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Conserved domains on  [gi|1893869119|gb|QNH68978|]
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ATP synthase F0 subunit 6 [Ergatettix serrifemora]

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
 1-223 4.90e-91

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 266.65  E-value: 4.90e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119   1 MMTNLFSSFDPSTSNMVSMNWVSMLLFTTIMPTSFWLIKSRSYTMMKMITKKMNNELNTIMNNKNKESTIMFISLFLLIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  81 INNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLSIRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1893869119 161 AANMIAGHLLMTLLGNTGSKLNYIMMMSMLTIQVLLLMLESAVSVIQAYVFSVLTTLYSSEMN 223
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-223 4.90e-91

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 266.65  E-value: 4.90e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119   1 MMTNLFSSFDPSTSNMVSMNWVSMLLFTTIMPTSFWLIKSRSYTMMKMITKKMNNELNTIMNNKNKESTIMFISLFLLIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  81 INNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLSIRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1893869119 161 AANMIAGHLLMTLLGNTGSKLNYIMMMSMLTIQVLLLMLESAVSVIQAYVFSVLTTLYSSEMN 223
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-221 1.78e-51

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: 166.23  E-value: 1.78e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119   5 LFSSFDPSTSNMV--SMNWVSMLLFTTIMPTSF----WLIKSRSYTMMKMITKKMNNELNTIMNNKNKESTIMFISLFLL 78
Cdd:TIGR01131   1 LFSQFDISPITLFslTLLSLILLLSLLIFLISSslsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  79 IMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLSI 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1893869119 159 RLAANMIAGHLLMTLLGNTGSKLNYIMMMSM-LTIQVLLLMLESAVSVIQAYVFSVLTTLYSSE 221
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIFALlLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 71-220 1.50e-45

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: 148.70  E-value: 1.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  71 MFISLFLLIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTI 150
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119 151 IRPGTLSIRLAANMIAGHLLMTLLGNTGSKLNYIMMMSMLTIQVLLLMLESAVSVIQAYVFSVLTTLYSS 220
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
19-220 3.92e-31

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 113.35  E-value: 3.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  19 MNWVSMLLFTTIMPTSFWLIK----SRSYTMMKMITKKMNNELNTIMNNKNKESTIMFI-SLFLLIMINNVMGLF---PY 90
Cdd:pfam00119   3 MSLIVALILLLFLLLATRKTKklvpGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLlTLFFFILVSNLLGLIpksPG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  91 IFTSSSHMVMTLSLALPMWLSFNIFG-WINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLSIRLAANMIAGHL 169
Cdd:pfam00119  83 GFTVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHL 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1893869119 170 LMTL---LGNTGSKLNYIMMMSMLTIQVLLLMLESAVSVIQAYVFSVLTTLYSS 220
Cdd:pfam00119 163 LLLLlagLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 45-218 5.55e-25

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: 97.45  E-value: 5.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  45 MMKMITKKMNNELNTIMNNKNKESTIMFISLFLLIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFG-WINKTNH 123
Cdd:COG0356    34 FVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119 124 MFEHMVPMGTPtILMPFMVAIETISTIIRPGTLSIRLAANMIAGHLLMTLLGNTGSKLnyIMMMSMLTIQVLLLMLESAV 203
Cdd:COG0356   114 YLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFL--LLGVLSLLLPVAWTAFELLV 190

                         170
                  ....*....|....*
gi 1893869119 204 SVIQAYVFSVLTTLY 218
Cdd:COG0356   191 GFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-223 4.90e-91

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 266.65  E-value: 4.90e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119   1 MMTNLFSSFDPSTSNMVSMNWVSMLLFTTIMPTSFWLIKSRSYTMMKMITKKMNNELNTIMNNKNKESTIMFISLFLLIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  81 INNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLSIRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1893869119 161 AANMIAGHLLMTLLGNTGSKLNYIMMMSMLTIQVLLLMLESAVSVIQAYVFSVLTTLYSSEMN 223
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-221 1.78e-51

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: 166.23  E-value: 1.78e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119   5 LFSSFDPSTSNMV--SMNWVSMLLFTTIMPTSF----WLIKSRSYTMMKMITKKMNNELNTIMNNKNKESTIMFISLFLL 78
Cdd:TIGR01131   1 LFSQFDISPITLFslTLLSLILLLSLLIFLISSslsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  79 IMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLSI 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1893869119 159 RLAANMIAGHLLMTLLGNTGSKLNYIMMMSM-LTIQVLLLMLESAVSVIQAYVFSVLTTLYSSE 221
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIFALlLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-221 3.09e-48

