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Conserved domains on  [gi|50404157|gb|AAT76825|]
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ATP synthase subunit 6 (mitochondrion) [Pyrilia pulchra]

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 7.67e-102

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177190  Cd Length: 227  Bit Score: 294.47  E-value: 7.67e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157    1 MILTFFDQFSSPYFLGIPLTLLSMLLPPLLFPTPNNRWITNRLSTLQLSLINTTTKQLMTPLNKPGHKWAIILTSLMMLL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   81 LTTNLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50404157  161 LTANLTAGHLLIQLISTAAITLLPIMPAVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-227 7.67e-102

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 294.47  E-value: 7.67e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157    1 MILTFFDQFSSPYFLGIPLTLLSMLLPPLLFPTPNNRWITNRLSTLQLSLINTTTKQLMTPLNKPGHKWAIILTSLMMLL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   81 LTTNLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50404157  161 LTANLTAGHLLIQLISTAAITLLPIMPAVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQENI 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 ...
35-227 8.82e-46

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: 151.59  E-value: 8.82e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157    35 NNRWITNRLSTLQLSLINTTTKQLMTPLNKPGHKWAIILTSLMMLLLTTNLLGLLPYTFTPTTQLSMNMALAFPLWLATL 114
Cdd:TIGR01131  36 SRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLT 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   115 LTGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVRLTANLTAGHLLIQLISTAAITLlpIMPAVSILTI 194
Cdd:TIGR01131 116 ISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSL--MSSAIFALLL 193
                         170       180       190
                  ....*....|....*....|....*....|...
gi 50404157   195 TVLFLLTMLELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:TIGR01131 194 LILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
90-224 3.36e-36

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: 124.82  E-value: 3.36e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157  90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVRLTANLTAGH 169
Cdd:cd00310  25 PYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGH 104
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 50404157 170 LLIQLISTAAITLLPImpaVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310 105 LLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
90-224 1.17e-31

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 114.89  E-value: 1.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157    90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTIC-LGHLLPEGTPTPLVPALILIETISLFIRPLALGVRLTANLTAG 168
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 50404157   169 HLLIQLISTAAITLLPIMPAVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
90-225 3.25e-20

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: 84.74  E-value: 3.25e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157  90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTIC-LGHLLPEGTPtPLVPALILIETISLFIRPLALGVRLTANLTAG 168
Cdd:COG0356  78 PGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAG 156
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 50404157 169 HLLIqlistAAITLLPIMPAVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQE 225
Cdd:COG0356 157 HIIL-----LLLAGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-227 7.67e-102

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 294.47  E-value: 7.67e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157    1 MILTFFDQFSSPYFLGIPLTLLSMLLPPLLFPTPNNRWITNRLSTLQLSLINTTTKQLMTPLNKPGHKWAIILTSLMMLL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   81 LTTNLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50404157  161 LTANLTAGHLLIQLISTAAITLLPIMPAVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
1-227 1.06e-99

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 289.03  E-value: 1.06e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157    1 MILTFFDQFSSPYFLGIPLTLLSMLLPPLLFPTPNNRWITNRLSTLQLSLINTTTKQLMTPLNKPGHKWAIILTSLMMLL 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   81 LTTNLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50404157  161 LTANLTAGHLLIQLISTAAITLLPIMPAVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
1-227 1.57e-95

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 278.39  E-value: 1.57e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157    1 MILTFFDQFSSPYFLGIPLTLLSMLLPPLLFPTPNNRWITNRLSTLQLSLINTTTKQLMTPLNKPGHKWAIILTSLMMLL 80
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   81 LTTNLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVR 160
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50404157  161 LTANLTAGHLLIQLISTAAITLLPIMPAVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
1-226 1.41e-79

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 237.92  E-value: 1.41e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157    1 MILTFFDQFSSPYFLGIPLTLLSMLLPPLLFPTPNNRWITNRLSTLQLSLINTTTKQLMTPLNKPGHKWAIILTSLMMLL 80
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   81 LTTNLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVR 160
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50404157  161 LTANLTAGHLLIQLISTAAITLLPIMPAVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
36-226 3.00e-67

