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Conserved domains on  [gi|1824661655|ref|YP_009734781|]
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ATP synthase F0 subunit 6 (mitochondrion) [Tetrix ruyuanensis]

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 2.00e-88

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 260.10  E-value: 2.00e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655   1 MMTNLFSSFDPSTSNSLSINWLSTLLFIMLVPMTFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  81 INNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1824661655 161 AANMIAGHLLLTLLGNTGNKLSEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSSEIN 223
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-223 2.00e-88

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 260.10  E-value: 2.00e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655   1 MMTNLFSSFDPSTSNSLSINWLSTLLFIMLVPMTFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  81 INNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1824661655 161 AANMIAGHLLLTLLGNTGNKLSEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSSEIN 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 ...
 5-223 1.48e-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: 153.52  E-value: 1.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655   5 LFSSFDPSTSNSLSINWLSTLLFIMLVPMTF------WLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFII 78
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLSLILLLSLLIFLIssslsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  79 IMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAI 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1824661655 159 RLAANMIAGHLLLTLLGNTGNKLSEIMLIGM-LTMQMMLLVLESAVSLIQAYVFSVLTTLYSSEIN 223
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIFALlLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-220 4.60e-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: 139.84  E-value: 4.60e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  65 NKGSTLLFISLFIIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCI 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1824661655 145 ETISTLIRPGTLAIRLAANMIAGHLLLTLLGNTGNKLSEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSS 220
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
21-220 9.16e-28

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 104.88  E-value: 9.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  21 WLSTLLFIMLVPMTFWLIK----SRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFI-SLFIIIMINNVMGLF---PYIF 92
Cdd:pfam00119   5 LIVALILLLFLLLATRKTKklvpGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLlTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  93 TSSSHMVMTLSLALPMWLSFNLFG-WINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRLAANMIAGHLLL 171
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1824661655 172 TLLGNTGNKLSEIML---IGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSS 220
Cdd:pfam00119 165 LLLAGLIFALLSAGFllgVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 21-218 4.08e-22

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: 89.75  E-value: 4.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  21 WLSTLLFIMLVPMTFWLIKSRPN---MLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIMINNVMGLFPYIFTSSSH 97
Cdd:COG0356     7 WLAMLLLLLLFLLATRKLKLVPGglqNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTAD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  98 MVMTLSLALPMWLSFNLFG-WINKTNHMFEHMVPSGTPAMlMPFMVCIETISTLIRPGTLAIRLAANMIAGHLLLTLLGN 176
Cdd:COG0356    87 INVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFPWL-APLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAG 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1824661655 177 TGNKLSEIMLIGMLTMQMMLlvLESAVSLIQAYVFSVLTTLY 218
Cdd:COG0356   166 LAPFLLLGVLSLLLPVAWTA--FELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-223 2.00e-88

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 260.10  E-value: 2.00e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655   1 MMTNLFSSFDPSTSNSLSINWLSTLLFIMLVPMTFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  81 INNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1824661655 161 AANMIAGHLLLTLLGNTGNKLSEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSSEIN 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 ...
 5-223 1.48e-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: 153.52  E-value: 1.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655   5 LFSSFDPSTSNSLSINWLSTLLFIMLVPMTF------WLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFII 78
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLSLILLLSLLIFLIssslsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  79 IMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAI 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1824661655 159 RLAANMIAGHLLLTLLGNTGNKLSEIMLIGM-LTMQMMLLVLESAVSLIQAYVFSVLTTLYSSEIN 223
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIFALlLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-221 1.37e-45

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 151.34  E-value: 1.37e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655   1 MMTNLFSSFDPSTSN---SLSINWLSTLLFIMLVPMTFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFI 77
Cdd:MTH00176    1 MLVDLFSSFDPPNKNifsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  78 IIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLA 157
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1824661655 158 IRLAANMIAGHLLLT---LLGNTGNKLSEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSSE 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 ...
 65-220 4.60e-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: 139.84  E-value: 4.60e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  65 NKGSTLLFISLFIIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCI 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1824661655 145 ETISTLIRPGTLAIRLAANMIAGHLLLTLLGNTGNKLSEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSS 220
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-221 1.12e-41

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 141.41  E-value: 1.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655   1 MMTNLFSSFDPSTSNSL-----SINWLSTLLFIMLVPMTFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISL 75
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFnnlssTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  76 FIIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGT 155
Cdd:MTH00005   81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1824661655 156 LAIRLAANMIAGHLLLTLLGNTGNKL---SEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSSE 221
Cdd:MTH00005  161 LSFRLAANMSAGHIVLSLIGIYAASAlfsSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-222 4.60e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 131.91  E-value: 4.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655   1 MMTNLFSSFDPSTSNSLSIN---WLSTLLFIMLVPMTFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFI 77
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSSLSflmWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  78 IIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLA 157
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1824661655 158 IRLAANMIAGHLLLT----LLGNTGNKLSEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSSEI 222
Cdd:MTH00173  161 VRLLANISAGHIVLTlignYLSSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDEH 229
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-221 8.13e-36

