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Conserved domains on  [gi|938339316|ref|YP_009171517|]
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ATP synthase F0 subunit 6 (mitochondrion) [Pseudothericles compressifrons]

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 9.51e-104

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 299.39  E-value: 9.51e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316   1 MTNLFSSFDPSTNiMNLSINWTSAFIGIMLVPSMFWIMPSRLNFMWSNLNFNLHKEFKVLLGNNSNGMTLIFISLFGILL 80
Cdd:MTH00157   2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  81 FNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETISNIIRPGTLAIRL 160
Cdd:MTH00157  81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 938339316 161 AANMIAGHLLLTLMGNTGPMLSYSILSILLMSQVLLFILESAVAMIQAYVFSVLSTLYSSEVY 223
Cdd:MTH00157 161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-223 9.51e-104

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 299.39  E-value: 9.51e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316   1 MTNLFSSFDPSTNiMNLSINWTSAFIGIMLVPSMFWIMPSRLNFMWSNLNFNLHKEFKVLLGNNSNGMTLIFISLFGILL 80
Cdd:MTH00157   2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  81 FNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETISNIIRPGTLAIRL 160
Cdd:MTH00157  81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 938339316 161 AANMIAGHLLLTLMGNTGPMLSYSILSILLMSQVLLFILESAVAMIQAYVFSVLSTLYSSEVY 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 ...
 4-223 1.05e-49

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: 161.99  E-value: 1.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316    4 LFSSFDPSTNIMNLSINWT---SAFIGIMLVPSMF--WIMPSRLNFMWSNLNFNLHKEFKVLLGNNSNGMTLIFISLFGI 78
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLSlilLLSLLIFLISSSLsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316   79 LLFNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETISNIIRPGTLAI 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938339316  159 RLAANMIAGHLLLTLMGNTGPML-SYSILSILLMSQVLLFILESAVAMIQAYVFSVLSTLYSSEVY 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 ...
 67-220 5.86e-43

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: 142.54  E-value: 5.86e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  67 GMTLIFISLFGILLFNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIET 146
Cdd:cd00310    3 KYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIEL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 938339316 147 ISNIIRPGTLAIRLAANMIAGHLLLTLMGNTGPMLSYSILSILLMSQVLLFILESAVAMIQAYVFSVLSTLYSS 220
Cdd:cd00310   83 ISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
72-220 3.08e-26

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 101.03  E-value: 3.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316   72 FISLFGILLFNNFMGLF---PYIFTSTSHMALTFSIALPLWMSFMLFG-WVNNTKHMFAHLVPQGTPGPLMSFMVIIETI 147
Cdd:pfam00119  61 LLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEII 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938339316  148 SNIIRPGTLAIRLAANMIAGHLLLTLMGNTGPMLSYSILSILLMS---QVLLFILESAVAMIQAYVFSVLSTLYSS 220
Cdd:pfam00119 141 SEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPpllGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 74-218 9.20e-24

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: 94.37  E-value: 9.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  74 SLFGILLFNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFG-WVNNTKHMFAHLVPQGTPgPLMSFMVIIETISNIIR 152
Cdd:COG0356   63 TLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISELAR 141

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938339316 153 PGTLAIRLAANMIAGHLLLTLMGNTGPMLSYSILSILLmsQVLLFILESAVAMIQAYVFSVLSTLY 218
Cdd:COG0356  142 PLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-223 9.51e-104

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 299.39  E-value: 9.51e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316   1 MTNLFSSFDPSTNiMNLSINWTSAFIGIMLVPSMFWIMPSRLNFMWSNLNFNLHKEFKVLLGNNSNGMTLIFISLFGILL 80
Cdd:MTH00157   2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  81 FNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETISNIIRPGTLAIRL 160
Cdd:MTH00157  81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 938339316 161 AANMIAGHLLLTLMGNTGPMLSYSILSILLMSQVLLFILESAVAMIQAYVFSVLSTLYSSEVY 223
Cdd:MTH00157 161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-223 1.23e-52

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 169.83  E-value: 1.23e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316   1 MTNLFSSFDP--STNIMNLSINWTSAFIGIMLVPSMFWIMPSRLNFMWSNLNFNLHKEFKVLLGNNSNGMTLIFISLFGI 78
Cdd:MTH00176   2 LVDLFSSFDPpnKNIFSMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  79 LLFNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETISNIIRPGTLAI 158
Cdd:MTH00176  82 VMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLAV 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 938339316 159 RLAANMIAGHLLLTLMGNTGP---MLSYSILSILLMSQVLLFILESAVAMIQAYVFSVLSTLYSSEVY 223
Cdd:MTH00176 162 RLAANLSAGHLLLGLLGAAMWgllPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 4-223 1.05e-49

