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Conserved domains on  [gi|110082723|ref|YP_665488|]
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ATP synthase F0 subunit 6 (mitochondrion) [Agamermis sp. BH-2006]

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 ...
 14-174 8.85e-27

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 MTH00087:

Pssm-ID: 469762  Cd Length: 195  Bit Score: 100.05  E-value: 8.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  14 FSMLPMILVFVALMFMSYKLKNKIIYTIVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFwsSHMLPI 93
Cdd:MTH00087  35 FGLLIIVFSYSNKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKF--SVYLSK 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  94 GSPLFLWSF-LVILELLSQMIRPLTLSLRLTCNLMTGHVMLSLI--MSSKHMILFLFVIMlFEMCVAVIQSVVFNLLLDS 170
Cdd:MTH00087 113 GSDSFLKTFsMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLLnfLGEKYVWLSILAIM-MECFVAFIQSYIFSRLIYL 191


                 ....
gi 110082723 171 YKFE 174
Cdd:MTH00087 192 YLNE 195
 
Name Accession Description Interval E-value
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 14-174 8.85e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 100.05  E-value: 8.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  14 FSMLPMILVFVALMFMSYKLKNKIIYTIVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFwsSHMLPI 93
Cdd:MTH00087  35 FGLLIIVFSYSNKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKF--SVYLSK 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  94 GSPLFLWSF-LVILELLSQMIRPLTLSLRLTCNLMTGHVMLSLI--MSSKHMILFLFVIMlFEMCVAVIQSVVFNLLLDS 170
Cdd:MTH00087 113 GSDSFLKTFsMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLLnfLGEKYVWLSILAIM-MECFVAFIQSYIFSRLIYL 191


                 ....
gi 110082723 171 YKFE 174
Cdd:MTH00087 192 YLNE 195
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 41-171 4.51e-21

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: 83.99  E-value: 4.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  41 IVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFWSSHMLPIGSPLFLWSFLVILELLSQMIRPLTLSL 120
Cdd:cd00310   15 ILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSV 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723 121 RLTCNLMTGHVMLSLIMS---------SKHMILFLFVIMLFEMCVAVIQSVVFNLLLDSY 171
Cdd:cd00310   95 RLFANMFAGHLLLALLSGlvpsllssvGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVY 154
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 41-171 1.95e-16

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: 73.78  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723   41 IVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFWSSHMLPIGSPLFLWSFLVILELLSQMIRPLTLSL 120
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110082723  121 RLTCNLMTGHVMLSLI----------MSSKHMILFLFVIMLFEMCVAVIQSVVFNLLLDSY 171
Cdd:TIGR01131 161 RLFANISAGHLLLTLLsgllfslmssAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLY 221
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 41-167 3.75e-12

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: 61.63  E-value: 3.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  41 IVMLNMLGLIPEFWSPTSYLWGNMLMGFFTW--MLYSMNKIFNNFKFWSSHMLPigSPLFLWSFLVILELLSQMIRPLTL 118
Cdd:COG0356   68 ILVSNLLGLIPGLFPPTADINVTLALALIVFvlVHYYGIKKKGLGGYLKHLFFP--PFPWLAPLMLPIEIISELARPLSL 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 110082723 119 SLRLTCNLMTGHVMLSLI-------MSSKHMILFLFVIMLFEMCVAVIQSVVFNLL 167
Cdd:COG0356  146 SLRLFGNMFAGHIILLLLaglapflLLGVLSLLLPVAWTAFELLVGFLQAYIFTML 201
ATP-synt_A pfam00119
ATP synthase A chain;
41-171 9.55e-11

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 57.88  E-value: 9.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723   41 IVMLNMLGLI---PEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNN-FKFWSSHMLPIGSPLFLWSFLVILELLSQMIRPL 116
Cdd:pfam00119  68 ILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPV 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110082723  117 TLSLRLTCNLMTGHVMLSLIMSSKHM------------ILFLFVIMLFEMCVAVIQSVVFNLLLDSY 171
Cdd:pfam00119 148 SLSLRLFGNMLAGHLLLLLLAGLIFAllsagfllgvipPLLGVAWTLFELLVAFIQAYVFTMLTAVY 214
 
