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Conserved domains on  [gi|1916859047|gb|QOL00807|]
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ATP synthase F0 subunit 6 (mitochondrion) [Yunnanites coriacea]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009593)

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 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 1.71e-46

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 153.40  E-value: 1.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047   1 MMTNLFSTFDPSTdIFILSLNWTSTFIGLLLIPSLFWLTPSRINLMWNKLNLNLYNDFFTLFVvPSFNGTTFIFFFSIFI 80
Cdd:MTH00157    1 MMTNLFSIFDPST-SFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLG-PKNKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047  81 MMFFNFFLGFSSFFFSSSRFVVFLLIALPMWLSFMLFLWIFNTKLKLAHLVPQGAPLAVLFFMVfLVAIISIILRP-TML 159
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMV-LIETISNLIRPgTLA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1916859047 160 VRLAANMIAGHLLLTLLGNTGTSISINMMTILIISQMLLLMLESAVALIQAYVFSILSILYSSESH 225
Cdd:MTH00157  158 VRLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 1.71e-46

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 153.40  E-value: 1.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047   1 MMTNLFSTFDPSTdIFILSLNWTSTFIGLLLIPSLFWLTPSRINLMWNKLNLNLYNDFFTLFVvPSFNGTTFIFFFSIFI 80
Cdd:MTH00157    1 MMTNLFSIFDPST-SFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLG-PKNKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047  81 MMFFNFFLGFSSFFFSSSRFVVFLLIALPMWLSFMLFLWIFNTKLKLAHLVPQGAPLAVLFFMVfLVAIISIILRP-TML 159
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMV-LIETISNLIRPgTLA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1916859047 160 VRLAANMIAGHLLLTLLGNTGTSISINMMTILIISQMLLLMLESAVALIQAYVFSILSILYSSESH 225
Cdd:MTH00157  158 VRLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 104-222 2.39e-12

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: 62.42  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047 104 LLIALPMWLSFMLFLWIFNTKLKLAHLVPQGAPLAVLFFMVFLvAIISIILRP-TMLVRLAANMIAGHLLLTLLGNTGTS 182
Cdd:cd00310    38 LALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI-ELISELIRPlSLSVRLFANMFAGHLLLALLSGLVPS 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1916859047 183 ISINMMTILIISQMLLLMLESAVALIQAYVFSILSILYSS 222
Cdd:cd00310   117 LLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-224 3.46e-12

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: 63.38  E-value: 3.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047   5 LFSTFDPSTDIFI-LSLNWTSTFIGLLLIPSLFWLTPSRINLMWNKLNLNLYNDFFTLFVVPSFNGTTFIFFFSIFIMMF 83
Cdd:TIGR01131   1 LFSQFDISPITLFsLTLLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047  84 FNFFLGFSSFFFSSSR---FVVFLLIALPMWLSFMLFLWIFNTKLKLAHLVPQGAPLAVLFFMVfLVAIISIILRPTML- 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPtshLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLV-IIETISYLARPISLs 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1916859047 160 VRLAANMIA-GHLLLTLLGNTGTSISINMMTILIISQMLLLMLESAVALIQAYVFSILSILYSSES 224
Cdd:TIGR01131 160 VRLFANISAgHLLLTLLSGLLFSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 136-225 1.89e-04

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: 41.21  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047 136 PLAVLFFMVFLVAIISIILRP-TMLVRLAANMIAGHLLLTLLGNTGTSISINMMTILIisQMLLLMLESAVALIQAYVFS 214
Cdd:COG0356   122 PFPWLAPLMLPIEIISELARPlSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFT 199

                          90
                  ....*....|.
gi 1916859047 215 ILSILYSSESH 225
Cdd:COG0356   200 MLTAVYISLAV 210
ATP-synt_A pfam00119
ATP synthase A chain;
106-222 2.66e-04

