0356   53 KGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLML 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424 143 IIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSispatASITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:COG0356  132 PIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206


                 ..
gi 529217424 223 HD 224
Cdd:COG0356  207 SL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.62e-131

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 369.28  E-value: 1.62e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424   1 MNENLFASFITPTIVGIPIVIFIIMIPSIIFPSPTRLINNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFIG 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFRHKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529217424 161 TANITAGHLLMHLIGGATLVLTSISPATASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-226 1.43e-85

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 253.21  E-value: 1.43e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424   1 MNENLFASFITPTIVGIPIVIFIIMIPSIIFPSPT-RLINNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFI 79
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKnRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFRHKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529217424 160 LTANITAGHLLMHLIGGATLVLTSISPATASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-226 3.05e-82

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 244.49  E-value: 3.05e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424   1 MNENLFASFITPTIVGIPIVIFIIMIPSIIFPSPT-RLINNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFI 79
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTnKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFRHKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529217424 160 LTANITAGHLLMHLIGGATLVLTSISPATASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-225 2.41e-79

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 237.08  E-value: 2.41e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424   1 MNENLFASFITPTIVGIPIVIFIIMIPSIIFPSPT-RLINNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFI 79
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTsRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFRHKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529217424 160 LTANITAGHLLMHLIGGATLVLTSISPATASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-226 1.59e-70

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 214.81  E-value: 1.59e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424   1 MNENLFASFITPTIVGIPIVIFIIMIPSIIFPSPT-RLINNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFI 79
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTnRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFRHKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529217424 160 LTANITAGHLLMHLIGGATLVLTSISPATASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 36-225 3.78e-54

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: 173.16  E-value: 3.78e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424   36 RLINNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIK 115
Cdd:TIGR01131  38 WLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTIS 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  116 GFRHKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGatLVLTSISPATASITFII 195
Cdd:TIGR01131 118 GFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSG--LLFSLMSSAIFALLLLI 195

                         170       180       190
                  ....*....|....*....|....*....|
gi 529217424  196 LTLLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 196 LVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 33-225 1.37e-48

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 158.98  E-value: 1.37e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  33 SPTRLINNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAT 112
Cdd:MTH00035  37 NPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424 113 VIKGFRHKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSiSPATASIT 192
Cdd:MTH00035 117 NILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRLAANLTAGHLLIFLLSTAIWELSN-SPLISIIT 195

                        170       180       190
                 ....*....|....*....|....*....|...
gi 529217424 193 FIILTLLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00035 196 LIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 37-221 2.24e-48

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 158.02  E-value: 2.24e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  37 LINNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKG 116
Cdd:MTH00157  37 LIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFG 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424 117 FRHKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSIspaTASITFIIL 196
Cdd:MTH00157 117 WINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSSM---ILSILILIQ 193

                        170       180
                 ....*....|....*....|....*
gi 529217424 197 TLLTILEFAVALIQAYVFTLLVSLY 221
Cdd:MTH00157 194 ILLLILESAVAIIQSYVFSVLSTLY 218
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 3.06e-44

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: 145.23  E-value: 3.06e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  65 GQTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFRHKTKASLAHFLPQGTPIPLIPMLVII 144
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529217424 145 ETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISpatASITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSV---GLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 33-224 5.13e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 136.92  E-value: 5.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  33 SPTRLINNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAT 112
Cdd:MTH00173  36 SSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424 113 VIKGFRHKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGA-TLVLTSISPATASI 191
Cdd:MTH00173 116 ILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYlSSSLFSSSVVSLLL 195

                        170       180       190
                 ....*....|....*....|....*....|...
gi 529217424 192 TFIILTLLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00173 196 VLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_A pfam00119
ATP synthase A chain;
35-223 7.69e-40

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 136.08  E-value: 7.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424   35 TRLINNRLTSLQQWLVRLILKQLMS-IHSIKGQTWSLMLISLILFIGSTNLLGLL---PHSFTPTTQLSMNLGMAIPLWA 110
Cdd:pfam00119  23 KKLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  111 ATVIKGFR-HKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPATA 189
Cdd:pfam00119 103 LVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLG 182

                         170       180       190
                  ....*....|....*....|....*....|....
gi 529217424  190 SITFIILTLLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 183 VIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 68-226 2.35e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 135.16  E-value: 2.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  68 WSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFRHKTKASLAHFLPQGTPIPLIPMLVIIETI 147
Cdd:MTH00176  71 SASIIISLFILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELV 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529217424 148 SLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPATASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00176 151 SLLIRPLTLAVRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 39-226 2.37e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 114.44  E-value: 2.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  39 NNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFR 118
Cdd:MTH00005  44 PNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVT 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424 119 HKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPATASITFIILTL 198
Cdd:MTH00005 124 FSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGIYAASALFSSISSTILLILTQMG 203

                        170       180
                 ....*....|....*....|....*...
gi 529217424 199 LTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00005 204 YILFEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 35-224 3.80e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 113.98  E-value: 3.80e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  35 TRLINNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVI 114
Cdd:MTH00172  38 IKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424 115 KGFRHKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPATASITFI 194
Cdd:MTH00172 118 AGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLL 197

