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Conserved domains on  [gi|1824665903|ref|YP_009740840|]
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ATP synthase F0 subunit 6 (mitochondrion) [Atractomorpha psittacina]

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
 1-224 6.24e-94

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 273.97  E-value: 6.24e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903   1 MMTNLFSTFDPSTSlFNLSINWSSTIMGMFLLPSMFWILPSRNSLFWNKLMLKIHQEFKTLTGNKHYGMTLMFISLFIMM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  81 MFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISNIIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1824665903 161 LAANMIAGHMMLTLLGNSGTMIKFNLLSMVIIAQMLLMMLESAVTLIQAYVFSILSTLYASETY 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-224 6.24e-94

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 273.97  E-value: 6.24e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903   1 MMTNLFSTFDPSTSlFNLSINWSSTIMGMFLLPSMFWILPSRNSLFWNKLMLKIHQEFKTLTGNKHYGMTLMFISLFIMM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  81 MFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISNIIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1824665903 161 LAANMIAGHMMLTLLGNSGTMIKFNLLSMVIIAQMLLMMLESAVTLIQAYVFSILSTLYASETY 224
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 9.50e-47

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: 153.90  E-value: 9.50e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903   5 LFSTFDPST-SLFNLSINW----SSTIMGMFLLPSMFWILPSRNSLFWNKLMLKIHQEFKTLTGNKHYGMTLMFISLFIM 79
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSlillLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  80 MMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISNIIRPGTLAV 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1824665903 160 RLAANMIAGHMMLTLLGNSG-TMIKFNLLSMVIIAQMLLMMLESAVTLIQAYVFSILSTLYASE 222
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLfSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 68-219 7.41e-42

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: 139.07  E-value: 7.41e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  68 GMTLMFISLFIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIET 147
Cdd:cd00310     3 KYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIEL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1824665903 148 ISNIIRPGTLAVRLAANMIAGHMMLTLLGNSGTMIKFNLLSMVIIAQMLLMMLESAVTLIQAYVFSILSTLY 219
Cdd:cd00310    83 ISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVY 154
ATP-synt_A pfam00119
ATP synthase A chain;
40-219 1.32e-25

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 99.10  E-value: 1.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  40 PSRNSLFWNKLMLKIHQEFKTLTGNKHYGM-TLMFISLFIMMMFNNFMGLF---PYIFTSTSHMVMTFSIALPMWMSFML 115
Cdd:pfam00119  27 PGRLQNFVEMLVEFVDNIVKDNIGKKKGRKfFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHY 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903 116 FGWINN-TTHMLTHLVPQGTPKLLMPFMVMIETISNIIRPGTLAVRLAANMIAGHMMLTLLGNSGTMIKFNLLSMVII-- 192
Cdd:pfam00119 107 YGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIpp 186

                         170       180
                  ....*....|....*....|....*...
gi 1824665903 193 -AQMLLMMLESAVTLIQAYVFSILSTLY 219
Cdd:pfam00119 187 lLGVAWTLFELLVAFIQAYVFTMLTAVY 214
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 72-219 1.69e-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: 88.21  E-value: 1.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  72 MFISLFIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFG-WINNTTHMLTHLVPQGTPkLLMPFMVMIETISN 150
Cdd:COG0356    60 LLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISE 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1824665903 151 IIRPGTLAVRLAANMIAGHMMLTLLGNSGTMIKFNLLSmvIIAQMLLMMLESAVTLIQAYVFSILSTLY 219
Cdd:COG0356   139 LARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLS--LLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-224 6.24e-94

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 273.97  E-value: 6.24e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903   1 MMTNLFSTFDPSTSlFNLSINWSSTIMGMFLLPSMFWILPSRNSLFWNKLMLKIHQEFKTLTGNKHYGMTLMFISLFIMM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  81 MFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISNIIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1824665903 161 LAANMIAGHMMLTLLGNSGTMIKFNLLSMVIIAQMLLMMLESAVTLIQAYVFSILSTLYASETY 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-224 4.66e-48

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 157.50  E-value: 4.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903   1 MMTNLFSTFDPSTSLF--NLSINWSSTIMGMFLLPSMFWILPSRNSLFWNKLMLKIHQEFKTLTGNKHYGMTLMFISLFI 78
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIfsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  79 MMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISNIIRPGTLA 158
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1824665903 159 VRLAANMIAGHMMLTLLGNSG---TMIKFNLLSMVIIAQMLLMMLESAVTLIQAYVFSILSTLYASETY 224
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMwglLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-222 9.50e-47

