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Conserved domains on  [gi|292486439|ref|YP_003541076|]
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ATP synthase F0 subunit 6 (mitochondrion) [triploid Megalobrama amblycephala x Xenocypris davidi]

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 3.42e-138

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177190  Cd Length: 227  Bit Score: 386.15  E-value: 3.42e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   1 MMTSFFDQFASPSFLGIPLIAIAIALPWLLFPTPSSRWINNRLITLQTWFINRFTNQLMMPLNVGGHKWALLLASLMVFL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  81 ITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 292486439 161 LTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-227 3.42e-138

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 386.15  E-value: 3.42e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   1 MMTSFFDQFASPSFLGIPLIAIAIALPWLLFPTPSSRWINNRLITLQTWFINRFTNQLMMPLNVGGHKWALLLASLMVFL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  81 ITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 292486439 161 LTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 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 ...
6-227 1.55e-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: 151.20  E-value: 1.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439    6 FDQFASPSF----LGIPLIAIAIALPWLLFPTPSSR-WINNRLITLQTWFINRFTNQLMMPLNVGGHKWALLLASLMVFL 80
Cdd:TIGR01131   2 FSQFDISPItlfsLTLLSLILLLSLLIFLISSSLSRwLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   81 ITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVR 160
Cdd:TIGR01131  82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 292486439  161 LTANLTAGHLLIQLIATAVFVLlpMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLLFSL--MSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
66-224 1.21e-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: 123.28  E-value: 1.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  66 GHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIII 145
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 292486439 146 ETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMmptVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
19-224 2.85e-30

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 111.43  E-value: 2.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   19 LIAIAIALPWLLFPTP-SSRWINNRLITLQTWFINRFTNQLMMPLNV-GGHKWALLLASLMVFLITINMLGLL---PYTF 93
Cdd:pfam00119   5 LIVALILLLFLLLATRkTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKkKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   94 TPTTQLSLNMGFAVPLWLATVIIGMRNQPTVA-LGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLI 172
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 292486439  173 QLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
66-225 8.02e-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: 86.28  E-value: 8.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  66 GHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVA-LGHLLPEGTPIPLIPVLII 144
Cdd:COG0356   54 GRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFPWLAPLMLPI 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439 145 iETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLpmmptVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:COG0356  134 -EIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLL-----LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYIS 207

                 .
gi 292486439 225 E 225
Cdd:COG0356  208 L 208
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-227 3.42e-138

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 386.15  E-value: 3.42e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   1 MMTSFFDQFASPSFLGIPLIAIAIALPWLLFPTPSSRWINNRLITLQTWFINRFTNQLMMPLNVGGHKWALLLASLMVFL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  81 ITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 292486439 161 LTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
1-227 3.60e-119

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 338.09  E-value: 3.60e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   1 MMTSFFDQFASPSFLGIPLIAIAIALPWLLFPTPSSRWINNRLITLQTWFINRFTNQLMMPLNVGGHKWALLLASLMVFL 80
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  81 ITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 292486439 161 LTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
1-227 1.63e-106

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 305.98  E-value: 1.63e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   1 MMTSFFDQFASPSFLGIPLIAIAIALPWLLFPTPSSRWINNRLITLQTWFINRFTNQLMMPLNVGGHKWALLLASLMVFL 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  81 ITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 292486439 161 LTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
1-227 1.38e-92

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 271.05  E-value: 1.38e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   1 MMTSFFDQFASPSFLGIPLIAIAIALPWLLFPTPSSRWINNRLITLQTWFINRFTNQLMMPLNVGGHKWALLLASLMVFL 80
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  81 ITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 292486439 161 LTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 2.48e-77

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 232.15  E-value: 2.48e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   1 MMTSFFDQFASPSFLGIPLIAIAIALPWLLFPTPSsRWINNRLITLQTWFINRFTNQLMMPLNVGGHKWALLLASLMVFL 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPN-RLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  81 ITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00101  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 292486439 161 LTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00101 160 LTANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
3-227 1.17e-48

