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Conserved domains on  [gi|1237408488|ref|YP_009414945|]
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ATP synthase F0 subunit 6 (mitochondrion) [Microcebus simmonsi]

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 1.60e-130

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 366.97  E-value: 1.60e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488   1 MNENLFASFITPTIVGIPVVIFIIMFPSIFFHKPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237408488 161 TANITAGHLLIHLIGGATMVLTSISPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.60e-130

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 366.97  E-value: 1.60e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488   1 MNENLFASFITPTIVGIPVVIFIIMFPSIFFHKPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237408488 161 TANITAGHLLIHLIGGATMVLTSISPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 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 ...
 5-225 1.67e-47

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: 156.21  E-value: 1.67e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488   5 LFASFITP--TIVGIPVVIFIIMFPS----IFFHKPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILF 78
Cdd:TIGR01131   1 LFSQFDISpiTLFSLTLLSLILLLSLliflISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  79 IGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAV 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237408488 159 RLTANITAGHLLIHLIGGATMVLTSISptISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 6.09e-36

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: 124.05  E-value: 6.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  65 GRTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237408488 145 ETISLFIQPMALAVRLTANITAGHLLIHLIGGATMVLTSIsptISSITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
19-223 3.30e-34

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 121.44  E-value: 3.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  19 VVIFIIMFPSIFFHKPYRLIGNRLMSLQQWLIKLVLKQMMA-MHNIKGRTWSLMLMSLILFIGSTNLLGLL---PHSFTP 94
Cdd:pfam00119   7 VALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  95 TTQLSMNLGMAIPLWAAAVITGFR-HKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHL 173
Cdd:pfam00119  87 TADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLL 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237408488 174 IGGATMVLTSISPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 167 LAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 64-224 1.45e-21

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: 88.59  E-value: 1.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  64 KGRTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHK-MKASLAHFLPQGTPIPLIPMLI 142
Cdd:COG0356    53 KGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPWLAPLMLP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488 143 IiETISLFIQPMALAVRLTANITAGHLLIHLIGGATMVLTSisptiSSITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:COG0356   133 I-EIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206


                  ..
gi 1237408488 223 HD 224
Cdd:COG0356   207 SL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.60e-130

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 366.97  E-value: 1.60e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488   1 MNENLFASFITPTIVGIPVVIFIIMFPSIFFHKPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237408488 161 TANITAGHLLIHLIGGATMVLTSISPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-226 1.92e-84

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 250.13  E-value: 1.92e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488   1 MNENLFASFITPTIVGIPVVIFIIMFPSIFF-HKPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFI 79
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIpSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237408488 160 LTANITAGHLLIHLIGGATMVLTSISPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-226 1.52e-81

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 242.95  E-value: 1.52e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488   1 MNENLFASFITPTIVGIPVVIFIIMFPSIFFHKPY-RLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFI 79
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTnKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237408488 160 LTANITAGHLLIHLIGGATMVLTSISPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-225 2.03e-77

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 232.46  E-value: 2.03e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488   1 MNENLFASFITPTIVGIPVVIFIIMFPSIFFHKPY-RLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFI 79
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTsRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237408488 160 LTANITAGHLLIHLIGGATMVLTSISPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-226 1.02e-66

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 205.18  E-value: 1.02e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488   1 MNENLFASFITPTIVGIPVVIFIIMFPSIFFHKPY-RLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFI 79
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTnRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237408488 160 LTANITAGHLLIHLIGGATMVLTSISPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 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 ...
 5-225 1.67e-47

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: 156.21  E-value: 1.67e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488   5 LFASFITP--TIVGIPVVIFIIMFPS----IFFHKPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILF 78
Cdd:TIGR01131   1 LFSQFDISpiTLFSLTLLSLILLLSLliflISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  79 IGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAV 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237408488 159 RLTANITAGHLLIHLIGGATMVLTSISptISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-225 1.37e-44

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 148.58  E-value: 1.37e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488   1 MNENLFASFITPTIVGIPVVIF--IIMFPSIFFHKPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILF 78
Cdd:MTH00035    3 INNSIFGQFSPDTILFIPLTLLssVIALSWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  79 IGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAV 158
Cdd:MTH00035   83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237408488 159 RLTANITAGHLLIHLIGGATMVLTSiSPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00035  163 RLAANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-221 1.56e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 137.99  E-value: 1.56e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488   1 MNENLFASFITPTIVGIPVVIFIIMFPSIFFHKPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFIG 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237408488 161 TANITAGHLLIHLIGGATMvltSISPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLY 221
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGP---SLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLY 218
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 6.09e-36

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: 124.05  E-value: 6.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  65 GRTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237408488 145 ETISLFIQPMALAVRLTANITAGHLLIHLIGGATMVLTSIsptISSITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 1.19e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 125.53  E-value: 1.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488   1 MNENLFASFITPTIVGIPVVIFIIMFPSIF---FHKPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLIL 77
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFSMISLSWITLLLFlllMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  78 FIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALA 157
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237408488 158 VRLTANITAGHLLIHLIGGATMVLTSISPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP-synt_A pfam00119
ATP synthase A chain;
19-223 3.30e-34