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 40.55  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047 106 IALPMWLSFMLFLWIFNTKLK-------LAHLVPQGAPLAVLFFMvFLVAIISIILRP-TMLVRLAANMIA---GHLLLT 174
Cdd:pfam00119  90 INVTLALALIVFLLVHYYGIKkhglggyFKKLFVPPVPLPLVPLL-LPIEIISEFARPvSLSLRLFGNMLAghlLLLLLA 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1916859047 175 LLGNTGTSISINMMTILIISQMLLLMLESAVALIQAYVFSILSILYSS 222
Cdd:pfam00119 169 GLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 1.71e-46

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 153.40  E-value: 1.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047   1 MMTNLFSTFDPSTdIFILSLNWTSTFIGLLLIPSLFWLTPSRINLMWNKLNLNLYNDFFTLFVvPSFNGTTFIFFFSIFI 80
Cdd:MTH00157    1 MMTNLFSIFDPST-SFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLG-PKNKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047  81 MMFFNFFLGFSSFFFSSSRFVVFLLIALPMWLSFMLFLWIFNTKLKLAHLVPQGAPLAVLFFMVfLVAIISIILRP-TML 159
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMV-LIETISNLIRPgTLA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1916859047 160 VRLAANMIAGHLLLTLLGNTGTSISINMMTILIISQMLLLMLESAVALIQAYVFSILSILYSSESH 225
Cdd:MTH00157  158 VRLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-223 5.63e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 87.40  E-value: 5.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047   1 MMTNLFSTFDPSTDIFI--LSLNWTSTFIGLLLIPSLFWLTPSRINLMWNKLNlNLYNDFFTLFVVPSFNGTTFIFFFSI 78
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFsmISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFS-TFLPEMILRSNGSYILGSASIIISLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047  79 FIMMFFNFFLGFSSFFFSSSRFVVFLLIALPMWLSFMLFLWIFNTKLKLAHLVPQGAPLAVLFFMVFLVAIISIILRPTM 158
Cdd:MTH00176   80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1916859047 159 LVRLAANMIA---GHLLLTLLGNTGTSISINMMTILIISQMLLLMLESAVALIQAYVFSILSILYSSE 223
Cdd:MTH00176  160 AVRLAANLSAghlLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDE 227
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-223 7.48e-16

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 73.61  E-value: 7.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047   1 MMTNLFSTFDPSTDIFILSLN----WTSTFIGLLLIPSLFWLTPSRINLMWNKLnLNLYNDFFTLFVVPSFNGTTFIFFF 76
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFNNLSstafWAFNFSIILLLSSSFWITPNRLSSIMSPP-KSTMHTQLSRTFGKHLKGFSSLISA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047  77 SIFIMMFFNFFLGFSSFFFSSSRFVVFLLIALPMWLSFMLFLWIFNTKLKLAHLVPQGAPLAVLFFMVfLVAIISIILRP 156
Cdd:MTH00005   80 LFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLV-LIETISILVRP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1916859047 157 -TMLVRLAANMIAGHLLLTLLGNTGTSI---SINMMTILIISQMLLLMLESAVALIQAYVFSILSILYSSE 223
Cdd:MTH00005  159 iTLSFRLAANMSAGHIVLSLIGIYAASAlfsSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-224 1.36e-12

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 64.50  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047   1 MMTNLFSTFDPSTDIFIL--SLNWTSTFIGLLLIPSLFWLTPSRINLMWNKLnLNLYNDFFTLFVVPSFNGTTFIFFFSI 78
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSSlsFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLF-VLTVSSQVTRSSGLNLGGFSLLLSSLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047  79 FIMMFFNFFLGFSSFFFSSSRFVVFLLIALPMWLSFMLFLWIFNTKLKLAHLVPQGAPLAVLFFMVfLVAIISIILRP-T 157
Cdd:MTH00173   80 LFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLV-LIETVSILIRPlT 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1916859047 158 MLVRLAANMIA----GHLLLTLLGNTGTSISINMMTILIISQMLLLMLESAVALIQAYVFSILSILYSSES 224
Cdd:MTH00173  159 LTVRLLANISAghivLTLIGNYLSSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDEH 229
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 104-222 2.39e-12