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: 161.99  E-value: 1.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316    4 LFSSFDPSTNIMNLSINWT---SAFIGIMLVPSMF--WIMPSRLNFMWSNLNFNLHKEFKVLLGNNSNGMTLIFISLFGI 78
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLSlilLLSLLIFLISSSLsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316   79 LLFNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETISNIIRPGTLAI 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938339316  159 RLAANMIAGHLLLTLMGNTGPML-SYSILSILLMSQVLLFILESAVAMIQAYVFSVLSTLYSSEVY 223
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLmSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-221 4.80e-45

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 150.27  E-value: 4.80e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316   1 MTNLFSSFDPSTNIMNL----SINWTSAFIGIMLVPSMFWIMPSRLNFMWSNLNFNLHKEFKVLLGNNSNGMTLIFISLF 76
Cdd:MTH00005   2 LTDIFSSFDPATNSLFNnlssTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  77 GILLFNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETISNIIRPGTL 156
Cdd:MTH00005  82 TMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 938339316 157 AIRLAANMIAGHLLLTLMGN-TGPMLSYSILS--ILLMSQVLLFILESAVAMIQAYVFSVLSTLYSSE 221
Cdd:MTH00005 162 SFRLAANMSAGHIVLSLIGIyAASALFSSISStiLLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 2-221 5.87e-44

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 147.43  E-value: 5.87e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316   2 TNLFSSFDPSTnIMNLSINWTSAFIGI---MLVPSMFWImPSRLNFMWSNLNFNLHKEFKVLLGNNSNGMTLIFISLFGI 78
Cdd:MTH00035   5 NSIFGQFSPDT-ILFIPLTLLSSVIALswlFFINPTNWL-PSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  79 LLFNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETISNIIRPGTLAI 158
Cdd:MTH00035  83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 938339316 159 RLAANMIAGHLLLTLMGNTGPML--SYSILSILLMSQVLLFILESAVAMIQAYVFSVLSTLYSSE 221
Cdd:MTH00035 163 RLAANLTAGHLLIFLLSTAIWELsnSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 67-220 5.86e-43

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: 142.54  E-value: 5.86e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  67 GMTLIFISLFGILLFNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIET 146
Cdd:cd00310    3 KYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIEL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 938339316 147 ISNIIRPGTLAIRLAANMIAGHLLLTLMGNTGPMLSYSILSILLMSQVLLFILESAVAMIQAYVFSVLSTLYSS 220
Cdd:cd00310   83 ISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-221 6.94e-42

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 142.31  E-value: 6.94e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316   1 MTNLFSSFDPST-NIMNLSIN-WTSAFIGIMLVPSMFWIMPSRLNFMWSNLNFNLHKEFKVLLGNNSNGMTLIFISLFGI 78
Cdd:MTH00173   2 MVDLFSSFDDHNsSFSSLSFLmWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  79 LLFNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETISNIIRPGTLAI 158
Cdd:MTH00173  82 LISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTV 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 938339316 159 RLAANMIAGHLLLTLMGNTGP----MLSYSILSILLMSQVLLFILESAVAMIQAYVFSVLSTLYSSE 221
Cdd:MTH00173 162 RLLANISAGHIVLTLIGNYLSsslfSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 3-218 7.33e-37

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 129.30  E-value: 7.33e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316   3 NLFSSFDPSTnIMNLSInwtsaFIGIMLVPSMFWIMPSRL-NFMWSNLNFNLHKEF--KVLLGNNSNGMT--LIFISLFG 77
Cdd:MTH00101   4 NLFASFITPT-ILGLPI-----VTLIIMFPSLLFPTPNRLiNNRLISIQQWLIQLTskQMMTIHNTKGQTwsLMLMSLIL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  78 ILLFNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETISNIIRPGTLA 157
Cdd:MTH00101  78 FIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 938339316 158 IRLAANMIAGHLLLTLMGNTGPML---SYSILSILLMSQVLLFILESAVAMIQAYVFSVLSTLY 218
Cdd:MTH00101 158 VRLTANITAGHLLIHLIGGATLALmsiSTTTALITFIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 69-221 2.13e-36

