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Conserved domains on  [gi|1938966152|gb|QPK42076|]
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ATP synthase F0 subunit 6 (mitochondrion) [Zhengitettix curvispinus]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009593)

ATP synthase F0 subunit 6 is part of the mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V), which produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-222 2.52e-80

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 239.30  E-value: 2.52e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152   1 MMTNLFSSFDPSTNMmNMSLNWTSTIMMMYIMPMSYWLNKSRSSMVFKLNLSILNKEFYSII--NHKSGVIIFISMFIMI 78
Cdd:MTH00157    1 MMTNLFSIFDPSTSF-NLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLgpKNKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  79 MMNNFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAIR 158
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1938966152 159 LAANMIAGHLLLTLLGNSGSTLNNIMLLSMLSIQMMLLMLESAVSIIQAYVFSILLTLYSSEIN 222
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-222 2.52e-80

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 239.30  E-value: 2.52e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152   1 MMTNLFSSFDPSTNMmNMSLNWTSTIMMMYIMPMSYWLNKSRSSMVFKLNLSILNKEFYSII--NHKSGVIIFISMFIMI 78
Cdd:MTH00157    1 MMTNLFSIFDPSTSF-NLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLgpKNKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  79 MMNNFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAIR 158
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1938966152 159 LAANMIAGHLLLTLLGNSGSTLNNIMLLSMLSIQMMLLMLESAVSIIQAYVFSILLTLYSSEIN 222
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-222 2.11e-41

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: 140.42  E-value: 2.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152   5 LFSSFDPST-NMMNMSLNWTSTIMMMYIMPMSYWLNK----SRSSMVFKLNLSILNKEFYSIINHKSGVIIFISMFIMIM 79
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFLISSSLSRwlipSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  80 --MNNFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAI 157
Cdd:TIGR01131  81 ilISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1938966152 158 RLAANMIAGHLLLTLLGNSGSTLNNIMLLSM-LSIQMMLLMLESAVSIIQAYVFSILLTLYSSEIN 222
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIFALlLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 81-219 2.86e-40

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: 135.22  E-value: 2.86e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  81 NNFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAIRLA 160
Cdd:cd00310    18 SNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLF 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1938966152 161 ANMIAGHLLLTLLGNSGSTLNNIMLLSMLSIQMMLLMLESAVSIIQAYVFSILLTLYSS 219
Cdd:cd00310    98 ANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
81-219 6.56e-24

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 94.48  E-value: 6.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  81 NNFLGLF---PYIFTSSSHMVMTLSIALPMWLSFNLFGWMKK--TNYMFSHLLPlGTPSLLMPFMVCIETISNLIRPGTL 155
Cdd:pfam00119  71 SNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIKKHglGGYFKKLFVP-PVPLPLVPLLLPIEIISEFARPVSL 149

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938966152 156 AIRLAANMIAGHLLLTL---LGNSGSTLNNIMLLSMLSIQMMLLMLESAVSIIQAYVFSILLTLYSS 219
Cdd:pfam00119 150 SLRLFGNMLAGHLLLLLlagLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 81-217 3.33e-18

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: 79.35  E-value: 3.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  81 NNFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAIRLA 160
Cdd:COG0356    71 SNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHLFFPPFPWLAPLMLPIEIISELARPLSLSLRLF 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1938966152 161 ANMIAGHLLLTLLGNSGSTLNNIMLLSMLSIQMMLlmLESAVSIIQAYVFSILLTLY 217
Cdd:COG0356   151 GNMFAGHIILLLLAGLAPFLLLGVLSLLLPVAWTA--FELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-222 2.52e-80

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 239.30  E-value: 2.52e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152   1 MMTNLFSSFDPSTNMmNMSLNWTSTIMMMYIMPMSYWLNKSRSSMVFKLNLSILNKEFYSII--NHKSGVIIFISMFIMI 78
Cdd:MTH00157    1 MMTNLFSIFDPSTSF-NLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLgpKNKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  79 MMNNFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAIR 158
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1938966152 159 LAANMIAGHLLLTLLGNSGSTLNNIMLLSMLSIQMMLLMLESAVSIIQAYVFSILLTLYSSEIN 222
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-222 2.11e-41

