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Conserved domains on  [gi|558478186|gb|AHA52575|]
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ATP synthase F0 subunit 6 (mitochondrion) [Triraphis sp. QL-2013]

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
 3-222 1.01e-63

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 197.31  E-value: 1.01e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186   3 MMLNLFSIFDFYTFF--FTNWVSSLLCLILIPQIYWLMNSRYIYLIDKFINLLWMEFLVIMvNKYNLNNLFYFIVLFIMI 80
Cdd:MTH00157   1 MMTNLFSIFDPSTSFnlSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLL-GPKNKGSTLIFISLFSFI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  81 MFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLSNLIRPMTLCIR 160
Cdd:MTH00157  80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 558478186 161 LTANMIAGHLLLTLLSSFIP--SFYLYLIIFLLQLLLLLLEIGVSLIQSYVFVILMILYFKETN 222
Cdd:MTH00157 160 LAANMIAGHLLLTLLGNTGPslSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 3-222 1.01e-63

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 197.31  E-value: 1.01e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186   3 MMLNLFSIFDFYTFF--FTNWVSSLLCLILIPQIYWLMNSRYIYLIDKFINLLWMEFLVIMvNKYNLNNLFYFIVLFIMI 80
Cdd:MTH00157   1 MMTNLFSIFDPSTSFnlSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLL-GPKNKGSTLIFISLFSFI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  81 MFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLSNLIRPMTLCIR 160
Cdd:MTH00157  80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 558478186 161 LTANMIAGHLLLTLLSSFIP--SFYLYLIIFLLQLLLLLLEIGVSLIQSYVFVILMILYFKETN 222
Cdd:MTH00157 160 LAANMIAGHLLLTLLGNTGPslSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 70-219 9.13e-31

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: 110.57  E-value: 9.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  70 LFYFIVLFIMIMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLS 149
Cdd:cd00310    5 LPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELIS 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 558478186 150 NLIRPMTLCIRLTANMIAGHLLLTLLSSFIPSFYLYLIIFLLQLLLLLLEIG--VSLIQSYVFVILMILYFK 219
Cdd:cd00310   85 ELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLElfVAFIQAYVFTLLTAVYIS 156
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 8-220 1.25e-30

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: 112.30  E-value: 1.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186    8 FSIFDFYTFFFTNWVSSLLCLILIPQIYWLMNSRYIYLIDKFINLLwMEFLVIMVNKYNLNNLFYFIVLFIMIMFNNFMG 87
Cdd:TIGR01131  10 ITLFSLTLLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFV-LSIVKSQIGGKKGKFFPLIFTLFLFILISNLLG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186   88 LFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLSNLIRPMTLCIRLTANMIA 167
Cdd:TIGR01131  89 LIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISA 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 558478186  168 GHLLLTLLSSFIPSFYLYLIIFLLQLLLLLLE---IGVSLIQSYVFVILMILYFKE 220
Cdd:TIGR01131 169 GHLLLTLLSGLLFSLMSSAIFALLLLILVALIileIFVAFIQAYVFTLLTCLYLND 224
ATP-synt_A pfam00119
ATP synthase A chain;
72-219 4.45e-18

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 79.07  E-value: 4.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186   72 YFIVLFIMIMFNNFMGLF---PYIFTSSSHLVFSMIFSLSVWLGLMFYGWIEN-TNHMLIHLVPQGTPFMLMFFMVFIES 147
Cdd:pfam00119  60 LLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEI 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558478186  148 LSNLIRPMTLCIRLTANMIAGHLLLTLLSSFIPSFYLYLIIFLLQLLLLLLEI-----GVSLIQSYVFVILMILYFK 219
Cdd:pfam00119 140 ISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWtlfelLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 72-218 1.75e-17

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: 77.42  E-value: 1.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  72 YFIVLFIMIMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIEN-TNHMLIHLVPQGTPFMlMFFMVFIESLSN 150
Cdd:COG0356   60 LLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPWL-APLMLPIEIISE 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558478186 151 LIRPMTLCIRLTANMIAGHLLLTLLSSFIPSFYLYLIIFLLQLLLLLLEIGVSLIQSYVFVILMILYF 218
Cdd:COG0356  139 LARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 3-222 1.01e-63