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 125.83  E-value: 8.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655   1 MMTNLFSSFDPSTSNSLSINWLSTLLFIMLVPM-TFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIII 79
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSlTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  80 MINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIR 159
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824661655 160 LAANMIAGHLLLTLLGNTGNKLSEIM-LIGMLT--MQMMLLVLESAVSLIQAYVFSVLTTLYSSE 221
Cdd:MTH00179  161 LTANITAGHLLMHLISSAVFVLMNFMgMVALLTllVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 3-221 9.67e-36

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 125.86  E-value: 9.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655   3 TNLFSSFDPSTSNSLSINWLST---LLFIMLVPMTFWLIkSRPNMLMEILTKNMnyeFNNILNNKNKGS---TLLFISLF 76
Cdd:MTH00035    5 NSIFGQFSPDTILFIPLTLLSSviaLSWLFFINPTNWLP-SRSQSIWLTFRQEI---LKLIFQNTNPNTapwAGLLTTVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  77 IIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTL 156
Cdd:MTH00035   81 ILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1824661655 157 AIRLAANMIAGHLLLTLLGNTGNKLSEIMLIGMLTMQM--MLLVLESAVSLIQAYVFSVLTTLYSSE 221
Cdd:MTH00035  161 GLRLAANLTAGHLLIFLLSTAIWELSNSPLISIITLIIffLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-221 7.39e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 123.40  E-value: 7.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655   1 MMTNLFSSFDPSTSNSLSINWLSTLLFIMLVP-MTFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIII 79
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPsPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  80 MINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIR 159
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824661655 160 LAANMIAGHLLLTLLGNTGNKLSEIM-LIGMLTMQMMLL--VLESAVSLIQAYVFSVLTTLYSSE 221
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMpTLSLLTLIILLLltILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-218 1.49e-31

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 115.05  E-value: 1.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655   1 MMTNLFSSFDPSTSNSLSINWLSTLLFIMLVPMTFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIM 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  81 INNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1824661655 161 AANMIAGHLLLTLLGNTGNKLSEIMLIGML---TMQMMLLVLESAVSLIQAYVFSVLTTLY 218
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALitfIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-221 4.57e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 113.52  E-value: 4.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655   1 MMTNLFSSFDPSTSNSLSINWLSTLLFIMLVPM-TFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIII 79
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTpTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  80 MINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIR 159
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824661655 160 LAANMIAGHLLLTLLGNTGNKLSEIM-LIGMLTMQMMLL--VLESAVSLIQAYVFSVLTTLYSSE 221
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMpTVSILTMIVLFLltLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 70-221 1.16e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 112.66  E-value: 1.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  70 LLFISLFIIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETIST 149
Cdd:MTH00132   71 LLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISL 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824661655 150 LIRPGTLAIRLAANMIAGHLLLTLLGNTGNKLSEIM-LIGMLTMQMMLL--VLESAVSLIQAYVFSVLTTLYSSE 221
Cdd:MTH00132  151 FIRPLALGVRLTANLTAGHLLIQLIATAAFVLLPLMpTVAILTATLLFLltLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP-synt_A pfam00119
ATP synthase A chain;
21-220 9.16e-28

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 104.88  E-value: 9.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  21 WLSTLLFIMLVPMTFWLIK----SRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFI-SLFIIIMINNVMGLF---PYIF 92
Cdd:pfam00119   5 LIVALILLLFLLLATRKTKklvpGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLlTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  93 TSSSHMVMTLSLALPMWLSFNLFG-WINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRLAANMIAGHLLL 171
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1824661655 172 TLLGNTGNKLSEIML---IGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSS 220
Cdd:pfam00119 165 LLLAGLIFALLSAGFllgVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 36-218 4.69e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 103.55  E-value: 4.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  36 WLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLF 115
Cdd:MTH00175   50 KLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655 116 GWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRLAANMIAGHLLLTLLGNTGNKL--SEIMLIGMLTMQ 193
Cdd:MTH00175  130 GFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMlsNGLIILSLFPML 209

                         170       180
                  ....*....|....*....|....*..
gi 1824661655 194 MMLLV--LESAVSLIQAYVFSVLTTLY 218
Cdd:MTH00175  210 IMIFItlLEMAVAVIQAYVFCLLTTIY 236
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 37-218 1.74e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 96.65  E-value: 1.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  37 LIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFG 116
Cdd:MTH00172   40 LIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAG 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655 117 WINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRLAANMIAGHLLLTLLGNTGNK-LSEIMLIGMLTMQMM 195
Cdd:MTH00172  120 FWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNmLCASGFLSLFPLLIM 199

                         170       180
                  ....*....|....*....|....*
gi 1824661655 196 LLV--LESAVSLIQAYVFSVLTTLY 218
Cdd:MTH00172  200 VFItlLEIAVAVIQAYVFCLLTTIY 224
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 21-218 4.08e-22

