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Conserved domains on  [gi|2130418494|gb|UEK25003|]
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ATP synthase F0 subunit 6 (mitochondrion) [Conepatus semistriatus]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009564)

ATP synthase F0 subunit 6 is part of the mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V), which produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 2.66e-131

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 368.90  E-value: 2.66e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494   1 MNENLFASFITPTLIGLPIVIIIIMFPSIMFPTSNRLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  81 STNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2130418494 161 TANITAGHLLIHLIGGATLALMDINTTTAMVTFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 2.66e-131

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 368.90  E-value: 2.66e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494   1 MNENLFASFITPTLIGLPIVIIIIMFPSIMFPTSNRLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  81 STNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2130418494 161 TANITAGHLLIHLIGGATLALMDINTTTAMVTFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 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 1.03e-52

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: 169.31  E-value: 1.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494   5 LFASFITP--TLIGLPIVIIIIMFPSIMF----PTSNRLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILF 78
Cdd:TIGR01131   1 LFSQFDISpiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  79 IGSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALAV 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130418494 159 RLTANITAGHLLIHLIGGATLALMDIntTTAMVTFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSS--AIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 4.42e-41

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 137.15  E-value: 4.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  65 GRTWALMLVSLILFIGSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130418494 145 ETISLLIQPMALAVRLTANITAGHLLIHLIGGATLALMdinTTTAMVTFIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLL---SSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
34-223 1.24e-37

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 130.30  E-value: 1.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  34 SNRLINNRLISIQQWLVQMTSKQMLS-IHNYKGRTWALMLVSLILFIGSTNLLGLL---PHTFTSTTQLSMNLGMAIPLW 109
Cdd:pfam00119  22 TKKLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494 110 AGTVLVGFR-HKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALAVRLTANITAGHLLIHLIGGATLALMDINTTT 188
Cdd:pfam00119 102 LLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLL 181

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2130418494 189 AMVTFIILILLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 182 GVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 36-224 8.88e-25

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: 96.68  E-value: 8.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  36 RLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILFIGSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLV 115
Cdd:COG0356    25 KLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYY 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494 116 GFRHK-TKASLAHLLPQGTPILlIPMLVIIETISLLIQPMALAVRLTANITAGHLLIHLIGGATLALmdintTTAMVTFI 194
Cdd:COG0356   105 GIKKKgLGGYLKHLFFPPFPWL-APLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFL-----LLGVLSLL 178

                         170       180       190
                  ....*....|....*....|....*....|
gi 2130418494 195 ILILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:COG0356   179 LPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 2.66e-131

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 368.90  E-value: 2.66e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494   1 MNENLFASFITPTLIGLPIVIIIIMFPSIMFPTSNRLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  81 STNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2130418494 161 TANITAGHLLIHLIGGATLALMDINTTTAMVTFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-226 3.01e-84

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 249.74  E-value: 3.01e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494   1 MNENLFASFITPTLIGLPIVIIIIMFPSIMFPT-SNRLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILFI 79
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSpKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  80 GSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALAVR 159
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130418494 160 LTANITAGHLLIHLIGGATLALMDINTTTAMVTFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-226 3.49e-81

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 241.79  E-value: 3.49e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494   1 MNENLFASFITPTLIGLPIVIIIIMFPSIMFPT-SNRLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILFI 79
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTpTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  80 GSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALAVR 159
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130418494 160 LTANITAGHLLIHLIGGATLALMDINTTTAMVTFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-225 2.63e-79

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 237.08  E-value: 2.63e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494   1 MNENLFASFITPTLIGLPIVIIIIMFPSIMFPT-SNRLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILFI 79
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTpTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  80 GSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALAVR 159
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2130418494 160 LTANITAGHLLIHLIGGATLALMDINTTTAMVTFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-226 2.61e-69

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 211.73  E-value: 2.61e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494   1 MNENLFASFITPTLIGLPIVIIIIMFPSIMFPTS-NRLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILFI 79
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLtNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  80 GSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALAVR 159
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130418494 160 LTANITAGHLLIHLIGGATLALMDINTTTAMVTFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 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 1.03e-52

