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Conserved domains on  [gi|19111750|ref|NP_579947|]
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ATP synthase F0 subunit 6 (mitochondrion) [Ancylostoma duodenale]

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 1.38e-60

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177152  Cd Length: 195  Bit Score: 187.49  E-value: 1.38e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750    1 MNQVFFLDIFMFVFFLQYLLYFKESMLNSLVKKFFKGLIEVFSYTSVLPMSSVISFFTFIVLLICCFGGYFTYSFCPCGM 80
Cdd:MTH00087   1 MNQVFFLDVFMFVFLLQYLLYFKESMLNVLVKKFFGLLIIVFSYSNKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   81 VEFTFIYAMVAWMSTLLTFIS-SEKFSIYMSKSGDTFFKTFSMLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLymgi 159
Cdd:MTH00087  81 VEFTFLYALVAWLSTFLSFLSkSEKFSVYLSKGSDSFLKTFSMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLL---- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 19111750  160 eNFLGEKYLWISILAIMMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00087 157 -NFLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
 
Name Accession Description Interval E-value
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 1-199 1.38e-60

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 187.49  E-value: 1.38e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750    1 MNQVFFLDIFMFVFFLQYLLYFKESMLNSLVKKFFKGLIEVFSYTSVLPMSSVISFFTFIVLLICCFGGYFTYSFCPCGM 80
Cdd:MTH00087   1 MNQVFFLDVFMFVFLLQYLLYFKESMLNVLVKKFFGLLIIVFSYSNKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   81 VEFTFIYAMVAWMSTLLTFIS-SEKFSIYMSKSGDTFFKTFSMLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLymgi 159
Cdd:MTH00087  81 VEFTFLYALVAWLSTFLSFLSkSEKFSVYLSKGSDSFLKTFSMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLL---- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 19111750  160 eNFLGEKYLWISILAIMMECFVFFIQSYIFSRLIYLYLNE 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 ...
 56-198 2.79e-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: 58.95  E-value: 2.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750  56 FFTFIVLLICCFGGYFTYSFCPCGMVEFTFIYAMVAWMSTLLTFISSEKFSIY--MSKSGDTFFKTFSMLLVEIVSEFSR 133
Cdd:cd00310   9 GTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFlhFLPPGTPLPLAPLMVPIELISELIR 88

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19111750 134 PLALTVRLTVNIMVGHLISMMLYMGIENFLGEKYLWISILAIMM---ECFVFFIQSYIFSRLIYLYLN 198
Cdd:cd00310  89 PLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALtllELFVAFIQAYVFTLLTAVYIS 156
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 56-199 3.97e-10

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: 57.22  E-value: 3.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750    56 FFTFIVLLICCFGGYFTYSFCPCGMVEFTFIYAMVAWMSTLLT--FISSEKFSIYMSKSGDTFFKTFSMLLVEIVSEFSR 133
Cdd:TIGR01131  75 FTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISgfRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLAR 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   134 PLALTVRLTVNIMVGH----LISMMLYMGIENFLGEKYLWISILAIMMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:TIGR01131 155 PISLSVRLFANISAGHllltLLSGLLFSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 122-199 4.98e-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: 53.92  E-value: 4.98e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19111750 122 MLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLYMGIENFLGEKYLWISILAIMM-ECFVFFIQSYIFSRLIYLYLNE 199
Cdd:COG0356 130 MLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLLPVAWTAfELLVGFLQAYIFTMLTAVYISL 208
ATP-synt_A pfam00119
ATP synthase A chain;
122-198 1.36e-08

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 52.49  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   122 MLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLYMGIENFLGEKYLWISILAIMM------ECFVFFIQSYIFSRLIYL 195
Cdd:pfam00119 134 LLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGvawtlfELLVAFIQAYVFTMLTAV 213


                  ...
gi 19111750   196 YLN 198
Cdd:pfam00119 214 YIS 216
 
Name Accession Description Interval E-value
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 1-199 1.38e-60