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: 140.42  E-value: 2.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152   5 LFSSFDPST-NMMNMSLNWTSTIMMMYIMPMSYWLNK----SRSSMVFKLNLSILNKEFYSIINHKSGVIIFISMFIMIM 79
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFLISSSLSRwlipSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  80 --MNNFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAI 157
Cdd:TIGR01131  81 ilISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1938966152 158 RLAANMIAGHLLLTLLGNSGSTLNNIMLLSM-LSIQMMLLMLESAVSIIQAYVFSILLTLYSSEIN 222
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIFALlLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 81-219 2.86e-40

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: 135.22  E-value: 2.86e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  81 NNFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAIRLA 160
Cdd:cd00310    18 SNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLF 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1938966152 161 ANMIAGHLLLTLLGNSGSTLNNIMLLSMLSIQMMLLMLESAVSIIQAYVFSILLTLYSS 219
Cdd:cd00310    98 ANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-220 8.19e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 136.32  E-value: 8.19e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152   1 MMTNLFSSFDP--STNMMNMSLNWTSTIMMMYIMPMSYWLNKSRSSMVFKLNLSILNKEFYSIINHKSG--VIIFISMFI 76
Cdd:MTH00176    1 MLVDLFSSFDPpnKNIFSMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILgsASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  77 MIMMNNFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLA 156
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938966152 157 IRLAANMIAGHLLLTLLGNSGSTLNNIMLLSMLSI---QMMLLMLESAVSIIQAYVFSILLTLYSSE 220
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLlivQILYFMFEIAVCMIQAYVFTLLLSLYLDE 227
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-220 1.54e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 125.23  E-value: 1.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152   1 MMTNLFSSFDPSTNMMNMSLN----WTSTIMMMYIMPMSYWLNKSRSSMVFKLNLSILNKEF--YSIINHKSGVIIFISM 74
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFNNLSstafWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLsrTFGKHLKGFSSLISAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  75 FIMIMMNNFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGT 154
Cdd:MTH00005   81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1938966152 155 LAIRLAANMIAGHLLLTLLGNS------GSTLNNIMLlsmLSIQMMLLMLESAVSIIQAYVFSILLTLYSSE 220
Cdd:MTH00005  161 LSFRLAANMSAGHIVLSLIGIYaasalfSSISSTILL---ILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-221 2.18e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 124.98  E-value: 2.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152   1 MMTNLFSSFDP--STNMMNMSLNWTSTIMMMYIMPMSYWLNKSRSSMVFKLNLSILNKEFY--SIINHKSGVIIFISMFI 76
Cdd:MTH00173    1 MMVDLFSSFDDhnSSFSSLSFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTrsSGLNLGGFSLLLSSLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  77 MIMMNNFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLA 156
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1938966152 157 IRLAANMIAGHLLLTLLGNSGSTL----NNIMLLSMLSIQMMLLMLESAVSIIQAYVFSILLTLYSSEI 221
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYLSSSlfssSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDEH 229
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-220 9.08e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 123.13  E-value: 9.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152   1 MMTNLFSSFDpSTNMMNMSLNWTSTIMMMYIMPMSY--WLNkSRSSMVFKLNLSILNKEFYSIINHK--SGVIIFISMFI 76
Cdd:MTH00179    1 MMLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLTnrWLN-NRLSTLQSWFFGSFTFQLMQPINKKghKWAVLFLSLML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  77 MIMMNNFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLA 156
Cdd:MTH00179   79 FLLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938966152 157 IRLAANMIAGHLLLTLLGNSGSTLNNIM---LLSMLSIQMMLLMLESAVSIIQAYVFSILLTLYSSE 220
Cdd:MTH00179  159 VRLTANITAGHLLMHLISSAVFVLMNFMgmvALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 82-220 1.04e-32

