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Conserved domains on  [gi|1707765439|gb|QDP18021|]
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ATP synthase F0 subunit 6 (mitochondrion) [Sphenacris crassicornis]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009593)

ATP synthase F0 subunit 6 is part of the mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V), which produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-224 6.41e-97

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 281.67  E-value: 6.41e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439   1 MTNLFSTFDPATSlFNLSINWSSTIIGLSLMPMMFWILPSRIQLLWNKMNISLHKEFKTLIGPSSsNGTTFIFISTFIMI 80
Cdd:MTH00157    2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKN-KGSTLIFISLFSFI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  81 MFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707765439 161 LAANMIAGHLLLTLIGNTGSMISFSMTSILIISQTLLLMLESAVALIQAYVFSILSTLYSSETY 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-224 6.41e-97

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 281.67  E-value: 6.41e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439   1 MTNLFSTFDPATSlFNLSINWSSTIIGLSLMPMMFWILPSRIQLLWNKMNISLHKEFKTLIGPSSsNGTTFIFISTFIMI 80
Cdd:MTH00157    2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKN-KGSTLIFISLFSFI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  81 MFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707765439 161 LAANMIAGHLLLTLIGNTGSMISFSMTSILIISQTLLLMLESAVALIQAYVFSILSTLYSSETY 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 ...
4-222 2.33e-44

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: 148.12  E-value: 2.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439   4 LFSTFDP-ATSLFNLSINWSSTIIGLSLMPMMF----WILPSRIQLLWNKMNISLHKEFKTLIGPSSSNGTTFIFiSTFI 78
Cdd:TIGR01131   1 LFSQFDIsPITLFSLTLLSLILLLSLLIFLISSslsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  79 MIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIRPGTLA 158
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1707765439 159 VRLAANMIAGHLLLTLIGNTG-SMISFSMTSILIISQTLLLMLESAVALIQAYVFSILSTLYSSE 222
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLfSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
72-221 4.55e-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: 4.55e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  72 IFISTFIMIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETISNL 151
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439 152 IRPGTLAVRLAANMIAGHLLLTLIGNTGSMISFSMTSILIISQTLLLMLESAVALIQAYVFSILSTLYSS 221
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
39-221 9.94e-27

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 102.18  E-value: 9.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  39 PSRIQLLWNKMNISLHKEFKTLIGPSSSNGTTFIFISTFIMIMFNNFMGLF---PYIFTSTSHMALTFSIALPMWLSFML 115
Cdd:pfam00119  27 PGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439 116 FG-WINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIRPGTLAVRLAANMIAGHLLLTLIGNTGSMISFSMTSILIIS- 193
Cdd:pfam00119 107 YGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPp 186
                         170       180       190
                  ....*....|....*....|....*....|
gi 1707765439 194 --QTLLLMLESAVALIQAYVFSILSTLYSS 221
Cdd:pfam00119 187 llGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
77-219 1.10e-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: 91.29  E-value: 1.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  77 FIMIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFG-WINNTKHMLMHLVPQGTPtALMSFMVIIETISNLIRPG 155
Cdd:COG0356    65 FLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPL 143
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707765439 156 TLAVRLAANMIAGHLLLTLIGNTGSMISFSMTSILIisQTLLLMLESAVALIQAYVFSILSTLY 219
Cdd:COG0356   144 SLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-224 6.41e-97

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 281.67  E-value: 6.41e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439   1 MTNLFSTFDPATSlFNLSINWSSTIIGLSLMPMMFWILPSRIQLLWNKMNISLHKEFKTLIGPSSsNGTTFIFISTFIMI 80
Cdd:MTH00157    2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKN-KGSTLIFISLFSFI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  81 MFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707765439 161 LAANMIAGHLLLTLIGNTGSMISFSMTSILIISQTLLLMLESAVALIQAYVFSILSTLYSSETY 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
1-224 1.15e-51

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 166.75  E-value: 1.15e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439   1 MTNLFSTFDPATSLF--NLSINWSSTIIGLSLMPMMFWILPSRIQLLWNKMNiSLHKEFKTLIGPSSSNGTTFIFISTFI 78
Cdd:MTH00176    2 LVDLFSSFDPPNKNIfsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFS-TFLPEMILRSNGSYILGSASIIISLFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  79 MIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIRPGTLA 158
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707765439 159 VRLAANMIAGHLLLTLIGNTGS---MISFSMTSILIISQTLLLMLESAVALIQAYVFSILSTLYSSETY 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 ...
4-222 2.33e-44

