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Conserved domains on  [gi|1829777429|ref|YP_009755711|]
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ATP synthase F0 subunit 6 (mitochondrion) [Cavia aperea]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009564)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.13e-129

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 364.66  E-value: 1.13e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429   1 MNENLFASFITPTLMGLPVVIIIIMFPIILFPSPMHLINNRLITIQQWLVKLVLKQMMMMHNIKGRTWSLMLISLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  81 TTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLILIETISLFIQPIALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1829777429 161 TANITAGHLLMHLIGGATLVLTTISTPTALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYLHDNS 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.13e-129

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 364.66  E-value: 1.13e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429   1 MNENLFASFITPTLMGLPVVIIIIMFPIILFPSPMHLINNRLITIQQWLVKLVLKQMMMMHNIKGRTWSLMLISLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  81 TTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLILIETISLFIQPIALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1829777429 161 TANITAGHLLMHLIGGATLVLTTISTPTALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYLHDNS 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 8.02e-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: 167.00  E-value: 8.02e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  15 MGLPVVIIIIMFPIILFPSPMHLINNRLITIQQWLVKLVLKQMMMMHNIKGRTWSLMLISLILFIGTTNLLGLLPHSFTP 94
Cdd:TIGR01131  17 LLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  95 TTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLILIETISLFIQPIALAVRLTANITAGHLLMHLI 174
Cdd:TIGR01131  97 TSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1829777429 175 GGATLVLTTIStpTALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 177 SGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 7.28e-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: 141.77  E-value: 7.28e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  65 GRTWSLMLISLILFIGTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLILI 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1829777429 145 ETISLFIQPIALAVRLTANITAGHLLMHLIGGATLVLTTISTPtalITFTILFLLTMLEIAVAMIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGL---LPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
35-223 5.23e-39

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 133.77  E-value: 5.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  35 MHLINNRLITIQQWLVKLVLKQMM-MMHNIKGRTWSLMLISLILFIGTTNLLGLL---PHSFTPTTQLSMNLAMAIPLWA 110
Cdd:pfam00119  23 KKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429 111 ATVILGFRYK-TKASLAHFLPQGTPGPLIPMLILIETISLFIQPIALAVRLTANITAGHLLMHLIGGATLVLTTISTPTA 189
Cdd:pfam00119 103 LVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLG 182

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1829777429 190 LITFTILFLLTMLEIAVAMIQAYVFTLLVSLYLH 223
Cdd:pfam00119 183 VIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 64-224 2.65e-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: 103.61  E-value: 2.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  64 KGRTWSLMLISLILFIGTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYK-TKASLAHFLPQGTPgPLIPMLI 142
Cdd:COG0356    53 KGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLML 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429 143 LIETISLFIQPIALAVRLTANITAGHLLMHLIGGATLVLTtistpTALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYL 222
Cdd:COG0356   132 PIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLL-----LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206


                  ..
gi 1829777429 223 HD 224
Cdd:COG0356   207 SL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.13e-129

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 364.66  E-value: 1.13e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429   1 MNENLFASFITPTLMGLPVVIIIIMFPIILFPSPMHLINNRLITIQQWLVKLVLKQMMMMHNIKGRTWSLMLISLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  81 TTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLILIETISLFIQPIALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1829777429 161 TANITAGHLLMHLIGGATLVLTTISTPTALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYLHDNS 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-226 5.84e-85

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 251.67  E-value: 5.84e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429   1 MNENLFASFITPTLMGLPVVIIIIMFPIILFPSPMH-LINNRLITIQQWLVKLVLKQMMMMHNIKGRTWSLMLISLILFI 79
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNrLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  80 GTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLILIETISLFIQPIALAVR 159
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1829777429 160 LTANITAGHLLMHLIGGATLVLTTISTPTALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYLHDNS 226
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-225 9.33e-85