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 128.02  E-value: 2.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  69 TLIFISLFGILLFNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETIS 148
Cdd:MTH00120  70 ALILTSLMLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETIS 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316 149 NIIRPGTLAIRLAANMIAGHLLLTLMG-------NTGPMLSYSILSILLmsqvLLFILESAVAMIQAYVFSVLSTLYSSE 221
Cdd:MTH00120 150 LLIRPLALGVRLTANLTAGHLLIQLIStatlnllPTMPTLSLLTLIILL----LLTILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 70-221 1.27e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 125.76  E-value: 1.27e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  70 LIFISLFGILLFNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETISN 149
Cdd:MTH00132  71 LLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISL 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 938339316 150 IIRPGTLAIRLAANMIAGHLLLTLMGNTGPMLSYSILSILLMSQVLLF---ILESAVAMIQAYVFSVLSTLYSSE 221
Cdd:MTH00132 151 FIRPLALGVRLTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFlltLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-221 1.74e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 125.45  E-value: 1.74e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316   1 MTNLFSSFDpSTNIMNLSINWTSAFIGIMLVPSMFWIMPSRLNFMWSNLNFN-LHKEFKVLLGNNSNGMTLIFISLFGIL 79
Cdd:MTH00179   2 MLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGsFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  80 LFNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETISNIIRPGTLAIR 159
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 938339316 160 LAANMIAGHLLLTLMGNTGPMLSYSILSILLMSQVLLF---ILESAVAMIQAYVFSVLSTLYSSE 221
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFlltLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 29-221 1.19e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 115.83  E-value: 1.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  29 MLVPSMFWIMPS------RLNFMWSNLNFNLHKEFKVLLGNNSNGMTLIFISLFGILLFNNFMGLFPYIFTSTSHMALTF 102
Cdd:MTH00073  24 MLLPWLLFPTPTnkwlnnRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFLITMNLLGLLPYTFTPTTQLSLNL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316 103 SIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETISNIIRPGTLAIRLAANMIAGHLLLTLMGNTGPMLS 182
Cdd:MTH00073 104 GLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVRLTANLTAGHLLIQLISTATLVLL 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 938339316 183 YSILSILLMSQVLLF---ILESAVAMIQAYVFSVLSTLYSSE 221
Cdd:MTH00073 184 PLMPTVSILTMIVLFlltLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 14-218 1.39e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 105.12  E-value: 1.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  14 IMNLSINWTSAFIGIMLVPSMFWIMPSRLNFMWSNLNFNLHKEFKVLLGNNSNGMTLIFISLFGILLFNNFMGLFPYIFT 93
Cdd:MTH00172  17 LTNSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  94 STSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETISNIIRPGTLAIRLAANMIAGHLLLTL 173
Cdd:MTH00172  97 PTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAI 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 938339316 174 MGNTG-PMLSYSILSILLMSQVLLFI--LESAVAMIQAYVFSVLSTLY 218
Cdd:MTH00172 177 LAGFGfNMLCASGFLSLFPLLIMVFItlLEIAVAVIQAYVFCLLTTIY 224
ATP-synt_A pfam00119
ATP synthase A chain;
72-220 3.08e-26

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 101.03  E-value: 3.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316   72 FISLFGILLFNNFMGLF---PYIFTSTSHMALTFSIALPLWMSFMLFG-WVNNTKHMFAHLVPQGTPGPLMSFMVIIETI 147
Cdd:pfam00119  61 LLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEII 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938339316  148 SNIIRPGTLAIRLAANMIAGHLLLTLMGNTGPMLSYSILSILLMS---QVLLFILESAVAMIQAYVFSVLSTLYSS 220
Cdd:pfam00119 141 SEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPpllGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 16-218 1.56e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 100.08  E-value: 1.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  16 NLSINWTSAFIGIMLVPSMFWIM-------PSRLNFMWSNLNFNLHKEFKVLLGNNSNGMTLIFISLFGILLFNNFMGLF 88
Cdd:MTH00175  23 DWLVTFTNSSMMMVLAVIIFWLLlkgdkliPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  89 PYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETISNIIRPGTLAIRLAANMIAGH 168
Cdd:MTH00175 103 PYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGH 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 938339316 169 LLLTLM-GNTGPMLS--YSILSILLMSqVLLFI--LESAVAMIQAYVFSVLSTLY 218
Cdd:MTH00175 183 LLFAILsGFAFNMLSngLIILSLFPML-IMIFItlLEMAVAVIQAYVFCLLTTIY 236
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 74-218 9.20e-24

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: 94.37  E-value: 9.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  74 SLFGILLFNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFG-WVNNTKHMFAHLVPQGTPgPLMSFMVIIETISNIIR 152
Cdd:COG0356   63 TLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISELAR 141

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938339316 153 PGTLAIRLAANMIAGHLLLTLMGNTGPMLSYSILSILLmsQVLLFILESAVAMIQAYVFSVLSTLY 218
Cdd:COG0356  142 PLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 71-218 6.99e-19

