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Conserved domains on  [gi|2476356605|gb|WFG53768|]
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ATP synthase F0 subunit 6 (mitochondrion) [Chelonoidis vicina]

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
 1-227 3.33e-110

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177190  Cd Length: 227  Bit Score: 315.66  E-value: 3.33e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605   1 MNLTFFDQFMSPQTLGIPLIILALLTPSLMLPTQNNRWLTNRLSTLQLWAINLFTKQLMMPINKTGHKWSITLTSLMAML 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2476356605 161 LTANLTAGHLLIQLTSTAVLALLSMTMTLSILTMTILFLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 3.33e-110

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 315.66  E-value: 3.33e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605   1 MNLTFFDQFMSPQTLGIPLIILALLTPSLMLPTQNNRWLTNRLSTLQLWAINLFTKQLMMPINKTGHKWSITLTSLMAML 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2476356605 161 LTANLTAGHLLIQLTSTAVLALLSMTMTLSILTMTILFLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 19-227 3.19e-45

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: 150.43  E-value: 3.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  19 LIILALLTPSLMLPTQNNRWLTNRLSTLQLWAINLFTKQLMMPINKTGHKWSITLTSLMAMLLMINLLGLLPYTFTPTTQ 98
Cdd:TIGR01131  20 LILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  99 LSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAGHLLIQLTSTA 178
Cdd:TIGR01131 100 LSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2476356605 179 VLALLSMTMTLsiLTMTILFLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:TIGR01131 180 LFSLMSSAIFA--LLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 90-224 7.43e-35

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: 121.35  E-value: 7.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAGH 169
Cdd:cd00310    25 PYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGH 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2476356605 170 LLIQLTSTAVLALLSMTMTLSILtmtILFLLTILELAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310   105 LLLALLSGLVPSLLSSVGLLPLL---LPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
90-224 7.92e-30

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 110.27  E-value: 7.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTS-LGHLLPEGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2476356605 169 HLLIQLTSTAVLALLSMTMTLSILTMTILFLLTILELAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 90-225 6.64e-21

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: 86.67  E-value: 6.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTS-LGHLLPEGTPtPLIPILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:COG0356    78 PGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAG 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2476356605 169 HLLIqltstAVLALLSMTMTLSILTMTILFLLTILELAVAMIQAYVFVLLLSLYLQE 225
Cdd:COG0356   157 HIIL-----LLLAGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 3.33e-110

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 315.66  E-value: 3.33e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605   1 MNLTFFDQFMSPQTLGIPLIILALLTPSLMLPTQNNRWLTNRLSTLQLWAINLFTKQLMMPINKTGHKWSITLTSLMAML 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2476356605 161 LTANLTAGHLLIQLTSTAVLALLSMTMTLSILTMTILFLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-227 9.09e-106

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 304.44  E-value: 9.09e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605   1 MNLTFFDQFMSPQTLGIPLIILALLTPSLMLPTQNNRWLTNRLSTLQLWAINLFTKQLMMPINKTGHKWSITLTSLMAML 80
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGVR 160
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2476356605 161 LTANLTAGHLLIQLTSTAVLALLSMTMTLSILTMTILFLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-227 8.86e-105

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 301.89  E-value: 8.86e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605   1 MNLTFFDQFMSPQTLGIPLIILALLTPSLMLPTQNNRWLTNRLSTLQLWAINLFTKQLMMPINKTGHKWSITLTSLMAML 80
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGVR 160
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2476356605 161 LTANLTAGHLLIQLTSTAVLALLSMTMTLSILTMTILFLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-226 7.86e-82

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 243.70  E-value: 7.86e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605   1 MNLTFFDQFMSPQTLGIPLIILALLTPSLMLPTQNNRWLTNRLSTLQLWAINLFTKQLMMPINKTGHKWSITLTSLMAML 80
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGVR 160
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2476356605 161 LTANLTAGHLLIQLTSTAVLALLSMTMTLSILTMTILFLLTILELAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00179  161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.56e-79

