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Conserved domains on  [gi|1896069427|gb|QNJ46869|]
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ATP synthase F0 subunit 6, partial (mitochondrion) [Systella rafflesii]

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
 1-221 2.92e-84

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 249.31  E-value: 2.92e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427   1 MMSNLFSTFDPSTNiMNLSLKWTSTMIGLMMIPSWYWLLSSRTMMIWNKMNNSIKNEFKSISKKSNM---LMFTSMLIML 77
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKgstLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  78 LTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETISNLIRPGTLSIR 157
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069427 158 LAANMIAGHLLMTLLGNNGPSTSMNLISILIFSQMMLLILESAVTIIQAYVFSVLSILYSSETN 221
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-221 2.92e-84

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 249.31  E-value: 2.92e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427   1 MMSNLFSTFDPSTNiMNLSLKWTSTMIGLMMIPSWYWLLSSRTMMIWNKMNNSIKNEFKSISKKSNM---LMFTSMLIML 77
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKgstLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  78 LTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETISNLIRPGTLSIR 157
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069427 158 LAANMIAGHLLMTLLGNNGPSTSMNLISILIFSQMMLLILESAVTIIQAYVFSVLSILYSSETN 221
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-219 1.04e-41

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: 141.19  E-value: 1.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427   5 LFSTFDPSTNIM---NLSLKWTSTMIGLMMIPSWY--WLLSSRTMMIWNKMNNSIKNEFKSISKKSNM---LMFTSMLIM 76
Cdd:TIGR01131   1 LFSQFDISPITLfslTLLSLILLLSLLIFLISSSLsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGkffPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  77 LLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETISNLIRPGTLSI 156
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069427 157 RLAANMIAGHLLMTLLGNNGPS-TSMNLISILIFSQMMLLILESAVTIIQAYVFSVLSILYSSE 219
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSlMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 64-218 8.98e-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: 8.98e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  64 KSNMLMFTSMLIMLLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIE 143
Cdd:cd00310     2 KKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIE 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896069427 144 TISNLIRPGTLSIRLAANMIAGHLLMTLLGNNGPSTSMNLISILIFSQMMLLILESAVTIIQAYVFSVLSILYSS 218
Cdd:cd00310    82 LISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
45-218 1.67e-24

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 96.02  E-value: 1.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  45 MIWNKMNNSIKNEFKSISKKSNMLMFTSMLIMLLTNNFMGLF---PYIFTSTSHMLMTFSIAMPMWTSFMLFGWTIN-TK 120
Cdd:pfam00119  36 MLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIKKHgLG 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427 121 KMFTHLVPMGTPSMIMPFMVIIETISNLIRPGTLSIRLAANMIAGHLLMTLLGNNGPSTSMNLISILIFS---QMMLLIL 197
Cdd:pfam00119 116 GYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPpllGVAWTLF 195

                         170       180
                  ....*....|....*....|.
gi 1896069427 198 ESAVTIIQAYVFSVLSILYSS 218
Cdd:pfam00119 196 ELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 69-216 3.10e-20

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: 84.74  E-value: 3.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  69 MFTSMLIMLLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTIN-TKKMFTHLVPMGTPSMImPFMVIIETISN 147
Cdd:COG0356    60 LLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPWLA-PLMLPIEIISE 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1896069427 148 LIRPGTLSIRLAANMIAGHLLMTLLGNNGPSTSMNLISILIfsQMMLLILESAVTIIQAYVFSVLSILY 216
Cdd:COG0356   139 LARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-221 2.92e-84

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 249.31  E-value: 2.92e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427   1 MMSNLFSTFDPSTNiMNLSLKWTSTMIGLMMIPSWYWLLSSRTMMIWNKMNNSIKNEFKSISKKSNM---LMFTSMLIML 77
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKgstLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  78 LTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETISNLIRPGTLSIR 157
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069427 158 LAANMIAGHLLMTLLGNNGPSTSMNLISILIFSQMMLLILESAVTIIQAYVFSVLSILYSSETN 221
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-219 1.04e-41