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 197.31  E-value: 1.01e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186   3 MMLNLFSIFDFYTFF--FTNWVSSLLCLILIPQIYWLMNSRYIYLIDKFINLLWMEFLVIMvNKYNLNNLFYFIVLFIMI 80
Cdd:MTH00157   1 MMTNLFSIFDPSTSFnlSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLL-GPKNKGSTLIFISLFSFI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  81 MFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLSNLIRPMTLCIR 160
Cdd:MTH00157  80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 558478186 161 LTANMIAGHLLLTLLSSFIP--SFYLYLIIFLLQLLLLLLEIGVSLIQSYVFVILMILYFKETN 222
Cdd:MTH00157 160 LAANMIAGHLLLTLLGNTGPslSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 3-220 1.35e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 117.83  E-value: 1.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186   3 MMLNLFSIFDF-----YTFFFTNWVSSLLCLILIPQIYWLMNSRYIYLIDKFINLLwMEFLVIMVNKYNLNNLFYFIVLF 77
Cdd:MTH00176   1 MLVDLFSSFDPpnkniFSMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFL-PEMILRSNGSYILGSASIIISLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  78 IMIMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLSNLIRPMTL 157
Cdd:MTH00176  80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558478186 158 CIRLTANMIAGHLLLTLLSSFIP-----SFYLYLIIFLLQLLLLLLEIGVSLIQSYVFVILMILYFKE 220
Cdd:MTH00176 160 AVRLAANLSAGHLLLGLLGAAMWgllpvSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDE 227
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 70-219 9.13e-31

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: 110.57  E-value: 9.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  70 LFYFIVLFIMIMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLS 149
Cdd:cd00310    5 LPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELIS 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 558478186 150 NLIRPMTLCIRLTANMIAGHLLLTLLSSFIPSFYLYLIIFLLQLLLLLLEIG--VSLIQSYVFVILMILYFK 219
Cdd:cd00310   85 ELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLElfVAFIQAYVFTLLTAVYIS 156
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 8-220 1.25e-30

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: 112.30  E-value: 1.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186    8 FSIFDFYTFFFTNWVSSLLCLILIPQIYWLMNSRYIYLIDKFINLLwMEFLVIMVNKYNLNNLFYFIVLFIMIMFNNFMG 87
Cdd:TIGR01131  10 ITLFSLTLLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFV-LSIVKSQIGGKKGKFFPLIFTLFLFILISNLLG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186   88 LFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLSNLIRPMTLCIRLTANMIA 167
Cdd:TIGR01131  89 LIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISA 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 558478186  168 GHLLLTLLSSFIPSFYLYLIIFLLQLLLLLLE---IGVSLIQSYVFVILMILYFKE 220
Cdd:TIGR01131 169 GHLLLTLLSGLLFSLMSSAIFALLLLILVALIileIFVAFIQAYVFTLLTCLYLND 224
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 3-221 1.97e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 101.48  E-value: 1.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186   3 MMLNLFSIFD-----FYTFFFTNWVSSLLCLILIPQIYWLMNSRYIYLIDKFINLLWMEFLVIMVNKYNLNNLFYFIvLF 77
Cdd:MTH00173   1 MMVDLFSSFDdhnssFSSLSFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSS-LF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  78 IMIMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLSNLIRPMTL 157
Cdd:MTH00173  80 LFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186 158 CIRLTANMIAGHLLLTLLSSFIPSFYLYLIIFLLQLLLLLLE------IGVSLIQSYVFVILMILYFKET 221
Cdd:MTH00173 160 TVRLLANISAGHIVLTLIGNYLSSSLFSSSVVSLLLVLLIQVgyfifeVAVMLIQAYIFTLLIKLYSDEH 229
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 3-220 4.69e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 98.10  E-value: 4.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186   3 MMLNLFSIFD---FYTFFFTNWVSSLLCLILIPQIYWLMNSRYIYLIDKFINLLWMEFLVIMVNKYNLNNLFyFIVLFIM 79
Cdd:MTH00179   1 MMLSMFDQFEspsLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVL-FLSLMLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  80 IMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLSNLIRPMTLCI 159
Cdd:MTH00179  80 LLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 558478186 160 RLTANMIAGHLLLTLLSS-----FIPSFYLYLIIFLLQLLLLLLEIGVSLIQSYVFVILMILYFKE 220
Cdd:MTH00179 160 RLTANITAGHLLMHLISSavfvlMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 3-220 6.58e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 97.59  E-value: 6.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186   3 MMLNLFSIFDFYTFFFtnwVSSLLCLILIPQIYW------LMNSRYIYLIDKFINLLwMEFLVIMVNKYNLNNLFYFIVL 76
Cdd:MTH00120   1 MNLNFFDQFSSPELLG---IPLILLAMLIPALLIpspknrLLTNRLTTLQLWLIKLI-TKQLMLPLNKKGHKWALILTSL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  77 FIMIMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLSNLIRPMT 156
Cdd:MTH00120  77 MLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 558478186 157 LCIRLTANMIAGHLLLTLLSS----FIPSFYLYLIIFLLQLLLLLLE-IGVSLIQSYVFVILMILYFKE 220
Cdd:MTH00120 157 LGVRLTANLTAGHLLIQLISTatlnLLPTMPTLSLLTLIILLLLTILeLAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-220 9.77e-24