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: 89.75  E-value: 4.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  21 WLSTLLFIMLVPMTFWLIKSRPN---MLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIMINNVMGLFPYIFTSSSH 97
Cdd:COG0356     7 WLAMLLLLLLFLLATRKLKLVPGglqNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTAD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  98 MVMTLSLALPMWLSFNLFG-WINKTNHMFEHMVPSGTPAMlMPFMVCIETISTLIRPGTLAIRLAANMIAGHLLLTLLGN 176
Cdd:COG0356    87 INVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFPWL-APLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAG 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1824661655 177 TGNKLSEIMLIGMLTMQMMLlvLESAVSLIQAYVFSVLTTLY 218
Cdd:COG0356   166 LAPFLLLGVLSLLLPVAWTA--FELLVGFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 21-218 2.07e-19

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 82.92  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  21 WLSTLLFIMLVPMTFWLIKSRPN---MLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIMINNVMGLFP-YIFTSSS 96
Cdd:PRK05815   22 LLGVLILLLFALVATRKLSGVPGglqNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  97 HMVMTLSLALPMWLSFNLFG-WINKTNHMFEHMVPSgtpamLMPFMVCIETISTLIRPGTLAIRLAANMIAGHLLLTLLG 175
Cdd:PRK05815  102 DINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQ-----PHPLLLPIEIISEFSRPISLSLRLFGNMLAGELILALIA 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1824661655 176 NTGNkLSEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLY 218
Cdd:PRK05815  177 LLGG-AGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 37-218 5.75e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 79.60  E-value: 5.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  37 LIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFG 116
Cdd:MTH00174   59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAG 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655 117 WINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRLAANMIAGHLLLTLLGNTGNKL-SEIMLIGMLTMQMM 195
Cdd:MTH00174  139 LITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMiNTGILIGSFVPFAI 218

                         170       180
                  ....*....|....*....|....*.
gi 1824661655 196 LL---VLESAVSLIQAYVFSVLTTLY 218
Cdd:MTH00174  219 LIfvtILEMAVAIIQAYVFTLLTIVY 244
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 73-218 1.40e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 59.76  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  73 ISLFIIIMINNVMGLFPYIFTSSSHMVMTLSLALpmwlsFNLFgwINKTNHMFEHMV-------PSGTPAMLMPFMVCIE 145
Cdd:PRK13419  175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLAV-----FTFF--ITQYAAIKAHGIkgylahlTGGTHWSLWIIMIPIE 247

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1824661655 146 TISTLIRPGTLAIRLAANMIAGHLLLTLLGNTGNKL-SEIMLIGM-LTMQMMLLVLESAVSLIQAYVFSVLTTLY 218
Cdd:PRK13419  248 FIGLFTKPFALTVRLFANMTAGHIVILSLIFISFILkSYIVAVAVsVPFAIFIYLLELFVAFLQAYIFTMLSALF 322
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 93-218 7.64e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 48.73  E-value: 7.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  93 TSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLI-RPGTLAIRLAANMIAGHLLL 171
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIVSPMaKTFALTVRLLANMTAGHVII 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1824661655 172 TLLGNTGNkLSEIMLIGMLTM--QMMLLVLESAVSLIQAYVFSVLTTLY 218
Cdd:PRK13417  297 LALMGFIF-QFQSWGIVPVSVigSGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 22-221 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 1824661655  22 LSTLLFIMLVPMTFWLIKSRPNMLMEILTKNMNYEFNniLNNKNKGSTLLFISLFIIIMINNVMGLFPYIFTSSSHMVMT 101
Cdd:MTH00087    7 LDVFMFVFLLQYLLYFKESMLNVLVKKFFGLLIIVFS--YSNKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655 102 LSLALPMWLSFNLFGWINKTnhMFEHMVPSGTPAMLMPF-MVCIETISTLIRPGTLAIRLAANMIAGHLLLTLLGNTGNK 180
Cdd:MTH00087   85 FLYALVAWLSTFLSFLSKSE--KFSVYLSKGSDSFLKTFsMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLLNFLGEK 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1824661655 181 LSEIMLIgmltmqmmLLVLESAVSLIQAYVFSVLTTLYSSE 221
Cdd:MTH00087  163 YVWLSIL--------AIMMECFVAFIQSYIFSRLIYLYLNE 195
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 57-167 4.04e-06

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 45.26  E-value: 4.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  57 FNNILNNkNKGSTLLFISLFIIIMINnVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAM 136
Cdd:MTH00050   13 IYKLILG-GSVSYYYSVVLFIVLFLF-LLYRLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLY 90

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1824661655 137 LMPFMVCIETISTLIRPGTLAIRLAANMIAG 167
Cdd:MTH00050   91 ICPFVCIAETISYIIRPVVLILRPFINISLG 121
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 74-218 2.03e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 41.27  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824661655  74 SLFIIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINK--TNHMFEHMVPSgtpAMLMPFMVcietISTLI 151
Cdd:PRK13420   80 TLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEglREYLKHYLSPS---PFLLPFHL----ISEIT 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1824661655 152 RPGTLAIRLAANMIAGHLLLTLlgntgnklseIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLY 218
Cdd:PRK13420  153 RTLALAVRLFGNIMSLELAALL----------VLLVAGFLVPVPILMLHIIEALVQAYIFGMLALIY 209
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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