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 206.34  E-value: 3.00e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   36 NRWITNRLSTLQLSLINTTTKQLMTPLNKPGHKWAIILTSLMMLLLTTNLLGLLPYTFTPTTQLSMNMALAFPLWLATLL 115
Cdd:MTH00101  35 NRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157  116 TGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVRLTANLTAGHLLIQLISTAAITLLPIMPAVSILTIT 195
Cdd:MTH00101 115 TGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLALMSISTTTALITFI 194
                        170       180       190
                 ....*....|....*....|....*....|.
gi 50404157  196 VLFLLTMLELAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00101 195 ILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
35-227 8.82e-46

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: 151.59  E-value: 8.82e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157    35 NNRWITNRLSTLQLSLINTTTKQLMTPLNKPGHKWAIILTSLMMLLLTTNLLGLLPYTFTPTTQLSMNMALAFPLWLATL 114
Cdd:TIGR01131  36 SRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLT 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   115 LTGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVRLTANLTAGHLLIQLISTAAITLlpIMPAVSILTI 194
Cdd:TIGR01131 116 ISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSL--MSSAIFALLL 193
                         170       180       190
                  ....*....|....*....|....*....|...
gi 50404157   195 TVLFLLTMLELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:TIGR01131 194 LILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
6-227 3.62e-42

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 142.42  E-value: 3.62e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157    6 FDQFSSPYFLGIPLTLLSMLLPPL-LFPTPNNRWITNRLSTLQLSLINTTTKQLMTPLNKPGHKWAIILTSLMMLLLTTN 84
Cdd:MTH00035   8 FGQFSPDTILFIPLTLLSSVIALSwLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILILSIN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   85 LLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVRLTAN 164
Cdd:MTH00035  88 VLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRLAAN 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50404157  165 LTAGHLLIQLISTaAITLLPIMPAVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00035 168 LTAGHLLIFLLST-AIWELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
39-225 7.18e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 136.45  E-value: 7.18e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   39 ITNRLSTLQLSLINTTTKQLMTPLNKPGHKWAIILTSLMMLLLTTNLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGL 118
Cdd:MTH00157  38 IPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGW 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157  119 RNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVRLTANLTAGHLLIQLISTAAITLLPIMpavSILTITVLF 198
Cdd:MTH00157 118 INNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSSMI---LSILILIQI 194
                        170       180
                 ....*....|....*....|....*..
gi 50404157  199 LLTMLELAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00157 195 LLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
90-224 3.36e-36

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: 124.82  E-value: 3.36e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157  90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVRLTANLTAGH 169
Cdd:cd00310  25 PYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGH 104
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 50404157 170 LLIQLISTAAITLLPImpaVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310 105 LLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
90-226 1.41e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 125.53  E-value: 1.41e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVRLTANLTAGH 169
Cdd:MTH00176  92 PYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLAVRLAANLSAGH 171
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 50404157  170 LLIQLISTAAITLLPIMPAVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00176 172 LLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP-synt_A pfam00119
ATP synthase A chain;
90-224 1.17e-31

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 114.89  E-value: 1.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157    90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTIC-LGHLLPEGTPTPLVPALILIETISLFIRPLALGVRLTANLTAG 168
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 50404157   169 HLLIQLISTAAITLLPIMPAVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
90-225 2.14e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 114.58  E-value: 2.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVRLTANLTAGH 169
Cdd:MTH00173  92 PFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGH 171
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 50404157  170 LLIQLI-STAAITLLPIMPAVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00173 172 IVLTLIgNYLSSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
38-222 3.22e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 109.05  E-value: 3.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   38 WIT-NRLSTLQLSLINTTTKQLMTPLNKPGHKWAIILTSLMMLLLTTNLLGLLPYTFTPTTQLSMNMALAFPLWLATLLT 116
Cdd:MTH00005  41 WITpNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMS 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157  117 GLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVRLTANLTAGHLLIQLISTAAITLLPIMPAVSILTITV 196
Cdd:MTH00005 121 SVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGIYAASALFSSISSTILLILT 200
                        170       180
                 ....*....|....*....|....*.
gi 50404157  197 LFLLTMLELAVAMIQAYVFVLLLSLY 222
Cdd:MTH00005 201 QMGYILFEVGICLIQAYIFCLLLSLY 226
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
90-227 4.23e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 100.89  E-value: 4.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVRLTANLTAGH 169
Cdd:MTH00172  92 PYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGH 171
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 50404157  170 LLIQLISTAAITLLPIMPAVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00172 172 LLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTI 229
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
90-227 7.28e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 98.16  E-value: 7.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVRLTANLTAGH 169
Cdd:MTH00175 103 PYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGH 182
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 50404157  170 LLIQLISTAAITLLPI-MPAVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00175 183 LLFAILSGFAFNMLSNgLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGDTI 241
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
90-225 3.25e-20

