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Conserved domains on  [gi|1197511602|ref|YP_009368301|]
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ATP synthase F0 subunit 6 (mitochondrion) [Lepilemur hollandorum]

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 1.14e-130

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 367.36  E-value: 1.14e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602   1 MNENLFSSFITPTIVGIPIVILIILTPSIFFPSSPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILFIS 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1197511602 161 TANITAGHLLMHLIGGATLALTSINPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 1.14e-130

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 367.36  E-value: 1.14e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602   1 MNENLFSSFITPTIVGIPIVILIILTPSIFFPSSPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILFIS 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1197511602 161 TANITAGHLLMHLIGGATLALTSINPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
5-225 1.12e-54

ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be designated ATP synthase, F0 subunit A; eukaryotic (chloroplast and mitochondrial) forms should be designated ATP synthase, F0 subunit 6. The F1/F0 ATP synthase is a multisubunit, membrane associated enzyme found in bacteria and mitochondria and chloroplast. This enzyme is principally involved in the synthesis of ATP from ADP and inorganic phosphate by coupling the energy derived from the proton electrochemical gradient across the biological membrane. A brief description of this multisubunit enzyme complex: F1 and F0 represent two major clusters of subunits. Individual subunits in each of these clusters are named differently in prokaryotes and in organelles e.g., mitochondria and chloroplast. The bacterial equivalent of subunit 6 is named subunit 'A'. It has been shown that proton is conducted though this subunit. Typically, deprotonation and reprotonation of the acidic amino acid side-chains are implicated in the process. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273458  Cd Length: 226  Bit Score: 174.32  E-value: 1.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602   5 LFSSFITP--TIVGIPIVILIILTPSIFF----PSSPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILF 78
Cdd:TIGR01131   1 LFSQFDISpiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  79 ISSTNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAV 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1197511602 159 RLTANITAGHLLMHLIGGATLALTSinPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMS--SAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
65-222 7.96e-44

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: 144.46  E-value: 7.96e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  65 GRTWALMLTSLILFISSTNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1197511602 145 ETISLLIQPTALAVRLTANITAGHLLMHLIGGATLALTSInptISLITFIILVLLTALELAVALIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
19-223 2.78e-41

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 139.93  E-value: 2.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  19 IVILIILTPSIFFPSSPRLINNRLTSLQQWLIQLMLKQLMAT-HNTKGRTWALMLTSLILFISSTNLLGLL---PHSFTP 94
Cdd:pfam00119   7 VALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNiGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  95 TTQLSMNLGMAIPLWMATVTTGFR-HKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAVRLTANITAGHLLMHL 173
Cdd:pfam00119  87 TADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLL 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1197511602 174 IGGATLALTSINPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 167 LAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
13-224 1.50e-29

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: 109.39  E-value: 1.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  13 TIVGIPIVILIILTPSIFFPSSPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILFISSTNLLGLLPHSF 92
Cdd:COG0356     2 TVLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  93 TPTTQLSMNLGMAIPLWMATVTTGFRHK-TKASLAHLLPQGTPtPLIPMLIIIETISLLIQPTALAVRLTANITAGHLLM 171
Cdd:COG0356    82 PPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIIL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1197511602 172 HLIGGATLALTSinptiSLITFIILVLLTALELAVALIQAYVFTLLVSLYLHD 224
Cdd:COG0356   161 LLLAGLAPFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 1.14e-130

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 367.36  E-value: 1.14e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602   1 MNENLFSSFITPTIVGIPIVILIILTPSIFFPSSPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILFIS 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1197511602 161 TANITAGHLLMHLIGGATLALTSINPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
1-226 6.10e-91

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 266.69  E-value: 6.10e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602   1 MNENLFSSFITPTIVGIPIVILIILTPSIFFPS-SPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILFI 79
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSpKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  80 SSTNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAVR 159
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1197511602 160 LTANITAGHLLMHLIGGATLALTSINPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
1-226 3.80e-86