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 237.93  E-value: 1.56e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605   1 MNLTFFDQFMSPQTLGIPLIILALLTPSLMLPTqNNRWLTNRLSTLQLWAINLFTKQLMMPINKTGHKWSITLTSLMAML 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPT-PNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGVR 160
Cdd:MTH00101   80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2476356605 161 LTANLTAGHLLIQLTSTAVLALLSMTMTLSILTMTILFLLTILELAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00101  160 LTANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-227 3.84e-46

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 152.82  E-value: 3.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605   1 MNLTFFDQFMSPQTLGIPLIILAL-LTPSLMLPTQNNRWLTNRLSTLQLWAINLFTKQLMMPINKTGHKWSITLTSLMAM 79
Cdd:MTH00035    3 INNSIFGQFSPDTILFIPLTLLSSvIALSWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  80 LLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGV 159
Cdd:MTH00035   83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2476356605 160 RLTANLTAGHLLIQLTSTAVlALLSMTMTLSILTMTILFLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00035  163 RLAANLTAGHLLIFLLSTAI-WELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 19-227 3.19e-45

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: 150.43  E-value: 3.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  19 LIILALLTPSLMLPTQNNRWLTNRLSTLQLWAINLFTKQLMMPINKTGHKWSITLTSLMAMLLMINLLGLLPYTFTPTTQ 98
Cdd:TIGR01131  20 LILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  99 LSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAGHLLIQLTSTA 178
Cdd:TIGR01131 100 LSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2476356605 179 VLALLSMTMTLsiLTMTILFLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:TIGR01131 180 LFSLMSSAIFA--LLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 39-225 5.60e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 131.44  E-value: 5.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  39 LTNRLSTLQLWAINLFTKQLMMPINKTGHKWSITLTSLMAMLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGL 118
Cdd:MTH00157   38 IPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGW 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605 119 RNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAGHLLIQLTSTAVLALLSMTMTLSILTMTILF 198
Cdd:MTH00157  118 INNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLL 197

                         170       180
                  ....*....|....*....|....*..
gi 2476356605 199 lltILELAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00157  198 ---ILESAVAIIQSYVFSVLSTLYSSE 221
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 90-224 7.43e-35

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: 121.35  E-value: 7.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAGH 169
Cdd:cd00310    25 PYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGH 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2476356605 170 LLIQLTSTAVLALLSMTMTLSILtmtILFLLTILELAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310   105 LLLALLSGLVPSLLSSVGLLPLL---LPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-225 1.43e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 120.36  E-value: 1.43e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605   1 MNLTFFDQFMSPQTLGIPLIILALLTPSLMLPTQNNR--WLTNRLSTLQLWAINLFTKQLMMPINKTGHKWSITLTSLMA 78
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSSLSFLMWLLSLMSLFFFSSSvwVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  79 MLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALG 158
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2476356605 159 VRLTANLTAGHLLIQLTSTAVLALLSMTMTLSIL-TMTILFLLTILELAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYLSSSLFSSSVVSLLlVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 7.62e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 118.60  E-value: 7.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605   1 MNLTFFDQFMSPQTLGIPLIILALLTPSLMLPTQNNRW--LTNRLSTLQLWAINLFTKQLMMPINKTGHKWSITLTSLMA 78
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFSMISLSWITLLLFLLLMPSSVwfCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  79 MLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALG 158
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2476356605 159 VRLTANLTAGHLLIQLTSTAVLALLSMTMTLSILTMTILFLLTILELAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP-synt_A pfam00119
ATP synthase A chain;
90-224 7.92e-30