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: 141.19  E-value: 1.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427   5 LFSTFDPSTNIM---NLSLKWTSTMIGLMMIPSWY--WLLSSRTMMIWNKMNNSIKNEFKSISKKSNM---LMFTSMLIM 76
Cdd:TIGR01131   1 LFSQFDISPITLfslTLLSLILLLSLLIFLISSSLsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGkffPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  77 LLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETISNLIRPGTLSI 156
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069427 157 RLAANMIAGHLLMTLLGNNGPS-TSMNLISILIFSQMMLLILESAVTIIQAYVFSVLSILYSSE 219
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSlMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 64-218 8.98e-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: 8.98e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  64 KSNMLMFTSMLIMLLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIE 143
Cdd:cd00310     2 KKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIE 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896069427 144 TISNLIRPGTLSIRLAANMIAGHLLMTLLGNNGPSTSMNLISILIFSQMMLLILESAVTIIQAYVFSVLSILYSS 218
Cdd:cd00310    82 LISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-219 2.13e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 137.86  E-value: 2.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427   1 MMSNLFSTFDP--STNIMNLSLKWTSTMIGLMMIPSWYWLLSSRTMMIWNKMNNSIKnEFKSISKKSNMLM----FTSML 74
Cdd:MTH00176    1 MLVDLFSSFDPpnKNIFSMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLP-EMILRSNGSYILGsasiIISLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  75 IMLLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETISNLIRPGTL 154
Cdd:MTH00176   80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1896069427 155 SIRLAANMIAGHLLMTLLGNNGPS---TSMNLISILIFSQMMLLILESAVTIIQAYVFSVLSILYSSE 219
Cdd:MTH00176  160 AVRLAANLSAGHLLLGLLGAAMWGllpVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDE 227
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 3-219 1.31e-37

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 130.48  E-value: 1.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427   3 SNLFSTFDPSTnIMNLSLkwtsTMIGLMMIPSWYWL------LSSRTMMIWNKMNNSI-KNEFKSISKKSN--MLMFTSM 73
Cdd:MTH00035    5 NSIFGQFSPDT-ILFIPL----TLLSSVIALSWLFFinptnwLPSRSQSIWLTFRQEIlKLIFQNTNPNTApwAGLLTTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  74 LIMLLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETISNLIRPGT 153
Cdd:MTH00035   80 FILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896069427 154 LSIRLAANMIAGHLLMTLLGN------NGPSTSMNLISILIfsqmMLLILESAVTIIQAYVFSVLSILYSSE 219
Cdd:MTH00035  160 LGLRLAANLTAGHLLIFLLSTaiwelsNSPLISIITLIIFF----LLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-219 4.20e-37

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 129.47  E-value: 4.20e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427   1 MMSNLFSTFDPSTNIMNLSLK----WTSTMIGLMMIPSWYWLLSSRTMMIWNKMNNSIKNEFKSISK---KSNMLMFTSM 73
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFNNLSstafWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGkhlKGFSSLISAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  74 LIMLLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETISNLIRPGT 153
Cdd:MTH00005   81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1896069427 154 LSIRLAANMIAGHLLMTLLGNNGPS---TSMNLISILIFSQMMLLILESAVTIIQAYVFSVLSILYSSE 219
Cdd:MTH00005  161 LSFRLAANMSAGHIVLSLIGIYAASalfSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-220 1.74e-36

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 127.67  E-value: 1.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427   1 MMSNLFSTFDPSTNIMNL--SLKWTSTMIGLMMIPSWYWLLSSRT---MMIWNKMNNSIKNEFKSISKKSNMLMFTSMLI 75
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSSlsFLMWLLSLMSLFFFSSSVWVSSSNLssvFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  76 MLLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETISNLIRPGTLS 155
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1896069427 156 IRLAANMIAGHLLMTLLGNNGPSTSMNLIS----ILIFSQMMLLILESAVTIIQAYVFSVLSILYSSET 220
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYLSSSLFSSSVvsllLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDEH 229
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-219 4.65e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 116.08  E-value: 4.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427   1 MMSNLFSTFDpSTNIMNLSLKWTSTMIGLMMIPSW-YWLLSSR--TMMIWnKMNNSIKNEFKSISKKSNM--LMFTSMLI 75
Cdd:MTH00120    1 MNLNFFDQFS-SPELLGIPLILLAMLIPALLIPSPkNRLLTNRltTLQLW-LIKLITKQLMLPLNKKGHKwaLILTSLML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  76 MLLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETISNLIRPGTLS 155
Cdd:MTH00120   79 LLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896069427 156 IRLAANMIAGHLLMTLLGNNGPS--TSMNLISILIFSQMMLL-ILESAVTIIQAYVFSVLSILYSSE 219
Cdd:MTH00120  159 VRLTANLTAGHLLIQLISTATLNllPTMPTLSLLTLIILLLLtILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-219 6.27e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 115.82  E-value: 6.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427   1 MMSNLFSTFDpSTNIMNLSLKWTSTMIGLMMIPSWY--WLLSSRTMMIWNKMNNSIKNEFKSISKKSN--MLMFTSMLIM 76
Cdd:MTH00179    1 MMLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLTnrWLNNRLSTLQSWFFGSFTFQLMQPINKKGHkwAVLFLSLMLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  77 LLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETISNLIRPGTLSI 156
Cdd:MTH00179   80 LLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896069427 157 RLAANMIAGHLLMTLLGNN--GPSTSMNLISILIFSQ-MMLLILESAVTIIQAYVFSVLSILYSSE 219
Cdd:MTH00179  160 RLTANITAGHLLMHLISSAvfVLMNFMGMVALLTLLVlFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-216 1.73e-29