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 254.51  E-value: 3.80e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602   1 MNENLFSSFITPTIVGIPIVILIILTPSIFFPS-SPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILFI 79
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTpTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  80 SSTNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAVR 159
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1197511602 160 LTANITAGHLLMHLIGGATLALTSINPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-225 5.22e-86

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 254.03  E-value: 5.22e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602   1 MNENLFSSFITPTIVGIPIVILIILTPSIFFPS-SPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILFI 79
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTpTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  80 SSTNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAVR 159
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1197511602 160 LTANITAGHLLMHLIGGATLALTSINPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
1-226 7.70e-77

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 230.99  E-value: 7.70e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602   1 MNENLFSSFITPTIVGIPIVILIILTPSIFFPSS-PRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILFI 79
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLtNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  80 SSTNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAVR 159
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1197511602 160 LTANITAGHLLMHLIGGATLALTSINPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00179  161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
5-225 1.12e-54

ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be designated ATP synthase, F0 subunit A; eukaryotic (chloroplast and mitochondrial) forms should be designated ATP synthase, F0 subunit 6. The F1/F0 ATP synthase is a multisubunit, membrane associated enzyme found in bacteria and mitochondria and chloroplast. This enzyme is principally involved in the synthesis of ATP from ADP and inorganic phosphate by coupling the energy derived from the proton electrochemical gradient across the biological membrane. A brief description of this multisubunit enzyme complex: F1 and F0 represent two major clusters of subunits. Individual subunits in each of these clusters are named differently in prokaryotes and in organelles e.g., mitochondria and chloroplast. The bacterial equivalent of subunit 6 is named subunit 'A'. It has been shown that proton is conducted though this subunit. Typically, deprotonation and reprotonation of the acidic amino acid side-chains are implicated in the process. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273458  Cd Length: 226  Bit Score: 174.32  E-value: 1.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602   5 LFSSFITP--TIVGIPIVILIILTPSIFF----PSSPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILF 78
Cdd:TIGR01131   1 LFSQFDISpiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  79 ISSTNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAV 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1197511602 159 RLTANITAGHLLMHLIGGATLALTSinPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMS--SAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
1-225 6.56e-52

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 167.46  E-value: 6.56e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602   1 MNENLFSSFITPTIVGIPIVIL--IILTPSIFFPSSPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILF 78
Cdd:MTH00035    3 INNSIFGQFSPDTILFIPLTLLssVIALSWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  79 ISSTNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAV 158
Cdd:MTH00035   83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1197511602 159 RLTANITAGHLLMHLIGGATLALTSiNPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00035  163 RLAANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-221 1.37e-49

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 161.49  E-value: 1.37e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602   1 MNENLFSSFITPTIVGIPIVILIILTPSIFFPSSPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILFIS 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAVRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1197511602 161 TANITAGHLLMHLIGGATLaltSINPTISLITFIILVLLTALELAVALIQAYVFTLLVSLY 221
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGP---SLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLY 218
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
5-224 5.98e-45

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 149.63  E-value: 5.98e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602   5 LFSSFITPTIVGIPIVILIILTPS---IFFPSSPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILFISS 81
Cdd:MTH00173    5 LFSSFDDHNSSFSSLSFLMWLLSLmslFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLIS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  82 TNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAVRLT 161
Cdd:MTH00173   85 LNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLL 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1197511602 162 ANITAGHLLMHLIGGATLA-LTSINPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00173  165 ANISAGHIVLTLIGNYLSSsLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
65-222 7.96e-44

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: 144.46  E-value: 7.96e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  65 GRTWALMLTSLILFISSTNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1197511602 145 ETISLLIQPTALAVRLTANITAGHLLMHLIGGATLALTSInptISLITFIILVLLTALELAVALIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
1-226 6.29e-42

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 141.71  E-value: 6.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602   1 MNENLFSSFITPTIVGIPIVILIILTPSIF---FPSSPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLIL 77
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFSMISLSWITLLLFlllMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  78 FISSTNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALA 157
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1197511602 158 VRLTANITAGHLLMHLIGGATLALTSINPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP-synt_A pfam00119
ATP synthase A chain;
19-223 2.78e-41