Name Accession Description Interval E-value
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 14-174 8.85e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 100.05  E-value: 8.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  14 FSMLPMILVFVALMFMSYKLKNKIIYTIVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFwsSHMLPI 93
Cdd:MTH00087  35 FGLLIIVFSYSNKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKF--SVYLSK 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  94 GSPLFLWSF-LVILELLSQMIRPLTLSLRLTCNLMTGHVMLSLI--MSSKHMILFLFVIMlFEMCVAVIQSVVFNLLLDS 170
Cdd:MTH00087 113 GSDSFLKTFsMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLLnfLGEKYVWLSILAIM-MECFVAFIQSYIFSRLIYL 191


                 ....
gi 110082723 171 YKFE 174
Cdd:MTH00087 192 YLNE 195
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 41-171 4.51e-21

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: 83.99  E-value: 4.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  41 IVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFWSSHMLPIGSPLFLWSFLVILELLSQMIRPLTLSL 120
Cdd:cd00310   15 ILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSV 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723 121 RLTCNLMTGHVMLSLIMS---------SKHMILFLFVIMLFEMCVAVIQSVVFNLLLDSY 171
Cdd:cd00310   95 RLFANMFAGHLLLALLSGlvpsllssvGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVY 154
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 37-171 1.63e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 76.70  E-value: 1.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  37 IIYTIVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFWSSHMLPIGSPLFLWSFLVILELLSQMIRPL 116
Cdd:MTH00005  80 LFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPI 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110082723 117 TLSLRLTCNLMTGHVMLSLI------------MSSKHMILFLFVIMLFEMCVAVIQSVVFNLLLDSY 171
Cdd:MTH00005 160 TLSFRLAANMSAGHIVLSLIgiyaasalfssiSSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 9-168 3.93e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 75.20  E-value: 3.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723   9 SLNLSFSMLPMILVFVALMFMsyklknkiiytIVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFWSS 88
Cdd:MTH00157  58 KTLLGPKNKGSTLIFISLFSF-----------ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFA 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  89 HMLPIGSPLFLWSFLVILELLSQMIRPLTLSLRLTCNLMTGHVMLSLI-----MSSKHMILFLFVI----MLFEMCVAVI 159
Cdd:MTH00157 127 HLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLgntgpSLSSMILSILILIqillLILESAVAII 206


                 ....*....
gi 110082723 160 QSVVFNLLL 168
Cdd:MTH00157 207 QSYVFSVLS 215
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 41-171 1.95e-16

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: 73.78  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723   41 IVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFWSSHMLPIGSPLFLWSFLVILELLSQMIRPLTLSL 120
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110082723  121 RLTCNLMTGHVMLSLI----------MSSKHMILFLFVIMLFEMCVAVIQSVVFNLLLDSY 171
Cdd:TIGR01131 161 RLFANISAGHLLLTLLsgllfslmssAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLY 221
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-171 3.33e-16

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 73.14  E-value: 3.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723   1 MILMSPFHSLNLSFSMLPMILVFVALMFmsyklknKIIYTIVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIF 80
Cdd:MTH00176  49 MLMFSTFLPEMILRSNGSYILGSASIII-------SLFILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFI 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  81 NNFKFWSSHMLPIGSPLFLWSFLVILELLSQMIRPLTLSLRLTCNLMTGHVMLSL------------IMSSKHMILFLFV 148
Cdd:MTH00176 122 NNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLAVRLAANLSAGHLLLGLlgaamwgllpvsPLIGFLLLIVQIL 201

                        170       180
                 ....*....|....*....|...
gi 110082723 149 IMLFEMCVAVIQSVVFNLLLDSY 171
Cdd:MTH00176 202 YFMFEIAVCMIQAYVFTLLLSLY 224
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 12-171 4.39e-16

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 72.67  E-value: 4.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  12 LSFSMLPMILVFVALMFMsyklknkiiytIVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFWSSHML 91
Cdd:MTH00179  62 INKKGHKWAVLFLSLMLF-----------LLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLL 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  92 PIGSPLFLWSFLVILELLSQMIRPLTLSLRLTCNLMTGHVMLSLIMSSKHMI------------LFLFVIMLFEMCVAVI 159
Cdd:MTH00179 131 PEGTPTPLIPMLVWIETISLLIRPLALGVRLTANITAGHLLMHLISSAVFVLmnfmgmvalltlLVLFLLTLLEVAVAMI 210