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 157.89  E-value: 3.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119   1 MMTNLFSSFDPSTSN---MVSMNWVSMLLFTTIMPTSFWLIKSRSYTMMKMITKKMNNELNTIMNNKNKESTIMFISLFL 77
Cdd:MTH00176    1 MLVDLFSSFDPPNKNifsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  78 LIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLS 157
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1893869119 158 IRLAANMIAGHLLMTLLGNTGSKL---NYIMMMSMLTIQVLLLMLESAVSVIQAYVFSVLTTLYSSE 221
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLlpvSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDE 227
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 71-220 1.50e-45

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: 148.70  E-value: 1.50e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  71 MFISLFLLIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTI 150
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119 151 IRPGTLSIRLAANMIAGHLLMTLLGNTGSKLNYIMMMSMLTIQVLLLMLESAVSVIQAYVFSVLTTLYSS 220
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 3-221 4.50e-42

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 142.03  E-value: 4.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119   3 TNLFSSFDPSTSNMVSMNWVSM---LLFTTIMPTSFWLIkSRSYTMMKMITKKMNNELNTIMNNKNKESTIMFISLFLLI 79
Cdd:MTH00035    5 NSIFGQFSPDTILFIPLTLLSSviaLSWLFFINPTNWLP-SRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  80 MINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLSIR 159
Cdd:MTH00035   84 LSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLR 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1893869119 160 LAANMIAGHLLMTLLGNTGSKL--NYIMMMSMLTIQVLLLMLESAVSVIQAYVFSVLTTLYSSE 221
Cdd:MTH00035  164 LAANLTAGHLLIFLLSTAIWELsnSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-221 2.44e-41

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 140.25  E-value: 2.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119   1 MMTNLFSSFDPSTSNMV-----SMNWVSMLLFTTIMPTSFWLIKSRSYTMMKMITKKMNNELNTIMNNKNKESTIMFISL 75
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFnnlssTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  76 FLLIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGT 155
Cdd:MTH00005   81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1893869119 156 LSIRLAANMIAGHLLMTLLGNTGSKLNY---IMMMSMLTIQVLLLMLESAVSVIQAYVFSVLTTLYSSE 221
Cdd:MTH00005  161 LSFRLAANMSAGHIVLSLIGIYAASALFssiSSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-221 4.57e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 136.92  E-value: 4.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119   1 MMTNLFSSFDPSTSNMVSMN---WVSMLLFTTIMPTSFWLIKSRSYTMMKMITKKMNNELNTIMNNKNKESTIMFISLFL 77
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSSLSflmWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  78 LIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLS 157
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1893869119 158 IRLAANMIAGHLLMTLLGNTGSKL----NYIMMMSMLTIQVLLLMLESAVSVIQAYVFSVLTTLYSSE 221
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYLSSSlfssSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-221 9.27e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 136.23  E-value: 9.27e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119   1 MMTNLFSSFDPSTSNMVSMNWVSMLLFTTIMPTS-FWLIKSRSYTMMKMITKKMNNELNTIMNNKNKESTIMFISLFLLI 79
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLtNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  80 MINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLSIR 159
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1893869119 160 LAANMIAGHLLMTLLGNTGSKLNYIM-MMSMLT--IQVLLLMLESAVSVIQAYVFSVLTTLYSSE 221
Cdd:MTH00179  161 LTANITAGHLLMHLISSAVFVLMNFMgMVALLTllVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-221 5.96e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 134.18  E-value: 5.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119   1 MMTNLFSSFDPSTSNMVSMNWVSMLLFTTIMPT-SFWLIKSRSYTMMKMITKKMNNELNTIMNNKNKESTIMFISLFLLI 79
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSpKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  80 MINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLSIR 159
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1893869119 160 LAANMIAGHLLMTLLGN-TGSKLNYIMMMSMLTIQVLLL--MLESAVSVIQAYVFSVLTTLYSSE 221
Cdd:MTH00120  161 LTANLTAGHLLIQLISTaTLNLLPTMPTLSLLTLIILLLltILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-218 2.32e-38