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 250.95  E-value: 9.33e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429   1 MNENLFASFITPTLMGLPVVIIIIMFPIILFPSPM-HLINNRLITIQQWLVKLVLKQMMMMHNIKGRTWSLMLISLILFI 79
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTsRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  80 GTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLILIETISLFIQPIALAVR 159
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1829777429 160 LTANITAGHLLMHLIGGATLVLTTISTPTALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-225 1.04e-82

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 245.65  E-value: 1.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429   1 MNENLFASFITPTLMGLPVVIIIIMFPIILFPSPM-HLINNRLITIQQWLVKLVLKQMMMMHNIKGRTWSLMLISLILFI 79
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTnKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  80 GTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLILIETISLFIQPIALAVR 159
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1829777429 160 LTANITAGHLLMHLIGGATLVLTTISTPTALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYLHDN 225
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-225 3.48e-70

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 214.04  E-value: 3.48e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429   1 MNENLFASFITPTLMGLPVVIIIIMFPIILFPSPMH-LINNRLITIQQWLVKLVLKQMMMMHNIKGRTWSLMLISLILFI 79
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNrWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  80 GTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLILIETISLFIQPIALAVR 159
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1829777429 160 LTANITAGHLLMHLIGGATLVLTTISTPTALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYLHDN 225
Cdd:MTH00179  161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 15-225 8.02e-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: 167.00  E-value: 8.02e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  15 MGLPVVIIIIMFPIILFPSPMHLINNRLITIQQWLVKLVLKQMMMMHNIKGRTWSLMLISLILFIGTTNLLGLLPHSFTP 94
Cdd:TIGR01131  17 LLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  95 TTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLILIETISLFIQPIALAVRLTANITAGHLLMHLI 174
Cdd:TIGR01131  97 TSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1829777429 175 GGATLVLTTIStpTALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 177 SGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-221 7.18e-49

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 159.56  E-value: 7.18e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429   1 MNENLFASFITPTLMGLPVVIIIIMFPIILFPSPMHLINNRLITIQQWLVKLVLKQMMMMHNIKGRTWSLMLISLILFIG 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  81 TTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLILIETISLFIQPIALAVRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1829777429 161 TANITAGHLLMHLIGGATLVLTTISTPtalITFTILFLLTMLEIAVAMIQAYVFTLLVSLY 221
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMILS---ILILIQILLLILESAVAIIQSYVFSVLSTLY 218
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-225 2.99e-47

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 155.52  E-value: 2.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429   1 MNENLFASFITPTLMGLP--VVIIIIMFPIILFPSPMHLINNRLITIQQWLVKLVLKQMMMMHNIKGRTWSLMLISLILF 78
Cdd:MTH00035    3 INNSIFGQFSPDTILFIPltLLSSVIALSWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  79 IGTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLILIETISLFIQPIALAV 158
Cdd:MTH00035   83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1829777429 159 RLTANITAGHLLMHLIGGATLVLTTiSTPTALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYLHDN 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 7.28e-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: 141.77  E-value: 7.28e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  65 GRTWSLMLISLILFIGTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLILI 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1829777429 145 ETISLFIQPIALAVRLTANITAGHLLMHLIGGATLVLTTISTPtalITFTILFLLTMLEIAVAMIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGL---LPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 30-224 1.21e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 138.46  E-value: 1.21e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  30 LFPSPMHLINNRLITIQQWLVKLVLKQMMMMHNIKGRTWSLMLISLILFIGTTNLLGLLPHSFTPTTQLSMNLAMAIPLW 109
Cdd:MTH00173   33 FFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSLALPLW 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429 110 AATVILGFRYKTKASLAHFLPQGTPGPLIPMLILIETISLFIQPIALAVRLTANITAGHLLMHLIGGA-TLVLTTISTPT 188
Cdd:MTH00173  113 LSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYlSSSLFSSSVVS 192