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: 169.31  E-value: 1.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494   5 LFASFITP--TLIGLPIVIIIIMFPSIMF----PTSNRLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILF 78
Cdd:TIGR01131   1 LFSQFDISpiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  79 IGSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALAV 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130418494 159 RLTANITAGHLLIHLIGGATLALMDIntTTAMVTFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSS--AIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-221 7.60e-48

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 156.87  E-value: 7.60e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494   1 MNENLFASFITPTLIGLPIVIIIIMFPSIMFPTSNRLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILFIG 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  81 STNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALAVRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2130418494 161 TANITAGHLLIHLIGGATLALMDINTttaMVTFIILILLTILEFAVALIQAYVFTLLVSLY 221
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMIL---SILILIQILLLILESAVAIIQSYVFSVLSTLY 218
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-225 4.23e-46

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 152.43  E-value: 4.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494   1 MNENLFASFITPTLIGLPIVIIIIMFPS--IMFPTSNRLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILF 78
Cdd:MTH00035    3 INNSIFGQFSPDTILFIPLTLLSSVIALswLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  79 IGSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALAV 158
Cdd:MTH00035   83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130418494 159 RLTANITAGHLLIHLIGGATLALMDiNTTTAMVTFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00035  163 RLAANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 4.42e-41

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 137.15  E-value: 4.42e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  65 GRTWALMLVSLILFIGSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130418494 145 ETISLLIQPMALAVRLTANITAGHLLIHLIGGATLALMdinTTTAMVTFIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLL---SSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 25-224 7.80e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 133.84  E-value: 7.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  25 MFPSIMFPTSNRLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILFIGSTNLLGLLPHTFTSTTQLSMNLGM 104
Cdd:MTH00173   28 LMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494 105 AIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALAVRLTANITAGHLLIHLIGGATLA-LMD 183
Cdd:MTH00173  108 ALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYLSSsLFS 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2130418494 184 INTTTAMVTFIILILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00173  188 SSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 9.35e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 131.31  E-value: 9.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494   1 MNENLFASFITPTLIGLPIVII---IIMFPSIMFPTSNRLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLIL 77
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFSMISLswiTLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  78 FIGSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALA 157
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2130418494 158 VRLTANITAGHLLIHLIGGATLALMDINTTTAMVTFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP-synt_A pfam00119
ATP synthase A chain;
34-223 1.24e-37

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 130.30  E-value: 1.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  34 SNRLINNRLISIQQWLVQMTSKQMLS-IHNYKGRTWALMLVSLILFIGSTNLLGLL---PHTFTSTTQLSMNLGMAIPLW 109
Cdd:pfam00119  22 TKKLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494 110 AGTVLVGFR-HKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALAVRLTANITAGHLLIHLIGGATLALMDINTTT 188
Cdd:pfam00119 102 LLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLL 181

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2130418494 189 AMVTFIILILLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 182 GVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 29-226 2.99e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 111.75  E-value: 2.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  29 IMFPTSNRLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILFIGSTNLLGLLPHTFTSTTQLSMNLGMAIPL 108
Cdd:MTH00005   34 LLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494 109 WAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALAVRLTANITAGHLLIHLIGGATLALMDINTTT 188
Cdd:MTH00005  114 WLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGIYAASALFSSISS 193

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2130418494 189 AMVTFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00005  194 TILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 1-224 4.74e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 105.89  E-value: 4.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494   1 MNENLFASFITPTLIGL---PIVIIIIMFPSIMFPTSNRLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLIL 77
Cdd:MTH00172    1 MSSSYFDQFNIVWLIGLtnsSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  78 FIGSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALA 157
Cdd:MTH00172   81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130418494 158 VRLTANITAGHLLIHLIGGATLALMDINTTTAMVTFIILILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00172  161 VRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 36-224 8.88e-25