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 159.37  E-value: 1.17e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   3 TSFFDQFASPSFLGIPL--IAIAIALPWLLFPTPSSrWINNRLITLQTWFINRFTNQLMMPLNVGGHKWALLLASLMVFL 80
Cdd:MTH00035   5 NSIFGQFSPDTILFIPLtlLSSVIALSWLFFINPTN-WLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  81 ITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00035  84 LSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLR 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 292486439 161 LTANLTAGHLLIQLIATAVFVLLPmMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00035 164 LAANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
6-227 1.55e-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: 151.20  E-value: 1.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439    6 FDQFASPSF----LGIPLIAIAIALPWLLFPTPSSR-WINNRLITLQTWFINRFTNQLMMPLNVGGHKWALLLASLMVFL 80
Cdd:TIGR01131   2 FSQFDISPItlfsLTLLSLILLLSLLIFLISSSLSRwLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   81 ITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVR 160
Cdd:TIGR01131  82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 292486439  161 LTANLTAGHLLIQLIATAVFVLlpMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLLFSL--MSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-225 3.30e-41

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 139.92  E-value: 3.30e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   1 MMTSFFDQFASPSFLGIPLIAIAIALPWLLFPtpSSRW-INNRLITLQTWFINRFTNQLMMPLNVGGHKWALLLASLMVF 79
Cdd:MTH00157   1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIP--SSFWlIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  80 LITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGV 159
Cdd:MTH00157  79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 292486439 160 RLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTaavLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00157 159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILI---QILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
1-226 5.43e-37

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 129.38  E-value: 5.43e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   1 MMTSFFDQFASPSFLGIPLIAIAIALPWL-LFPTPSSRWI-NNRLITLQTWFINRFTNQLMMPLNVGGHKWALLLASLMV 78
Cdd:MTH00176   1 MLVDLFSSFDPPNKNIFSMISLSWITLLLfLLLMPSSVWFcPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  79 FLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLALG 158
Cdd:MTH00176  81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 292486439 159 VRLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
66-224 1.21e-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: 123.28  E-value: 1.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  66 GHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIII 145
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 292486439 146 ETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMmptVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
4-225 3.16e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 119.59  E-value: 3.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   4 SFFDQFASPSFLGIPLIAIAIALPWLLFPTPSSrWINNRLITLQTWFINRFTNQLMMPLNVGGHKWALLLASLMVFLITI 83
Cdd:MTH00173   7 SSFDDHNSSFSSLSFLMWLLSLMSLFFFSSSVW-VSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  84 NMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVRLTA 163
Cdd:MTH00173  86 NLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLA 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 292486439 164 NLTAGHLLIQLIATAV-FVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00173 166 NISAGHIVLTLIGNYLsSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_A pfam00119
ATP synthase A chain;
19-224 2.85e-30

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 111.43  E-value: 2.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   19 LIAIAIALPWLLFPTP-SSRWINNRLITLQTWFINRFTNQLMMPLNV-GGHKWALLLASLMVFLITINMLGLL---PYTF 93
Cdd:pfam00119   5 LIVALILLLFLLLATRkTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKkKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   94 TPTTQLSLNMGFAVPLWLATVIIGMRNQPTVA-LGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLI 172
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 292486439  173 QLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
1-223 3.47e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 111.67  E-value: 3.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   1 MMTSFFDQFASPSFLGIP----LIAIAIALPWLLFPtpSSRWINNRLITLQTWFINRFTNQLMMPLNVGGHKWALLLASL 76
Cdd:MTH00172   1 MSSSYFDQFNIVWLIGLTnssiMMILVIIVVLLLFK--GIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  77 MVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLA 156
Cdd:MTH00172  79 FFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAIS 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 292486439 157 LGVRLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYL 223
Cdd:MTH00172 159 LGVRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYL 225
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
2-222 2.33e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 104.43  E-value: 2.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   2 MTSFFDQFASPSFLGIPLIAIAIalpwllfpTPSSRWI-NNRLITLQTWFINRFTNQLMMPLNVGGHKWALLLASLMVFL 80
Cdd:MTH00005  13 TNSLFNNLSSTAFWAFNFSIILL--------LSSSFWItPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  81 ITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00005  85 ILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFR 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 292486439 161 LTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLY 222
Cdd:MTH00005 165 LAANMSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
1-227 1.44e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 97.38  E-value: 1.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439   1 MMTSFFDQFASPSFLGIP---------------LIAIAIALPWLLFptpssrwINNRLITLQTWFINRFTNQLMMP---- 61
Cdd:MTH00175   1 MLAAYFDQFNIIRLITIQaflgdwlvtftnssmMMVLAVIIFWLLL-------KGDKLIPNRWQSIMELIYLNIRSvvhd 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  62 -LNVGGHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIP 140
Cdd:MTH00175  74 nLGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439 141 VLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPM-MPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLL 219
Cdd:MTH00175 154 FLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNgLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLT 233