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: 153.90  E-value: 9.50e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903   5 LFSTFDPST-SLFNLSINW----SSTIMGMFLLPSMFWILPSRNSLFWNKLMLKIHQEFKTLTGNKHYGMTLMFISLFIM 79
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSlillLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  80 MMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISNIIRPGTLAV 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1824665903 160 RLAANMIAGHMMLTLLGNSG-TMIKFNLLSMVIIAQMLLMMLESAVTLIQAYVFSILSTLYASE 222
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLfSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-222 1.14e-42

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 143.72  E-value: 1.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903   1 MMTNLFSTFDPSTSLFNL----SINWSSTIMGMFLLPSMFWILPSRNSLFWNKLMLKIHQEFKTLTGNKHYGMTLMFISL 76
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFNnlssTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  77 FIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISNIIRPGT 156
Cdd:MTH00005   81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1824665903 157 LAVRLAANMIAGHMMLTLLGNSGTMIKFN---LLSMVIIAQMLLMMLESAVTLIQAYVFSILSTLYASE 222
Cdd:MTH00005  161 LSFRLAANMSAGHIVLSLIGIYAASALFSsisSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 68-219 7.41e-42

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: 139.07  E-value: 7.41e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  68 GMTLMFISLFIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIET 147
Cdd:cd00310     3 KYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIEL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1824665903 148 ISNIIRPGTLAVRLAANMIAGHMMLTLLGNSGTMIKFNLLSMVIIAQMLLMMLESAVTLIQAYVFSILSTLY 219
Cdd:cd00310    83 ISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVY 154
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-223 1.83e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 135.38  E-value: 1.83e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903   1 MMTNLFSTFDPSTSLFNL--SINWSSTIMGMFLLPSMFWILPSRNSLFWNKLMLKIHQEFKTLTGNKHYGMTLMFISLFI 78
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSSlsFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  79 MMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISNIIRPGTLA 158
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1824665903 159 VRLAANMIAGHMMLTLLGNSGT----MIKFNLLSMVIIAQMLLMMLESAVTLIQAYVFSILSTLYASET 223
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYLSsslfSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDEH 229
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 3-222 4.24e-39

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 134.72  E-value: 4.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903   3 TNLFSTFDPSTSLFnlsinWSSTIMGMFLLPSMFWI------LPSRNSLFWNKLMLKIHQEFKTLTGNKHYGMTLMFISL 76
Cdd:MTH00035    5 NSIFGQFSPDTILF-----IPLTLLSSVIALSWLFFinptnwLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  77 FIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISNIIRPGT 156
Cdd:MTH00035   80 FILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1824665903 157 LAVRLAANMIAGHMMLTLLGNSGTMIKFNLL--SMVIIAQMLLMMLESAVTLIQAYVFSILSTLYASE 222
Cdd:MTH00035  160 LGLRLAANLTAGHLLIFLLSTAIWELSNSPLisIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-222 4.56e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 121.59  E-value: 4.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903   1 MMTNLFSTFDpSTSLFNLSINWSSTIMGMFLLPSM-FWILPSRNSLFWNKLMLKIHQEFKTLTGNKHYGMTLMFISLFIM 79
Cdd:MTH00179    1 MMLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLtNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  80 MMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISNIIRPGTLAV 159
Cdd:MTH00179   80 LLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1824665903 160 RLAANMIAGHMMLTLLGnSGTMIKFNLLSMVIIAQ----MLLMMLESAVTLIQAYVFSILSTLYASE 222
Cdd:MTH00179  160 RLTANITAGHLLMHLIS-SAVFVLMNFMGMVALLTllvlFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-222 7.37e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 121.08  E-value: 7.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903   1 MMTNLFSTFDPSTSLFnlsinwSSTIMGMFLLPSMFWILPSrNSLFWNKLMLKIHQEFKTLTGN-------KHYGMTLMF 73
Cdd:MTH00120    1 MNLNFFDQFSSPELLG------IPLILLAMLIPALLIPSPK-NRLLTNRLTTLQLWLIKLITKQlmlplnkKGHKWALIL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  74 ISLFIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISNIIR 153
Cdd:MTH00120   74 TSLMLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1824665903 154 PGTLAVRLAANMIAGHMMLTLLGNSG-----TMIKFNLLSMVIIaqMLLMMLESAVTLIQAYVFSILSTLYASE 222
Cdd:MTH00120  154 PLALGVRLTANLTAGHLLIQLISTATlnllpTMPTLSLLTLIIL--LLLTILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 71-222 1.07e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 118.05  E-value: 1.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  71 LMFISLFIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISN 150
Cdd:MTH00132   71 LLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISL 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1824665903 151 IIRPGTLAVRLAANMIAGHMMLTLLGnSGTMIKFNLLSMVIIAQM----LLMMLESAVTLIQAYVFSILSTLYASE 222
Cdd:MTH00132  151 FIRPLALGVRLTANLTAGHLLIQLIA-TAAFVLLPLMPTVAILTAtllfLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-219 1.10e-31