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 94.65  E-value: 9.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186   1 MSMMLNLFSIFDFYTFFFT--NWVSSLLCL---ILIPQIYWLmNSRYIYLIDKFINLLWmEFLVIMVNKYNLNNLFYFIV 75
Cdd:MTH00035   1 MIINNSIFGQFSPDTILFIplTLLSSVIALswlFFINPTNWL-PSRSQSIWLTFRQEIL-KLIFQNTNPNTAPWAGLLTT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  76 LFIMIMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLSNLIRPM 155
Cdd:MTH00035  79 VFILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPI 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 558478186 156 TLCIRLTANMIAGHLLLTLLSS----FIPSFYLYLIIFLLQLLLLLLEIGVSLIQSYVFVILMILYFKE 220
Cdd:MTH00035 159 ALGLRLAANLTAGHLLIFLLSTaiweLSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 3-217 1.30e-23

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 94.41  E-value: 1.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186   3 MMLNLFSIFDFYTFFFTNWVSSLL-------CLILIPQIYWLMNSRYIYLIDKFINLlwMEFLVIMVNKYNLNNLFYFIV 75
Cdd:MTH00005   1 MLTDIFSSFDPATNSLFNNLSSTAfwafnfsIILLLSSSFWITPNRLSSIMSPPKST--MHTQLSRTFGKHLKGFSSLIS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  76 -LFIMIMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLSNLIRP 154
Cdd:MTH00005  79 aLFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRP 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558478186 155 MTLCIRLTANMIAGHLLLTLL-----SSFIPSFYLYLIIFLLQLLLLLLEIGVSLIQSYVFVILMILY 217
Cdd:MTH00005 159 ITLSFRLAANMSAGHIVLSLIgiyaaSALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 73-220 8.70e-20

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 83.77  E-value: 8.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  73 FIVLFIMIMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLSNLI 152
Cdd:MTH00132  73 LTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFI 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 558478186 153 RPMTLCIRLTANMIAGHLLLTLLSSfiPSFYLYLII-------FLLQLLLLLLEIGVSLIQSYVFVILMILYFKE 220
Cdd:MTH00132 153 RPLALGVRLTANLTAGHLLIQLIAT--AAFVLLPLMptvailtATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 74-217 4.06e-18

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 79.61  E-value: 4.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  74 IVLFIMIMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLSNLIR 153
Cdd:MTH00101  73 MSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQ 152

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 558478186 154 PMTLCIRLTANMIAGHLLLTLLSSFI-----PSFYLYLIIFLLQLLLLLLEIGVSLIQSYVFVILMILY 217
Cdd:MTH00101 153 PMALAVRLTANITAGHLLIHLIGGATlalmsISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP-synt_A pfam00119
ATP synthase A chain;
72-219 4.45e-18

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 79.07  E-value: 4.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186   72 YFIVLFIMIMFNNFMGLF---PYIFTSSSHLVFSMIFSLSVWLGLMFYGWIEN-TNHMLIHLVPQGTPFMLMFFMVFIES 147
Cdd:pfam00119  60 LLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEI 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 558478186  148 LSNLIRPMTLCIRLTANMIAGHLLLTLLSSFIPSFYLYLIIFLLQLLLLLLEI-----GVSLIQSYVFVILMILYFK 219
Cdd:pfam00119 140 ISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWtlfelLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 71-220 1.61e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 78.08  E-value: 1.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  71 FYFIVLFIMIMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLSN 150
Cdd:MTH00073  71 LILTSLMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISL 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 558478186 151 LIRPMTLCIRLTANMIAGHLLLTLLSSFIPSFYLYLIIFLLQLLLLLLE-----IGVSLIQSYVFVILMILYFKE 220
Cdd:MTH00073 151 FIRPLALGVRLTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLltlleIAVAMIQAYVFVLLLSLYLQE 225
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 72-218 1.75e-17