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: 148.12  E-value: 2.33e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439   4 LFSTFDP-ATSLFNLSINWSSTIIGLSLMPMMF----WILPSRIQLLWNKMNISLHKEFKTLIGPSSSNGTTFIFiSTFI 78
Cdd:TIGR01131   1 LFSQFDIsPITLFSLTLLSLILLLSLLIFLISSslsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  79 MIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIRPGTLA 158
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1707765439 159 VRLAANMIAGHLLLTLIGNTG-SMISFSMTSILIISQTLLLMLESAVALIQAYVFSILSTLYSSE 222
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLfSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
72-221 4.55e-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: 4.55e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  72 IFISTFIMIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETISNL 151
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439 152 IRPGTLAVRLAANMIAGHLLLTLIGNTGSMISFSMTSILIISQTLLLMLESAVALIQAYVFSILSTLYSS 221
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
2-222 9.10e-40

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 136.26  E-value: 9.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439   2 TNLFSTFDPATSLFnLSINWSSTIIGLSLMPMMF---WiLPSRIQLLWNKMNISLHKEFKTLIGPSSSNGTTFIFiSTFI 78
Cdd:MTH00035    5 NSIFGQFSPDTILF-IPLTLLSSVIALSWLFFINptnW-LPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLT-TVFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  79 MIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIRPGTLA 158
Cdd:MTH00035   82 LILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALG 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1707765439 159 VRLAANMIAGHLLLTLIGNTGSMISFSMT--SILIISQTLLLMLESAVALIQAYVFSILSTLYSSE 222
Cdd:MTH00035  162 LRLAANLTAGHLLIFLLSTAIWELSNSPLisIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
1-222 7.93e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 131.39  E-value: 7.93e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439   1 MTNLFSTFDPATSLFNL----SINWSSTIIGLSLMPMMFWILPSRIQLLWNKMNISLHKEFKTLIGpSSSNGTTFIFIST 76
Cdd:MTH00005    2 LTDIFSSFDPATNSLFNnlssTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFG-KHLKGFSSLISAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  77 FIMIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIRPGT 156
Cdd:MTH00005   81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707765439 157 LAVRLAANMIAGHLLLTLIGNTGSMISFSMTS---ILIISQTLLLMLESAVALIQAYVFSILSTLYSSE 222
Cdd:MTH00005  161 LSFRLAANMSAGHIVLSLIGIYAASALFSSISstiLLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
23-222 4.26e-36

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 126.86  E-value: 4.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  23 STIIGLSLMPMMFWILPSRiQLLWNKM----NISLHKEFKTLIGPSSSNGT--TFIFISTFIMIMFNNFMGLFPYIFTST 96
Cdd:MTH00120   18 PLILLAMLIPALLIPSPKN-RLLTNRLttlqLWLIKLITKQLMLPLNKKGHkwALILTSLMLLLLLINLLGLLPYTFTPT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  97 SHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIRPGTLAVRLAANMIAGHLLLTLIG 176
Cdd:MTH00120   97 TQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVRLTANLTAGHLLIQLIS 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1707765439 177 NTGSMISFSMTSILIISQTLLL---MLESAVALIQAYVFSILSTLYSSE 222
Cdd:MTH00120  177 TATLNLLPTMPTLSLLTLIILLlltILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
1-223 5.17e-36

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 126.52  E-value: 5.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439   1 MTNLFSTFDPATSLFNL--SINWSSTIIGLSLMPMMFWILPSRIQLLWNKMNISLHKEFKTLIGpSSSNGTTFIFISTFI 78
Cdd:MTH00173    2 MVDLFSSFDDHNSSFSSlsFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSG-LNLGGFSLLLSSLFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  79 MIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIRPGTLA 158
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707765439 159 VRLAANMIAGHLLLTLIGNTGSMISFSM----TSILIISQTLLLMLESAVALIQAYVFSILSTLYSSET 223
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYLSSSLFSSsvvsLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDEH 229
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
1-222 1.03e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 125.83  E-value: 1.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439   1 MTNLFSTFDpATSLFNLSINWSSTIIGLSLMPMM-FWILPSRIQLLWNKMNISLHKEFKTLIGPSSSNGTtFIFISTFIM 79
Cdd:MTH00179    2 MLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLtNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWA-VLFLSLMLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  80 IMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIRPGTLAV 159
Cdd:MTH00179   80 LLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGV 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1707765439 160 RLAANMIAGHLLLTLIGNTGSMISFSMTSILIISQT---LLLMLESAVALIQAYVFSILSTLYSSE 222
Cdd:MTH00179  160 RLTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLvlfLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
72-222 3.00e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 124.60  E-value: 3.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  72 IFISTFIMIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETISNL 151
Cdd:MTH00132   72 LLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLF 151
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707765439 152 IRPGTLAVRLAANMIAGHLLLTLIGNTGSMISFSMTSILIISQTLLLM---LESAVALIQAYVFSILSTLYSSE 222
Cdd:MTH00132  152 IRPLALGVRLTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLltlLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
70-219 1.47e-34

