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Conserved domains on  [gi|1824665973|ref|YP_009740931|]
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ATP synthase F0 subunit 6 (mitochondrion) [Filchnerella tenggerensis]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009593)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 3.33e-104

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 300.16  E-value: 3.33e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973   1 MMSNLFSTFDPSTSiFNLSLNWTSTFIGLLIIPSLFWLTPSRINILWNKLNLTLHNEFKTLLGPKsFNGTTFIFISIFIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  81 MLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNIIRPGTLAV 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824665973 161 RLAANMIAGHLLLTLLGNTGPMIGFNLISILIIGQMMLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 3.33e-104

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 300.16  E-value: 3.33e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973   1 MMSNLFSTFDPSTSiFNLSLNWTSTFIGLLIIPSLFWLTPSRINILWNKLNLTLHNEFKTLLGPKsFNGTTFIFISIFIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  81 MLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNIIRPGTLAV 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824665973 161 RLAANMIAGHLLLTLLGNTGPMIGFNLISILIIGQMMLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-225 6.37e-46

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: 151.98  E-value: 6.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973   5 LFSTFDPST-SIFNLSLNWTSTFIGLLIIPSLF----WLTPSRINILWNKLNLTLHNEFKTLLGPKSFNGTTFIFiSIFI 79
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFLISSslsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  80 MMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNIIRPGTLA 159
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1824665973 160 VRLAANMIAGHLLLTLLGNTGP-MIGFNLISILIIGQMMLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFsLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 73-222 5.44e-41

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: 137.15  E-value: 5.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  73 IFISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNI 152
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973 153 IRPGTLAVRLAANMIAGHLLLTLLGNTGPMIGFNLISILIIGQMMLLILESAVAMIQAYVFSILSTLYSS 222
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
22-222 1.94e-25

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 98.72  E-value: 1.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  22 WTSTFIGLLIIPSLFWLT----PSRINILWNKLNLTLHNEFKTLLGPKSFNGTTFIFISIFIMMLFNNFMGLF---PYIF 94
Cdd:pfam00119   5 LIVALILLLFLLLATRKTkklvPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  95 TSTSHLALTFAIALPMWLSFMLFGWINH-TNHMFAHLVPQGTPPALMSFMVLIETISNIIRPGTLAVRLAANMIAGHLLL 173
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1824665973 174 TLLGNTGPMIGFNLIS---ILIIGQMMLLILESAVAMIQAYVFSILSTLYSS 222
Cdd:pfam00119 165 LLLAGLIFALLSAGFLlgvIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 76-220 3.24e-21

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: 87.44  E-value: 3.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  76 SIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINH-TNHMFAHLVPQGTPPaLMSFMVLIETISNIIR 154
Cdd:COG0356    63 TLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPW-LAPLMLPIEIISELAR 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1824665973 155 PGTLAVRLAANMIAGHLLLTLLGNTGPMIGFNLISILIigQMMLLILESAVAMIQAYVFSILSTLY 220
Cdd:COG0356   142 PLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 3.33e-104

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 300.16  E-value: 3.33e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973   1 MMSNLFSTFDPSTSiFNLSLNWTSTFIGLLIIPSLFWLTPSRINILWNKLNLTLHNEFKTLLGPKsFNGTTFIFISIFIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  81 MLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNIIRPGTLAV 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824665973 161 RLAANMIAGHLLLTLLGNTGPMIGFNLISILIIGQMMLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-225 3.76e-54

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 173.30  E-value: 3.76e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973   1 MMSNLFSTFDPSTSIF--NLSLNWTSTFIGLLIIPSLFWLTPSRINILWNKLNlTLHNEFKTLLGPKSFNGTTFIFISIF 78
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIfsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFS-TFLPEMILRSNGSYILGSASIIISLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  79 IMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNIIRPGTL 158
Cdd:MTH00176   80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973 159 AVRLAANMIAGHLLLTLLGNTGP---MIGFNLISILIIGQMMLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:MTH00176  160 AVRLAANLSAGHLLLGLLGAAMWgllPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-225 6.37e-46

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: 151.98  E-value: 6.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973   5 LFSTFDPST-SIFNLSLNWTSTFIGLLIIPSLF----WLTPSRINILWNKLNLTLHNEFKTLLGPKSFNGTTFIFiSIFI 79
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFLISSslsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  80 MMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNIIRPGTLA 159
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1824665973 160 VRLAANMIAGHLLLTLLGNTGP-MIGFNLISILIIGQMMLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFsLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 73-222 5.44e-41

