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Conserved domains on  [gi|225622190|ref|YP_002725705|]
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ATP synthase F0 subunit 6 (mitochondrion) [Bunostomum phlebotomum]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009557)

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 MTH00087
ATP synthase F0 subunit 6; Provisional
 1-199 6.46e-59

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177152  Cd Length: 195  Bit Score: 183.26  E-value: 6.46e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190   1 MNQVFFLDIFMFVFFLQYILYFKEGMLNVLVKNFLGSLVNVFSYSKCLPLSFVVSFFTFIILLICCFGGYFTYSFCPCGM 80
Cdd:MTH00087   1 MNQVFFLDVFMFVFLLQYLLYFKESMLNVLVKKFFGLLIIVFSYSNKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  81 VEFTFVYAMIAWMSTLLSFIS-SEKFSVYMSKGGDIFLKTFSMLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLymgi 159
Cdd:MTH00087  81 VEFTFLYALVAWLSTFLSFLSkSEKFSVYLSKGSDSFLKTFSMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLL---- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 225622190 160 eNYIGESFFWFSILAIMMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00087 157 -NFLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
 
Name Accession Description Interval E-value
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 1-199 6.46e-59

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 183.26  E-value: 6.46e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190   1 MNQVFFLDIFMFVFFLQYILYFKEGMLNVLVKNFLGSLVNVFSYSKCLPLSFVVSFFTFIILLICCFGGYFTYSFCPCGM 80
Cdd:MTH00087   1 MNQVFFLDVFMFVFLLQYLLYFKESMLNVLVKKFFGLLIIVFSYSNKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  81 VEFTFVYAMIAWMSTLLSFIS-SEKFSVYMSKGGDIFLKTFSMLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLymgi 159
Cdd:MTH00087  81 VEFTFLYALVAWLSTFLSFLSkSEKFSVYLSKGSDSFLKTFSMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLL---- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 225622190 160 eNYIGESFFWFSILAIMMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00087 157 -NFLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 50-198 3.68e-11

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: 58.56  E-value: 3.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  50 LSFVVSFFTFIilLICCFGGYFTYSFCPCGMVEFTFVYAMIAWMSTLLSFISSEKFSVY--MSKGGDIFLKTFSMLLVEI 127
Cdd:cd00310    5 LPLLGTLFLFI--LFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFlhFLPPGTPLPLAPLMVPIEL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225622190 128 VSEFSRPLALTVRLTVNIMVGHLISMMLYMGIENYIGESFFWFSILAIMM---ECFVFFIQSYIFSRLIYLYLN 198
Cdd:cd00310   83 ISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALtllELFVAFIQAYVFTLLTAVYIS 156
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 52-199 9.11e-11

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: 58.76  E-value: 9.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190   52 FVVSFFTFIILLICCFGGYFTYSFCPCGMVEFTFVYAMIAWMSTLLSFISSEK---FSVYMSKGGDIFLKTFsMLLVEIV 128
Cdd:TIGR01131  71 FPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPkgfLAHLVPSGTPLPLIPF-LVIIETI 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225622190  129 SEFSRPLALTVRLTVNIMVGH----LISMMLYMGIENYIGESFFWFSILAIMMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:TIGR01131 150 SYLARPISLSVRLFANISAGHllltLLSGLLFSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 50-199 2.92e-09

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: 54.31  E-value: 2.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  50 LSFVVSFFTFIilLICCFGGYFTYSFCPCGMVEFTFVYAMIAWMSTLLSFISSEKFSVYMSKG--GDIFLKTFSMLLVEI 127
Cdd:COG0356   58 APLLLTLFLFI--LVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHLffPPFPWLAPLMLPIEI 135

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225622190 128 VSEFSRPLALTVRLTVNIMVGHLISMMLYMGIENYIGESFFWFSILAIMM-ECFVFFIQSYIFSRLIYLYLNE 199
Cdd:COG0356  136 ISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLLPVAWTAfELLVGFLQAYIFTMLTAVYISL 208
ATP-synt_A pfam00119
ATP synthase A chain;
52-198 5.05e-08

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 50.95  E-value: 5.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190   52 FVVSFFTFIILL-ICCFGGYFTYSFCPCGMVEFTFVYAMIAWMSTLLSFISSEKFSVYMSK---GGDIFLKTFSMLLVEI 127
Cdd:pfam00119  60 LLLTLFFFILVSnLLGLIPKSPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKlfvPPVPLPLVPLLLPIEI 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225622190  128 VSEFSRPLALTVRLTVNIMVGHLISMMLYMGIENYIGESFFWFSILAIMM------ECFVFFIQSYIFSRLIYLYLN 198
Cdd:pfam00119 140 ISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGvawtlfELLVAFIQAYVFTMLTAVYIS 216
 
