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Conserved domains on  [gi|1707765453|gb|QDP18034|]
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ATP synthase F0 subunit 6 (mitochondrion) [Psedna nana]

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 1.19e-100

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 290.92  E-value: 1.19e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453   1 MTNLFSTFDPSTSmFSLSLNWLSTIIGLLMIPSLYWMMPSRTNIIWNKMNLTLHNEFKTLLGPNsFNGTTFIFISIFIMM 80
Cdd:MTH00157    2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  81 LFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNIIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707765453 161 LAANMIAGHLLLTLLGNTGPLMSYNLMSILIFGQMLLLILESAVAMIQAYVFSILSTLYSSEVY 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-224 1.19e-100

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 290.92  E-value: 1.19e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453   1 MTNLFSTFDPSTSmFSLSLNWLSTIIGLLMIPSLYWMMPSRTNIIWNKMNLTLHNEFKTLLGPNsFNGTTFIFISIFIMM 80
Cdd:MTH00157    2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  81 LFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNIIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707765453 161 LAANMIAGHLLLTLLGNTGPLMSYNLMSILIFGQMLLLILESAVAMIQAYVFSILSTLYSSEVY 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 ...
 4-224 1.19e-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: 156.21  E-value: 1.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453   4 LFSTFDPST-SMFSLSLNWLSTIIGLLMI----PSLYWMMPSRTNIIWNKMNLTLHNEFKTLLGPNSFNGTTFIFiSIFI 78
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  79 MMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNIIRPGTLA 158
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1707765453 159 VRLAANMIAGHLLLTLLGNTGP-LMSYNLMSILIFGQMLLLILESAVAMIQAYVFSILSTLYSSEVY 224
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFsLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 72-221 8.96e-41

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 136.38  E-value: 8.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  72 IFISIFIMMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNI 151
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453 152 IRPGTLAVRLAANMIAGHLLLTLLGNTGPLMSYNLMSILIFGQMLLLILESAVAMIQAYVFSILSTLYSS 221
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
21-221 7.53e-25

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 97.18  E-value: 7.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  21 WLSTIIGLLMIPSLYWMM----PSRTNIIWNKMNLTLHNEFKTLLGPNSFNGTTFIFISIFIMMLFNNFMGLF---PYIF 93
Cdd:pfam00119   5 LIVALILLLFLLLATRKTkklvPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  94 TSTSHMVLTFTIALPMWMSFMLFGWINH-TKHMLAHLVPQGTPPALMSFMVLIETISNIIRPGTLAVRLAANMIAGHLLL 172
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1707765453 173 TLLGNTGPLMSYNLMS---ILIFGQMLLLILESAVAMIQAYVFSILSTLYSS 221
Cdd:pfam00119 165 LLLAGLIFALLSAGFLlgvIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 75-219 6.79e-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: 86.67  E-value: 6.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  75 SIFIMMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINH-TKHMLAHLVPQGTPPaLMSFMVLIETISNIIR 153
Cdd:COG0356    63 TLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPW-LAPLMLPIEIISELAR 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1707765453 154 PGTLAVRLAANMIAGHLLLTLLGNTGPLMSYNLMSILIfgQMLLLILESAVAMIQAYVFSILSTLY 219
Cdd:COG0356   142 PLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-224 1.19e-100

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 290.92  E-value: 1.19e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453   1 MTNLFSTFDPSTSmFSLSLNWLSTIIGLLMIPSLYWMMPSRTNIIWNKMNLTLHNEFKTLLGPNsFNGTTFIFISIFIMM 80
Cdd:MTH00157    2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  81 LFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNIIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707765453 161 LAANMIAGHLLLTLLGNTGPLMSYNLMSILIFGQMLLLILESAVAMIQAYVFSILSTLYSSEVY 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-224 1.20e-51

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 166.75  E-value: 1.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453   1 MTNLFSTFDPSTSMF--SLSLNWLSTIIGLLMIPSLYWMMPSRTNIIWNKMNlTLHNEFKTLLGPNSFNGTTFIFISIFI 78
Cdd:MTH00176    2 LVDLFSSFDPPNKNIfsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFS-TFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  79 MMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNIIRPGTLA 158
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707765453 159 VRLAANMIAGHLLLTLLGNTGPL---MSYNLMSILIFGQMLLLILESAVAMIQAYVFSILSTLYSSEVY 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 ...
 4-224 1.19e-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: 156.21  E-value: 1.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453   4 LFSTFDPST-SMFSLSLNWLSTIIGLLMI----PSLYWMMPSRTNIIWNKMNLTLHNEFKTLLGPNSFNGTTFIFiSIFI 78
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  79 MMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNIIRPGTLA 158
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1707765453 159 VRLAANMIAGHLLLTLLGNTGP-LMSYNLMSILIFGQMLLLILESAVAMIQAYVFSILSTLYSSEVY 224
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFsLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 72-221 8.96e-41