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: 137.15  E-value: 5.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  73 IFISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNI 152
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973 153 IRPGTLAVRLAANMIAGHLLLTLLGNTGPMIGFNLISILIIGQMMLLILESAVAMIQAYVFSILSTLYSS 222
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-223 8.86e-41

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 139.10  E-value: 8.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973   1 MMSNLFSTFDPSTSIFNLSLN----WTSTFIGLLIIPSLFWLTPSRINILWNKLNLTLHNEFKTLLGpKSFNGTTFIFIS 76
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFNNLSstafWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFG-KHLKGFSSLISA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  77 IFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNIIRPG 156
Cdd:MTH00005   80 LFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973 157 TLAVRLAANMIAGHLLLTLLGNTGPMIGFNLIS---ILIIGQMMLLILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00005  160 TLSFRLAANMSAGHIVLSLIGIYAASALFSSISstiLLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-223 1.24e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 133.45  E-value: 1.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973   1 MMSNLFSTFDPSTSIFNL--SLNWTSTFIGLLIIPSLFWLTPSRINILWNKLNLTLHNEFKTLLGpKSFNGTTFIFISIF 78
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSSlsFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSG-LNLGGFSLLLSSLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  79 IMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNIIRPGTL 158
Cdd:MTH00173   80 LFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1824665973 159 AVRLAANMIAGHLLLTLLGNTGP----MIGFNLISILIIGQMMLLILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00173  160 TVRLLANISAGHIVLTLIGNYLSsslfSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 3-223 4.13e-38

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 132.02  E-value: 4.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973   3 SNLFSTFDPSTsIFNLSLNWTSTFIGL---LIIPSLFWLtPSRINILWNKLNLTLHNEFKTLLGPKSFNGTTFIFiSIFI 79
Cdd:MTH00035    5 NSIFGQFSPDT-ILFIPLTLLSSVIALswlFFINPTNWL-PSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLT-TVFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  80 MMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNIIRPGTLA 159
Cdd:MTH00035   82 LILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALG 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973 160 VRLAANMIAGHLLLTLLGNT------GPMIGFNLISILIIgqmmLLILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00035  162 LRLAANLTAGHLLIFLLSTAiwelsnSPLISIITLIIFFL----LFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-223 1.12e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 123.13  E-value: 1.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973   1 MMSNLFSTFDpSTSIFNLSLNWTSTFIGLLIIPSL-FWLTPSRINILWNKLNLTLHNEFKTLLGPKSFNGTtFIFISIFI 79
Cdd:MTH00179    1 MMLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLtNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWA-VLFLSLML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  80 MMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNIIRPGTLA 159
Cdd:MTH00179   79 FLLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1824665973 160 VRLAANMIAGHLLLTLLGNT--GPMIGFNLISILI-IGQMMLLILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00179  159 VRLTANITAGHLLMHLISSAvfVLMNFMGMVALLTlLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-223 8.55e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 120.70  E-value: 8.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973   1 MMSNLFSTFDPSTSIFnlslnwTSTFIGLLIIPSLFWLTPS---RINILWNKLNLTLHNEFKTLLGPKSFNGT--TFIFI 75
Cdd:MTH00120    1 MNLNFFDQFSSPELLG------IPLILLAMLIPALLIPSPKnrlLTNRLTTLQLWLIKLITKQLMLPLNKKGHkwALILT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  76 SIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNIIRP 155
Cdd:MTH00120   75 SLMLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRP 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824665973 156 GTLAVRLAANMIAGH-------LLLTLLGNTGPMIGFNLISILiigqMMLLILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00120  155 LALGVRLTANLTAGHlliqlisTATLNLLPTMPTLSLLTLIIL----LLLTILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 73-223 1.31e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 112.66  E-value: 1.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  73 IFISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNI 152
Cdd:MTH00132   72 LLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLF 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1824665973 153 IRPGTLAVRLAANMIAGHLLLTLLGNTGPMIGFNLISILIIGQMMLL---ILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00132  152 IRPLALGVRLTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFlltLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-223 1.39e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 112.37  E-value: 1.39e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973   1 MMSNLFSTFdPSTSIFNLSLNWTSTFIGLLII--PSLFWLTpSRINILwnkLNLTLHNEFKTLLGPKSFNGT--TFIFIS 76
Cdd:MTH00073    1 MNLSFFDQF-LSPTLLGIPLIMLAMLLPWLLFptPTNKWLN-NRLSTL---QIWFLQNFTKQLMLPLNTPGHkwALILTS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  77 IFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNIIRPG 156
Cdd:MTH00073   76 LMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973 157 TLAVRLAANMIAGHLLLTLLGNTGPMIGFNLISILIIGQMMLL---ILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00073  156 ALGVRLTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFlltLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 71-220 8.43e-28

