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Conserved domains on  [gi|2035790907|gb|QVE47026|]
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ATP synthase F0 subunit 6 (mitochondrion) [Megaloceros giganteus]

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 7.15e-141

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 393.16  E-value: 7.15e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907   1 MNENLFASFITPMILGLPLATLIVMFPSLLFPTSNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035790907 161 TANITAGHLLIHLIGGATLALMSISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 7.15e-141

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 393.16  E-value: 7.15e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907   1 MNENLFASFITPMILGLPLATLIVMFPSLLFPTSNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035790907 161 TANITAGHLLIHLIGGATLALMSISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHDNT 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 2.30e-57

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: 181.25  E-value: 2.30e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907   5 LFASFITP--MILGLPLATLIVMFPSLLF----PTSNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILF 78
Cdd:TIGR01131   1 LFSQFDISpiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  79 IGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAV 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035790907 159 RLTANITAGHLLIHLIGGATLALMSISttMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHDN 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 1.53e-43

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: 143.69  E-value: 1.53e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  65 GQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2035790907 145 ETISLLIQPIALAVRLTANITAGHLLIHLIGGATLALMSIsttMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
13-223 2.59e-40

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 137.24  E-value: 2.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  13 MILGLPLATLIVMFPSLLFPTSNRLVNNRLISLQQWALQLVSKQMMG-IHNAKGQTWALMLMSLILFIGSTNLLGLL--- 88
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpks 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  89 PHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNK-TKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAVRLTANITAG 167
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2035790907 168 HLLIHLIGGATLALMSISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLH 223
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 19-224 1.75e-27

FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 104.00  E-value: 1.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  19 LATLIVMFPSLLFPTSNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQL 98
Cdd:COG0356     8 LAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  99 SMNLGMAIPLWAGAVVTGFRNK-TKASLAHFLPQGTPtPLIPMLVIIETISLLIQPIALAVRLTANITAGHLLIHLIgga 177
Cdd:COG0356    88 NVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLL--- 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2035790907 178 tlALMSISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHD 224
Cdd:COG0356   164 --AGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 7.15e-141

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 393.16  E-value: 7.15e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907   1 MNENLFASFITPMILGLPLATLIVMFPSLLFPTSNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035790907 161 TANITAGHLLIHLIGGATLALMSISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-226 1.89e-91

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 267.85  E-value: 1.89e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907   1 MNENLFASFITPMILGLPLATLIVMFPSLLFPT-SNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILFI 79
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSpKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAVR 159
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035790907 160 LTANITAGHLLIHLIGGATLALMSISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-226 5.50e-87

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 256.82  E-value: 5.50e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907   1 MNENLFASFITPMILGLPLATLIVMFPSLLFPT-SNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILFI 79
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTpTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAVR 159
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035790907 160 LTANITAGHLLIHLIGGATLALMSISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-225 6.03e-85

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 251.33  E-value: 6.03e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907   1 MNENLFASFITPMILGLPLATLIVMFPSLLFPT-SNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILFI 79
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTpTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAVR 159
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035790907 160 LTANITAGHLLIHLIGGATLALMSISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-226 2.94e-74

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 224.44  E-value: 2.94e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907   1 MNENLFASFITPMILGLPLATLIVMFPSLLFPTS-NRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILFI 79
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLtNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAVR 159
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035790907 160 LTANITAGHLLIHLIGGATLALMSISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHDNT 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 2.30e-57

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: 181.25  E-value: 2.30e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907   5 LFASFITP--MILGLPLATLIVMFPSLLF----PTSNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILF 78
Cdd:TIGR01131   1 LFSQFDISpiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  79 IGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAV 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035790907 159 RLTANITAGHLLIHLIGGATLALMSISttMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-221 3.46e-50

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 162.64  E-value: 3.46e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907   1 MNENLFASFITPMILGLPLATLIVMFPSLLFPTSNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILFIG 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAVRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2035790907 161 TANITAGHLLIHLIGGatlALMSISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLY 221
Cdd:MTH00157  161 AANMIAGHLLLTLLGN---TGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLY 218
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-225 5.96e-49

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 159.75  E-value: 5.96e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907   1 MNENLFASFITPMILGLPLATLIVMFPS--LLFPTSNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILF 78
Cdd:MTH00035    3 INNSIFGQFSPDTILFIPLTLLSSVIALswLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  79 IGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAV 158
Cdd:MTH00035   83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2035790907 159 RLTANITAGHLLIHLIGGATLALMSiSTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHDN 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 1.53e-43

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: 143.69  E-value: 1.53e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  65 GQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2035790907 145 ETISLLIQPIALAVRLTANITAGHLLIHLIGGATLALMSIsttMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
13-223 2.59e-40

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 137.24  E-value: 2.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  13 MILGLPLATLIVMFPSLLFPTSNRLVNNRLISLQQWALQLVSKQMMG-IHNAKGQTWALMLMSLILFIGSTNLLGLL--- 88
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpks 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  89 PHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNK-TKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAVRLTANITAG 167
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2035790907 168 HLLIHLIGGATLALMSISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLH 223
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 25-224 3.68e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 137.30  E-value: 3.68e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  25 MFPSLLFPTSNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGM 104
Cdd:MTH00173   28 LMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907 105 AIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAVRLTANITAGHLLIHLIGGATLA-LMS 183
Cdd:MTH00173  108 ALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYLSSsLFS 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2035790907 184 ISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHD 224
Cdd:MTH00173  188 SSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 8.17e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 136.32  E-value: 8.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907   1 MNENLFASFITPMILGLPLATLI---VMFPSLLFPTSNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLIL 77
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFSMISLSwitLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  78 FIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALA 157
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2035790907 158 VRLTANITAGHLLIHLIGGATLALMSISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 22-224 8.97e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 120.92  E-value: 8.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  22 LIVMFPSLLFPTSNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQLSMN 101
Cdd:MTH00172   25 ILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHIVVT 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907 102 LGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAVRLTANITAGHLLIHLIGGATLAL 181
Cdd:MTH00172  105 LGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNM 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2035790907 182 MSISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHD 224
Cdd:MTH00172  185 LCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 29-226 6.53e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 115.99  E-value: 6.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  29 LLFPTSNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL 108
Cdd:MTH00005   34 LLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907 109 WAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAVRLTANITAGHLLIHLIGGATLALMSISTTM 188
Cdd:MTH00005  114 WLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGIYAASALFSSISS 193