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: 96.68  E-value: 8.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  36 RLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILFIGSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLV 115
Cdd:COG0356    25 KLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYY 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494 116 GFRHK-TKASLAHLLPQGTPILlIPMLVIIETISLLIQPMALAVRLTANITAGHLLIHLIGGATLALmdintTTAMVTFI 194
Cdd:COG0356   105 GIKKKgLGGYLKHLFFPPFPWL-APLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFL-----LLGVLSLL 178

                         170       180       190
                  ....*....|....*....|....*....|
gi 2130418494 195 ILILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:COG0356   179 LPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 35-224 9.13e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 97.77  E-value: 9.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  35 NRLINNRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILFIGSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVL 114
Cdd:MTH00175   49 DKLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494 115 VGFRHKTKASLAHLLPQGTPILLIPMLVIIETISLLIQPMALAVRLTANITAGHLLIHLIGGATL-ALMDINTTTAMVTF 193
Cdd:MTH00175  129 LGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFnMLSNGLIILSLFPM 208

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2130418494 194 IILILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00175  209 LIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 40-224 4.22e-20

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 84.85  E-value: 4.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  40 NRLISIQQWLVQMTSKQMLSIHNYKGRTWALMLVSLILFIGSTNLLGLLP-HTFTSTTQLSMNLGMAIPLWAGTVLVGFR 118
Cdd:PRK05815   44 GGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494 119 -HKTKASLAHLLPQGTPILLIpmlviIETISLLIQPMALAVRLTANITAGHLLIHLIGGATLALMdintTTAMVTFIILI 197
Cdd:PRK05815  124 kKGLGGYLKEFYLQPHPLLLP-----IEIISEFSRPISLSLRLFGNMLAGELILALIALLGGAGL----LLALAPLILPV 194

                         170       180
                  ....*....|....*....|....*..
gi 2130418494 198 LLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:PRK05815  195 AWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 64-224 4.32e-19

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 82.68  E-value: 4.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  64 KGRTWALMLVSLILFIGSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVI 143
Cdd:MTH00174   86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494 144 IETISLLIQPMALAVRLTANITAGHLLIHLIGGATLALMDINTTT-AMVTFIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00174  166 IETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245


                  ..
gi 2130418494 223 HD 224
Cdd:MTH00174  246 RD 247
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 72-222 2.73e-15

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 73.62  E-value: 2.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  72 LVSLILFIGSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFR-HKTKASLAHLlPQGTPILLIPMLVIIETISLL 150
Cdd:PRK13419  174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAHL-TGGTHWSLWIIMIPIEFIGLF 252

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2130418494 151 IQPMALAVRLTANITAGHLLIHLIGGATLALMDINTTTAM-VTFiiLILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13419  253 TKPFALTVRLFANMTAGHIVILSLIFISFILKSYIVAVAVsVPF--AIFIYLLELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 73-222 1.27e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 53.06  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  73 VSLILFIGSTNLLGLLPHTFTSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASlaHLLPQGTPILLIPM-LVIIETISLLI 151
Cdd:MTH00087   56 FFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTFsMLFVEIVSELS 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2130418494 152 QPMALAVRLTANITAGHLLIHLIGGATLALMDINTTTAMVtfiililltilEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00087  134 RPLALTLRLTVNLMVGHLISSLLNFLGEKYVWLSILAIMM-----------ECFVAFIQSYIFSRLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 93-222 4.02e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 52.59  E-value: 4.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130418494  93 TSTTQLSMNLGMAIPLWAGTVLVGFRHKTKASLAHLLPQGTPILLIPMLVIIETI-SLLIQPMALAVRLTANITAGHLLI 171
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2130418494 172 HLIGGatLALMDINTTTAMVTFIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13417  297 LALMG--FIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 126-167 8.47e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 36.02  E-value: 8.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2130418494 126 AHLLPQGTPILLIPMLVIIETISLLIQPMALAVRLTANITAG 167
Cdd:MTH00050   80 SSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLG 121
 
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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