                        170       180       190
                 ....*....|....*....|....*....|
gi 529217424 195 ILTLLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00172 198 IMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 36-224 2.71e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 112.02  E-value: 2.71e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  36 RLINNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIK 115
Cdd:MTH00175  50 KLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424 116 GFRHKTKASLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATL-VLTSISPATASITFI 194
Cdd:MTH00175 130 GFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFnMLSNGLIILSLFPML 209

                        170       180       190
                 ....*....|....*....|....*....|
gi 529217424 195 ILTLLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00175 210 IMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 64-224 6.74e-27

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: 102.46  E-value: 6.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  64 KGQTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFRHK-TKASLAHFLPQGTPiPLIPMLV 142
Cdd:COG0356   53 KGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLML 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424 143 IIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSispatASITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:COG0356  132 PIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206


                 ..
gi 529217424 223 HD 224
Cdd:COG0356  207 SL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 35-224 1.06e-23

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 94.48  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  35 TRLINNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFIGSTNLLGLLP-HSFTPTTQLSMNLGMAIPLWAATV 113
Cdd:PRK05815  39 LSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVI 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424 114 IKGFRHKtkaSLAHFLPQGTPIPlIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGatlvLTSISPATASITF 193
Cdd:PRK05815 119 YYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGELILALIAL----LGGAGLLLALAPL 190

                        170       180       190
                 ....*....|....*....|....*....|.
gi 529217424 194 IILTLLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:PRK05815 191 ILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 64-224 9.41e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 87.30  E-value: 9.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  64 KGQTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFRHKTKASLAHFLPQGTPIPLIPMLVI 143
Cdd:MTH00174  86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424 144 IETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPATAS-ITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00174 166 IETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSfVPFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245


                 ..
gi 529217424 223 HD 224
Cdd:MTH00174 246 RD 247
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 72-222 1.56e-19

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 85.18  E-value: 1.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  72 LISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFR-HKTKASLAHfLPQGTPIPLIPMLVIIETISLF 150
Cdd:PRK13419 174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAH-LTGGTHWSLWIIMIPIEFIGLF 252

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529217424 151 IQPMALAVRLTANITAGHL-LMHLIGGATLVLTSISPATASITFIILTLLtiLEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13419 253 TKPFALTVRLFANMTAGHIvILSLIFISFILKSYIVAVAVSVPFAIFIYL--LELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 71-222 5.98e-12

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 62.30  E-value: 5.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  71 MLISLILFigstNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFRHKTKASlaHFLPQGTPIPLIPM-LVIIETISL 149
Cdd:MTH00087  58 TFIVLLLF----CFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTFsMLFVEIVSE 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529217424 150 FIQPMALAVRLTANITAGHLLMHLIGgatlvltsispaTASITFIILTLLTIL-EFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00087 132 LSRPLALTLRLTVNLMVGHLISSLLN------------FLGEKYVWLSILAIMmECFVAFIQSYIFSRLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 93-222 3.34e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 58.75  E-value: 3.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  93 TPTTQLSMNLGMAIPLWAATVIKGFRHKTKASLAHFLPQGTPIPLIPMLVIIETI-SLFIQPMALAVRLTANITAGHLLM 171
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 529217424 172 HLIGGatLVLTSISPATASITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13417 297 LALMG--FIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 74-222 7.20e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 39.34  E-value: 7.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  74 SLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIKGFRHK-TKASLAHFLPQGtpipliPMLVIIETISLFIQ 152
Cdd:PRK13420  80 TLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEgLREYLKHYLSPS------PFLLPFHLISEITR 153

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424 153 PMALAVRLTANITAghllMHLIGGATLVLTSispatasitFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13420 154 TLALAVRLFGNIMS----LELAALLVLLVAG---------FLVPVPILMLHIIEALVQAYIFGMLALIYI 210
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 126-215 1.75e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 37.94  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424 126 AHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSIspatasitFIILTLLTILEFA 205
Cdd:MTH00050  80 SSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGCFGGVALGNLCFISYWW--------FLVLFFLFFYEVF 151

                         90
                 ....*....|
gi 529217424 206 VALIQAYVFT 215
Cdd:MTH00050 152 VALVHWFIVS 161
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
 36-217 8.78e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 36.21  E-value: 8.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424  36 RLINNRLTSLQQWLVRLILKQLMSIHSIKGQTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAATVIK 115
Cdd:PRK13421  45 SLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRALIGTLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYY 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529217424 116 GFRHK-TKASLAHFLpqgTPIPLIPMLVIIETISlfiQPMALAVRLTANITAGhllMHLIGgatlVLTSISPATASITFI 194
Cdd:PRK13421 125 GVRARgVRGYLATFA---EPTWVMIPLNLVEQLT---RTFSLIVRLFGNVMSG---VFVIG----IVLSLAGLLVPIPLM 191

                        170       180
                 ....*....|....*....|...
gi 529217424 195 ILTLLTilefavALIQAYVFTLL 217
Cdd:PRK13421 192 ALDLLT------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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