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2035790907 189 ALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00005  194 TILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 19-224 6.69e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 111.25  E-value: 6.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  19 LATLIVMFPSLLFpTSNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQL 98
Cdd:MTH00175   34 MMVLAVIIFWLLL-KGDKLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHI 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  99 SMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLLIQPIALAVRLTANITAGHLLIHLIGGAT 178
Cdd:MTH00175  113 IITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFA 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2035790907 179 LALMSIS-TTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHD 224
Cdd:MTH00175  193 FNMLSNGlIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 19-224 1.75e-27

FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 104.00  E-value: 1.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  19 LATLIVMFPSLLFPTSNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQL 98
Cdd:COG0356     8 LAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  99 SMNLGMAIPLWAGAVVTGFRNK-TKASLAHFLPQGTPtPLIPMLVIIETISLLIQPIALAVRLTANITAGHLLIHLIgga 177
Cdd:COG0356    88 NVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLL--- 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2035790907 178 tlALMSISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHD 224
Cdd:COG0356   164 --AGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 10-224 3.08e-25

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 98.33  E-value: 3.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  10 ITPMILGLPLATLIVMFPSLLFPTSNRLVNNRLISLQQWALQLVSKQMMGIHNAKGQTWALMLMSLILFIGSTNLLGLLP 89
Cdd:PRK05815   14 FDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  90 -HSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKtkaSLAHFLPQGTPTPlIPMLVIIETISLLIQPIALAVRLTANITAGH 168
Cdd:PRK05815   94 yLLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGE 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2035790907 169 LLIHLIGGatlaLMSISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYLHD 224
Cdd:PRK05815  170 LILALIAL----LGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 64-224 8.77e-22

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 90.00  E-value: 8.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  64 KGQTWALMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVI 143
Cdd:MTH00174   86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907 144 IETISLLIQPIALAVRLTANITAGHLLIHLIGGATLALMSISTTM-ALITFIILVLLTILEFAVAMIQAYVFTLLVSLYL 222
Cdd:MTH00174  166 IETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245


                  ..
gi 2035790907 223 HD 224
Cdd:MTH00174  246 RD 247
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 72-222 3.38e-16

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 75.93  E-value: 3.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  72 LMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFR-NKTKASLAHfLPQGTPTPLIPMLVIIETISLL 150
Cdd:PRK13419  174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAH-LTGGTHWSLWIIMIPIEFIGLF 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907 151 IQPIALAVRLTANITAGHLLIhliggatLALMSISttMALITFIILVLLTI--------LEFAVAMIQAYVFTLLVSLYL 222
Cdd:PRK13419  253 TKPFALTVRLFANMTAGHIVI-------LSLIFIS--FILKSYIVAVAVSVpfaifiylLELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 74-222 2.36e-12

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 63.46  E-value: 2.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  74 SLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASlaHFLPQGTPTPLIPM-LVIIETISLLIQ 152
Cdd:MTH00087   57 FTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTFsMLFVEIVSELSR 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907 153 PIALAVRLTANITAGHLLIHLIggatlalmsisTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYL 222
Cdd:MTH00087  135 PLALTLRLTVNLMVGHLISSLL-----------NFLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 93-222 1.72e-11

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 62.60  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  93 TPTTQLSMNLGMAIPLWAGAVVTGFRNKTKASLAHFLPQGTPTPLIPMLVIIETI-SLLIQPIALAVRLTANITAGHLLI 171
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2035790907 172 HLIGGatLALMSISTTMALITFIILVLLTILEFAVAMIQAYVFTLLVSLYL 222
Cdd:PRK13417  297 LALMG--FIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 71-222 1.87e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 41.27  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907  71 MLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVVTGFRNK-TKASLAHFLpqgTPTPLIPMLVIIETISl 149
Cdd:PRK13420   77 FVGTLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEgLREYLKHYL---SPSPFLLPFHLISEIT- 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035790907 150 liQPIALAVRLTANITA---GHLLIHLIGGatlalmsisttmalitFIILVLLTILEFAVAMIQAYVFTLLVSLYL 222
Cdd:PRK13420  153 --RTLALAVRLFGNIMSlelAALLVLLVAG----------------FLVPVPILMLHIIEALVQAYIFGMLALIYI 210
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 126-215 3.93e-04

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 39.87  E-value: 3.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035790907 126 AHFLPQGTPTPLIPMLVIIETISLLIQPIALAVRLTANITAGHLlihliGGATLALMSISTtmaLITFIILVLLTILEFA 205
Cdd:MTH00050   80 SSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGCF-----GGVALGNLCFIS---YWWFLVLFFLFFYEVF 151

                          90
                  ....*....|
gi 2035790907 206 VAMIQAYVFT 215
Cdd:MTH00050  152 VALVHWFIVS 161
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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