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 122.75  E-value: 1.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  70 TFIFISTFIMIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETIS 149
Cdd:MTH00101   69 SLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETIS 148
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1707765439 150 NLIRPGTLAVRLAANMIAGHLLLTLIGNTG---SMISFSMTSILIISQTLLLMLESAVALIQAYVFSILSTLY 219
Cdd:MTH00101  149 LFIQPMALAVRLTANITAGHLLIHLIGGATlalMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
53-222 5.64e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 116.22  E-value: 5.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  53 LHKEFKTLIGPSSSNGT--TFIFISTFIMIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLV 130
Cdd:MTH00073   51 LQNFTKQLMLPLNTPGHkwALILTSLMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLL 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439 131 PQGTPTALMSFMVIIETISNLIRPGTLAVRLAANMIAGHLLLTLIGNTGSMISFSMTSILIISQTLLL---MLESAVALI 207
Cdd:MTH00073  131 PEGTPTLLIPILIIIETISLFIRPLALGVRLTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFlltLLEIAVAMI 210
                         170
                  ....*....|....*
gi 1707765439 208 QAYVFSILSTLYSSE 222
Cdd:MTH00073  211 QAYVFVLLLSLYLQE 225
ATP-synt_A pfam00119
ATP synthase A chain;
39-221 9.94e-27

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 102.18  E-value: 9.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  39 PSRIQLLWNKMNISLHKEFKTLIGPSSSNGTTFIFISTFIMIMFNNFMGLF---PYIFTSTSHMALTFSIALPMWLSFML 115
Cdd:pfam00119  27 PGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439 116 FG-WINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIRPGTLAVRLAANMIAGHLLLTLIGNTGSMISFSMTSILIIS- 193
Cdd:pfam00119 107 YGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPp 186
                         170       180       190
                  ....*....|....*....|....*....|
gi 1707765439 194 --QTLLLMLESAVALIQAYVFSILSTLYSS 221
Cdd:pfam00119 187 llGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
37-223 2.93e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 101.27  E-value: 2.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  37 ILPSRIQLLWNKMNISLHKEFKTLIGPSSSNGTTFIfISTFIMIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLF 116
Cdd:MTH00172   40 LIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFI-ISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLA 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439 117 GWINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIRPGTLAVRLAANMIAGHLLLTLIGNTG-SMISFSMTSIL--IIS 193
Cdd:MTH00172  119 GFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGfNMLCASGFLSLfpLLI 198
                         170       180       190
                  ....*....|....*....|....*....|
gi 1707765439 194 QTLLLMLESAVALIQAYVFSILSTLYSSET 223
Cdd:MTH00172  199 MVFITLLEIAVAVIQAYVFCLLTTIYLADT 228
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
20-224 4.65e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 100.85  E-value: 4.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  20 NWSSTIIGLSLMP----MMFWIL-------PSRIQLLWNKMNISLHKEFKTLIGPSSSNGTTFIFiSTFIMIMFNNFMGL 88
Cdd:MTH00175   23 DWLVTFTNSSMMMvlavIIFWLLlkgdkliPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFIL-SLFLFIAILNILGL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  89 FPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIRPGTLAVRLAANMIAG 168
Cdd:MTH00175  102 FPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAG 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439 169 HLLLTLI-GNTGSMIS---FSMTSILIISQTLLLMLESAVALIQAYVFSILSTLYSSETY 224
Cdd:MTH00175  182 HLLFAILsGFAFNMLSnglIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGDTI 241
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
77-219 1.10e-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: 91.29  E-value: 1.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  77 FIMIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFG-WINNTKHMLMHLVPQGTPtALMSFMVIIETISNLIRPG 155
Cdd:COG0356    65 FLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPL 143
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707765439 156 TLAVRLAANMIAGHLLLTLIGNTGSMISFSMTSILIisQTLLLMLESAVALIQAYVFSILSTLY 219
Cdd:COG0356   144 SLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
72-219 5.57e-18

