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Conserved domains on  [gi|226464094|ref|YP_002791216|]
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ATP synthase F0 subunit 6 (mitochondrion) [Rattus praetor]

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 5.03e-135

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 378.14  E-value: 5.03e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   1 MNENLFASFITPTVMGLPIVVTIIMFPSILFPSSERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIG 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  81 STNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226464094 161 TANITAGHLLMHLIGGATLVLMNISPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 5.03e-135

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 378.14  E-value: 5.03e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   1 MNENLFASFITPTVMGLPIVVTIIMFPSILFPSSERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIG 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  81 STNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226464094 161 TANITAGHLLMHLIGGATLVLMNISPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHDNT 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 ...
15-225 1.42e-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: 168.92  E-value: 1.42e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   15 MGLPIVVTIIMFPSILFPSSERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIGSTNLLGLLPHTFTP 94
Cdd:TIGR01131  17 LLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   95 TTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLI 174
Cdd:TIGR01131  97 TSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLL 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 226464094  175 GGATLVLMniSPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 177 SGLLFSLM--SSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
65-222 3.03e-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: 137.92  E-value: 3.03e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  65 GRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIII 144
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226464094 145 ETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLMNISPPtatITFIILLLLTMLEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGL---LPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
13-223 4.59e-39

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 134.15  E-value: 4.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   13 TVMGLPIVVTIIMFPSILFPSSERLISNRLHSFQHWLIKLIIKQMM-LIHTPKGRTWALMIVSLIMFIGSTNLLGLL--- 88
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpks 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   89 PHTFTPTTQLSMNLSMAIPLWAGAVILGFR-HKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAG 167
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 226464094  168 HLLMHLIGGATLVLMNISPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
19-224 7.01e-26

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: 99.76  E-value: 7.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  19 IVVTIIMFPSILFPSSERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQL 98
Cdd:COG0356    8 LAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  99 SMNLSMAIPLWAGAVILGFRHK-LKNSLAHFLPQGTPIsLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLIGGA 177
Cdd:COG0356   88 NVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPW-LAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGL 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 226464094 178 TLVLMnisppTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHD 224
Cdd:COG0356  167 APFLL-----LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 5.03e-135

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 378.14  E-value: 5.03e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   1 MNENLFASFITPTVMGLPIVVTIIMFPSILFPSSERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIG 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  81 STNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226464094 161 TANITAGHLLMHLIGGATLVLMNISPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
1-226 2.64e-87

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 257.45  E-value: 2.64e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   1 MNENLFASFITPTVMGLPIVVTIIMFPSILFPSSE-RLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFI 79
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKnRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  80 GSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226464094 160 LTANITAGHLLMHLIGGATLVLMNISPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-225 8.05e-83

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 245.94  E-value: 8.05e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   1 MNENLFASFITPTVMGLPIVVTIIMFPSILFPS-SERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFI 79
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTpTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  80 GSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226464094 160 LTANITAGHLLMHLIGGATLVLMNISPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
1-226 2.13e-82

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 244.88  E-value: 2.13e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   1 MNENLFASFITPTVMGLPIVVTIIMFPSILFPS-SERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFI 79
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTpTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  80 GSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226464094 160 LTANITAGHLLMHLIGGATLVLMNISPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
1-226 5.28e-71

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 215.97  E-value: 5.28e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   1 MNENLFASFITPTVMGLPIVVTIIMFPSILFPSS-ERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFI 79
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLtNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  80 GSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226464094 160 LTANITAGHLLMHLIGGATLVLMNISPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHDNT 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 ...
15-225 1.42e-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: 168.92  E-value: 1.42e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   15 MGLPIVVTIIMFPSILFPSSERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIGSTNLLGLLPHTFTP 94
Cdd:TIGR01131  17 LLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   95 TTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLI 174
Cdd:TIGR01131  97 TSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLL 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 226464094  175 GGATLVLMniSPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 177 SGLLFSLM--SSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
1-225 5.85e-51

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 165.15  E-value: 5.85e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   1 MNENLFASFITPTVMGLPIVVT--IIMFPSILFPSSERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMF 78
Cdd:MTH00035   3 INNSIFGQFSPDTILFIPLTLLssVIALSWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  79 IGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAV 158
Cdd:MTH00035  83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226464094 159 RLTANITAGHLLMHLIGGATLVLMNiSPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00035 163 RLAANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-221 7.26e-49

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 159.56  E-value: 7.26e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   1 MNENLFASFITPTVMGLPIVVTIIMFPSILFPSSERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIG 80
Cdd:MTH00157   1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  81 STNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00157  81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226464094 161 TANITAGHLLMHLIGGATLVLMNISPPtatITFIILLLLTMLEFAVALIQAYVFTLLVSLY 221
Cdd:MTH00157 161 AANMIAGHLLLTLLGNTGPSLSSMILS---ILILIQILLLILESAVAIIQSYVFSVLSTLY 218
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
1-226 1.57e-41

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 140.94  E-value: 1.57e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   1 MNENLFASFITPTVMGLPIVV---TIIMFPSILFPSSERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIM 77
Cdd:MTH00176   1 MLVDLFSSFDPPNKNIFSMISlswITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  78 FIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALA 157
Cdd:MTH00176  81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226464094 158 VRLTANITAGHLLMHLIGGATLVLMNISPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
65-222 3.03e-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: 137.92  E-value: 3.03e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  65 GRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIII 144
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226464094 145 ETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLMNISPPtatITFIILLLLTMLEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGL---LPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
13-223 4.59e-39