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 115.43  E-value: 1.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903   1 MMTNLFSTFDPSTsLFNLSINWSSTIMGMFLLPSMFWILPSRNSLFWNKLMLKIHQEFKTLTGNKHYGMTLMFISLFIMM 80
Cdd:MTH00101    1 MNENLFASFITPT-ILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  81 MFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISNIIRPGTLAVR 160
Cdd:MTH00101   80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1824665903 161 LAANMIAGHMMLTLLGNSG---TMIKFNLLSMVIIAQMLLMMLESAVTLIQAYVFSILSTLY 219
Cdd:MTH00101  160 LTANITAGHLLIHLIGGATlalMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 71-222 1.41e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 109.67  E-value: 1.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  71 LMFISLFIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISN 150
Cdd:MTH00073   71 LILTSLMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISL 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1824665903 151 IIRPGTLAVRLAANMIAGHMMLTLLgNSGTMIKFNLLSMVIIAQM----LLMMLESAVTLIQAYVFSILSTLYASE 222
Cdd:MTH00073  151 FIRPLALGVRLTANLTAGHLLIQLI-STATLVLLPLMPTVSILTMivlfLLTLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 4-224 4.24e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 106.24  E-value: 4.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903   4 NLFSTFDPSTSLFNLSINWSSTIMGMFLLPSMFWILPSRNSLF---WNKLMLKIHQEFKTLT----GNKHYGMTLMFISL 76
Cdd:MTH00175   10 NIIRLITIQAFLGDWLVTFTNSSMMMVLAVIIFWLLLKGDKLIpnrWQSIMELIYLNIRSVVhdnlGKSGQKYFPFILSL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  77 FIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISNIIRPGT 156
Cdd:MTH00175   90 FLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAIS 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1824665903 157 LAVRLAANMIAGHMMLTLLGNSGTMIKFNLLSMVIIAQMLLMM----LESAVTLIQAYVFSILSTLYASETY 224
Cdd:MTH00175  170 LGVRLAANISAGHLLFAILSGFAFNMLSNGLIILSLFPMLIMIfitlLEMAVAVIQAYVFCLLTTIYLGDTI 241
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 15-223 6.04e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 105.51  E-value: 6.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  15 LFNLSINWSSTIMGMFLLPSMFWILPSRNSLFWNKLMLKIHQEFKTLTGNKHYGMTLMFISLFIMMMFNNFMGLFPYIFT 94
Cdd:MTH00172   17 LTNSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  95 STSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISNIIRPGTLAVRLAANMIAGHMMLTL 174
Cdd:MTH00172   97 PTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAI 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1824665903 175 LGNSGTMIK-----FNLLSMVIIAQMLLmmLESAVTLIQAYVFSILSTLYASET 223
Cdd:MTH00172  177 LAGFGFNMLcasgfLSLFPLLIMVFITL--LEIAVAVIQAYVFCLLTTIYLADT 228
ATP-synt_A pfam00119
ATP synthase A chain;
40-219 1.32e-25

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 99.10  E-value: 1.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  40 PSRNSLFWNKLMLKIHQEFKTLTGNKHYGM-TLMFISLFIMMMFNNFMGLF---PYIFTSTSHMVMTFSIALPMWMSFML 115
Cdd:pfam00119  27 PGRLQNFVEMLVEFVDNIVKDNIGKKKGRKfFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHY 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903 116 FGWINN-TTHMLTHLVPQGTPKLLMPFMVMIETISNIIRPGTLAVRLAANMIAGHMMLTLLGNSGTMIKFNLLSMVII-- 192
Cdd:pfam00119 107 YGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIpp 186

                         170       180
                  ....*....|....*....|....*...
gi 1824665903 193 -AQMLLMMLESAVTLIQAYVFSILSTLY 219
Cdd:pfam00119 187 lLGVAWTLFELLVAFIQAYVFTMLTAVY 214
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 72-219 1.69e-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: 88.21  E-value: 1.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  72 MFISLFIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFG-WINNTTHMLTHLVPQGTPkLLMPFMVMIETISN 150
Cdd:COG0356    60 LLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISE 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1824665903 151 IIRPGTLAVRLAANMIAGHMMLTLLGNSGTMIKFNLLSmvIIAQMLLMMLESAVTLIQAYVFSILSTLY 219
Cdd:COG0356   139 LARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLS--LLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 16-219 1.65e-18