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 117.77  E-value: 1.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  82 NFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAIRLAA 161
Cdd:MTH00035   87 NVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRLAA 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1938966152 162 NMIAGHLLLTLLGNSGSTLNNIMLLSM--LSIQMMLLMLESAVSIIQAYVFSILLTLYSSE 220
Cdd:MTH00035  167 NLTAGHLLIFLLSTAIWELSNSPLISIitLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 82-220 1.20e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 114.92  E-value: 1.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  82 NFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAIRLAA 161
Cdd:MTH00120   84 NLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVRLTA 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1938966152 162 NMIAGHLLLTLLGNSGSTLNNIML---LSMLSIQMMLLMLESAVSIIQAYVFSILLTLYSSE 220
Cdd:MTH00120  164 NLTAGHLLIQLISTATLNLLPTMPtlsLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 82-220 7.81e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 110.35  E-value: 7.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  82 NFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAIRLAA 161
Cdd:MTH00132   84 NMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTA 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1938966152 162 NMIAGHLLLTLLGNSGSTLNNIM----LLSMLsIQMMLLMLESAVSIIQAYVFSILLTLYSSE 220
Cdd:MTH00132  164 NLTAGHLLIQLIATAAFVLLPLMptvaILTAT-LLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 81-217 1.41e-29

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 109.66  E-value: 1.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  81 NNFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAIRLA 160
Cdd:MTH00101   82 TNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLT 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152 161 ANMIAGHLLLTLLGNSGSTLNNIMLLSML---SIQMMLLMLESAVSIIQAYVFSILLTLY 217
Cdd:MTH00101  162 ANITAGHLLIHLIGGATLALMSISTTTALitfIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-220 2.25e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 106.59  E-value: 2.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152   1 MMTNLFSSFDPSTnMMNMSLNWTSTIM--MMYIMPMSYWLNkSRSSMVFKLNLSILNKEFYSIINHK--SGVIIFISMFI 76
Cdd:MTH00073    1 MNLSFFDQFLSPT-LLGIPLIMLAMLLpwLLFPTPTNKWLN-NRLSTLQIWFLQNFTKQLMLPLNTPghKWALILTSLMV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  77 MIMMNNFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLA 156
Cdd:MTH00073   79 FLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938966152 157 IRLAANMIAGHLLLTLLGNSGSTLNNIM-LLSMLSIQMMLL--MLESAVSIIQAYVFSILLTLYSSE 220
Cdd:MTH00073  159 VRLTANLTAGHLLIQLISTATLVLLPLMpTVSILTMIVLFLltLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 82-217 1.00e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 97.03  E-value: 1.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  82 NFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAIRLAA 161
Cdd:MTH00172   86 NLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAA 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1938966152 162 NMIAGHLLLTLLGNSG-STLNNIMLLSMLSIQMMLLM--LESAVSIIQAYVFSILLTLY 217
Cdd:MTH00172  166 NLSAGHLLFAILAGFGfNMLCASGFLSLFPLLIMVFItlLEIAVAVIQAYVFCLLTTIY 224
ATP-synt_A pfam00119
ATP synthase A chain;
81-219 6.56e-24

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 94.48  E-value: 6.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  81 NNFLGLF---PYIFTSSSHMVMTLSIALPMWLSFNLFGWMKK--TNYMFSHLLPlGTPSLLMPFMVCIETISNLIRPGTL 155
Cdd:pfam00119  71 SNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIKKHglGGYFKKLFVP-PVPLPLVPLLLPIEIISEFARPVSL 149

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938966152 156 AIRLAANMIAGHLLLTL---LGNSGSTLNNIMLLSMLSIQMMLLMLESAVSIIQAYVFSILLTLYSS 219
Cdd:pfam00119 150 SLRLFGNMLAGHLLLLLlagLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 82-217 2.21e-23

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 93.92  E-value: 2.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  82 NFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAIRLAA 161
Cdd:MTH00175   97 NILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAA 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1938966152 162 NMIAGHLLLTLLgnSGSTLNNIML-LSMLSIQMMLLM-----LESAVSIIQAYVFSILLTLY 217
Cdd:MTH00175  177 NISAGHLLFAIL--SGFAFNMLSNgLIILSLFPMLIMifitlLEMAVAVIQAYVFCLLTTIY 236
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 81-217 3.33e-18

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: 79.35  E-value: 3.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  81 NNFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAIRLA 160
Cdd:COG0356    71 SNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHLFFPPFPWLAPLMLPIEIISELARPLSLSLRLF 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1938966152 161 ANMIAGHLLLTLLGNSGSTLNNIMLLSMLSIQMMLlmLESAVSIIQAYVFSILLTLY 217
Cdd:COG0356   151 GNMFAGHIILLLLAGLAPFLLLGVLSLLLPVAWTA--FELLVGFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 82-217 4.90e-16

