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Conserved domains on  [gi|84488626|ref|YP_448821|]
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ATP synthase F0 subunit 6 (mitochondrion) [Stigmochelys pardalis]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009577)

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 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-226 5.85e-99

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177190  Cd Length: 227  Bit Score: 287.15  E-value: 5.85e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    1 MNLTLFNQFMSPQILGIPLIILALIMPSLIFPTQNNRWLTNRLSTLQSWAINLFTKQLMLPISKTGHKWSIILTSLMVML 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84488626  161 LTANLTAGHLLIQLTSTAVLALLSTTTLSLLTMIILLLLTILE-LAVAMIQAYVFILLLSLYLQENI 226
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLeVAVAMIQAYVFVLLLSLYLQENV 227
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-226 5.85e-99

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 287.15  E-value: 5.85e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    1 MNLTLFNQFMSPQILGIPLIILALIMPSLIFPTQNNRWLTNRLSTLQSWAINLFTKQLMLPISKTGHKWSIILTSLMVML 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84488626  161 LTANLTAGHLLIQLTSTAVLALLSTTTLSLLTMIILLLLTILE-LAVAMIQAYVFILLLSLYLQENI 226
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLeVAVAMIQAYVFVLLLSLYLQENV 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 19-226 2.98e-40

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: 137.34  E-value: 2.98e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    19 LIILALIMPSLIFPTQNNRWLTNRLSTLQSWAINLFTKQLMLPISKTGHKWSIILTSLMVMLLMINLLGLLPYTFTPTTQ 98
Cdd:TIGR01131  20 LILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    99 LSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALGVRLTANLTAGHLLIQLTSTA 178
Cdd:TIGR01131 100 LSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 84488626   179 VLAlLSTTTLSLLTMIILLLLTILELAVAMIQAYVFILLLSLYLQENI 226
Cdd:TIGR01131 180 LFS-LMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-223 1.55e-28

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: 105.17  E-value: 1.55e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626  66 GHKWSIILTSLMVMLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMI 145
Cdd:cd00310   1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84488626 146 ETISLFIRPMALGVRLTANLTAGHLLIQLTSTavLALLSTTTLSLLTMIILLLLTILELAVAMIQAYVFILLLSLYLQ 223
Cdd:cd00310  81 ELISELIRPLSLSVRLFANMFAGHLLLALLSG--LVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
90-223 6.74e-22

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 89.47  E-value: 6.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQ-LTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALGVRLTANLTAG 168
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 84488626   169 HLLIQLTSTAVLALLSTTTLSLLTMIILLLLTILE-LAVAMIQAYVFILLLSLYLQ 223
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFeLLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 90-224 2.45e-13

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: 66.25  E-value: 2.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQ-LTTSLGHLLPEGTPtPLIPILIMIETISLFIRPMALGVRLTANLTAG 168
Cdd:COG0356  78 PGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAG 156

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 84488626 169 HLLIQLtstaVLALLSTTTLSLLTMIILLLLTILELAVAMIQAYVFILLLSLYLQE 224
Cdd:COG0356 157 HIILLL----LAGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-226 5.85e-99

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 287.15  E-value: 5.85e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    1 MNLTLFNQFMSPQILGIPLIILALIMPSLIFPTQNNRWLTNRLSTLQSWAINLFTKQLMLPISKTGHKWSIILTSLMVML 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84488626  161 LTANLTAGHLLIQLTSTAVLALLSTTTLSLLTMIILLLLTILE-LAVAMIQAYVFILLLSLYLQENI 226
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLeVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-226 2.18e-98

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 285.57  E-value: 2.18e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    1 MNLTLFNQFMSPQILGIPLIILALIMPSLIFPTQNNRWLTNRLSTLQSWAINLFTKQLMLPISKTGHKWSIILTSLMVML 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84488626  161 LTANLTAGHLLIQLTSTAVLALLSTTTLSLLTMIILLLLTILE-LAVAMIQAYVFILLLSLYLQENI 226
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILeLAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-226 8.00e-96

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 279.16  E-value: 8.00e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    1 MNLTLFNQFMSPQILGIPLIILALIMPSLIFPTQNNRWLTNRLSTLQSWAINLFTKQLMLPISKTGHKWSIILTSLMVML 80
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALGVR 160
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84488626  161 LTANLTAGHLLIQLTSTAVLALLSTTTLSLLTMIILLLLTILE-LAVAMIQAYVFILLLSLYLQENI 226
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLeIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-225 1.86e-76

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 229.83  E-value: 1.86e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    1 MNLTLFNQFMSPQILGIPLIILALIMPSLIFPTQNNRWLTNRLSTLQSWAINLFTKQLMLPISKTGHKWSIILTSLMVML 80
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALGVR 160
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84488626  161 LTANLTAGHLLIQLTSTAVLALLSTTTLSLLTMIILLLLTILE-LAVAMIQAYVFILLLSLYLQEN 225
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLeVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-225 1.22e-70