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: 77.42  E-value: 1.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  72 YFIVLFIMIMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIEN-TNHMLIHLVPQGTPFMlMFFMVFIESLSN 150
Cdd:COG0356   60 LLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPWL-APLMLPIEIISE 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558478186 151 LIRPMTLCIRLTANMIAGHLLLTLLSSFIPSFYLYLIIFLLQLLLLLLEIGVSLIQSYVFVILMILYF 218
Cdd:COG0356  139 LARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 70-221 4.56e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 76.97  E-value: 4.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  70 LFYFIVLFIMIMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIESLS 149
Cdd:MTH00175  83 FPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLS 162

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558478186 150 NLIRPMTLCIRLTANMIAGHLLLTLLSSFIPS------FYLYLIIFLLQLLLLLLEIGVSLIQSYVFVILMILYFKET 221
Cdd:MTH00175 163 YLIRAISLGVRLAANISAGHLLFAILSGFAFNmlsnglIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGDT 240
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 49-221 7.46e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 76.23  E-value: 7.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  49 FINLLWMEFLVIMVNKYNLNNLFYF---IVLFIMIMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHM 125
Cdd:MTH00172  48 IIEIIYNHFHGVVKDNLGNEGLKYFpfiISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186 126 LIHLVPQGTPFMLMFFMVFIESLSNLIRPMTLCIRLTANMIAGHLLLTLLSSFI-----PSFYLYLIIFLLQLLLLLLEI 200
Cdd:MTH00172 128 FSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGfnmlcASGFLSLFPLLIMVFITLLEI 207

                        170       180
                 ....*....|....*....|.
gi 558478186 201 GVSLIQSYVFVILMILYFKET 221
Cdd:MTH00172 208 AVAVIQAYVFCLLTTIYLADT 228
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 68-221 8.38e-13

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 65.35  E-value: 8.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  68 NNLFYFIVLFIMIMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWLGLMFYGWIENTNHMLIHLVPQGTPFMLMFFMVFIES 147
Cdd:MTH00174  89 NYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIET 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186 148 LSNLIRPMTLCIRLTANMIAGHLLLTLLSSFIPSFYLYLII------FLLQLLLLLLEIGVSLIQSYVFVILMILYFKET 221
Cdd:MTH00174 169 LSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILigsfvpFAILIFVTILEMAVAIIQAYVFTLLTIVYLRDT 248
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 70-220 3.95e-12

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 63.27  E-value: 3.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  70 LFYFIVLFIMIMFNNFMGLFP-YIFTSSSHLVFSMIFSLSVWLGLMFYGWIEN-TNHMLIHLVPQGTPFMLmffmvFIES 147
Cdd:PRK05815  73 APLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKKgLGGYLKEFYLQPHPLLL-----PIEI 147

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 558478186 148 LSNLIRPMTLCIRLTANMIAGHLLLTLLSSFIP-SFYLYLIIFLLQLLLLLLEIGVSLIQSYVFVILMILYFKE 220
Cdd:PRK05815 148 ISEFSRPISLSLRLFGNMLAGELILALIALLGGaGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 63-220 5.33e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 45.35  E-value: 5.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  63 NKYNLNNLFYFIVLFIMIMFNnFMGLFPYIFTSSSHLVFSMIFSLSVWLGlMFYGWIENTNHMLIHLVPQGTPFMLMFFM 142
Cdd:MTH00087  46 NKLPLSSVISFFTFIVLLLFC-FGGLFPYSFSPCGMVEFTFLYALVAWLS-TFLSFLSKSEKFSVYLSKGSDSFLKTFSM 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 558478186 143 VFIESLSNLIRPMTLCIRLTANMIAGHLLLTLLSSFipsfylYLIIFLLQLLLLLLEIGVSLIQSYVFVILMILYFKE 220
Cdd:MTH00087 124 LFVEIVSELSRPLALTLRLTVNLMVGHLISSLLNFL------GEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 72-217 1.42e-05

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 45.12  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186  72 YFIVLFIMIMFNNFMGLFPYIFTSSSHLVFSMIFSLSVWL----------GLMFYgwientnhmLIHLVpQGTPFMLMFF 141
Cdd:PRK13419 173 YLLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFitqyaaikahGIKGY---------LAHLT-GGTHWSLWII 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558478186 142 MVFIESLSNLIRPMTLCIRLTANMIAGHL-LLTLLS-SFIPSFYLYLIIFLLQLLLLLLEIG--VSLIQSYVFVILMILY 217
Cdd:PRK13419 243 MIPIEFIGLFTKPFALTVRLFANMTAGHIvILSLIFiSFILKSYIVAVAVSVPFAIFIYLLElfVAFLQAYIFTMLSALF 322
 
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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