Name Accession Description Interval E-value
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 1-199 6.46e-59

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 183.26  E-value: 6.46e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190   1 MNQVFFLDIFMFVFFLQYILYFKEGMLNVLVKNFLGSLVNVFSYSKCLPLSFVVSFFTFIILLICCFGGYFTYSFCPCGM 80
Cdd:MTH00087   1 MNQVFFLDVFMFVFLLQYLLYFKESMLNVLVKKFFGLLIIVFSYSNKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  81 VEFTFVYAMIAWMSTLLSFIS-SEKFSVYMSKGGDIFLKTFSMLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLymgi 159
Cdd:MTH00087  81 VEFTFLYALVAWLSTFLSFLSkSEKFSVYLSKGSDSFLKTFSMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLL---- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 225622190 160 eNYIGESFFWFSILAIMMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00087 157 -NFLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 6-199 2.65e-12

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 62.88  E-value: 2.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190   6 FLDIFMFVFFLQYILYFKEGMLNVLVKNFLGSLVNVFSYSKCLPLSFVVSFFT--FIILLICCFGGYFTYSFCPCGMVEF 83
Cdd:MTH00157  21 WLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFIslFSFILFNNFLGLFPYIFTSTSHLSL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  84 TFVYAMIAWMSTLL--SFISSEKFSVYMSKGGDIFLKTFSMLLVEIVSEFSRPLALTVRLTVNIMVGHLI-----SMMLY 156
Cdd:MTH00157 101 TLSLALPLWLSFMLfgWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLltllgNTGPS 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 225622190 157 MGIENYIgeSFFWFSILAIMMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00157 181 LSSMILS--ILILIQILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 50-198 3.68e-11

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: 58.56  E-value: 3.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  50 LSFVVSFFTFIilLICCFGGYFTYSFCPCGMVEFTFVYAMIAWMSTLLSFISSEKFSVY--MSKGGDIFLKTFSMLLVEI 127
Cdd:cd00310    5 LPLLGTLFLFI--LFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFlhFLPPGTPLPLAPLMVPIEL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225622190 128 VSEFSRPLALTVRLTVNIMVGHLISMMLYMGIENYIGESFFWFSILAIMM---ECFVFFIQSYIFSRLIYLYLN 198
Cdd:cd00310   83 ISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALtllELFVAFIQAYVFTLLTAVYIS 156
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 52-199 9.11e-11

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: 58.76  E-value: 9.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190   52 FVVSFFTFIILLICCFGGYFTYSFCPCGMVEFTFVYAMIAWMSTLLSFISSEK---FSVYMSKGGDIFLKTFsMLLVEIV 128
Cdd:TIGR01131  71 FPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPkgfLAHLVPSGTPLPLIPF-LVIIETI 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225622190  129 SEFSRPLALTVRLTVNIMVGH----LISMMLYMGIENYIGESFFWFSILAIMMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:TIGR01131 150 SYLARPISLSVRLFANISAGHllltLLSGLLFSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 10-199 4.28e-10

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 57.18  E-value: 4.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  10 FMFVFFLQYILYFKEGMLNVLVKNFLGSLVNVFSYSKCLPLSFVVSFFTFIILLI--CCFGGYFTYSFCPCGMVEFTFVY 87
Cdd:MTH00173  28 LMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLisLNLSGLLPFVFSVTSHLAFTFSL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  88 AMIAWMSTLLS--FISSEKFSVYMSKGGDIFLKTFSMLLVEIVSEFSRPLALTVRLTVNIMVGHLISMML--YMGIENYI 163
Cdd:MTH00173 108 ALPLWLSLILSglFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIgnYLSSSLFS 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 225622190 164 GESFFWFSILAIMM-----ECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00173 188 SSVVSLLLVLLIQVgyfifEVAVMLIQAYIFTLLIKLYSDE 228
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 50-199 2.92e-09

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: 54.31  E-value: 2.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  50 LSFVVSFFTFIilLICCFGGYFTYSFCPCGMVEFTFVYAMIAWMSTLLSFISSEKFSVYMSKG--GDIFLKTFSMLLVEI 127
Cdd:COG0356   58 APLLLTLFLFI--LVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHLffPPFPWLAPLMLPIEI 135