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 132.38  E-value: 2.32e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119   1 MMTNLFSSFDPSTSNMVSMNWVSMLLFTTIMPTSFWLIKSRSYTMMKMITKKMNNELNTIMNNKNKESTIMFISLFLLIM 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  81 INNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLSIRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1893869119 161 AANMIAGHLLMTLLGNTGSKLNYIMMMSML---TIQVLLLMLESAVSVIQAYVFSVLTTLY 218
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALitfIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 25-221 2.30e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 124.60  E-value: 2.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  25 LLFTTimPTSFWLiKSRSYTMMKMITKKMNNELNTIMNNKNKESTIMFISLFLLIMINNVMGLFPYIFTSSSHMVMTLSL 104
Cdd:MTH00132   29 ILFPT--PTSRWL-NNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119 105 ALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLSIRLAANMIAGHLLMTLLGNTGSKLNYI 184
Cdd:MTH00132  106 AVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAAFVLLPL 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1893869119 185 MMM-SMLTIQVLLLM--LESAVSVIQAYVFSVLTTLYSSE 221
Cdd:MTH00132  186 MPTvAILTATLLFLLtlLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-221 7.30e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 123.54  E-value: 7.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119   1 MMTNLFSSFDPSTSNMVSMNWVSMLL--FTTIMPTSFWLiKSRSYTMMKMITKKMNNELNTIMNNKNKESTIMFISLFLL 78
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLpwLLFPTPTNKWL-NNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  79 IMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLSI 158
Cdd:MTH00073   80 LITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1893869119 159 RLAANMIAGHLLMTLLGNTGSKLNYIM-MMSMLTIQVLLL--MLESAVSVIQAYVFSVLTTLYSSE 221
Cdd:MTH00073  160 RLTANLTAGHLLIQLISTATLVLLPLMpTVSILTMIVLFLltLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP-synt_A pfam00119
ATP synthase A chain;
19-220 3.92e-31

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 113.35  E-value: 3.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  19 MNWVSMLLFTTIMPTSFWLIK----SRSYTMMKMITKKMNNELNTIMNNKNKESTIMFI-SLFLLIMINNVMGLF---PY 90
Cdd:pfam00119   3 MSLIVALILLLFLLLATRKTKklvpGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLlTLFFFILVSNLLGLIpksPG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  91 IFTSSSHMVMTLSLALPMWLSFNIFG-WINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLSIRLAANMIAGHL 169
Cdd:pfam00119  83 GFTVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHL 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1893869119 170 LMTL---LGNTGSKLNYIMMMSMLTIQVLLLMLESAVSVIQAYVFSVLTTLYSS 220
Cdd:pfam00119 163 LLLLlagLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 37-218 1.45e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 107.43  E-value: 1.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  37 LIKSRSYTMMKMItkkMNNELNTIMNNKNKESTIMF---ISLFLLIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFN 113
Cdd:MTH00172   40 LIPKRWQSIIEII---YNHFHGVVKDNLGNEGLKYFpfiISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVT 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119 114 IFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLSIRLAANMIAGHLLMTLLGNTGSKL---NYIMMMSML 190
Cdd:MTH00172  117 LAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNMlcaSGFLSLFPL 196

                         170       180
                  ....*....|....*....|....*...
gi 1893869119 191 TIQVLLLMLESAVSVIQAYVFSVLTTLY 218
Cdd:MTH00172  197 LIMVFITLLEIAVAVIQAYVFCLLTTIY 224
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 36-218 3.27e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 103.93  E-value: 3.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  36 WLIKSRSYTMMKMITKKMNNELNTIMNNKNKESTIMFISLFLLIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIF 115
Cdd:MTH00175   50 KLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119 116 GWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLSIRLAANMIAGHLLMTLLgntgSKLNYIMMMSML----- 190
Cdd:MTH00175  130 GFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAIL----SGFAFNMLSNGLiilsl 205

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1893869119 191 ---TIQVLLLMLESAVSVIQAYVFSVLTTLY 218
Cdd:MTH00175  206 fpmLIMIFITLLEMAVAVIQAYVFCLLTTIY 236
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 45-218 5.55e-25

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: 97.45  E-value: 5.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  45 MMKMITKKMNNELNTIMNNKNKESTIMFISLFLLIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFG-WINKTNH 123
Cdd:COG0356    34 FVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119 124 MFEHMVPMGTPtILMPFMVAIETISTIIRPGTLSIRLAANMIAGHLLMTLLGNTGSKLnyIMMMSMLTIQVLLLMLESAV 203
Cdd:COG0356   114 YLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFL--LLGVLSLLLPVAWTAFELLV 190

                         170
                  ....*....|....*
gi 1893869119 204 SVIQAYVFSVLTTLY 218
Cdd:COG0356   191 GFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 24-218 1.47e-21