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 136.38  E-value: 8.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  72 IFISIFIMMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNI 151
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453 152 IRPGTLAVRLAANMIAGHLLLTLLGNTGPLMSYNLMSILIFGQMLLLILESAVAMIQAYVFSILSTLYSS 221
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 2-222 4.10e-40

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 137.03  E-value: 4.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453   2 TNLFSTFDPSTsMFSLSLNWLSTIIGL---LMIPSLYWMmPSRTNIIWNKMNLTLHNEFKTLLGPNSFNGTTFIFiSIFI 78
Cdd:MTH00035    5 NSIFGQFSPDT-ILFIPLTLLSSVIALswlFFINPTNWL-PSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLT-TVFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  79 MMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNIIRPGTLA 158
Cdd:MTH00035   82 LILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALG 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1707765453 159 VRLAANMIAGHLLLTLLGNT-GPLMSYNLMSILIFGQM-LLLILESAVAMIQAYVFSILSTLYSSE 222
Cdd:MTH00035  162 LRLAANLTAGHLLIFLLSTAiWELSNSPLISIITLIIFfLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-222 1.95e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 132.68  E-value: 1.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453   1 MTNLFSTFDPSTSMFSL--SLNWLSTIIGLLMIPSLYWMMPSRTNIIWNKMNLTLHNEFKTLLGPNsFNGTTFIFISIFI 78
Cdd:MTH00173    2 MVDLFSSFDDHNSSFSSlsFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLN-LGGFSLLLSSLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  79 MMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNIIRPGTLA 158
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1707765453 159 VRLAANMIAGHLLLTLLGNTGP----LMSYNLMSILIFGQMLLLILESAVAMIQAYVFSILSTLYSSE 222
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYLSsslfSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-222 2.62e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 132.55  E-value: 2.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453   1 MTNLFSTFDPSTS----MFSLSLNWLSTIIGLLMIPSLYWMMPSRTNIIWNKMNLTLHNEFKTLLGPNsFNGTTFIFISI 76
Cdd:MTH00005    2 LTDIFSSFDPATNslfnNLSSTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKH-LKGFSSLISAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  77 FIMMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNIIRPGT 156
Cdd:MTH00005   81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707765453 157 LAVRLAANMIAGHLLLTLLG---NTGPLMSYNLMSILIFGQMLLLILESAVAMIQAYVFSILSTLYSSE 222
Cdd:MTH00005  161 LSFRLAANMSAGHIVLSLIGiyaASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-222 6.96e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 118.51  E-value: 6.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453   1 MTNLFSTFDpSTSMFSLSLNWLSTIIGLLMIPSLYWMMPSRTNIIWnkMNLTLHNEFKTLLGPNSFNGTTF--IFISIFI 78
Cdd:MTH00179    2 MLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTL--QSWFFGSFTFQLMQPINKKGHKWavLFLSLML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  79 MMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNIIRPGTLA 158
Cdd:MTH00179   79 FLLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1707765453 159 VRLAANMIAGHLLLTLLGnTGPLMSYNLMSILIF----GQMLLLILESAVAMIQAYVFSILSTLYSSE 222
Cdd:MTH00179  159 VRLTANITAGHLLMHLIS-SAVFVLMNFMGMVALltllVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-222 1.02e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 118.00  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453   1 MTNLFSTFDPSTSMFslslnwLSTIIGLLMIPSLYWMMPS---RTNIIWNKMNLTLHNEFKTLLGPNSFNGT--TFIFIS 75
Cdd:MTH00120    2 NLNFFDQFSSPELLG------IPLILLAMLIPALLIPSPKnrlLTNRLTTLQLWLIKLITKQLMLPLNKKGHkwALILTS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  76 IFIMMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNIIRPG 155
Cdd:MTH00120   76 LMLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707765453 156 TLAVRLAANMIAGH-------LLLTLLGNTGPLMSYNLMSILifgqMLLLILESAVAMIQAYVFSILSTLYSSE 222
Cdd:MTH00120  156 ALGVRLTANLTAGHlliqlisTATLNLLPTMPTLSLLTLIIL----LLLTILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 72-222 3.17e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 111.50  E-value: 3.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  72 IFISIFIMMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNI 151
Cdd:MTH00132   72 LLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLF 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707765453 152 IRPGTLAVRLAANMIAGHLLLTLLGNTGPLMSYNLMSILIFGQMLLL---ILESAVAMIQAYVFSILSTLYSSE 222
Cdd:MTH00132  152 IRPLALGVRLTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFlltLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 3-219 4.74e-30