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 73.68  E-value: 4.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  82 NFLGLFP-YIFTSSSHMVMTLSIALPMWLSFNLFG-WMKKTNYMFSHLLPLgtpslLMPFMVCIETISNLIRPGTLAIRL 159
Cdd:PRK05815   87 NLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQ-----PHPLLLPIEIISEFSRPISLSLRL 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1938966152 160 AANMIAGHLLLTLLGnSGSTLNNIMLLSMLSIQMMLLMLESAVSIIQAYVFSILLTLY 217
Cdd:PRK05815  162 FGNMLAGELILALIA-LLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 82-217 2.84e-15

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 72.28  E-value: 2.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  82 NFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAIRLAA 161
Cdd:MTH00174  105 NGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAA 184

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152 162 NMIAGHLLLTLLGNSGSTLNNIMLL----SMLSIQMMLLMLESAVSIIQAYVFSILLTLY 217
Cdd:MTH00174  185 NISSGHLLFSIIASFAWKMINTGILigsfVPFAILIFVTILEMAVAIIQAYVFTLLTIVY 244
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 82-217 1.15e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 57.06  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  82 NFLGLFPYIFTSSSHMVMTLSIALPMWL--SFNLFGWMKKTNYmFSHLLPlGTPSLLMPFMVCIETISNLIRPGTLAIRL 159
Cdd:PRK13419  185 NLLGLVPYGATATGNINVTLTLAVFTFFitQYAAIKAHGIKGY-LAHLTG-GTHWSLWIIMIPIEFIGLFTKPFALTVRL 262

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1938966152 160 AANMIAGHL-LLTLLGNSgSTLNNIMLLSMLSIQMMLL--MLESAVSIIQAYVFSILLTLY 217
Cdd:PRK13419  263 FANMTAGHIvILSLIFIS-FILKSYIVAVAVSVPFAIFiyLLELFVAFLQAYIFTMLSALF 322
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 16-220 2.00e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 49.59  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  16 MNMSLNWTSTIMMMYIMPMSYWLNKSRSSMVFKLNLSILNKEFYSIINHKSGVIIFISMFIMIMMNnFLGLFPYIFTSSS 95
Cdd:MTH00087    1 MNQVFFLDVFMFVFLLQYLLYFKESMLNVLVKKFFGLLIIVFSYSNKLPLSSVISFFTFIVLLLFC-FGGLFPYSFSPCG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  96 HMVMTLSIALPMWLSFNLFGWMKKtnYMFSHLLPLGTPSLLMPF-MVCIETISNLIRPGTLAIRLAANMIAGHLLLTLLg 174
Cdd:MTH00087   80 MVEFTFLYALVAWLSTFLSFLSKS--EKFSVYLSKGSDSFLKTFsMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLL- 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1938966152 175 nsgstlnNIMLLSMLSIQMMLLMLESAVSIIQAYVFSILLTLYSSE 220
Cdd:MTH00087  157 -------NFLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 92-217 1.01e-05

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 45.27  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  92 TSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETI-SNLIRPGTLAIRLAANMIAGH-LL 169
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHvII 296

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1938966152 170 LTLLG---NSGSTLnnIMLLSMLSiQMMLLMLESAVSIIQAYVFSILLTLY 217
Cdd:PRK13417  297 LALMGfifQFQSWG--IVPVSVIG-SGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 87-175 2.31e-05

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 43.33  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  87 FPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKKTNYMFSHLLPLGTPSLLMPFMVCIETISNLIRPGTLAIRLAANMIAG 166
Cdd:MTH00050   42 LPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLG 121


                  ....*....
gi 1938966152 167 HLLLTLLGN 175
Cdd:MTH00050  122 CFGGVALGN 130
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 82-217 2.57e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 37.80  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966152  82 NFLGLFPYIFTSSSHMVMTLSIALPMWLSFNLFGWMKK--TNYMFSHLLPlgTPSLLmPFMVcietISNLIRPGTLAIRL 159
Cdd:PRK13420   89 NLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEglREYLKHYLSP--SPFLL-PFHL----ISEITRTLALAVRL 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1938966152 160 AANMIAGHLLLTLlgnsgstlnnIMLLSMLSIQMMLLMLESAVSIIQAYVFSILLTLY 217
Cdd:PRK13420  162 FGNIMSLELAALL----------VLLVAGFLVPVPILMLHIIEALVQAYIFGMLALIY 209
 
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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