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Conserved domains on  [gi|1886411802|gb|QMV34614|]
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ATP synthase F0 subunit 6 (mitochondrion) [Galegeeska revoilii]

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 1.35e-136

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 382.38  E-value: 1.35e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802   1 MNENLFASFITPTLMGMPIVTLIIAFPNILFPQPKRLLNNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886411802 161 TANITAGHLLIHLIGGATLVLMSISTPTAMITFIILILLTILEFAVAMIQAYVFTLLVSLYLHDNA 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.35e-136

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 382.38  E-value: 1.35e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802   1 MNENLFASFITPTLMGMPIVTLIIAFPNILFPQPKRLLNNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886411802 161 TANITAGHLLIHLIGGATLVLMSISTPTAMITFIILILLTILEFAVAMIQAYVFTLLVSLYLHDNA 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 3-225 8.81e-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: 172.01  E-value: 8.81e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802   3 ENLFASFITPTLMGMPIVTLIIAFPNILFPQ--PKRLLNNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFIG 80
Cdd:TIGR01131   3 SQFDISPITLFSLTLLSLILLLSLLIFLISSslSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVRL 160
Cdd:TIGR01131  83 ISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886411802 161 TANITAGHLLIHLIGGATLVLMSIStpTAMITFIILILLTILEFAVAMIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 163 FANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 3.76e-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: 137.53  E-value: 3.76e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  65 GRTWSLMLVSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVI 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886411802 145 ETISLFIQPMALAVRLTANITAGHLLIHLIGGATLVLMSISTPTAMitfIILILLTILEFAVAMIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPL---LLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
19-223 7.62e-38

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 131.07  E-value: 7.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  19 IVTLIIAFPNILFPQPKRLLNNRWITIQQWLVNLILKQMMS-MHNIKGRTWSLMLVSLILFIGSTNLLGLL---PHSFTP 94
Cdd:pfam00119   7 VALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  95 TTQLSMNLGMAIPLWAGAVIMGFR-HKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVRLTANITAGHLLIHL 173
Cdd:pfam00119  87 TADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLL 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1886411802 174 IGGATLVLMSISTPTAMITFIILILLTILEFAVAMIQAYVFTLLVSLYLH 223
Cdd:pfam00119 167 LAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 40-224 2.31e-23

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: 93.21  E-value: 2.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  40 NRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRH 119
Cdd:COG0356    29 GGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802 120 K-TKASLAHFLPQGTPiPLIPMLIVIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLVLMSISTPTAMitfiiLIL 198
Cdd:COG0356   109 KgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL-----PVA 182

                         170       180
                  ....*....|....*....|....*.
gi 1886411802 199 LTILEFAVAMIQAYVFTLLVSLYLHD 224
Cdd:COG0356   183 WTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.35e-136

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 382.38  E-value: 1.35e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802   1 MNENLFASFITPTLMGMPIVTLIIAFPNILFPQPKRLLNNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886411802 161 TANITAGHLLIHLIGGATLVLMSISTPTAMITFIILILLTILEFAVAMIQAYVFTLLVSLYLHDNA 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-225 2.33e-85

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 252.44  E-value: 2.33e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802   1 MNENLFASFITPTLMGMPIVTLIIAFPNILFPQPK-RLLNNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFI 79
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKnRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVR 159
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886411802 160 LTANITAGHLLIHLIGGATLVLMSISTPTAMITFIILILLTILEFAVAMIQAYVFTLLVSLYLHDN 225
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-225 1.28e-83

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 248.25  E-value: 1.28e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802   1 MNENLFASFITPTLMGMPIVTLIIAFPNILFPQP-KRLLNNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFI 79
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPtSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVR 159
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886411802 160 LTANITAGHLLIHLIGGATLVLMSISTPTAMITFIILILLTILEFAVAMIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-225 1.38e-82

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 245.65  E-value: 1.38e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802   1 MNENLFASFITPTLMGMPIVTLIIAFPNILFPQP-KRLLNNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFI 79
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPtNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVR 159
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886411802 160 LTANITAGHLLIHLIGGATLVLMSISTPTAMITFIILILLTILEFAVAMIQAYVFTLLVSLYLHDN 225
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-225 6.62e-70