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 111.20  E-value: 4.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453   3 NLFSTFDPSTSMfslslnWLSTIIGLLMIPSLywMMPSRTNIIWNKMNLT----LHNEFKTLLGPNSFNGTTF--IFISI 76
Cdd:MTH00101    4 NLFASFITPTIL------GLPIVTLIIMFPSL--LFPTPNRLINNRLISIqqwlIQLTSKQMMTIHNTKGQTWslMLMSL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  77 FIMMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNIIRPGT 156
Cdd:MTH00101   76 ILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMA 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1707765453 157 LAVRLAANMIAGHLLLTLLGN-TGPLMSYNLMSILIFGQMLLL--ILESAVAMIQAYVFSILSTLY 219
Cdd:MTH00101  156 LAVRLTANITAGHLLIHLIGGaTLALMSISTTTALITFIILILltILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-222 1.24e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 104.66  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453   1 MTNLFSTFDPSTSMF------SLSLNWLstiigLLMIPSLYWMmpsrTNIIWNKMNLTLHNEFKTLLGPNSFNGT--TFI 72
Cdd:MTH00073    2 NLSFFDQFLSPTLLGiplimlAMLLPWL-----LFPTPTNKWL----NNRLSTLQIWFLQNFTKQLMLPLNTPGHkwALI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  73 FISIFIMMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNII 152
Cdd:MTH00073   73 LTSLMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFI 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707765453 153 RPGTLAVRLAANMIAGHLLLTLLgNTGPLMSYNLM---SILIFGQMLLL-ILESAVAMIQAYVFSILSTLYSSE 222
Cdd:MTH00073  153 RPLALGVRLTANLTAGHLLIQLI-STATLVLLPLMptvSILTMIVLFLLtLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 18-219 4.60e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 98.19  E-value: 4.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  18 SLNWLSTIIGLLMIPSLYWMMPSRTNIIWNKMNLTLHNEFKTLLGPNSFNGTTFIfISIFIMMLFNNFMGLFPYIFTSTS 97
Cdd:MTH00172   21 SIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFI-ISLFFFIVFLNLLGLFPYVFTPTT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  98 HMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNIIRPGTLAVRLAANMIAGHLLLTLLGN 177
Cdd:MTH00172  100 HIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAG 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1707765453 178 TGPLMSYNLMSILIFGQMLLL---ILESAVAMIQAYVFSILSTLY 219
Cdd:MTH00172  180 FGFNMLCASGFLSLFPLLIMVfitLLEIAVAVIQAYVFCLLTTIY 224
ATP-synt_A pfam00119
ATP synthase A chain;
21-221 7.53e-25

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 97.18  E-value: 7.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  21 WLSTIIGLLMIPSLYWMM----PSRTNIIWNKMNLTLHNEFKTLLGPNSFNGTTFIFISIFIMMLFNNFMGLF---PYIF 93
Cdd:pfam00119   5 LIVALILLLFLLLATRKTkklvPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  94 TSTSHMVLTFTIALPMWMSFMLFGWINH-TKHMLAHLVPQGTPPALMSFMVLIETISNIIRPGTLAVRLAANMIAGHLLL 172
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1707765453 173 TLLGNTGPLMSYNLMS---ILIFGQMLLLILESAVAMIQAYVFSILSTLYSS 221
Cdd:pfam00119 165 LLLAGLIFALLSAGFLlgvIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 74-219 1.51e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 97.00  E-value: 1.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  74 ISIFIMMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNIIR 153
Cdd:MTH00175   87 LSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIR 166

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453 154 PGTLAVRLAANMIAGHLLLTLLGNTGPLMSYNLMSILIFGQMLLLI----LESAVAMIQAYVFSILSTLY 219
Cdd:MTH00175  167 AISLGVRLAANISAGHLLFAILSGFAFNMLSNGLIILSLFPMLIMIfitlLEMAVAVIQAYVFCLLTTIY 236
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 75-219 6.79e-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: 86.67  E-value: 6.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  75 SIFIMMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINH-TKHMLAHLVPQGTPPaLMSFMVLIETISNIIR 153
Cdd:COG0356    63 TLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPW-LAPLMLPIEIISELAR 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1707765453 154 PGTLAVRLAANMIAGHLLLTLLGNTGPLMSYNLMSILIfgQMLLLILESAVAMIQAYVFSILSTLY 219
Cdd:COG0356   142 PLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAVY 205
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 74-219 3.77e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 77.67  E-value: 3.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  74 ISIFIMMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETISNIIR 153
Cdd:MTH00174   95 LSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISR 174