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 134.15  E-value: 4.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   13 TVMGLPIVVTIIMFPSILFPSSERLISNRLHSFQHWLIKLIIKQMM-LIHTPKGRTWALMIVSLIMFIGSTNLLGLL--- 88
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpks 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094   89 PHTFTPTTQLSMNLSMAIPLWAGAVILGFR-HKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAG 167
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 226464094  168 HLLMHLIGGATLVLMNISPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
25-224 1.57e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 133.07  E-value: 1.57e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  25 MFPSILFPSSERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSM 104
Cdd:MTH00173  28 LMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094 105 AIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLIGGA-TLVLMN 183
Cdd:MTH00173 108 ALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYlSSSLFS 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 226464094 184 ISPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00173 188 SSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
23-226 3.06e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 116.76  E-value: 3.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  23 IIMFPSILFPSSERLIS-NRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQLSMN 101
Cdd:MTH00005  27 AFNFSIILLLSSSFWITpNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFT 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094 102 LSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVL 181
Cdd:MTH00005 107 LTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGIYAASA 186
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 226464094 182 MNISPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00005 187 LFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
19-224 1.17e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 115.52  E-value: 1.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  19 IVVTIIMFPSILFPSSERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQL 98
Cdd:MTH00172  22 IMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHI 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  99 SMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLIGGAT 178
Cdd:MTH00172 102 VVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFG 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 226464094 179 LVLMNISPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00172 182 FNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
10-224 8.27e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 110.87  E-value: 8.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  10 ITPTVMGLPIVVTIIMFpsILFPSSERLISNRLHSFQHwLIKLIIKQMMLIHTPK-GRTWALMIVSLIMFIGSTNLLGLL 88
Cdd:MTH00175  26 VTFTNSSMMMVLAVIIF--WLLLKGDKLIPNRWQSIME-LIYLNIRSVVHDNLGKsGQKYFPFILSLFLFIAILNILGLF 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  89 PHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAGH 168
Cdd:MTH00175 103 PYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGH 182
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 226464094 169 LLMHLIGGATL-VLMNISPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00175 183 LLFAILSGFAFnMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
19-224 7.01e-26

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: 99.76  E-value: 7.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  19 IVVTIIMFPSILFPSSERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQL 98
Cdd:COG0356    8 LAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  99 SMNLSMAIPLWAGAVILGFRHK-LKNSLAHFLPQGTPIsLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLIGGA 177
Cdd:COG0356   88 NVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPW-LAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGL 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 226464094 178 TLVLMnisppTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHD 224
Cdd:COG0356  167 APFLL-----LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
10-224 7.30e-23

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 92.16  E-value: 7.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  10 ITPTVMGLPIVVTIIMFPSILFPSSERLISNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIGSTNLLGLLP 89
Cdd:PRK05815  14 FDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  90 -HTFTPTTQLSMNLSMAIPLWAGAVILGFR-HKLKNSLAHFLPQGTPIslipmLIIIETISLFIQPMALAVRLTANITAG 167
Cdd:PRK05815  94 yLLFPPTADINVTLALALIVFVLVIYYGIKkKGLGGYLKEFYLQPHPL-----LLPIEIISEFSRPISLSLRLFGNMLAG 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 226464094 168 HLLMHLIGGatlvLMNISPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYLHD 224
Cdd:PRK05815 169 ELILALIAL----LGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
64-224 3.12e-20

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 85.76  E-value: 3.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  64 KGRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLII 143
Cdd:MTH00174  86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094 144 IETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLMNISPPTAT-ITFIILLLLTMLEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00174 166 IETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSfVPFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245

                 ..
gi 226464094 223 HD 224
Cdd:MTH00174 246 RD 247
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
72-222 1.34e-17

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 79.79  E-value: 1.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  72 IVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFR-HKLKNSLAHfLPQGTPISLIPMLIIIETISLF 150
Cdd:PRK13419 174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAH-LTGGTHWSLWIIMIPIEFIGLF 252
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226464094 151 IQPMALAVRLTANITAGHL-LMHLIGGATLVLMNISPPTATITFIILLLLtmLEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13419 253 TKPFALTVRLFANMTAGHIvILSLIFISFILKSYIVAVAVSVPFAIFIYL--LELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
71-222 6.79e-11

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 59.22  E-value: 6.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  71 MIVSLIMFigstNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKnsLAHFLPQGTPISLIPM-LIIIETISL 149
Cdd:MTH00087  58 TFIVLLLF----CFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEK--FSVYLSKGSDSFLKTFsMLFVEIVSE 131
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226464094 150 FIQPMALAVRLTANITAGHLLMHLIGGATLvlmnispptatITFIILLLLTMLEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00087 132 LSRPLALTLRLTVNLMVGHLISSLLNFLGE-----------KYVWLSILAIMMECFVAFIQSYIFSRLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
93-222 9.37e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 54.51  E-value: 9.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  93 TPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETI-SLFIQPMALAVRLTANITAGHLLM 171
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 226464094 172 HLIGGatLVLMNISPPTATITFIILLLLTMLEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13417 297 LALMG--FIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
71-222 8.22e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 45.12  E-value: 8.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226464094  71 MIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHK-LKNSLAHFLpqgtpiSLIPMLIIIETISL 149
Cdd:PRK13420  77 FVGTLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEgLREYLKHYL------SPSPFLLPFHLISE 150
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226464094 150 FIQPMALAVRLTANItaghllMHLIGGATLVLMnispptaTITFIILLLLTMLEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13420 151 ITRTLALAVRLFGNI------MSLELAALLVLL-------VAGFLVPVPILMLHIIEALVQAYIFGMLALIYI 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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