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 105.03  E-value: 8.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  71 TFIFISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETIS 150
Cdd:MTH00101   69 SLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETIS 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1824665973 151 NIIRPGTLAVRLAANMIAGHLLLTLLGNTG---PMIGFNLISILIIGQMMLLILESAVAMIQAYVFSILSTLY 220
Cdd:MTH00101  149 LFIQPMALAVRLTANITAGHLLIHLIGGATlalMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP-synt_A pfam00119
ATP synthase A chain;
22-222 1.94e-25

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 98.72  E-value: 1.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  22 WTSTFIGLLIIPSLFWLT----PSRINILWNKLNLTLHNEFKTLLGPKSFNGTTFIFISIFIMMLFNNFMGLF---PYIF 94
Cdd:pfam00119   5 LIVALILLLFLLLATRKTkklvPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  95 TSTSHLALTFAIALPMWLSFMLFGWINH-TNHMFAHLVPQGTPPALMSFMVLIETISNIIRPGTLAVRLAANMIAGHLLL 173
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1824665973 174 TLLGNTGPMIGFNLIS---ILIIGQMMLLILESAVAMIQAYVFSILSTLYSS 222
Cdd:pfam00119 165 LLLAGLIFALLSAGFLlgvIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 15-220 8.78e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 94.72  E-value: 8.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  15 IFNLSLNWTSTFIGLLIIPSLFWLTPSRINILWNKLNLTLHNEFKTLLGPKSFNGTTFIfISIFIMMLFNNFMGLFPYIF 94
Cdd:MTH00172   17 LTNSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFI-ISLFFFIVFLNLLGLFPYVF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  95 TSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNIIRPGTLAVRLAANMIAGHLLLT 174
Cdd:MTH00172   96 TPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFA 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1824665973 175 LLGNTG-----PMIGFNLISILIIgqMMLLILESAVAMIQAYVFSILSTLY 220
Cdd:MTH00172  176 ILAGFGfnmlcASGFLSLFPLLIM--VFITLLEIAVAVIQAYVFCLLTTIY 224
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 37-220 1.85e-22

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 91.61  E-value: 1.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  37 WLTPSRINILWNKLNLTLHNEFKTLLGPKSFNGTTFIFiSIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFML 116
Cdd:MTH00175   50 KLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFIL-SLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973 117 FGWINHTNHMFAHLVPQGTPPALMSFMVLIETISNIIRPGTLAVRLAANMIAGHLLLTLLGNTGPMIGFNLISILIIGQM 196
Cdd:MTH00175  129 LGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNGLIILSLFPM 208

                         170       180
                  ....*....|....*....|....*...
gi 1824665973 197 MLLI----LESAVAMIQAYVFSILSTLY 220
Cdd:MTH00175  209 LIMIfitlLEMAVAVIQAYVFCLLTTIY 236
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 76-220 3.24e-21

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: 87.44  E-value: 3.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  76 SIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINH-TNHMFAHLVPQGTPPaLMSFMVLIETISNIIR 154
Cdd:COG0356    63 TLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPW-LAPLMLPIEIISELAR 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1824665973 155 PGTLAVRLAANMIAGHLLLTLLGNTGPMIGFNLISILIigQMMLLILESAVAMIQAYVFSILSTLY 220
Cdd:COG0356   142 PLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 73-220 1.96e-17

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 77.53  E-value: 1.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  73 IFISIFIMMLFNNFMGLFP-YIFTSTSHLALTFAIALPMWLSFMLFG-WINHTNHMFAHLVPQGTPpalmsFMVLIETIS 150
Cdd:PRK05815   75 LAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQPHP-----LLLPIEIIS 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973 151 NIIRPGTLAVRLAANMIAGHLLLTLLGNTGPMIGFNLISILIIGqMMLLILESAVAMIQAYVFSILSTLY 220
Cdd:PRK05815  150 EFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILP-VAWTIFEIFVGTLQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 38-220 2.64e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 78.06  E-value: 2.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  38 LTPSRINILWNKLNLTLHNEFKTLLGPKSFNGTTFIfISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLF 117
Cdd:MTH00174   59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFV-LSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973 118 GWINHTNHMFAHLVPQGTPPALMSFMVLIETISNIIRPGTLAVRLAANMIAGHLLLTLLG-------NTGPMIG-FNLIS 189
Cdd:MTH00174  138 GLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIAsfawkmiNTGILIGsFVPFA 217