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 213.27  E-value: 6.62e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802   1 MNENLFASFITPTLMGMPIVTLIIAFPNILFPQP-KRLLNNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFI 79
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLtNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVR 159
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886411802 160 LTANITAGHLLIHLIGGATLVLMSISTPTAMITFIILILLTILEFAVAMIQAYVFTLLVSLYLHDN 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 ...
 3-225 8.81e-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: 172.01  E-value: 8.81e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802   3 ENLFASFITPTLMGMPIVTLIIAFPNILFPQ--PKRLLNNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFIG 80
Cdd:TIGR01131   3 SQFDISPITLFSLTLLSLILLLSLLIFLISSslSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVRL 160
Cdd:TIGR01131  83 ISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886411802 161 TANITAGHLLIHLIGGATLVLMSIStpTAMITFIILILLTILEFAVAMIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 163 FANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-225 6.74e-47

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 154.75  E-value: 6.74e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802   1 MNENLFASFITPTLMGMP--IVTLIIAFPNILFPQPKRLLNNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILF 78
Cdd:MTH00035    3 INNSIFGQFSPDTILFIPltLLSSVIALSWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  79 IGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAV 158
Cdd:MTH00035   83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1886411802 159 RLTANITAGHLLIHLIGGATLVLMSiSTPTAMITFIILILLTILEFAVAMIQAYVFTLLVSLYLHDN 225
Cdd:MTH00035  163 RLAANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-221 1.24e-45

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 151.09  E-value: 1.24e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802   1 MNENLFASFITPTLMGMPIVTLIIAFPNILFPQPKRLLNNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFIG 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886411802 161 TANITAGHLLIHLIGGATLVLMSISTPTAMitfIILILLTILEFAVAMIQAYVFTLLVSLY 221
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMILSILI---LIQILLLILESAVAIIQSYVFSVLSTLY 218
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 3.76e-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: 137.53  E-value: 3.76e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  65 GRTWSLMLVSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVI 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886411802 145 ETISLFIQPMALAVRLTANITAGHLLIHLIGGATLVLMSISTPTAMitfIILILLTILEFAVAMIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPL---LLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
19-223 7.62e-38

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 131.07  E-value: 7.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  19 IVTLIIAFPNILFPQPKRLLNNRWITIQQWLVNLILKQMMS-MHNIKGRTWSLMLVSLILFIGSTNLLGLL---PHSFTP 94
Cdd:pfam00119   7 VALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  95 TTQLSMNLGMAIPLWAGAVIMGFR-HKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVRLTANITAGHLLIHL 173
Cdd:pfam00119  87 TADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLL 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1886411802 174 IGGATLVLMSISTPTAMITFIILILLTILEFAVAMIQAYVFTLLVSLYLH 223
Cdd:pfam00119 167 LAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 39-224 2.59e-37

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 129.99  E-value: 2.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  39 NNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFR 118
Cdd:MTH00173   42 SSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802 119 HKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVRLTANITAGHLLIHLIGGA-TLVLMSISTPTAMITFIILI 197
Cdd:MTH00173  122 YNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYlSSSLFSSSVVSLLLVLLIQV 201

                         170       180
                  ....*....|....*....|....*..
gi 1886411802 198 LLTILEFAVAMIQAYVFTLLVSLYLHD 224
Cdd:MTH00173  202 GYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-225 1.24e-36

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 128.23  E-value: 1.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802   1 MNENLFASFITPTL----MGMPIVTLIIAFPNiLFPQPKRLLNNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLI 76
Cdd:MTH00176    1 MLVDLFSSFDPPNKnifsMISLSWITLLLFLL-LMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  77 LFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMAL 156
Cdd:MTH00176   80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886411802 157 AVRLTANITAGHLLIHLIGGATLVLMSISTPTAMITFIILILLTILEFAVAMIQAYVFTLLVSLYLHDN 225
Cdd:MTH00176  160 AVRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 19-224 2.20e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 112.06  E-value: 2.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  19 IVTLIIAFPNILFPQPKRLLNNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFIGSTNLLGLLPHSFTPTTQL 98
Cdd:MTH00172   22 IMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHI 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  99 SMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVRLTANITAGHLLIHLIGGAT 178
Cdd:MTH00172  102 VVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFG 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1886411802 179 LVLMSISTPTAMITFIILILLTILEFAVAMIQAYVFTLLVSLYLHD 224
Cdd:MTH00172  182 FNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 37-226 1.59e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 109.82  E-value: 1.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  37 LLNNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMG 116
Cdd:MTH00005   42 ITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSS 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802 117 FRHKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLVLMSISTPTAMITFIIL 196
Cdd:MTH00005  122 VTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGIYAASALFSSISSTILLILTQ 201