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 110.27  E-value: 7.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTS-LGHLLPEGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2476356605 169 HLLIQLTSTAVLALLSMTMTLSILTMTILFLLTILELAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 1-227 2.61e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 106.66  E-value: 2.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605   1 MNLTFFDQFMSPQTLGI--PLIILALLTPSLMLPTQNNRWLTNRLSTLQLWAINLFTKQLMMPINKTGHKWSITLTSLMA 78
Cdd:MTH00172    1 MSSSYFDQFNIVWLIGLtnSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  79 MLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALG 158
Cdd:MTH00172   81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2476356605 159 VRLTANLTAGHLLIQLTSTAVLALLSMTMTLSILTMTILFLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00172  161 VRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTI 229
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 6-222 3.52e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 103.66  E-value: 3.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605   6 FDQFMSPQTLGIPLIILALLTPSLMLPTQNNRWLT-NRLSTLQLWAINLFTKQLMMPINKTGHKWSITLTSLMAMLLMIN 84
Cdd:MTH00005    9 FDPATNSLFNNLSSTAFWAFNFSIILLLSSSFWITpNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  85 LLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGVRLTAN 164
Cdd:MTH00005   89 LSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAAN 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2476356605 165 LTAGHLLIQLTSTAVLALLSMTMTLSILTMTILFLLTILELAVAMIQAYVFVLLLSLY 222
Cdd:MTH00005  169 MSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 62-227 6.63e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 100.85  E-value: 6.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  62 INKTGHKWSITLTSLMAMLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPI 141
Cdd:MTH00175   75 LGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPF 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605 142 LIMIETISLFIRPLALGVRLTANLTAGHLLIQLTSTAVLALLSMTMT-LSILTMTILFLLTILELAVAMIQAYVFVLLLS 220
Cdd:MTH00175  155 LVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNGLIiLSLFPMLIMIFITLLEMAVAVIQAYVFCLLTT 234


                  ....*..
gi 2476356605 221 LYLQENI 227
Cdd:MTH00175  235 IYLGDTI 241
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 90-225 6.64e-21

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: 86.67  E-value: 6.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTS-LGHLLPEGTPtPLIPILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:COG0356    78 PGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAG 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2476356605 169 HLLIqltstAVLALLSMTMTLSILTMTILFLLTILELAVAMIQAYVFVLLLSLYLQE 225
Cdd:COG0356   157 HIIL-----LLLAGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 90-227 4.65e-19

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 82.68  E-value: 4.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAGH 169
Cdd:MTH00174  111 PYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGH 190

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2476356605 170 LLIQLTSTAVLALLSMTMTL-SILTMTILFLLTILELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00174  191 LLFSIIASFAWKMINTGILIgSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYLRDTV 249
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 91-225 1.74e-17

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 77.91  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  91 YTFTPTTQLSMNMGLAIPMWMATVLTGLRNQpttSLGHLLPEGTPTPlIPILIMIETISLFIRPLALGVRLTANLTAGHL 170
Cdd:PRK05815   95 LLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGEL 170

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2476356605 171 LIQLtstaVLALLSMTMTLSILTMTILFLLTILELAVAMIQAYVFVLLLSLYLQE 225
Cdd:PRK05815  171 ILAL----IALLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 90-223 1.01e-13

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 69.00  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAGH 169
Cdd:PRK13419  191 PYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAGH 270

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2476356605 170 LLI--------QLTSTAVLALLSMTMTLSILtmtilflltILELAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13419  271 IVIlslifisfILKSYIVAVAVSVPFAIFIY---------LLELFVAFLQAYIFTMLSALFI 323
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 94-223 2.03e-12

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 65.30  E-value: 2.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  94 TPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETI-SLFIRPLALGVRLTANLTAGHLLI 172
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2476356605 173 qltsTAVLALLSMTMTLSILTMTIL--FLLTILELAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13417  297 ----LALMGFIFQFQSWGIVPVSVIgsGLIYVLEIFVAFLQAYIFVLLTSLFV 345
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 90-225 6.05e-11

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 59.61  E-value: 6.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSlgHLLPEGTPTPLIP-ILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:MTH00087   72 PYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTfSMLFVEIVSELSRPLALTLRLTVNLMVG 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2476356605 169 HLLIQLtstavlaLLSMTMTLSILTMTILFlltiLELAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00087  150 HLISSL-------LNFLGEKYVWLSILAIM----MECFVAFIQSYIFSRLIYLYLNE 195
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 90-220 4.08e-04

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 39.87  E-value: 4.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2476356605  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQPTTSLGHLLPEGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAGh 169
Cdd:MTH00050   43 PYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLG- 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2476356605 170 lliqltSTAVLALLSMTMtLSILTMTILFLLTILELAVAMIQAYVFVLLLS 220
Cdd:MTH00050  122 ------CFGGVALGNLCF-ISYWWFLVLFFLFFYEVFVALVHWFIVSSILS 165
 
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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