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225622190 128 VSEFSRPLALTVRLTVNIMVGHLISMMLYMGIENYIGESFFWFSILAIMM-ECFVFFIQSYIFSRLIYLYLNE 199
Cdd:COG0356  136 ISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLLPVAWTAfELLVGFLQAYIFTMLTAVYISL 208
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 59-199 1.18e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 53.11  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  59 FIILLICCFGGYFTYSFCPCGMVEFTFVYAMIAWMSTLLS---FISSEKFSVYMSKGGDIFLKTFsMLLVEIVSEFSRPL 135
Cdd:MTH00176  79 FILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSgfiNNFYSRLSHLVPQGTPPLLNPF-LVLIELVSLLIRPL 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190 136 ALTVRLTVNIMVGHLISMMLYMGIENYIGESFFWFSILAI------MMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00176 158 TLAVRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIvqilyfMFEIAVCMIQAYVFTLLLSLYLDE 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 5-199 1.31e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 53.03  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190   5 FFLDIFMFVFFLQYILYFKEGMLNVLVKNFLGSLVNVFSYSKCLPLS------FVVSFFTFIILLICCFGGYFTYSFCPC 78
Cdd:MTH00179  17 IPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINkkghkwAVLFLSLMLFLLTLNLLGLLPYTFTPT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  79 GMVEFTFVYAMIAWMST-LLSFISSEKFSV--YMSKGGDIFLKTFsMLLVEIVSEFSRPLALTVRLTVNIMVGHLI---- 151
Cdd:MTH00179  97 TQLSLNLGLALPLWLGTvLYGLFNQPTIALahLLPEGTPTPLIPM-LVWIETISLLIRPLALGVRLTANITAGHLLmhli 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 225622190 152 --SMMLYMGIENYIGESFFWFSILAIMMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00179 176 ssAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 122-199 3.27e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 51.75  E-value: 3.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190 122 MLLVEIVSEFSRPLALTVRLTVNIMVGHL----ISMMLYMGIENYIGESFFWFSILAIMM--ECFVFFIQSYIFSRLIYL 195
Cdd:MTH00120 142 LILIETISLLIRPLALGVRLTANLTAGHLliqlISTATLNLLPTMPTLSLLTLIILLLLTilELAVAMIQAYVFVLLLSL 221


                 ....
gi 225622190 196 YLNE 199
Cdd:MTH00120 222 YLQE 225
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 44-197 3.61e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 52.05  E-value: 3.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  44 YSKCLPlsFVVSFFTFIilLICCFGGYFTYSFCPCGMVEFTFVYAMIAWMSTLLSFISSEKFSVYMS--KGGDIFLKTFS 121
Cdd:PRK13419 167 YEKFLP--YLLTVFFFI--LVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAhlTGGTHWSLWII 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190 122 MLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLymgienyIGESF----FW--------FSILAIMMECFVFFIQSYIF 189
Cdd:PRK13419 243 MIPIEFIGLFTKPFALTVRLFANMTAGHIVILSL-------IFISFilksYIvavavsvpFAIFIYLLELFVAFLQAYIF 315


                 ....*...
gi 225622190 190 SRLIYLYL 197
Cdd:PRK13419 316 TMLSALFI 323
ATP-synt_A pfam00119
ATP synthase A chain;
52-198 5.05e-08

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 50.95  E-value: 5.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190   52 FVVSFFTFIILL-ICCFGGYFTYSFCPCGMVEFTFVYAMIAWMSTLLSFISSEKFSVYMSK---GGDIFLKTFSMLLVEI 127
Cdd:pfam00119  60 LLLTLFFFILVSnLLGLIPKSPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKlfvPPVPLPLVPLLLPIEI 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225622190  128 VSEFSRPLALTVRLTVNIMVGHLISMMLYMGIENYIGESFFWFSILAIMM------ECFVFFIQSYIFSRLIYLYLN 198
Cdd:pfam00119 140 ISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGvawtlfELLVAFIQAYVFTMLTAVYIS 216
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 83-199 1.14e-07

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 50.18  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  83 FTFVYAMIAWMSTLLSFISSEKFSVYMSKGgdIFLKTFSMLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLYMGIENY 162
Cdd:PRK05815 105 VTLALALIVFVLVIYYGIKKKGLGGYLKEF--YLQPHPLLLPIEIISEFSRPISLSLRLFGNMLAGELILALIALLGGAG 182

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 225622190 163 IGESFFWFSILAIMM--ECFVFFIQSYIFSRLIYLYLNE 199
Cdd:PRK05815 183 LLLALAPLILPVAWTifEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 69-199 4.29e-07