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 80.61  E-value: 1.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  16 FNLSINWSSTIMGMFLLPSMFWIL-------PSRNSLFWNKLMLKIHQEFKTLTGNKHYGMTLMFISLFIMMMFNNFMGL 88
Cdd:PRK05815   12 FNFDSLLLSVLLGVLILLLFALVAtrklsgvPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  89 FP-YIFTSTSHMVMTFSIALPMWMSFMLFG-WINNTTHMLTHLVPQgtpklLMPFMVMIETISNIIRPGTLAVRLAANMI 166
Cdd:PRK05815   92 IPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQ-----PHPLLLPIEIISEFSRPISLSLRLFGNML 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1824665903 167 AGHMMLTLLGNSGTMIKFNLLSMVIIAqMLLMMLESAVTLIQAYVFSILSTLY 219
Cdd:PRK05815  167 AGELILALIALLGGAGLLLALAPLILP-VAWTIFEIFVGTLQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 63-223 2.78e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 80.37  E-value: 2.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  63 GNKHYGMTLMFISLFIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFM 142
Cdd:MTH00174   84 GNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLL 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903 143 VMIETISNIIRPGTLAVRLAANMIAGHMMLTLLGN-SGTMIKFNLLSMVIIAQMLLM---MLESAVTLIQAYVFSILSTL 218
Cdd:MTH00174  164 TIIETLSYISRAISLGVRLAANISSGHLLFSIIASfAWKMINTGILIGSFVPFAILIfvtILEMAVAIIQAYVFTLLTIV 243


                  ....*
gi 1824665903 219 YASET 223
Cdd:MTH00174  244 YLRDT 248
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 74-219 1.73e-11

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 62.45  E-value: 1.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  74 ISLFIMMMFNNFMGLFPYIFTSTSHMVMTFSIALpmwMSFMLFGWINNTTH----MLTHLVpQGTPKLLMPFMVMIETIS 149
Cdd:PRK13419  175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLAV---FTFFITQYAAIKAHgikgYLAHLT-GGTHWSLWIIMIPIEFIG 250

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1824665903 150 NIIRPGTLAVRLAANMIAGHM-MLTLLGnsgtmIKFNLLSMVIIAQM------LLMMLESAVTLIQAYVFSILSTLY 219
Cdd:PRK13419  251 LFTKPFALTVRLFANMTAGHIvILSLIF-----ISFILKSYIVAVAVsvpfaiFIYLLELFVAFLQAYIFTMLSALF 322
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 94-219 5.85e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 55.28  E-value: 5.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  94 TSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETI-SNIIRPGTLAVRLAANMIAGH-MM 171
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHvII 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1824665903 172 LTLLGNSGTMIKFNLLSMVIIAQMLLMMLESAVTLIQAYVFSILSTLY 219
Cdd:PRK13417  297 LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 73-222 1.46e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 46.90  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  73 FISLFIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTthMLTHLVPQGTPKLLMPF-MVMIETISNI 151
Cdd:MTH00087   55 SFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSE--KFSVYLSKGSDSFLKTFsMLFVEIVSEL 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1824665903 152 IRPGTLAVRLAANMIAGHMMLTLLGNSGtmIKFNLLSMVIIaqmllmMLESAVTLIQAYVFSILSTLYASE 222
Cdd:MTH00087  133 SRPLALTLRLTVNLMVGHLISSLLNFLG--EKYVWLSILAI------MMECFVAFIQSYIFSRLIYLYLNE 195
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 73-177 8.70e-06

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 44.49  E-value: 8.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  73 FISLFIMMMFnnFMGL-FPYIFTSTSHMVMTFSIALPMWMSFMLFGWINNTTHMLTHLVPQGTPKLLMPFMVMIETISNI 151
Cdd:MTH00050   27 SVVLFIVLFL--FLLYrLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYI 104

                          90       100
                  ....*....|....*....|....*.
gi 1824665903 152 IRPGTLAVRLAANMIAGHMMLTLLGN 177
Cdd:MTH00050  105 IRPVVLILRPFINISLGCFGGVALGN 130
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 19-219 1.94e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 41.27  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  19 SINWSSTIMGMFLLPSM-----FWILPSRNSLFWNKLMLKIHQEFKTLTgNKHYGMTLMFI-SLFIMMMFNNFMGLFPYI 92
Cdd:PRK13420   19 SVLTTWGIMIVLVLASWlttrrLSLDPGRFQVALEGVVSTIEDAIKEVL-PRHARLVLPFVgTLWIFILVANLIGLIPGF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665903  93 FTSTSHMVMTFSIALPMWMSFMLFG-----WINNTTHmltHLVPqgTPkLLMPFMVmietISNIIRPGTLAVRLAANMIA 167
Cdd:PRK13420   98 HSPTADLSVTAALALLVFFSVHWFGiraegLREYLKH---YLSP--SP-FLLPFHL----ISEITRTLALAVRLFGNIMS 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1824665903 168 GHMMLTLLgnsgtmikfnLLSMVIIAQMLLMMLESAVTLIQAYVFSILSTLY 219
Cdd:PRK13420  168 LELAALLV----------LLVAGFLVPVPILMLHIIEALVQAYIFGMLALIY 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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