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Conserved domains on  [gi|189067753|dbj|BAG38251|]
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ATPase 6, partial (mitochondrion) [Takifugu sp. O1]

Protein Classification

FoF1 ATP synthase subunit a( domain architecture ID 116)

FoF1 ATP synthase subunit a is part of the membrane proton channel (Fo complex) of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane; it plays a direct role in the translocation of protons across the membrane

Gene Ontology:  GO:0045263|GO:0015078|GO:0015986
PubMed:  11533110|12370007|30901262

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP-synt_Fo_a_6 super family cl00413
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 1-102 9.35e-61

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.


The actual alignment was detected with superfamily member MTH00132:

Pssm-ID: 469762  Cd Length: 227  Bit Score: 184.69  E-value: 9.35e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:MTH00132  91 YTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTAGHL 170

                         90       100
                 ....*....|....*....|..
gi 189067753  81 LIQLIATAAFVLLPLMPTVAIL 102
Cdd:MTH00132 171 LIQLIATAAFVLLPLMPTVAIL 192
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-102 9.35e-61

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 184.69  E-value: 9.35e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:MTH00132  91 YTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTAGHL 170

                         90       100
                 ....*....|....*....|..
gi 189067753  81 LIQLIATAAFVLLPLMPTVAIL 102
Cdd:MTH00132 171 LIQLIATAAFVLLPLMPTVAIL 192
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 1-102 2.14e-29

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: 104.60  E-value: 2.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753    1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:TIGR01131  92 YSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHL 171

                          90       100
                  ....*....|....*....|..
gi 189067753   81 LIQLIATAAFVLLPLMPTVAIL 102
Cdd:TIGR01131 172 LLTLLSGLLFSLMSSAIFALLL 193
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 1-102 8.60e-26

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: 93.62  E-value: 8.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:cd00310   26 YSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGHL 105

                         90       100
                 ....*....|....*....|..
gi 189067753  81 LIQLIATAAFVLLPLMPTVAIL 102
Cdd:cd00310  106 LLALLSGLVPSLLSSVGLLPLL 127
ATP-synt_A pfam00119
ATP synthase A chain;
1-102 1.53e-20

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 81.38  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753    1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAA-LGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGH 79
Cdd:pfam00119  82 GGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGH 161

                          90       100
                  ....*....|....*....|...
gi 189067753   80 LLIQLIATAAFVLLPLMPTVAIL 102
Cdd:pfam00119 162 LLLLLLAGLIFALLSAGFLLGVI 184
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 1-101 1.00e-13

FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 63.55  E-value: 1.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAA-LGHLLPEGTPnALIPILIIIETVSLFIRPLALGVRLTANLTAGH 79
Cdd:COG0356   79 GLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGH 157

                         90       100
                 ....*....|....*....|..
gi 189067753  80 LLIQLIATAAFVLLPLMPTVAI 101
Cdd:COG0356  158 IILLLLAGLAPFLLLGVLSLLL 179
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-102 9.35e-61

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 184.69  E-value: 9.35e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:MTH00132  91 YTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTAGHL 170

                         90       100
                 ....*....|....*....|..
gi 189067753  81 LIQLIATAAFVLLPLMPTVAIL 102
Cdd:MTH00132 171 LIQLIATAAFVLLPLMPTVAIL 192
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-102 1.67e-53

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 166.30  E-value: 1.67e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:MTH00073  91 YTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVRLTANLTAGHL 170

                         90       100
                 ....*....|....*....|..
gi 189067753  81 LIQLIATAAFVLLPLMPTVAIL 102
Cdd:MTH00073 171 LIQLISTATLVLLPLMPTVSIL 192
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-102 1.37e-49

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 156.52  E-value: 1.37e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:MTH00120  91 YTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVRLTANLTAGHL 170

                         90       100
                 ....*....|....*....|..
gi 189067753  81 LIQLIATAAFVLLPLMPTVAIL 102
Cdd:MTH00120 171 LIQLISTATLNLLPTMPTLSLL 192
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-102 9.60e-46

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 146.63  E-value: 9.60e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:MTH00179  91 YTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVRLTANITAGHL 170

                         90       100
                 ....*....|....*....|..
gi 189067753  81 LIQLIATAAFVLLPLMPTVAIL 102
Cdd:MTH00179 171 LMHLISSAVFVLMNFMGMVALL 192
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-102 1.35e-37

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 125.83  E-value: 1.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:MTH00101  90 HSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGHL 169

                         90       100
                 ....*....|....*....|..
gi 189067753  81 LIQLIATAAFVLLPLMPTVAIL 102
Cdd:MTH00101 170 LIHLIGGATLALMSISTTTALI 191
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 1-102 2.14e-29

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: 104.60  E-value: 2.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753    1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:TIGR01131  92 YSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHL 171

                          90       100
                  ....*....|....*....|..
gi 189067753   81 LIQLIATAAFVLLPLMPTVAIL 102
Cdd:TIGR01131 172 LLTLLSGLLFSLMSSAIFALLL 193
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-85 3.59e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 104.09  E-value: 3.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:MTH00157  90 YIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGHL 169