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 48.41  E-value: 4.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  69 GYFTYSFCPCGMVEFTFVYAMIAWMST-LLSFISSEKFSV--YMSKGGDIFLktFSMLLV-EIVSEFSRPLALTVRLTVN 144
Cdd:MTH00101  86 GLLPHSFTPTTQLSMNLGMAIPLWAGTvITGFRNKTKASLahFLPQGTPTPL--IPMLVIiETISLFIQPMALAVRLTAN 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225622190 145 IMVGHLI------SMMLYMGIENYIGESFFWFSILAIMMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00101 164 ITAGHLLihliggATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHD 224
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 122-199 5.05e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 45.34  E-value: 5.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190 122 MLLVEIVSEFSRPLALTVRLTVNIMVGH----LISMMLYMGIENYIGESFFWFSILAI--MMECFVFFIQSYIFSRLIYL 195
Cdd:MTH00073 142 LIIIETISLFIRPLALGVRLTANLTAGHlliqLISTATLVLLPLMPTVSILTMIVLFLltLLEIAVAMIQAYVFVLLLSL 221


                 ....
gi 225622190 196 YLNE 199
Cdd:MTH00073 222 YLQE 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 56-199 3.44e-05

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 43.04  E-value: 3.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  56 FFTFIILLICCFGGYFTYSFCPCGMVEFTFVYAMIAWMS-TLLSFISS--EKFSVYMSKGGDIFLKTFsMLLVEIVSEFS 132
Cdd:MTH00035  77 TTVFILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSvNILGFYLAfnSRLSHLVPQGTPSFLIPL-MVWIETLSLFA 155

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225622190 133 RPLALTVRLTVNIMVGHLISMMLYMGIENYIGESFFWFSILAI-----MMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00035 156 QPIALGLRLAANLTAGHLLIFLLSTAIWELSNSPLISIITLIIffllfILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 122-199 4.89e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 42.55  E-value: 4.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190 122 MLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLYMGIenyigesffwFSILAIMM----------------ECFVFFIQ 185
Cdd:MTH00132 142 LIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAA----------FVLLPLMPtvailtatllflltllEVAVAMIQ 211

                         90
                 ....*....|....
gi 225622190 186 SYIFSRLIYLYLNE 199
Cdd:MTH00132 212 AYVFVLLLSLYLQE 225
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 50-199 5.39e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 42.34  E-value: 5.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  50 LSFVVSFFTFIILLICCfgGYFTYSFCPCGMVEFTFVYAMIAWMSTLLSFISSEK---FSVYMSKGGDIFLKTFsMLLVE 126
Cdd:MTH00172  72 FPFIISLFFFIVFLNLL--GLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKwdfFSILMPSGAPLGLAPL-LVLIE 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190 127 IVSEFSRPLALTVRLTVNIMVGHLISMMLYMGIENYIGESFFwFSILAIMMECF-------VFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00172 149 TVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNMLCASGF-LSLFPLLIMVFitlleiaVAVIQAYVFCLLTTIYLAD 227
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 51-196 2.43e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 40.49  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  51 SFVVSFFTFIILLicCFGGYFTYSFCPCGMVEFTFVYAMIAWMSTLLSFI--SSEKFSVYMSKGGDIFLKTFSMLLVEIV 128
Cdd:MTH00005  75 SLISALFTMIILM--NLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVtfSPKKFAAHLLPGGAPDWLNPFLVLIETI 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225622190 129 SEFSRPLALTVRLTVNIMVGHLIsmMLYMGIenYIGESFFW----------FSILAIMMECFVFFIQSYIFSRLIYLY 196
Cdd:MTH00005 153 SILVRPITLSFRLAANMSAGHIV--LSLIGI--YAASALFSsisstillilTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 50-197 2.21e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 37.68  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225622190  50 LSFVVSFFTFIILLICCfgGYFTYSFCPCGMVEFTFVYAM-IAWMSTLLSFIS--SEKFSVYMSKGGDIFLKTFsMLLVE 126
Cdd:MTH00175  83 FPFILSLFLFIAILNIL--GLFPYVFTPTAHIIITFGLSLsIIIAVTLLGFLTfkWNFLSILMPGGAPLVLAPF-LVLIE 159

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225622190 127 IVSEFSRPLALTVRLTVNIMVGHLISMMLYMGIENYIGESFFWFSILAIM-------MECFVFFIQSYIFSRLIYLYL 197
Cdd:MTH00175 160 TLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNGLIILSLFPMLimifitlLEMAVAVIQAYVFCLLTTIYL 237
 
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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