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1829777429 189 ALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYLHD 224
Cdd:MTH00173  193 LLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_A pfam00119
ATP synthase A chain;
35-223 5.23e-39

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 133.77  E-value: 5.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  35 MHLINNRLITIQQWLVKLVLKQMM-MMHNIKGRTWSLMLISLILFIGTTNLLGLL---PHSFTPTTQLSMNLAMAIPLWA 110
Cdd:pfam00119  23 KKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429 111 ATVILGFRYK-TKASLAHFLPQGTPGPLIPMLILIETISLFIQPIALAVRLTANITAGHLLMHLIGGATLVLTTISTPTA 189
Cdd:pfam00119 103 LVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLG 182

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1829777429 190 LITFTILFLLTMLEIAVAMIQAYVFTLLVSLYLH 223
Cdd:pfam00119 183 VIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 3.00e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 132.46  E-value: 3.00e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429   1 MNENLFASFITPTLMGLPVVII---IIMFPIILFPSPMHLINNRLITIQQWLVKLVLKQMMMMHNIKGRTWSLMLISLIL 77
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFSMISLswiTLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  78 FIGTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLILIETISLFIQPIALA 157
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1829777429 158 VRLTANITAGHLLMHLIGGATLVLTTISTPTALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYLHDNS 226
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 39-226 1.50e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 112.52  E-value: 1.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  39 NNRLITIQQWLVKLVLKQMMMMHNIKGRTWSLMLISLILFIGTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFR 118
Cdd:MTH00005   44 PNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVT 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429 119 YKTKASLAHFLPQGTPGPLIPMLILIETISLFIQPIALAVRLTANITAGHLLMHLIG--GATLVLTTISTPTALITFTIL 196
Cdd:MTH00005  124 FSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGiyAASALFSSISSTILLILTQMG 203

                         170       180       190
                  ....*....|....*....|....*....|
gi 1829777429 197 FllTMLEIAVAMIQAYVFTLLVSLYLHDNS 226
Cdd:MTH00005  204 Y--ILFEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 64-224 1.97e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 109.75  E-value: 1.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  64 KGRTWSLMLISLILFIGTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLIL 143
Cdd:MTH00172   67 EGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429 144 IETISLFIQPIALAVRLTANITAGHLLMHLIGGATLVLTTISTPTALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYLH 223
Cdd:MTH00172  147 IETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLA 226


                  .
gi 1829777429 224 D 224
Cdd:MTH00172  227 D 227
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 64-224 2.65e-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: 103.61  E-value: 2.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  64 KGRTWSLMLISLILFIGTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYK-TKASLAHFLPQGTPgPLIPMLI 142
Cdd:COG0356    53 KGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLML 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429 143 LIETISLFIQPIALAVRLTANITAGHLLMHLIGGATLVLTtistpTALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYL 222
Cdd:COG0356   132 PIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLL-----LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206


                  ..
gi 1829777429 223 HD 224
Cdd:COG0356   207 SL 208
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 62-224 5.54e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 103.55  E-value: 5.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  62 NIKGRTWSLMLISLILFIGTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPML 141
Cdd:MTH00175   76 GKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFL 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429 142 ILIETISLFIQPIALAVRLTANITAGHLLMHLIGGATL-VLTTISTPTALITFTILFLLTMLEIAVAMIQAYVFTLLVSL 220
Cdd:MTH00175  156 VLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFnMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTI 235


                  ....
gi 1829777429 221 YLHD 224
Cdd:MTH00175  236 YLGD 239
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 35-224 8.58e-24

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 94.86  E-value: 8.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  35 MHLINNRLITIQQWLVKLVLKQMMMMHNIKGRTWSLMLISLILFIGTTNLLGLLP-HSFTPTTQLSMNLAMAIPLWAATV 113
Cdd:PRK05815   39 LSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVI 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429 114 ILGFRYKtkaSLAHFLPQGTPGPlIPMLILIETISLFIQPIALAVRLTANITAGHLLMHLIGGatlvLTTISTPTALITF 193
Cdd:PRK05815  119 YYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGELILALIAL----LGGAGLLLALAPL 190