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 139.93  E-value: 2.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  19 IVILIILTPSIFFPSSPRLINNRLTSLQQWLIQLMLKQLMAT-HNTKGRTWALMLTSLILFISSTNLLGLL---PHSFTP 94
Cdd:pfam00119   7 VALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNiGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  95 TTQLSMNLGMAIPLWMATVTTGFR-HKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAVRLTANITAGHLLMHL 173
Cdd:pfam00119  87 TADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLL 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1197511602 174 IGGATLALTSINPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 167 LAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
4-226 2.55e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 119.84  E-value: 2.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602   4 NLFSSFITPTIVGIPIVILIILTPSIFFPSsprliNNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILFISSTN 83
Cdd:MTH00005   14 NSLFNNLSSTAFWAFNFSIILLLSSSFWIT-----PNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  84 LLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAVRLTAN 163
Cdd:MTH00005   89 LSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAAN 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1197511602 164 ITAGHLLMHLIG--GATLALTSINPTISLITFIILVLLtaLELAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00005  169 MSAGHIVLSLIGiyAASALFSSISSTILLILTQMGYIL--FEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
1-224 8.54e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 113.21  E-value: 8.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602   1 MNENLFSSFITPTIVGI---PIVILIILTPSIFFPSSPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLIL 77
Cdd:MTH00172    1 MSSSYFDQFNIVWLIGLtnsSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  78 FISSTNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALA 157
Cdd:MTH00172   81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1197511602 158 VRLTANITAGHLLMHLIGGATLALTSINPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00172  161 VRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
13-224 1.50e-29

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: 109.39  E-value: 1.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  13 TIVGIPIVILIILTPSIFFPSSPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILFISSTNLLGLLPHSF 92
Cdd:COG0356     2 TVLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  93 TPTTQLSMNLGMAIPLWMATVTTGFRHK-TKASLAHLLPQGTPtPLIPMLIIIETISLLIQPTALAVRLTANITAGHLLM 171
Cdd:COG0356    82 PPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIIL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1197511602 172 HLIGGATLALTSinptiSLITFIILVLLTALELAVALIQAYVFTLLVSLYLHD 224
Cdd:COG0356   161 LLLAGLAPFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
19-224 5.20e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 106.24  E-value: 5.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  19 IVILIILTPSIFFPSSpRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILFISSTNLLGLLPHSFTPTTQL 98
Cdd:MTH00175   34 MMVLAVIIFWLLLKGD-KLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHI 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  99 SMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAVRLTANITAGHLLMHLIGGAT 178
Cdd:MTH00175  113 IITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFA 192
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1197511602 179 L-ALTSINPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00175  193 FnMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
10-224 1.45e-24

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 96.79  E-value: 1.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  10 ITPTIVGIPIVILIILTPSIFFPSSPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILFISSTNLLGLLP 89
Cdd:PRK05815   14 FDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  90 -HSFTPTTQLSMNLGMAIPLWMATVTTGFRHKtkaSLAHLLPQGTPTPlIPMLIIIETISLLIQPTALAVRLTANITAGH 168
Cdd:PRK05815   94 yLLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGE 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1197511602 169 LLMHLIGGatlaLTSINPTISLITFIILVLLTALELAVALIQAYVFTLLVSLYLHD 224
Cdd:PRK05815  170 LILALIAL----LGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
37-224 1.44e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 89.61  E-value: 1.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  37 LINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILFISSTNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTG 116
Cdd:MTH00174   59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAG 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602 117 FRHKTKASLAHLLPQGTPTPLIPMLIIIETISLLIQPTALAVRLTANITAGHLLMHLIGGATLALTSINPTI-SLITFII 195
Cdd:MTH00174  139 LITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPFAI 218
                         170       180
                  ....*....|....*....|....*....
gi 1197511602 196 LVLLTALELAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00174  219 LIFVTILEMAVAIIQAYVFTLLTIVYLRD 247
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
72-222 4.28e-18