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 215.20  E-value: 1.22e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    1 MNLTLFNQFMSPQILGIPLIILALIMPSLIFPTqNNRWLTNRLSTLQSWAINLFTKQLMLPISKTGHKWSIILTSLMVML 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPT-PNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALGVR 160
Cdd:MTH00101  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 84488626  161 LTANLTAGHLLIQLTSTAVLALLSTTTLSLLTMIILLLLTILE-LAVAMIQAYVFILLLSLYLQEN 225
Cdd:MTH00101 160 LTANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILeFAVALIQAYVFTLLVSLYLHDN 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-226 9.35e-42

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 141.26  E-value: 9.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    1 MNLTLFNQFMSPQILGIPLIILALIMP-SLIFPTQNNRWLTNRLSTLQSWAINLFTKQLMLPISKTGHKWSIILTSLMVM 79
Cdd:MTH00035   3 INNSIFGQFSPDTILFIPLTLLSSVIAlSWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   80 LLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALGV 159
Cdd:MTH00035  83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84488626  160 RLTANLTAGHLLIQLTSTAVLALLSTTTLSLLTMIILLLLTILELAVAMIQAYVFILLLSLYLQENI 226
Cdd:MTH00035 163 RLAANLTAGHLLIFLLSTAIWELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 19-226 2.98e-40

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: 137.34  E-value: 2.98e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    19 LIILALIMPSLIFPTQNNRWLTNRLSTLQSWAINLFTKQLMLPISKTGHKWSIILTSLMVMLLMINLLGLLPYTFTPTTQ 98
Cdd:TIGR01131  20 LILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    99 LSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALGVRLTANLTAGHLLIQLTSTA 178
Cdd:TIGR01131 100 LSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 84488626   179 VLAlLSTTTLSLLTMIILLLLTILELAVAMIQAYVFILLLSLYLQENI 226
Cdd:TIGR01131 180 LFS-LMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 15-224 3.78e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 119.12  E-value: 3.78e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   15 LGIPLIILALIMPSLIFPtqNNRWLT-NRLSTLQSWAINLFTKQLMLPISKTGHKWSIILTSLMVMLLMINLLGLLPYTF 93
Cdd:MTH00157  15 FNLSLNWLSTFLGLLFIP--SSFWLIpSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFILFNNFLGLFPYIF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   94 TPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALGVRLTANLTAGHLLIQ 173
Cdd:MTH00157  93 TSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLLT 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 84488626  174 LTSTAVLalLSTTTLSLLTMIILLLLTILELAVAMIQAYVFILLLSLYLQE 224
Cdd:MTH00157 173 LLGNTGP--SLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-225 2.24e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 112.05  E-value: 2.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    1 MNLTLFNQFMSPQILGIPLIILA---LIMPSLIFPTQNNRWLTNRLSTLQSWAiNLFTKQLMLPISKTGHKWSIILTSLM 77
Cdd:MTH00176   1 MLVDLFSSFDPPNKNIFSMISLSwitLLLFLLLMPSSVWFCPSKLQVFMLMFS-TFLPEMILRSNGSYILGSASIIISLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   78 VMLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMAL 157
Cdd:MTH00176  80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84488626  158 GVRLTANLTAGHLLIQLTSTA-VLALLSTTTLSLLTMIILLLLTILELAVAMIQAYVFILLLSLYLQEN 225
Cdd:MTH00176 160 AVRLAANLSAGHLLLGLLGAAmWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-223 1.55e-28

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: 105.17  E-value: 1.55e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626  66 GHKWSIILTSLMVMLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMI 145
Cdd:cd00310   1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84488626 146 ETISLFIRPMALGVRLTANLTAGHLLIQLTSTavLALLSTTTLSLLTMIILLLLTILELAVAMIQAYVFILLLSLYLQ 223
Cdd:cd00310  81 ELISELIRPLSLSVRLFANMFAGHLLLALLSG--LVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-224 2.14e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 104.18  E-value: 2.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    1 MNLTLFNQFMSPQILGIPLIILALIMPSLIFPTQNNR--WLTNRLSTLQSWAINLFTKQLMLPISKTGHKWSIILTSLMV 78
Cdd:MTH00173   1 MMVDLFSSFDDHNSSFSSLSFLMWLLSLMSLFFFSSSvwVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   79 MLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALG 158
Cdd:MTH00173  81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84488626  159 VRLTANLTAGHLLIQLTSTAVLALLSTTTLSLLTMIILLLLTILE--LAVAMIQAYVFILLLSLYLQE 224
Cdd:MTH00173 161 VRLLANISAGHIVLTLIGNYLSSSLFSSSVVSLLLVLLIQVGYFIfeVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 28-221 3.65e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 95.96  E-value: 3.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   28 SLIFPTQNNRWLT-NRLSTLQSWAINLFTKQLMLPISKTGHKWSIILTSLMVMLLMINLLGLLPYTFTPTTQLSMNMGLA 106
Cdd:MTH00005  31 SIILLLSSSFWITpNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626  107 IPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALGVRLTANLTAGHLLIQLTST-AVLALLST 185
Cdd:MTH00005 111 LPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGIyAASALFSS 190