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1829777429 194 TILFLLTMLEIAVAMIQAYVFTLLVSLYLHD 224
Cdd:PRK05815  191 ILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 72-222 4.07e-19

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 84.02  E-value: 4.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  72 LISLILFIGTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFR-YKTKASLAHfLPQGTPGPLIPMLILIETISLF 150
Cdd:PRK13419  174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAH-LTGGTHWSLWIIMIPIEFIGLF 252

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1829777429 151 IQPIALAVRLTANITAGHL-LMHLIGGATLVLTTISTPTALITFTILFLLtmLEIAVAMIQAYVFTLLVSLYL 222
Cdd:PRK13419  253 TKPFALTVRLFANMTAGHIvILSLIFISFILKSYIVAVAVSVPFAIFIYL--LELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 64-224 1.30e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 81.52  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  64 KGRTWSLMLISLILFIGTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLIL 143
Cdd:MTH00174   86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429 144 IETISLFIQPIALAVRLTANITAGHLLMHLIGG-ATLVLTTISTPTALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYL 222
Cdd:MTH00174  166 IETLSYISRAISLGVRLAANISSGHLLFSIIASfAWKMINTGILIGSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245


                  ..
gi 1829777429 223 HD 224
Cdd:MTH00174  246 RD 247
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 57-222 1.49e-10

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 58.45  E-value: 1.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  57 MMMMHNIKGRTWSLMLISLILFIGTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKASlaHFLPQGTPGP 136
Cdd:MTH00087   40 IVFSYSNKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429 137 LIPM-LILIETISLFIQPIALAVRLTANITAGHLLMHLIggatlvlttisTPTALITFTILFLLTMLEIAVAMIQAYVFT 215
Cdd:MTH00087  118 LKTFsMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLL-----------NFLGEKYVWLSILAIMMECFVAFIQSYIFS 186


                  ....*..
gi 1829777429 216 LLVSLYL 222
Cdd:MTH00087  187 RLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 93-222 2.01e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 56.44  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  93 TPTTQLSMNLAMAIPLWAATVILGFRYKTKASLAHFLPQGTPGPLIPMLILIETI-SLFIQPIALAVRLTANITAGHLLM 171
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1829777429 172 HLIGGatLVLTTISTPTALITFTILFLLTMLEIAVAMIQAYVFTLLVSLYL 222
Cdd:PRK13417  297 LALMG--FIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 74-222 6.43e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 45.50  E-value: 6.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  74 SLILFIGTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYK-TKASLAHFLpqgTPGPLipmLILIETISLFIQ 152
Cdd:PRK13420   80 TLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEgLREYLKHYL---SPSPF---LLPFHLISEITR 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429 153 PIALAVRLTANITAghllMHLIGGATLVLTTISTPTALItftilflltMLEIAVAMIQAYVFTLLVSLYL 222
Cdd:PRK13420  154 TLALAVRLFGNIMS----LELAALLVLLVAGFLVPVPIL---------MLHIIEALVQAYIFGMLALIYI 210
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
 74-217 1.98e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 38.14  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829777429  74 SLILFIGTTNLLGLLPHSFTPTTQLSMNLAMAIPLWAATVILGFRYKTKAS-LAHFLpqgTPGPLIPMLILIETISlfiQ 152
Cdd:PRK13421   83 TLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVRARGVRGyLATFA---EPTWVMIPLNLVEQLT---R 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1829777429 153 PIALAVRLTANITAGHLLMhligGATLVLTTISTPTALITftilflltmLEIAVAMIQAYVFTLL 217
Cdd:PRK13421  157 TFSLIVRLFGNVMSGVFVI----GIVLSLAGLLVPIPLMA---------LDLLTGAVQAYIFAVL 208
 
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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