                        170
                 ....*....|..
gi 110082723 160 QSVVFNLLLDSY 171
Cdd:MTH00179 211 QAYVFVLLLSLY 222
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 40-168 3.51e-15

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 70.28  E-value: 3.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  40 TIVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFWSSHMLPIGSPLFLWSFLVILELLSQMIRPLTLS 119
Cdd:MTH00173  81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110082723 120 LRLTCNLMTGHVMLSLI-------------MSSKHMILFLFVIMLFEMCVAVIQSVVFNLLL 168
Cdd:MTH00173 161 VRLLANISAGHIVLTLIgnylssslfsssvVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLI 222
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 38-171 5.26e-15

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 69.85  E-value: 5.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  38 IYTIVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFWSSHMLPIGSPLFLWSFLVILELLSQMIRPLT 117
Cdd:MTH00120  77 MLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLA 156

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110082723 118 LSLRLTCNLMTGHVMLSLIMS------------SKHMILFLFVIMLFEMCVAVIQSVVFNLLLDSY 171
Cdd:MTH00120 157 LGVRLTANLTAGHLLIQLISTatlnllptmptlSLLTLIILLLLTILELAVAMIQAYVFVLLLSLY 222
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 25-171 8.52e-15

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 69.13  E-value: 8.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  25 ALMFMSYKLknkiiyTIVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFWSSHMLPIGSPLFLWSFLV 104
Cdd:MTH00132  70 ALLLTSLML------FLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLI 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110082723 105 ILELLSQMIRPLTLSLRLTCNLMTGHVMLSLIMSSKHMIL------------FLFVIMLFEMCVAVIQSVVFNLLLDSY 171
Cdd:MTH00132 144 IIETISLFIRPLALGVRLTANLTAGHLLIQLIATAAFVLLplmptvailtatLLFLLTLLEVAVAMIQAYVFVLLLSLY 222
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 41-171 1.79e-13

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 65.77  E-value: 1.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  41 IVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFWSSHMLPIGSPLFLWSFLVILELLSQMIRPLTLSL 120
Cdd:MTH00035  83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110082723 121 RLTCNLMTGHVMLSL------IMSSKHMI-----LFLFVIMLFEMCVAVIQSVVFNLLLDSY 171
Cdd:MTH00035 163 RLAANLTAGHLLIFLlstaiwELSNSPLIsiitlIIFFLLFILEIGVACIQAYVFTALVHFY 224
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 25-171 2.61e-13

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 65.36  E-value: 2.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  25 ALMFMSyklknkIIYTIVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFWSSHMLPIGSPLFLWSFLV 104
Cdd:MTH00101  69 SLMLMS------LILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLV 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723 105 ILELLSQMIRPLTLSLRLTCNLMTGHVMLSLI------MSSKHM--------ILFLFVIMlfEMCVAVIQSVVFNLLLDS 170
Cdd:MTH00101 143 IIETISLFIQPMALAVRLTANITAGHLLIHLIggatlaLMSISTttalitfiILILLTIL--EFAVALIQAYVFTLLVSL 220


                 .
gi 110082723 171 Y 171
Cdd:MTH00101 221 Y 221
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 41-171 2.01e-12

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 62.68  E-value: 2.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  41 IVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFWSSHMLPIGSPLFLWSFLVILELLSQMIRPLTLSL 120
Cdd:MTH00073  80 LITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGV 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110082723 121 RLTCNLMTGHVMLSLIMSSKHMILF------------LFVIMLFEMCVAVIQSVVFNLLLDSY 171
Cdd:MTH00073 160 RLTANLTAGHLLIQLISTATLVLLPlmptvsiltmivLFLLTLLEIAVAMIQAYVFVLLLSLY 222
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 41-167 3.75e-12