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 81.76  E-value: 6.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  71 IFISLFGILLFNNFMGLFP-YIFTSTSHMALTFSIALPLWMSFMLFG-WVNNTKHMFAHLVPQGTPgplmsFMVIIETIS 148
Cdd:PRK05815  75 LAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQPHP-----LLLPIEIIS 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316 149 NIIRPGTLAIRLAANMIAGHLLLTLMGNTGPMLSYSILSILLMSqVLLFILESAVAMIQAYVFSVLSTLY 218
Cdd:PRK05815 150 EFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILP-VAWTIFEIFVGTLQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 61-218 6.10e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 79.98  E-value: 6.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  61 LGNNSNGMTLIFISLFGILLFNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSF 140
Cdd:MTH00174  83 LGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPL 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316 141 MVIIETISNIIRPGTLAIRLAANMIAGHLLLTLMGNTG-PMLSYSILS---ILLMSQVLLFILESAVAMIQAYVFSVLST 216
Cdd:MTH00174 163 LTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAwKMINTGILIgsfVPFAILIFVTILEMAVAIIQAYVFTLLTI 242


                 ..
gi 938339316 217 LY 218
Cdd:MTH00174 243 VY 244
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 73-218 7.88e-12

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 63.61  E-value: 7.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  73 ISLFGILLFNNFMGLFPYIFTSTSHMALTFSIALplwMSFMLFGW----VNNTKHMFAHLVpQGTPGPLMSFMVIIETIS 148
Cdd:PRK13419 175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLAV---FTFFITQYaaikAHGIKGYLAHLT-GGTHWSLWIIMIPIEFIG 250

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 938339316 149 NIIRPGTLAIRLAANMIAGHL-LLTLMGNTGPMLSYsILSILLMSQVLLFI--LESAVAMIQAYVFSVLSTLY 218
Cdd:PRK13419 251 LFTKPFALTVRLFANMTAGHIvILSLIFISFILKSY-IVAVAVSVPFAIFIylLELFVAFLQAYIFTMLSALF 322
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 93-218 6.95e-11

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 61.06  E-value: 6.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  93 TSTSHMALTFSIALPLWMSFMLFGWVNNTKHMFAHLVPQGTPGPLMSFMVIIETI-SNIIRPGTLAIRLAANMIAGH-LL 170
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHvII 296

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 938339316 171 LTLMGNTGPMLSYSILSILLMSQVLLFILESAVAMIQAYVFSVLSTLY 218
Cdd:PRK13417 297 LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 71-221 7.97e-09

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 53.83  E-value: 7.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  71 IFISLFGILLFNNFMGLFPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKhmFAHLVPQGTPGPLMSF-MVIIETISN 149
Cdd:MTH00087  54 ISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEK--FSVYLSKGSDSFLKTFsMLFVEIVSE 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 938339316 150 IIRPGTLAIRLAANMIAGHLLLTLMGNTGpmLSYSILSILLMsqvllfILESAVAMIQAYVFSVLSTLYSSE 221
Cdd:MTH00087 132 LSRPLALTLRLTVNLMVGHLISSLLNFLG--EKYVWLSILAI------MMECFVAFIQSYIFSRLIYLYLNE 195
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 47-215 3.74e-07

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 48.73  E-value: 3.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  47 SNLNFNLHKEFKVLLGNNSNGMTLIFISLFGILLFnnFMGL-FPYIFTSTSHMALTFSIALPLWMSFMLFGWVNNTKHMF 125
Cdd:MTH00050   2 FVNDFSSLFSLIYKLILGGSVSYYYSVVLFIVLFL--FLLYrLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316 126 AHLVPQGTPGPLMSFMVIIETISNIIRPGTLAIRLAANMIAGHLLLTLMGNTGpMLSYSILSILlmsqVLLFILESAVAM 205
Cdd:MTH00050  80 SSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGCFGGVALGNLC-FISYWWFLVL----FFLFFYEVFVAL 154

                        170
                 ....*....|.
gi 938339316 206 IQAY-VFSVLS 215
Cdd:MTH00050 155 VHWFiVSSILS 165
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 25-218 3.53e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 40.50  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316  25 FIGIMLVPSMFWIMPSRLNFMWSNLNFNLHKEFKVLLGNNSNGMTLIFISLFGILLFNNFMGLFPYIFTSTSHMALTFSI 104
Cdd:PRK13420  31 VLASWLTTRRLSLDPGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFVGTLWIFILVANLIGLIPGFHSPTADLSVTAAL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938339316 105 ALPLWMSFMLFG-----WVNNTKHMFahlvpqgTPGPlmsFMVIIETISNIIRPGTLAIRLAANM----IAGHLLLTLMG 175
Cdd:PRK13420 111 ALLVFFSVHWFGiraegLREYLKHYL-------SPSP---FLLPFHLISEITRTLALAVRLFGNImsleLAALLVLLVAG 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 938339316 176 ntgpmlsysilsilLMSQVLLFILESAVAMIQAYVFSVLSTLY 218
Cdd:PRK13420 181 --------------FLVPVPILMLHIIEALVQAYIFGMLALIY 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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