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 79.07  E-value: 5.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  72 IFISTFIMIMFNNFMGLFP-YIFTSTSHMALTFSIALPMWLSFMLFG-WINNTKHMLMHLVPQGTPtalmsFMVIIETIS 149
Cdd:PRK05815   75 LAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQPHP-----LLLPIEIIS 149
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439 150 NLIRPGTLAVRLAANMIAGHLLLTLIGNTGSMISFSMTSILIISqTLLLMLESAVALIQAYVFSILSTLY 219
Cdd:PRK05815  150 EFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILP-VAWTIFEIFVGTLQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
37-223 7.67e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 79.21  E-value: 7.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  37 ILPSRIQLLWNKMNISLHKEFKTLIGPSSSNGTTFIfISTFIMIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLF 116
Cdd:MTH00174   59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFV-LSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439 117 GWINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIRPGTLAVRLAANMIAGHLLLTLIG-------NTGSMI-SFSMTS 188
Cdd:MTH00174  138 GLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIAsfawkmiNTGILIgSFVPFA 217
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1707765439 189 ILIisqtLLLMLESAVALIQAYVFSILSTLYSSET 223
Cdd:MTH00174  218 ILI----FVTILEMAVAIIQAYVFTLLTIVYLRDT 248
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
74-219 9.23e-13

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 66.30  E-value: 9.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  74 ISTFIMIMFNNFMGLFPYIFTSTSHMALTFSIALpmwLSFMLFGW----INNTKHMLMHLVpQGTPTALMSFMVIIETIS 149
Cdd:PRK13419  175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLAV---FTFFITQYaaikAHGIKGYLAHLT-GGTHWSLWIIMIPIEFIG 250
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1707765439 150 NLIRPGTLAVRLAANMIAGHL-LLTLIGntgsmISFSMTSILIISQT------LLLMLESAVALIQAYVFSILSTLY 219
Cdd:PRK13419  251 LFTKPFALTVRLFANMTAGHIvILSLIF-----ISFILKSYIVAVAVsvpfaiFIYLLELFVAFLQAYIFTMLSALF 322
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
71-222 2.72e-10

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 57.68  E-value: 2.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  71 FIFISTFIMIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKhmLMHLVPQGTPTALMSF-MVIIETIS 149
Cdd:MTH00087   53 VISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEK--FSVYLSKGSDSFLKTFsMLFVEIVS 130
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1707765439 150 NLIRPGTLAVRLAANMIAGHLLLTLIGNTGSMisFSMTSILIIsqtlllMLESAVALIQAYVFSILSTLYSSE 222
Cdd:MTH00087  131 ELSRPLALTLRLTVNLMVGHLISSLLNFLGEK--YVWLSILAI------MMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
94-219 3.73e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 55.67  E-value: 3.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  94 TSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETI-SNLIRPGTLAVRLAANMIAGH-LL 171
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHvII 296
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1707765439 172 LTLIGNTGSMISFSMTSILIISQTLLLMLESAVALIQAYVFSILSTLY 219
Cdd:PRK13417  297 LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
75-216 1.26e-04

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 41.02  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  75 STFIMIMFNNFMGL-FPYIFTSTSHMALTFSIALPMWLSFMLFGWINNTKHMLMHLVPQGTPTALMSFMVIIETISNLIR 153
Cdd:MTH00050   27 SVVLFIVLFLFLLYrLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIR 106
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707765439 154 PGTLAVRLAANMIAGHLLLTLIGNTgSMISFSMTSILIIsqtlLLMLESAVALIQAY-VFSILS 216
Cdd:MTH00050  107 PVVLILRPFINISLGCFGGVALGNL-CFISYWWFLVLFF----LFFYEVFVALVHWFiVSSILS 165
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
37-219 3.86e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 40.11  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439  37 ILPSRIQLLWNKMNISLHKEFKTLIgpSSSNGTTFIFISTF-IMIMFNNFMGLFPYIFTSTSHMALTFSIALPMWLSFML 115
Cdd:PRK13420   43 LDPGRFQVALEGVVSTIEDAIKEVL--PRHARLVLPFVGTLwIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHW 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707765439 116 FG-----WINNTKHMLmhlvpqgTPTAlmsFMVIIETISNLIRPGTLAVRLAANMIA---GHLLLTLIGNTGSMISFsmt 187
Cdd:PRK13420  121 FGiraegLREYLKHYL-------SPSP---FLLPFHLISEITRTLALAVRLFGNIMSlelAALLVLLVAGFLVPVPI--- 187
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1707765439 188 siliisqtllLMLESAVALIQAYVFSILSTLY 219
Cdd:PRK13420  188 ----------LMLHIIEALVQAYIFGMLALIY 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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