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: 62.42  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047 104 LLIALPMWLSFMLFLWIFNTKLKLAHLVPQGAPLAVLFFMVFLvAIISIILRP-TMLVRLAANMIAGHLLLTLLGNTGTS 182
Cdd:cd00310    38 LALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI-ELISELIRPlSLSVRLFANMFAGHLLLALLSGLVPS 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1916859047 183 ISINMMTILIISQMLLLMLESAVALIQAYVFSILSILYSS 222
Cdd:cd00310   117 LLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-224 3.46e-12

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: 63.38  E-value: 3.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047   5 LFSTFDPSTDIFI-LSLNWTSTFIGLLLIPSLFWLTPSRINLMWNKLNLNLYNDFFTLFVVPSFNGTTFIFFFSIFIMMF 83
Cdd:TIGR01131   1 LFSQFDISPITLFsLTLLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047  84 FNFFLGFSSFFFSSSR---FVVFLLIALPMWLSFMLFLWIFNTKLKLAHLVPQGAPLAVLFFMVfLVAIISIILRPTML- 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPtshLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLV-IIETISYLARPISLs 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1916859047 160 VRLAANMIA-GHLLLTLLGNTGTSISINMMTILIISQMLLLMLESAVALIQAYVFSILSILYSSES 224
Cdd:TIGR01131 160 VRLFANISAgHLLLTLLSGLLFSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 104-220 1.51e-10

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 58.81  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047 104 LLIALPMWLSFMLFLWIFNTKLKLAHLVPQGAPLAvLFFMVFLVAIISIILRPTML-VRLAANMIA---GHLLLTLLGNT 179
Cdd:MTH00101  102 LGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTP-LIPMLVIIETISLFIQPMALaVRLTANITAghlLIHLIGGATLA 180

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1916859047 180 GTSISINMMTILIISQMLLLMLESAVALIQAYVFSILSILY 220
Cdd:MTH00101  181 LMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 3-223 2.42e-08

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 52.67  E-value: 2.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047   3 TNLFSTFDPSTdIFILSLNWTSTFIGL---LLIPSLFWLtPSRINLMWNKLNLNLYNDFFTLFVvPSFNGTTFIFFFSIF 79
Cdd:MTH00035    5 NSIFGQFSPDT-ILFIPLTLLSSVIALswlFFINPTNWL-PSRSQSIWLTFRQEILKLIFQNTN-PNTAPWAGLLTTVFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047  80 IMMFFNFFLGFSSFFFSSSRFVVFLLIALPMWLSFMLFLWIFNTKLKLAHLVPQGAPLAVLFFMVfLVAIISIILRPTML 159
Cdd:MTH00035   82 LILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMV-WIETLSLFAQPIAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1916859047 160 -VRLAANMIAGHLLLTLLGNTGTSISINMM--TILIISQMLLLMLESAVALIQAYVFSILSILYSSE 223
Cdd:MTH00035  161 gLRLAANLTAGHLLIFLLSTAIWELSNSPLisIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 104-223 1.13e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 50.72  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047 104 LLIALPMWLSFMLFLWIFNTKLKLAHLVPQGAPLAVLFFMVfLVAIISIILRPTML-VRLAANMIAGHLLLTLLGNTGTS 182
Cdd:MTH00179  103 LGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLV-WIETISLLIRPLALgVRLTANITAGHLLMHLISSAVFV 181