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 121.44  E-value: 3.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  19 VVIFIIMFPSIFFHKPYRLIGNRLMSLQQWLIKLVLKQMMA-MHNIKGRTWSLMLMSLILFIGSTNLLGLL---PHSFTP 94
Cdd:pfam00119   7 VALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  95 TTQLSMNLGMAIPLWAAAVITGFR-HKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHL 173
Cdd:pfam00119  87 TADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLL 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237408488 174 IGGATMVLTSISPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 167 LAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 25-224 5.53e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 116.12  E-value: 5.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  25 MFPSIFFHKPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGM 104
Cdd:MTH00173   28 LMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488 105 AIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATMV-LTS 183
Cdd:MTH00173  108 ALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYLSSsLFS 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1237408488 184 ISPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00173  188 SSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 4-226 6.82e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 102.89  E-value: 6.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488   4 NLFASFITPTIVGIPVVIFIIMFPSIFFHKPyrligNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFIGSTN 83
Cdd:MTH00005   14 NSLFNNLSSTAFWAFNFSIILLLSSSFWITP-----NRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  84 LLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRLTAN 163
Cdd:MTH00005   89 LSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAAN 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237408488 164 ITAGHLLIHLIGGATMVlTSISPTISSITFIILTLLTIL-EFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00005  169 MSAGHIVLSLIGIYAAS-ALFSSISSTILLILTQMGYILfEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 1-224 3.32e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 98.57  E-value: 3.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488   1 MNENLFASFITPTIVGI---PVVIFIIMFPSIFFHKPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLIL 77
Cdd:MTH00172    1 MSSSYFDQFNIVWLIGLtnsSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  78 FIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALA 157
Cdd:MTH00172   81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237408488 158 VRLTANITAGHLLIHLIGGATMVLTSISPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00172  161 VRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 20-224 3.92e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 95.84  E-value: 3.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  20 VIFIIMFPSIFFHKPyRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQLS 99
Cdd:MTH00175   35 MVLAVIIFWLLLKGD-KLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHII 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488 100 MNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATM 179
Cdd:MTH00175  114 ITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAF 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1237408488 180 -VLTSISPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00175  194 nMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 64-224 1.45e-21

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: 88.59  E-value: 1.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  64 KGRTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHK-MKASLAHFLPQGTPIPLIPMLI 142
Cdd:COG0356    53 KGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPWLAPLMLP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488 143 IiETISLFIQPMALAVRLTANITAGHLLIHLIGGATMVLTSisptiSSITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:COG0356   133 I-EIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206


                  ..
gi 1237408488 223 HD 224
Cdd:COG0356   207 SL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 10-224 1.96e-19

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 82.92  E-value: 1.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  10 ITPTIVGIPVVIFIIMFPSIFFHKPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFIGSTNLLGLLP 89
Cdd:PRK05815   14 FDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  90 -HSFTPTTQLSMNLGMAIPLWAAAVITGFR-HKMKASLAHFLPQGTPIPLIPmliiiETISLFIQPMALAVRLTANITAG 167
Cdd:PRK05815   94 yLLFPPTADINVTLALALIVFVLVIYYGIKkKGLGGYLKEFYLQPHPLLLPI-----EIISEFSRPISLSLRLFGNMLAG 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1237408488 168 HLLIHLIGGatmvLTSISPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:PRK05815  169 ELILALIAL----LGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 72-222 1.23e-16

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 77.09  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  72 LMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFR-HKMKASLAHfLPQGTPIPLIPMLIIIETISLF 150
Cdd:PRK13419  174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAH-LTGGTHWSLWIIMIPIEFIGLF 252

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237408488 151 IQPMALAVRLTANITAGHLLI-HLIGGATMVLTSISPTISSITFIILTLLtiLEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13419  253 TKPFALTVRLFANMTAGHIVIlSLIFISFILKSYIVAVAVSVPFAIFIYL--LELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 64-224 6.11e-16

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 74.21  E-value: 6.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  64 KGRTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLII 143
Cdd:MTH00174   86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488 144 IETISLFIQPMALAVRLTANITAGHLLIHLIGGATMVLTSISPTISS-ITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00174  166 IETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSfVPFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245


                  ..
gi 1237408488 223 HD 224
Cdd:MTH00174  246 RD 247
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 74-222 6.09e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 51.13  E-value: 6.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  74 SLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASlaHFLPQGT-PIPLIPMLIIIETISLFIQ 152
Cdd:MTH00087   57 FTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSdSFLKTFSMLFVEIVSELSR 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488 153 PMALAVRLTANITAGHLLIHLIGgatmvltsispTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00087  135 PLALTLRLTVNLMVGHLISSLLN-----------FLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 93-222 2.19e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 50.66  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  93 TPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETI-SLFIQPMALAVRLTANITAGHLLI 171
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1237408488 172 HLIGGatMVLTSISPTISSITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13417  297 LALMG--FIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 71-222 1.79e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 38.18  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237408488  71 MLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHK-MKASLAHFLpqgtpiPLIPMLIIIETISL 149
Cdd:PRK13420   77 FVGTLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEgLREYLKHYL------SPSPFLLPFHLISE 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237408488 150 FIQPMALAVRLTANITA---GHLLIHLIGGatmvltsisptissitFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13420  151 ITRTLALAVRLFGNIMSlelAALLVLLVAG----------------FLVPVPILMLHIIEALVQAYIFGMLALIYI 210
 
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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