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1824665973 190 ILIigqmMLLILESAVAMIQAYVFSILSTLY 220
Cdd:MTH00174  218 ILI----FVTILEMAVAIIQAYVFTLLTIVY 244
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 75-220 9.84e-12

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 63.22  E-value: 9.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  75 ISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALpmwLSFMLFGWINHTNH----MFAHLVpQGTPPALMSFMVLIETIS 150
Cdd:PRK13419  175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLAV---FTFFITQYAAIKAHgikgYLAHLT-GGTHWSLWIIMIPIEFIG 250

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1824665973 151 NIIRPGTLAVRLAANMIAGHLLLTLLGNTGPMIGFNLISILIIGQMMLLI--LESAVAMIQAYVFSILSTLY 220
Cdd:PRK13419  251 LFTKPFALTVRLFANMTAGHIVILSLIFISFILKSYIVAVAVSVPFAIFIylLELFVAFLQAYIFTMLSALF 322
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 72-223 7.31e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 50.75  E-value: 7.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  72 FIFISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINhtNHMFAHLVPQGTPPALMSF-MVLIETIS 150
Cdd:MTH00087   53 VISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSK--SEKFSVYLSKGSDSFLKTFsMLFVEIVS 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1824665973 151 NIIRPGTLAVRLAANMIAGHLLLTLLGNTGpmIGFNLISILIIgqmmllILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00087  131 ELSRPLALTLRLTVNLMVGHLISSLLNFLG--EKYVWLSILAI------MMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 75-220 5.33e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 46.42  E-value: 5.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  75 ISIFIMMLFNNFMGLFPYI-----------------------------------FTSTSHLALTFAIALPMWLSFMLFGW 119
Cdd:PRK13417  162 FTLFFFILFCNLMGLVPSVgeltvvasdygglvalgvmdhtphalptfakvwsgITVTGDISVTMTLALLTMFLIYGAGF 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973 120 INHTNHMFAHLVPQGTPPALMSFMVLIETI-SNIIRPGTLAVRLAANMIAGHLLLT-LLGNTGPMIGFNLISILIIGQMM 197
Cdd:PRK13417  242 SYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVIILaLMGFIFQFQSWGIVPVSVIGSGL 321

                         170       180
                  ....*....|....*....|...
gi 1824665973 198 LLILESAVAMIQAYVFSILSTLY 220
Cdd:PRK13417  322 IYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 67-217 6.09e-05

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 42.18  E-value: 6.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  67 FNGTTFIFISIFIMMLFNNFMGL-FPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFAHLVPQGTPPALMSFMVL 145
Cdd:MTH00050   18 LGGSVSYYYSVVLFIVLFLFLLYrLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCI 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1824665973 146 IETISNIIRPGTLAVRLAANMIAGHLLLTLLGNTGpMIGFNLISILIIgqmmLLILESAVAMIQAY-VFSILS 217
Cdd:MTH00050   98 AETISYIIRPVVLILRPFINISLGCFGGVALGNLC-FISYWWFLVLFF----LFFYEVFVALVHWFiVSSILS 165
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 38-220 5.30e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 39.73  E-value: 5.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973  38 LTPSRINILWNKLNLTLHNEFKTLLgPKSFNGTTFIFISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLF 117
Cdd:PRK13420   43 LDPGRFQVALEGVVSTIEDAIKEVL-PRHARLVLPFVGTLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665973 118 G-----WINHTNHmfaHLVPQgtpPALMSFMVlietISNIIRPGTLAVRLAANMIAGHLLLTLLgntgPMIGFNLISILI 192
Cdd:PRK13420  122 GiraegLREYLKH---YLSPS---PFLLPFHL----ISEITRTLALAVRLFGNIMSLELAALLV----LLVAGFLVPVPI 187

                         170       180
                  ....*....|....*....|....*...
gi 1824665973 193 igqMMLLILEsavAMIQAYVFSILSTLY 220
Cdd:PRK13420  188 ---LMLHIIE---ALVQAYIFGMLALIY 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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