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: 84.74  E-value: 3.25e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157  90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTIC-LGHLLPEGTPtPLVPALILIETISLFIRPLALGVRLTANLTAG 168
Cdd:COG0356  78 PGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAG 156
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 50404157 169 HLLIqlistAAITLLPIMPAVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQE 225
Cdd:COG0356 157 HIIL-----LLLAGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
91-225 1.78e-18

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 80.61  E-value: 1.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   91 YTFTPTTQLSMNMALAFPLWLATLLTGLRNQPticLGHLLPEGTPTPlVPALILIETISLFIRPLALGVRLTANLTAGHL 170
Cdd:PRK05815  95 LLFPPTADINVTLALALIVFVLVIYYGIKKKG---LGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGEL 170
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 50404157  171 LIQLISTAAITLLPIMPAVSILTItvlfLLTMLELAVAMIQAYVFVLLLSLYLQE 225
Cdd:PRK05815 171 ILALIALLGGAGLLLALAPLILPV----AWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
90-227 5.34e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 79.98  E-value: 5.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTICLGHLLPEGTPTPLVPALILIETISLFIRPLALGVRLTANLTAGH 169
Cdd:MTH00174 111 PYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGH 190
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 50404157  170 LLIQLISTAAITLLPIMPAV-SILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00174 191 LLFSIIASFAWKMINTGILIgSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYLRDTV 249
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
90-225 5.94e-13

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 65.00  E-value: 5.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQptICLGHLLPEGTPTPLVP-ALILIETISLFIRPLALGVRLTANLTAG 168
Cdd:MTH00087  72 PYSFSPCGMVEFTFLYALVAWLSTFLSFLSKS--EKFSVYLSKGSDSFLKTfSMLFVEIVSELSRPLALTLRLTVNLMVG 149
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 50404157  169 HLLIQLISTaaitllpimpaVSILTITVLFLLTMLELAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00087 150 HLISSLLNF-----------LGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
90-223 8.51e-12

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 63.61  E-value: 8.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTicLGHL--LPEGTPTPLVPALILIETISLFIRPLALGVRLTANLTA 167
Cdd:PRK13419 191 PYGATATGNINVTLTLAVFTFFITQYAAIKAHGI--KGYLahLTGGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTA 268
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 50404157  168 GHLLI-QLISTAAITLLPIM-PAVSILTITVLFLltmLELAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13419 269 GHIVIlSLIFISFILKSYIVaVAVSVPFAIFIYL---LELFVAFLQAYIFTMLSALFI 323
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
94-223 3.55e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 58.75  E-value: 3.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   94 TPTTQLSMNMALAFPLWLATLLTGLRNQPTICLGHLLPEGTPTPLVPALILIETI-SLFIRPLALGVRLTANLTAGHLLI 172
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 50404157  173 qlisTAAITLLPIMPAVSILTITVL--FLLTMLELAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13417 297 ----LALMGFIFQFQSWGIVPVSVIgsGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
86-218 6.59e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 36.60  E-value: 6.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50404157   86 LGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPTicLGHLLPEGTPTPLVPALILIETISlfiRPLALGVRLTANL 165
Cdd:PRK13421  94 SSLVPGVEPPTAHLETDAALALIVFLATIYYGVRARGV--RGYLATFAEPTWVMIPLNLVEQLT---RTFSLIVRLFGNV 168
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 50404157  166 TAGHLLIQLISTAAITLLPIMpavsiltitvlflLTMLELAVAMIQAYVFVLL 218
Cdd:PRK13421 169 MSGVFVIGIVLSLAGLLVPIP-------------LMALDLLTGAVQAYIFAVL 208
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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