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 81.33  E-value: 4.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  72 LTSLILFISSTNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFR-HKTKASLAHLlPQGTPTPLIPMLIIIETISLL 150
Cdd:PRK13419  174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAHL-TGGTHWSLWIIMIPIEFIGLF 252
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1197511602 151 IQPTALAVRLTANITAGHLLMHLIGGATLALTS--INPTISlITFIILVLLtaLELAVALIQAYVFTLLVSLYL 222
Cdd:PRK13419  253 TKPFALTVRLFANMTAGHIVILSLIFISFILKSyiVAVAVS-VPFAIFIYL--LELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
74-222 1.49e-14

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 69.24  E-value: 1.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  74 SLILFISSTNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRHKTKASlaHLLPQGTPTPLIPM-LIIIETISLLIQ 152
Cdd:MTH00087   57 FTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTFsMLFVEIVSELSR 134
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602 153 PTALAVRLTANITAGHLLMHLIGgatlaltsinpTISLITFIILVLLTALELAVALIQAYVFTLLVSLYL 222
Cdd:MTH00087  135 PLALTLRLTVNLMVGHLISSLLN-----------FLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
93-222 1.18e-11

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 62.99  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  93 TPTTQLSMNLGMAIPLWMATVTTGFRHKTKASLAHLLPQGTPTPLIPMLIIIETI-SLLIQPTALAVRLTANITAGHLLM 171
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1197511602 172 HLIGGATLALTSInpTISLITFIILVLLTALELAVALIQAYVFTLLVSLYL 222
Cdd:PRK13417  297 LALMGFIFQFQSW--GIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
10-217 2.97e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 46.61  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  10 ITPTIVGIPIV----ILIILTP-SIFFPSSPRLINNRLTSLQQWLIQLMLKQLMATHNTKGRTWALMLTSLILFISSTNL 84
Cdd:PRK13421   14 LGPVPISAPVVvtwaIMAVLAAgSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRALIGTLFLFVLVANW 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  85 LGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRhkTKASLAHLLPQGTPTPLIPMLIIIETISlliQPTALAVRLTANI 164
Cdd:PRK13421   94 SSLVPGVEPPTAHLETDAALALIVFLATIYYGVR--ARGVRGYLATFAEPTWVMIPLNLVEQLT---RTFSLIVRLFGNV 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1197511602 165 TAGHLLMHLIggatlaltsinptISLITFIILVLLTALELAVALIQAYVFTLL 217
Cdd:PRK13421  169 MSGVFVIGIV-------------LSLAGLLVPIPLMALDLLTGAVQAYIFAVL 208
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
126-215 5.09e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 36.40  E-value: 5.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602 126 AHLLPQGTPTPLIPMLIIIETISLLIQPTALAVRLTANITAGHLlmhliGGATLALTSInptISLITFIILVLLTALELA 205
Cdd:MTH00050   80 SSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGCF-----GGVALGNLCF---ISYWWFLVLFFLFFYEVF 151
                          90
                  ....*....|
gi 1197511602 206 VALIQAYVFT 215
Cdd:MTH00050  152 VALVHWFIVS 161
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
74-222 5.73e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 36.64  E-value: 5.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197511602  74 SLILFISSTNLLGLLPHSFTPTTQLSMNLGMAIPLWMATVTTGFRhkTKASLAHLLPQGTPTPLIPMLIIIETISLLIqp 153
Cdd:PRK13420   80 TLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIR--AEGLREYLKHYLSPSPFLLPFHLISEITRTL-- 155
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1197511602 154 tALAVRLTANITA---GHLLMHLIGGatlaltsinptislitFIILVLLTALELAVALIQAYVFTLLVSLYL 222
Cdd:PRK13420  156 -ALAVRLFGNIMSlelAALLVLLVAG----------------FLVPVPILMLHIIEALVQAYIFGMLALIYI 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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