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 88.70  E-value: 1.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  24 MLLFTTIMPTSFWLIKSRSYTM--------MKMITKKMNNELNTIMNNKNKESTIMFISLFLLIMINNVMGLFP-YIFTS 94
Cdd:PRK05815   20 SVLLGVLILLLFALVATRKLSGvpgglqnfVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  95 SSHMVMTLSLALPMWLSFNIFG-WINKTNHMFEHMVPmgtptILMPFMVAIETISTIIRPGTLSIRLAANMIAGHLLMTL 173
Cdd:PRK05815  100 TADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYL-----QPHPLLLPIEIISEFSRPISLSLRLFGNMLAGELILAL 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1893869119 174 LGNTGSkLNYIMMMSMLTIQVLLLMLESAVSVIQAYVFSVLTTLY 218
Cdd:PRK05815  175 IALLGG-AGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 14-218 3.07e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 88.46  E-value: 3.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  14 SNMVSMNWVSMLLFTTIMPTSF--WLIKSRSYTMMKMITKKMNNELNTIMNNKNKESTIMFISLFLLIMINNVMGLFPYI 91
Cdd:MTH00174   34 TNTFFMMSFAVFLFYTIGAKGNnnTLVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  92 FTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETISTIIRPGTLSIRLAANMIAGHLLM 171
Cdd:MTH00174  114 FTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLF 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1893869119 172 TLLGNTGSKL--NYIMMMSMLTIQVLLL--MLESAVSVIQAYVFSVLTTLY 218
Cdd:MTH00174  194 SIIASFAWKMinTGILIGSFVPFAILIFvtILEMAVAIIQAYVFTLLTIVY 244
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 73-218 3.71e-11

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 61.68  E-value: 3.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  73 ISLFLLIMINNVMGLFPYIFTSSSHMVMTLSLALpmwlsFNIFgwINKTNHMFEHMV-------PMGTPTILMPFMVAIE 145
Cdd:PRK13419  175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLAV-----FTFF--ITQYAAIKAHGIkgylahlTGGTHWSLWIIMIPIE 247

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1893869119 146 TISTIIRPGTLSIRLAANMIAGHL-LMTLLGNTGSKLNYIMMMSM-LTIQVLLLMLESAVSVIQAYVFSVLTTLY 218
Cdd:PRK13419  248 FIGLFTKPFALTVRLFANMTAGHIvILSLIFISFILKSYIVAVAVsVPFAIFIYLLELFVAFLQAYIFTMLSALF 322
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 93-218 6.56e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 54.90  E-value: 6.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  93 TSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETIST-IIRPGTLSIRLAANMIAGH-LL 170
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIVSpMAKTFALTVRLLANMTAGHvII 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1893869119 171 MTLLGNTGSKLNYIMMMSMLTIQVLLLMLESAVSVIQAYVFSVLTTLY 218
Cdd:PRK13417  297 LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 45-221 2.93e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 51.90  E-value: 2.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  45 MMKMITKKMNNELNTIMN--NKNKESTIMFISLFLLIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTn 122
Cdd:MTH00087   26 MLNVLVKKFFGLLIIVFSysNKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSE- 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119 123 hMFEHMVPMGTPTILMPF-MVAIETISTIIRPGTLSIRLAANMIAGHLLMTLLGNTGSKLNYIMmmsmltiqVLLLMLES 201
Cdd:MTH00087  105 -KFSVYLSKGSDSFLKTFsMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLLNFLGEKYVWLS--------ILAIMMEC 175

                         170       180
                  ....*....|....*....|
gi 1893869119 202 AVSVIQAYVFSVLTTLYSSE 221
Cdd:MTH00087  176 FVAFIQSYIFSRLIYLYLNE 195
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 68-187 7.71e-07

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 47.57  E-value: 7.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  68 STIMFISLFLLIMINnvmglFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINKTNHMFEHMVPMGTPTILMPFMVAIETI 147
Cdd:MTH00050   27 SVVLFIVLFLFLLYR-----LPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETI 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1893869119 148 STIIRPGTLSIRLAANMIAGHLLMTLLGNTGSKLNYIMMM 187
Cdd:MTH00050  102 SYIIRPVVLILRPFINISLGCFGGVALGNLCFISYWWFLV 141
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 74-218 2.47e-05

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 43.96  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  74 SLFLLIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWINK--TNHMFEHMVPmgTPtILMPFMVaietISTII 151
Cdd:PRK13420   80 TLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEglREYLKHYLSP--SP-FLLPFHL----ISEIT 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1893869119 152 RPGTLSIRLAANMIAGHLLMTLlgntgsklnyIMMMSMLTIQVLLLMLESAVSVIQAYVFSVLTTLY 218
Cdd:PRK13420  153 RTLALAVRLFGNIMSLELAALL----------VLLVAGFLVPVPILMLHIIEALVQAYIFGMLALIY 209
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
 74-214 4.48e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 36.98  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893869119  74 SLFLLIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNIFGWinKTNHMFEHMVPMGTPTilmPFMVAIETISTIIRP 153
Cdd:PRK13421   83 TLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGV--RARGVRGYLATFAEPT---WVMIPLNLVEQLTRT 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1893869119 154 GTLSIRLAANMIAGHLLMTLlgntgsklnyIMMMSMLTIQVLLLMLESAVSVIQAYVFSVL 214
Cdd:PRK13421  158 FSLIVRLFGNVMSGVFVIGI----------VLSLAGLLVPIPLMALDLLTGAVQAYIFAVL 208
 
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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