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1916859047 183 ISINMMTILIISQ---MLLLMLESAVALIQAYVFSILSILYSSE 223
Cdd:MTH00179  182 LMNFMGMVALLTLlvlFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 106-223 1.95e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 49.82  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047 106 IALPMWLSFMLFLWIFNTKLKLAHLVPQGAPLAVLFFMVfLVAIISIILRPTML-VRLAANMIA-------GHLLLTLLG 177
Cdd:MTH00120  105 LAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALI-LIETISLLIRPLALgVRLTANLTAghlliqlISTATLNLL 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1916859047 178 NTGTSISINMMTILiisqMLLLMLESAVALIQAYVFSILSILYSSE 223
Cdd:MTH00120  184 PTMPTLSLLTLIIL----LLLTILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 106-224 1.14e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 47.56  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047 106 IALPMWLSFMLFLWIFNTKLKLAHLVPQGAPLAvLFFMVFLVAIISIILRPTML-VRLAANMIAGHLLLTLLGNTGTSIS 184
Cdd:MTH00132  105 LAVPLWLATVIIGMRNQPTHALGHLLPEGTPTP-LIPVLIIIETISLFIRPLALgVRLTANLTAGHLLIQLIATAAFVLL 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1916859047 185 INMMTILIISQMLLLM---LESAVALIQAYVFSILSILYSSES 224
Cdd:MTH00132  184 PLMPTVAILTATLLFLltlLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 104-223 1.44e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 44.57  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047 104 LLIALPMWLSFMLFLWIFNTKLKLAHLVPQGAPlAVLFFMVFLVAIISIILRPTML-VRLAANMIAGHLLLTLLGNTGTS 182
Cdd:MTH00073  103 LGLAVPLWLATVLIGLRNQPTASLGHLLPEGTP-TLLIPILIIIETISLFIRPLALgVRLTANLTAGHLLIQLISTATLV 181

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1916859047 183 ISINMMTILIISQMLLL---MLESAVALIQAYVFSILSILYSSE 223
Cdd:MTH00073  182 LLPLMPTVSILTMIVLFlltLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 127-220 3.59e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 43.46  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047 127 LAHLVPQGAPLAVLFFMVFLVAIISIILRPTMLVRLAANMIAGHLLLTLLGNTGTSISINMMTILIISQMLLLM----LE 202
Cdd:MTH00175  139 LSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNGLIILSLFPMLIMIfitlLE 218

                          90
                  ....*....|....*...
gi 1916859047 203 SAVALIQAYVFSILSILY 220
Cdd:MTH00175  219 MAVAVIQAYVFCLLTTIY 236
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 136-225 1.89e-04

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: 41.21  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047 136 PLAVLFFMVFLVAIISIILRP-TMLVRLAANMIAGHLLLTLLGNTGTSISINMMTILIisQMLLLMLESAVALIQAYVFS 214
Cdd:COG0356   122 PFPWLAPLMLPIEIISELARPlSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFT 199

                          90
                  ....*....|.
gi 1916859047 215 ILSILYSSESH 225
Cdd:COG0356   200 MLTAVYISLAV 210
ATP-synt_A pfam00119
ATP synthase A chain;
106-222 2.66e-04

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 40.55  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047 106 IALPMWLSFMLFLWIFNTKLK-------LAHLVPQGAPLAVLFFMvFLVAIISIILRP-TMLVRLAANMIA---GHLLLT 174
Cdd:pfam00119  90 INVTLALALIVFLLVHYYGIKkhglggyFKKLFVPPVPLPLVPLL-LPIEIISEFARPvSLSLRLFGNMLAghlLLLLLA 168

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1916859047 175 LLGNTGTSISINMMTILIISQMLLLMLESAVALIQAYVFSILSILYSS 222
Cdd:pfam00119 169 GLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 127-220 2.02e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 38.72  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916859047 127 LAHLVPQGAPLAVLFFMVFLVAIISIILRPTML-VRLAANMIAGHLLLTLLG-NTGTSISINMMTILIISQMLLLMLESA 204
Cdd:PRK13417  249 IWHSVPNGVPLLLYPIMWPLEFIVSPMAKTFALtVRLLANMTAGHVIILALMgFIFQFQSWGIVPVSVIGSGLIYVLEIF 328

                          90
                  ....*....|....*.
gi 1916859047 205 VALIQAYVFSILSILY 220
Cdd:PRK13417  329 VAFLQAYIFVLLTSLF 344
 
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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