                 ....*
gi 189067753  81 LIQLI 85
Cdd:MTH00157 170 LLTLL 174
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-92 1.05e-27

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 100.43  E-value: 1.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:MTH00035  94 YAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRLAANLTAGHL 173

                         90
                 ....*....|..
gi 189067753  81 LIQLIATAAFVL 92
Cdd:MTH00035 174 LIFLLSTAIWEL 185
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-97 4.34e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 96.26  E-value: 4.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:MTH00176  93 YVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLAVRLAANLSAGHL 172

                         90
                 ....*....|....*..
gi 189067753  81 LIQLIATAAFVLLPLMP 97
Cdd:MTH00176 173 LLGLLGAAMWGLLPVSP 189
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 1-102 8.60e-26

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: 93.62  E-value: 8.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:cd00310   26 YSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGHL 105

                         90       100
                 ....*....|....*....|..
gi 189067753  81 LIQLIATAAFVLLPLMPTVAIL 102
Cdd:cd00310  106 LLALLSGLVPSLLSSVGLLPLL 127
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-86 6.71e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 93.39  E-value: 6.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:MTH00173  93 FVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHI 172


                 ....*.
gi 189067753  81 LIQLIA 86
Cdd:MTH00173 173 VLTLIG 178
ATP-synt_A pfam00119
ATP synthase A chain;
1-102 1.53e-20

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 81.38  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753    1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAA-LGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGH 79
Cdd:pfam00119  82 GGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGH 161

                          90       100
                  ....*....|....*....|...
gi 189067753   80 LLIQLIATAAFVLLPLMPTVAIL 102
Cdd:pfam00119 162 LLLLLLAGLIFALLSAGFLLGVI 184
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-89 6.59e-20

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 80.16  E-value: 6.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:MTH00005  95 YVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHI 174


                 ....*....
gi 189067753  81 LIQLIATAA 89
Cdd:MTH00005 175 VLSLIGIYA 183
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 1-93 8.10e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 72.00  E-value: 8.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:MTH00172  93 YVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHL 172

                         90
                 ....*....|...
gi 189067753  81 LIQLIATAAFVLL 93
Cdd:MTH00172 173 LFAILAGFGFNML 185
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 1-93 3.92e-14

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 65.03  E-value: 3.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:MTH00175 104 YVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHL 183

                         90
                 ....*....|...
gi 189067753  81 LIQLIATAAFVLL 93
Cdd:MTH00175 184 LFAILSGFAFNML 196
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 1-101 1.00e-13

FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 63.55  E-value: 1.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAA-LGHLLPEGTPnALIPILIIIETVSLFIRPLALGVRLTANLTAGH 79
Cdd:COG0356   79 GLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGH 157

                         90       100
                 ....*....|....*....|..
gi 189067753  80 LLIQLIATAAFVLLPLMPTVAI 101
Cdd:COG0356  158 IILLLLAGLAPFLLLGVLSLLL 179
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 1-102 2.05e-11

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 57.50  E-value: 2.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNptaALGHLLPEGTPNaLIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:PRK05815  95 LLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQ-PHPLLLPIEIISEFSRPISLSLRLFGNMLAGEL 170

                         90       100
                 ....*....|....*....|..
gi 189067753  81 LIQLIATAAFVLLPLMPTVAIL 102
Cdd:PRK05815 171 ILALIALLGGAGLLLALAPLIL 192
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 1-93 7.14e-11

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 56.49  E-value: 7.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:MTH00174 112 YVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHL 191

                         90
                 ....*....|...
gi 189067753  81 LIQLIATAAFVLL 93
Cdd:MTH00174 192 LFSIIASFAWKMI 204
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 1-85 9.91e-09

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 49.98  E-value: 9.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNptAALGHLLPEGTPNALIP-ILIIIETVSLFIRPLALGVRLTANLTAGH 79
Cdd:MTH00087  73 YSFSPCGMVEFTFLYALVAWLSTFLSFLSKS--EKFSVYLSKGSDSFLKTfSMLFVEIVSELSRPLALTLRLTVNLMVGH 150


                 ....*.
gi 189067753  80 LLIQLI 85
Cdd:MTH00087 151 LISSLL 156
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 1-92 1.61e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 50.13  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   1 YTFTPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIETVSLFIRPLALGVRLTANLTAGHL 80
Cdd:PRK13419 192 YGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAGHI 271

                         90
                 ....*....|..
gi 189067753  81 LIQLIATAAFVL 92
Cdd:PRK13419 272 VILSLIFISFIL 283
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 4-82 1.06e-05

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 42.18  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067753   4 TPTTQLSVNMALAVPLWLATVIIGMRNNPTAALGHLLPEGTPNALIPILIIIE-TVSLFIRPLALGVRLTANLTAGHLLI 82
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEfIVSPMAKTFALTVRLLANMTAGHVII 296
 
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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