                         170       180       190
                  ....*....|....*....|....*....|
gi 1886411802 197 ILLTILEFAVAMIQAYVFTLLVSLYLHDNA 226
Cdd:MTH00005  202 MGYILFEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 10-224 7.13e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 103.16  E-value: 7.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  10 ITPTLMGMPIVTLIIAFpnILFPQPKRLLNNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFIGSTNLLGLLP 89
Cdd:MTH00175   26 VTFTNSSMMMVLAVIIF--WLLLKGDKLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  90 HSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVIETISLFIQPMALAVRLTANITAGHL 169
Cdd:MTH00175  104 YVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1886411802 170 LIHLIGGATLVLMSISTP-TAMITFIILILLTILEFAVAMIQAYVFTLLVSLYLHD 224
Cdd:MTH00175  184 LFAILSGFAFNMLSNGLIiLSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 40-224 2.31e-23

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: 93.21  E-value: 2.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  40 NRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRH 119
Cdd:COG0356    29 GGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802 120 K-TKASLAHFLPQGTPiPLIPMLIVIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLVLMSISTPTAMitfiiLIL 198
Cdd:COG0356   109 KgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL-----PVA 182

                         170       180
                  ....*....|....*....|....*.
gi 1886411802 199 LTILEFAVAMIQAYVFTLLVSLYLHD 224
Cdd:COG0356   183 WTAFELLVGFLQAYIFTMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 10-224 2.08e-21

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 88.31  E-value: 2.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  10 ITPTLMGMPIVTLIIAFPNILFPQPKRLLNNRWITIQQWLVNLILKQMMSMHNIKGRTWSLMLVSLILFIGSTNLLGLLP 89
Cdd:PRK05815   14 FDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  90 -HSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKtkaSLAHFLPQGTPIPlIPMLIVIETISLFIQPMALAVRLTANITAGH 168
Cdd:PRK05815   94 yLLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGE 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1886411802 169 LLIHLIGGatlvLMSISTPTAMITFIILILLTILEFAVAMIQAYVFTLLVSLYLHD 224
Cdd:PRK05815  170 LILALIAL----LGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 72-222 5.85e-17

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 78.25  E-value: 5.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  72 LVSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFR-HKTKASLAHfLPQGTPIPLIPMLIVIETISLF 150
Cdd:PRK13419  174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAH-LTGGTHWSLWIIMIPIEFIGLF 252

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886411802 151 IQPMALAVRLTANITAGHLLI-HLIG-----GATLVLMSISTPTAMitfiiliLLTILEFAVAMIQAYVFTLLVSLYL 222
Cdd:PRK13419  253 TKPFALTVRLFANMTAGHIVIlSLIFisfilKSYIVAVAVSVPFAI-------FIYLLELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 64-224 7.11e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 76.90  E-value: 7.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  64 KGRTWSLMLVSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIV 143
Cdd:MTH00174   86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802 144 IETISLFIQPMALAVRLTANITAGHLLIHLIGGATLVLMSISTPT-AMITFIILILLTILEFAVAMIQAYVFTLLVSLYL 222
Cdd:MTH00174  166 IETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245


                  ..
gi 1886411802 223 HD 224
Cdd:MTH00174  246 RD 247
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 73-222 2.08e-09

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 55.37  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  73 VSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASlaHFLPQGTPIPLIPM-LIVIETISLFI 151
Cdd:MTH00087   56 FFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTFsMLFVEIVSELS 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1886411802 152 QPMALAVRLTANITAGHLLIHLIG--GATLVLMSIstptamitfiiliLLTILEFAVAMIQAYVFTLLVSLYL 222
Cdd:MTH00087  134 RPLALTLRLTVNLMVGHLISSLLNflGEKYVWLSI-------------LAIMMECFVAFIQSYIFSRLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 93-222 3.64e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 55.67  E-value: 3.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  93 TPTTQLSMNLGMAIPLWAGAVIMGFRHKTKASLAHFLPQGTPIPLIPMLIVIETI-SLFIQPMALAVRLTANITAGHLLI 171
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1886411802 172 HLIGGatLVLMSISTPTAMITFIILILLTILEFAVAMIQAYVFTLLVSLYL 222
Cdd:PRK13417  297 LALMG--FIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 74-222 4.72e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 37.03  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802  74 SLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVIMGFRHK-TKASLAHFLpqgTPIPLipmLIVIETISLFIQ 152
Cdd:PRK13420   80 TLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEgLREYLKHYL---SPSPF---LLPFHLISEITR 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886411802 153 PMALAVRLTANITAghllIHLIGGATLVLMSISTPTAMitfiilillTILEFAVAMIQAYVFTLLVSLYL 222
Cdd:PRK13420  154 TLALAVRLFGNIMS----LELAALLVLLVAGFLVPVPI---------LMLHIIEALVQAYIFGMLALIYI 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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