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 187.49  E-value: 1.38e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750    1 MNQVFFLDIFMFVFFLQYLLYFKESMLNSLVKKFFKGLIEVFSYTSVLPMSSVISFFTFIVLLICCFGGYFTYSFCPCGM 80
Cdd:MTH00087   1 MNQVFFLDVFMFVFLLQYLLYFKESMLNVLVKKFFGLLIIVFSYSNKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   81 VEFTFIYAMVAWMSTLLTFIS-SEKFSIYMSKSGDTFFKTFSMLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLymgi 159
Cdd:MTH00087  81 VEFTFLYALVAWLSTFLSFLSkSEKFSVYLSKGSDSFLKTFSMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLL---- 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 19111750  160 eNFLGEKYLWISILAIMMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00087 157 -NFLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 6-199 2.42e-13

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 65.96  E-value: 2.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750    6 FLDIFMFVFFLQYLLYFKESMLNSLVKKFFKGLIEVFSYTSVLPMSSVISFFT--FIVLLICCFGGYFTYSFCPCGMVEF 83
Cdd:MTH00157  21 WLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFIslFSFILFNNFLGLFPYIFTSTSHLSL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   84 TFIYAMVAWMSTLL--TFISSEKFSIYMSKSGDTFFKTFSMLLVEIVSEFSRPLALTVRLTVNIMVGHLIsMMLYMGIEN 161
Cdd:MTH00157 101 TLSLALPLWLSFMLfgWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLL-LTLLGNTGP 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 19111750  162 FLGEKYLWISILAIMM----ECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00157 180 SLSSMILSILILIQILllilESAVAIIQSYVFSVLSTLYSSE 221
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 56-198 2.79e-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: 58.95  E-value: 2.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750  56 FFTFIVLLICCFGGYFTYSFCPCGMVEFTFIYAMVAWMSTLLTFISSEKFSIY--MSKSGDTFFKTFSMLLVEIVSEFSR 133
Cdd:cd00310   9 GTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFlhFLPPGTPLPLAPLMVPIELISELIR 88

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19111750 134 PLALTVRLTVNIMVGHLISMMLYMGIENFLGEKYLWISILAIMM---ECFVFFIQSYIFSRLIYLYLN 198
Cdd:cd00310  89 PLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALtllELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 10-199 1.02e-10

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 58.72  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   10 FMFVFFLQYLLYFKESMLNSLVKKFFKGLIEVFSYTSVLPMS--SVISFFTFIVLLICCFGGYFTYSFCPCGMVEFTFIY 87
Cdd:MTH00173  28 LMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGgfSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   88 AMVAWMSTLL--TFISSEKFSIYMSKSGDTFFKTFSMLLVEIVSEFSRPLALTVRLTVNIMVGHLIS-------MMLYMG 158
Cdd:MTH00173 108 ALPLWLSLILsgLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLtlignylSSSLFS 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 19111750  159 IENFLGEKYLWISILAIMMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00173 188 SSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 5-199 2.03e-10

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 58.04  E-value: 2.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750    5 FFLDIFMFVFFLQYLLYFKESMLNSLVKKFFKGLIEVFSYTSVLPMS------SVISFFTFIVLLICCFGGYFTYSFCPC 78
Cdd:MTH00179  17 IPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINkkghkwAVLFLSLMLFLLTLNLLGLLPYTFTPT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   79 GMVEFTFIYAMVAWMST-LLTFISSEKFSI-YMSKSGDTFFKTFSMLLVEIVSEFSRPLALTVRLTVNIMVGHLI----- 151
Cdd:MTH00179  97 TQLSLNLGLALPLWLGTvLYGLFNQPTIALaHLLPEGTPTPLIPMLVWIETISLLIRPLALGVRLTANITAGHLLmhlis 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 19111750  152 -SMMLYMGIENFLGEKYLWISILAIMMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00179 177 sAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 56-199 3.97e-10