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707765453 154 PGTLAVRLAANMIAGHLLLTLLG-------NTGPLM-SYNLMSILIFgqmlLLILESAVAMIQAYVFSILSTLY 219
Cdd:MTH00174  175 AISLGVRLAANISSGHLLFSIIAsfawkmiNTGILIgSFVPFAILIF----VTILEMAVAIIQAYVFTLLTIVY 244
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 72-219 7.85e-17

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 75.99  E-value: 7.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  72 IFISIFIMMLFNNFMGLFP-YIFTSTSHMVLTFTIALPMWMSFMLFG-WINHTKHMLAHLVPQGTPpalmsFMVLIETIS 149
Cdd:PRK05815   75 LAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQPHP-----LLLPIEIIS 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453 150 NIIRPGTLAVRLAANMIAGHLLLTLLGNTGPLMSYNLMSILIFGqMLLLILESAVAMIQAYVFSILSTLY 219
Cdd:PRK05815  150 EFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILP-VAWTIFEIFVGTLQAYIFMMLTIVY 218
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 74-219 9.60e-13

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 66.30  E-value: 9.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  74 ISIFIMMLFNNFMGLFPYIFTSTSHMVLTFTIALpmwMSFMLFGWINHTKH----MLAHLVpQGTPPALMSFMVLIETIS 149
Cdd:PRK13419  175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLAV---FTFFITQYAAIKAHgikgYLAHLT-GGTHWSLWIIMIPIEFIG 250

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1707765453 150 NIIRPGTLAVRLAANMIAGHL-LLTLLGNTGPLMSYNL-------MSILIFgqmlllILESAVAMIQAYVFSILSTLY 219
Cdd:PRK13419  251 LFTKPFALTVRLFANMTAGHIvILSLIFISFILKSYIVavavsvpFAIFIY------LLELFVAFLQAYIFTMLSALF 322
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 94-219 1.23e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 51.04  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  94 TSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLAHLVPQGTPPALMSFMVLIETI-SNIIRPGTLAVRLAANMIAGHLLL 172
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1707765453 173 T-LLGNTGPLMSYNLMSILIFGQMLLLILESAVAMIQAYVFSILSTLY 219
Cdd:PRK13417  297 LaLMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 71-222 1.97e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 49.59  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  71 FIFISIFIMMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKhmLAHLVPQGTPPALMSF-MVLIETIS 149
Cdd:MTH00087   53 VISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEK--FSVYLSKGSDSFLKTFsMLFVEIVS 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707765453 150 NIIRPGTLAVRLAANMIAGHLLltllgntgpLMSYNLMSILIFGQMLLLIL-ESAVAMIQAYVFSILSTLYSSE 222
Cdd:MTH00087  131 ELSRPLALTLRLTVNLMVGHLI---------SSLLNFLGEKYVWLSILAIMmECFVAFIQSYIFSRLIYLYLNE 195
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 49-216 1.29e-04

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 41.02  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  49 MNLTLHNEFKTLLGPNSFNGTTFIFISIFIMMLFNNFMGL-FPYIFTSTSHMVLTFTIALPMWMSFMLFGWINHTKHMLA 127
Cdd:MTH00050    1 MFVNDFSSLFSLIYKLILGGSVSYYYSVVLFIVLFLFLLYrLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453 128 HLVPQGTPPALMSFMVLIETISNIIRPGTLAVRLAANMIAGHLLLTLLGNTGpLMSYNLMSILIFgqmlLLILESAVAMI 207
Cdd:MTH00050   81 SFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGCFGGVALGNLC-FISYWWFLVLFF----LFFYEVFVALV 155

                         170
                  ....*....|
gi 1707765453 208 QAY-VFSILS 216
Cdd:MTH00050  156 HWFiVSSILS 165
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 39-219 5.74e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 36.64  E-value: 5.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453  39 PSRTNIIWNKMNLTLHNEFKTLLGPNSFNGTTFIfISIFIMMLFNNFMGLFPYIFTSTSHMVLTFTIALPMWMSFMLFG- 117
Cdd:PRK13420   45 PGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFV-GTLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGi 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765453 118 ----WINHTKHmlaHLVPQgtpPALMSFMVlietISNIIRPGTLAVRLAANMiaghllltllgntgplMSYNLMSILI-- 191
Cdd:PRK13420  124 raegLREYLKH---YLSPS---PFLLPFHL----ISEITRTLALAVRLFGNI----------------MSLELAALLVll 177

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1707765453 192 ----FGQMLLLILESAVAMIQAYVFSILSTLY 219
Cdd:PRK13420  178 vagfLVPVPILMLHIIEALVQAYIFGMLALIY 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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