                 ....*...
gi 292486439 220 SLYLQENV 227
Cdd:MTH00175 234 TIYLGDTI 241
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
66-225 8.02e-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: 86.28  E-value: 8.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  66 GHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVA-LGHLLPEGTPIPLIPVLII 144
Cdd:COG0356   54 GRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFPWLAPLMLPI 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439 145 iETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLpmmptVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:COG0356  134 -EIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLL-----LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYIS 207

                 .
gi 292486439 225 E 225
Cdd:COG0356  208 L 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
66-225 3.56e-18

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 79.84  E-value: 3.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  66 GHKWALLLASLMVFLITINMLGLLP-YTFTPTTQLSLNMGFAVPLWLATVIIGMRNQptvALGHLLPEGTPIPLIPVLII 144
Cdd:PRK05815  69 GKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQPHPLLLPI 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439 145 iETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAvlflLTLLEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:PRK05815 146 -EIISEFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILPVA----WTIFEIFVGTLQAYIFMMLTIVYIS 220

                 .
gi 292486439 225 E 225
Cdd:PRK05815 221 M 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
39-227 1.79e-16

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 75.75  E-value: 1.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  39 INNRLITLQTWFINRFTNQLMMPLNVGGHKWALLLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGM 118
Cdd:MTH00174  60 VPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGL 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439 119 RNQPTVALGHLLPEGTPIPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAVFVLLPMMPTV-AILTAAVL 197
Cdd:MTH00174 140 ITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPFAIL 219
                        170       180       190
                 ....*....|....*....|....*....|
gi 292486439 198 FLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00174 220 IFVTILEMAVAIIQAYVFTLLTIVYLRDTV 249
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
73-223 7.82e-14

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 69.39  E-value: 7.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  73 LASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETISLFI 152
Cdd:PRK13419 174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGTHWSLWIIMIPIEFIGLFT 253
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 292486439 153 RPLALGVRLTANLTAGHLLIQLIATAVFVLLPMMPTVAILTAAVLFLLtLLEVAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13419 254 KPFALTVRLFANMTAGHIVILSLIFISFILKSYIVAVAVSVPFAIFIY-LLELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
75-225 1.75e-09

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 55.37  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  75 SLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQptVALGHLLP-EGTPIPLIPVLIIIETISLFIR 153
Cdd:MTH00087  57 FTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKS--EKFSVYLSkGSDSFLKTFSMLFVEIVSELSR 134
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 292486439 154 PLALGVRLTANLTAGHLLIQLIATAVFVLLPMMptvailtaavlFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00087 135 PLALTLRLTVNLMVGHLISSLLNFLGEKYVWLS-----------ILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
94-223 1.63e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 47.96  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  94 TPTTQLSLNMGFAVPLWLATVIIGMRNQPTVALGHLLPEGTPIPLIPVLIIIETI-SLFIRPLALGVRLTANLTAGHLLI 172
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 292486439 173 qlIATAVFVLLPMMPTVAILTAAVLFLLTLLEVAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13417 297 --LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
72-223 5.42e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 37.03  E-value: 5.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292486439  72 LLASLMVFLITINMLGLLPYTFTPTTQLSLNMGFAVPLWLATVIIGMRNQPTVA-LGHLLpegtpiPLIPVLIIIETISL 150
Cdd:PRK13420  77 FVGTLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEGLREyLKHYL------SPSPFLLPFHLISE 150
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 292486439 151 FIRPLALGVRLTANLTAghllIQLIATAVFVLLPMMPTVAILtaavlflltLLEVAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13420 151 ITRTLALAVRLFGNIMS----LELAALLVLLVAGFLVPVPIL---------MLHIIEALVQAYIFGMLALIYI 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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