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: 57.22  E-value: 3.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750    56 FFTFIVLLICCFGGYFTYSFCPCGMVEFTFIYAMVAWMSTLLT--FISSEKFSIYMSKSGDTFFKTFSMLLVEIVSEFSR 133
Cdd:TIGR01131  75 FTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISgfRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLAR 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   134 PLALTVRLTVNIMVGH----LISMMLYMGIENFLGEKYLWISILAIMMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:TIGR01131 155 PISLSVRLFANISAGHllltLLSGLLFSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 122-199 4.98e-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: 53.92  E-value: 4.98e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19111750 122 MLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLYMGIENFLGEKYLWISILAIMM-ECFVFFIQSYIFSRLIYLYLNE 199
Cdd:COG0356 130 MLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLLPVAWTAfELLVGFLQAYIFTMLTAVYISL 208
ATP-synt_A pfam00119
ATP synthase A chain;
122-198 1.36e-08

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 52.49  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   122 MLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLYMGIENFLGEKYLWISILAIMM------ECFVFFIQSYIFSRLIYL 195
Cdd:pfam00119 134 LLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGvawtlfELLVAFIQAYVFTMLTAV 213


                  ...
gi 19111750   196 YLN 198
Cdd:pfam00119 214 YIS 216
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 122-199 3.86e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 51.36  E-value: 3.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750  122 MLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLYMGIENFLgEKYLWISILAI-------MMECFVFFIQSYIFSRLIY 194
Cdd:MTH00120 142 LILIETISLLIRPLALGVRLTANLTAGHLLIQLISTATLNLL-PTMPTLSLLTLiilllltILELAVAMIQAYVFVLLLS 220


                 ....*
gi 19111750  195 LYLNE 199
Cdd:MTH00120 221 LYLQE 225
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 12-199 1.75e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 49.65  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   12 FVFFLQYLLYFKESMLNSLVKKFFKGLIEVFSYT--SVLPMSSVISFFTFIVLLICCFGGYFTYSFCPCGMVEFTFIYAM 89
Cdd:MTH00176  30 FLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSngSYILGSASIIISLFILVMSLNLSGLIPYVFTSTSHLVITLSLAL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   90 VAWMSTLLT--FISSEKFSIYMSKSGDTFFKTFSMLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLYMGIENFLGEKY 167
Cdd:MTH00176 110 PLWLGVILSgfINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLAVRLAANLSAGHLLLGLLGAAMWGLLPVSP 189

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 19111750  168 LWISILAI------MMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00176 190 LIGFLLLIvqilyfMFEIAVCMIQAYVFTLLLSLYLDE 227
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 83-199 6.76e-07

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 47.87  E-value: 6.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   83 FTFIYAMVAWMSTLLTFISSEKFSIYMSKSgdTFFKTFSMLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLYMGIENF 162
Cdd:PRK05815 105 VTLALALIVFVLVIYYGIKKKGLGGYLKEF--YLQPHPLLLPIEIISEFSRPISLSLRLFGNMLAGELILALIALLGGAG 182

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 19111750  163 LGEKYLWISILAIMM--ECFVFFIQSYIFSRLIYLYLNE 199
Cdd:PRK05815 183 LLLALAPLILPVAWTifEIFVGTLQAYIFMMLTIVYISM 221
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 122-197 8.44e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 48.20  E-value: 8.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750  122 MLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLyMGIENFLGEKYLWI------SILAIMMECFVFFIQSYIFSRLIYL 195
Cdd:PRK13419 243 MIPIEFIGLFTKPFALTVRLFANMTAGHIVILSL-IFISFILKSYIVAVavsvpfAIFIYLLELFVAFLQAYIFTMLSAL 321


                 ..
gi 19111750  196 YL 197
Cdd:PRK13419 322 FI 323
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 122-199 1.18e-06