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: 61.63  E-value: 3.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  41 IVMLNMLGLIPEFWSPTSYLWGNMLMGFFTW--MLYSMNKIFNNFKFWSSHMLPigSPLFLWSFLVILELLSQMIRPLTL 118
Cdd:COG0356   68 ILVSNLLGLIPGLFPPTADINVTLALALIVFvlVHYYGIKKKGLGGYLKHLFFP--PFPWLAPLMLPIEIISELARPLSL 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 110082723 119 SLRLTCNLMTGHVMLSLI-------MSSKHMILFLFVIMLFEMCVAVIQSVVFNLL 167
Cdd:COG0356  146 SLRLFGNMFAGHIILLLLaglapflLLGVLSLLLPVAWTAFELLVGFLQAYIFTML 201
ATP-synt_A pfam00119
ATP synthase A chain;
41-171 9.55e-11

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 57.88  E-value: 9.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723   41 IVMLNMLGLI---PEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNN-FKFWSSHMLPIGSPLFLWSFLVILELLSQMIRPL 116
Cdd:pfam00119  68 ILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPV 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110082723  117 TLSLRLTCNLMTGHVMLSLIMSSKHM------------ILFLFVIMLFEMCVAVIQSVVFNLLLDSY 171
Cdd:pfam00119 148 SLSLRLFGNMLAGHLLLLLLAGLIFAllsagfllgvipPLLGVAWTLFELLVAFIQAYVFTMLTAVY 214
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 41-171 5.62e-10

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 56.20  E-value: 5.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  41 IVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFWSSHMLPIGSPLFLWSFLVILELLSQMIRPLTLSL 120
Cdd:MTH00172  82 IVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGV 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110082723 121 RLTCNLMTGHVML--------SLIMSSKHMILFLFVIMLF----EMCVAVIQSVVFNLLLDSY 171
Cdd:MTH00172 162 RLAANLSAGHLLFailagfgfNMLCASGFLSLFPLLIMVFitllEIAVAVIQAYVFCLLTTIY 224
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 41-167 6.31e-10

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 56.17  E-value: 6.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  41 IVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFWSSHMLPIGSPLFLWSFLVILELLSQMIRPLTLSL 120
Cdd:MTH00175  93 IAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGV 172

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723 121 RLTCNLMTGHVMLS-------------LIMSSKHMILFLFVIMLFEMCVAVIQSVVFNLL 167
Cdd:MTH00175 173 RLAANISAGHLLFAilsgfafnmlsngLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLL 232
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 41-167 1.20e-07

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 49.41  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  41 IVMLNMLGLIPEFW-SPTSYLWGNMLMGFFTWMLYSMNKIFNN-FKFWSSHMLPIGSPlflwsFLVILELLSQMIRPLTL 118
Cdd:PRK05815  83 ILLMNLLGLIPYLLfPPTADINVTLALALIVFVLVIYYGIKKKgLGGYLKEFYLQPHP-----LLLPIEIISEFSRPISL 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 110082723 119 SLRLTCNLMTGHVMLSLIMSSKHMILFLF--------VIMLFEMCVAVIQSVVFNLL 167
Cdd:PRK05815 158 SLRLFGNMLAGELILALIALLGGAGLLLAlaplilpvAWTIFEIFVGTLQAYIFMML 214
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 41-171 4.12e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 42.62  E-value: 4.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  41 IVMLNMLGLIPEFWSPTSYLWGNMLMGFFTWMLYSMNKIFNNFKFWSSHMLPIGSPLFLWSFLVILELLSQMIRPLTLSL 120
Cdd:MTH00174 101 ILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGV 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110082723 121 RLTCNLMTGHVMLSLIMSSKHMIL-------------FLFVIMLFEMCVAVIQSVVFNLLLDSY 171
Cdd:MTH00174 181 RLAANISSGHLLFSIIASFAWKMIntgiligsfvpfaILIFVTILEMAVAIIQAYVFTLLTIVY 244
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 76-159 3.54e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 36.40  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110082723  76 MNKIFNNFKFWSSHMLPIGSPLFLWSFLVILELLSQMIRPLTLSLRLTCNL----MTGHVMLSLIMSSKHMILFLFVIML 151
Cdd:MTH00050  68 LSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINIslgcFGGVALGNLCFISYWWFLVLFFLFF 147


                 ....*...
gi 110082723 152 FEMCVAVI 159
Cdd:MTH00050 148 YEVFVALV 155
 
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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