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 84488626  186 TTLSLLTMIILLLLTILELAVAMIQAYVFILLLSLY 221
Cdd:MTH00005 191 ISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP-synt_A pfam00119
ATP synthase A chain;
90-223 6.74e-22

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 89.47  E-value: 6.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQ-LTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALGVRLTANLTAG 168
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 84488626   169 HLLIQLTSTAVLALLSTTTLSLLTMIILLLLTILE-LAVAMIQAYVFILLLSLYLQ 223
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFeLLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 1-226 8.13e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 87.02  E-value: 8.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626    1 MNLTLFNQFMSPQILGIP----LIILALIMPSLIFptQNNRWLTNRLSTLQSWAINLFTKQLMLPISKTGHKWSIILTSL 76
Cdd:MTH00172   1 MSSSYFDQFNIVWLIGLTnssiMMILVIIVVLLLF--KGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   77 MVMLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMA 156
Cdd:MTH00172  79 FFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAIS 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 84488626  157 LGVRLTANLTAGHLLIQ-LTSTAVLALLSTTTLSLLTMIILLLLTILELAVAMIQAYVFILLLSLYLQENI 226
Cdd:MTH00172 159 LGVRLAANLSAGHLLFAiLAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTI 229
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 64-226 1.36e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 78.51  E-value: 1.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   64 KTGHKWSIILTSLMVMLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILI 143
Cdd:MTH00175  77 KSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLV 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626  144 MIETISLFIRPMALGVRLTANLTAGHLLIQLTSTAVLALLS--TTTLSLLTMIILLLLTILELAVAMIQAYVFILLLSLY 221
Cdd:MTH00175 157 LIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSngLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIY 236


                 ....*
gi 84488626  222 LQENI 226
Cdd:MTH00175 237 LGDTI 241
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 35-226 1.54e-14

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 70.35  E-value: 1.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   35 NNRWLTNRLSTLQSWAINLFTKQLMLPISKTGHKWSIILTSLMVMLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATV 114
Cdd:MTH00174  56 NNTLVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTT 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626  115 LTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALGVRLTANLTAGHLLIQLTSTAV--LALLSTTTLSLLT 192
Cdd:MTH00174 136 LAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAwkMINTGILIGSFVP 215

                        170       180       190
                 ....*....|....*....|....*....|....
gi 84488626  193 MIILLLLTILELAVAMIQAYVFILLLSLYLQENI 226
Cdd:MTH00174 216 FAILIFVTILEMAVAIIQAYVFTLLTIVYLRDTV 249
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 90-224 2.45e-13

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: 66.25  E-value: 2.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQ-LTTSLGHLLPEGTPtPLIPILIMIETISLFIRPMALGVRLTANLTAG 168
Cdd:COG0356  78 PGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAG 156

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 84488626 169 HLLIQLtstaVLALLSTTTLSLLTMIILLLLTILELAVAMIQAYVFILLLSLYLQE 224
Cdd:COG0356 157 HIILLL----LAGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 91-224 8.59e-12

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 62.12  E-value: 8.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   91 YTFTPTTQLSMNMGLAIPMWMATVLTGLRNQlttSLGHLLPEGTPTPlIPILIMIETISLFIRPMALGVRLTANLTAGHL 170
Cdd:PRK05815  95 LLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGEL 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 84488626  171 LIQLtstAVLALLSTTTLSLLTMIILLLLTILELAVAMIQAYVFILLLSLYLQE 224
Cdd:PRK05815 171 ILAL---IALLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 90-222 3.82e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 55.52  E-value: 3.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQ-LTTSLGHLlPEGTPTPLIPILIMIETISLFIRPMALGVRLTANLTAG 168
Cdd:PRK13419 191 PYGATATGNINVTLTLAVFTFFITQYAAIKAHgIKGYLAHL-TGGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAG 269

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 84488626  169 HLLIQLTSTAVLALLSTTTLSLLTMIILLLLTILELAVAMIQAYVFILLLSLYL 222
Cdd:PRK13419 270 HIVILSLIFISFILKSYIVAVAVSVPFAIFIYLLELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 90-224 2.12e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 52.29  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSlgHLLPEGTPTPLIP-ILIMIETISLFIRPMALGVRLTANLTAG 168
Cdd:MTH00087  72 PYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTfSMLFVEIVSELSRPLALTLRLTVNLMVG 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 84488626  169 HLLIQLTSTavlallstttLSLLTMIILLLLTILELAVAMIQAYVFILLLSLYLQE 224
Cdd:MTH00087 150 HLISSLLNF----------LGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 94-222 8.56e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 51.81  E-value: 8.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84488626   94 TPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETI-SLFIRPMALGVRLTANLTAGHLLI 172
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 84488626  173 qLTSTAVLALLSTTTLSLLTMIILLLLTILELAVAMIQAYVFILLLSLYL 222
Cdd:PRK13417 297 -LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 90-168 1.56e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 37.94  E-value: 1.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84488626   90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPEGTPTPLIPILIMIETISLFIRPMALGVRLTANLTAG 168
Cdd:MTH00050  43 PYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLG 121
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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