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 47.25  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750  122 MLLV-EIVSEFSRPLALTVRLTVNIMVGHLI------SMMLYMGIENFLGEKYLWISILAIMMECFVFFIQSYIFSRLIY 194
Cdd:MTH00101 140 MLVIiETISLFIQPMALAVRLTANITAGHLLihliggATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVS 219


                 ....*
gi 19111750  195 LYLNE 199
Cdd:MTH00101 220 LYLHD 224
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 122-199 6.41e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 44.96  E-value: 6.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750  122 MLLVEIVSEFSRPLALTVRLTVNIMVGHL------------ISMMLYMGIENFLgekylwISILAIMMECFVFFIQSYIF 189
Cdd:MTH00073 142 LIIIETISLFIRPLALGVRLTANLTAGHLliqlistatlvlLPLMPTVSILTMI------VLFLLTLLEIAVAMIQAYVF 215

                         90
                 ....*....|
gi 19111750  190 SRLIYLYLNE 199
Cdd:MTH00073 216 VLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 122-199 8.72e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 41.78  E-value: 8.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750  122 MLLVEIVSEFSRPLALTVRLTVNIMVGHLI------------SMMLYMGIenfLGEKYLwisILAIMMECFVFFIQSYIF 189
Cdd:MTH00132 142 LIIIETISLFIRPLALGVRLTANLTAGHLLiqliataafvllPLMPTVAI---LTATLL---FLLTLLEVAVAMIQAYVF 215

                         90
                 ....*....|
gi 19111750  190 SRLIYLYLNE 199
Cdd:MTH00132 216 VLLLSLYLQE 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 25-199 3.28e-04

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 39.96  E-value: 3.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   25 SMLNSLVKKFFKGLIE-VFSYTSVLPMSSVISFFT-FIVLLICCFGGYFTYSFCPCGMVEFTFIYAMVAWMS-TLLTFIS 101
Cdd:MTH00035  44 SRSQSIWLTFRQEILKlIFQNTNPNTAPWAGLLTTvFILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSvNILGFYL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750  102 SEKFSI-YMSKSGDTFFKTFSMLLVEIVSEFSRPLALTVRLTVNIMVGHLISMMLYMGI-----ENFLGEKYLWISILAI 175
Cdd:MTH00035 124 AFNSRLsHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRLAANLTAGHLLIFLLSTAIwelsnSPLISIITLIIFFLLF 203

                        170       180
                 ....*....|....*....|....
gi 19111750  176 MMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00035 204 ILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 53-199 9.83e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 38.87  E-value: 9.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   53 VISFFTFIVLLICCfgGYFTYSFCPCGMVEFTFIYAMVAWMSTLLTFISSEK---FSIYMSkSGDTFFKTFSMLLVEIVS 129
Cdd:MTH00172  75 IISLFFFIVFLNLL--GLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKwdfFSILMP-SGAPLGLAPLLVLIETVS 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19111750  130 EFSRPLALTVRLTVNIMVGHLISMML------YMGIENFLGEKYLWISILAIMMECFVFFIQSYIFSRLIYLYLNE 199
Cdd:MTH00172 152 YISRAISLGVRLAANLSAGHLLFAILagfgfnMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 59-196 5.52e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 36.63  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111750   59 FIVLLICCFGGYFTYSFCPCGMVEFTFIYAMVAWMSTLLTFI--SSEKFSIYMSKSGDTFFKTFSMLLVEIVSEFSRPLA 136
Cdd:MTH00005  81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVtfSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19111750  137 LTVRLTVNIMVGHLI---------SMMLYMGIENFLgekYLWISILAIMMECFVFFIQSYIFSRLIYLY 196
Cdd:MTH00005 161 LSFRLAANMSAGHIVlsligiyaaSALFSSISSTIL---LILTQMGYILFEVGICLIQAYIFCLLLSLY 226
 
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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