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 109.27  E-value: 1.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427   1 MMSNLFSTFDPSTnIMNLSLKWTSTMIGLMMIPSWYWLLSSRTMMIWNKMNNSIKNEFKSISKKSNM---LMFTSMLIML 77
Cdd:MTH00101    1 MNENLFASFITPT-ILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQtwsLMLMSLILFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  78 LTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETISNLIRPGTLSIR 157
Cdd:MTH00101   80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896069427 158 LAANMIAGHLLMTLLGNNG---PSTSMNLISILIFSQMMLLILESAVTIIQAYVFSVLSILY 216
Cdd:MTH00101  160 LTANITAGHLLIHLIGGATlalMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 68-219 2.64e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 108.81  E-value: 2.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  68 LMFTSMLIMLLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETISN 147
Cdd:MTH00132   71 LLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISL 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1896069427 148 LIRPGTLSIRLAANMIAGHLLMTLLGNNG-------PSTSMnLISILIFsqmMLLILESAVTIIQAYVFSVLSILYSSE 219
Cdd:MTH00132  151 FIRPLALGVRLTANLTAGHLLIQLIATAAfvllplmPTVAI-LTATLLF---LLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-219 5.20e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 103.12  E-value: 5.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427   1 MMSNLFSTFDPSTnIMNLSLKWTSTMIGLMMI--PSWYWLLSSRTMMIWNKMNNSIKNEFKSISKKSN--MLMFTSMLIM 76
Cdd:MTH00073    1 MNLSFFDQFLSPT-LLGIPLIMLAMLLPWLLFptPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHkwALILTSLMVF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  77 LLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETISNLIRPGTLSI 156
Cdd:MTH00073   80 LITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896069427 157 RLAANMIAGHLLMTLLGNNGPS--TSMNLISILIFSQMMLL-ILESAVTIIQAYVFSVLSILYSSE 219
Cdd:MTH00073  160 RLTANLTAGHLLIQLISTATLVllPLMPTVSILTMIVLFLLtLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP-synt_A pfam00119
ATP synthase A chain;
45-218 1.67e-24

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 96.02  E-value: 1.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  45 MIWNKMNNSIKNEFKSISKKSNMLMFTSMLIMLLTNNFMGLF---PYIFTSTSHMLMTFSIAMPMWTSFMLFGWTIN-TK 120
Cdd:pfam00119  36 MLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIKKHgLG 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427 121 KMFTHLVPMGTPSMIMPFMVIIETISNLIRPGTLSIRLAANMIAGHLLMTLLGNNGPSTSMNLISILIFS---QMMLLIL 197
Cdd:pfam00119 116 GYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPpllGVAWTLF 195

                         170       180
                  ....*....|....*....|.
gi 1896069427 198 ESAVTIIQAYVFSVLSILYSS 218
Cdd:pfam00119 196 ELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 72-220 8.05e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 95.07  E-value: 8.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  72 SMLIMLLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETISNLIRP 151
Cdd:MTH00175   88 SLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRA 167

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896069427 152 GTLSIRLAANMIAGHLLMT--------LLGNNGPSTSMNLISILIFsqmmLLILESAVTIIQAYVFSVLSILYSSET 220
Cdd:MTH00175  168 ISLGVRLAANISAGHLLFAilsgfafnMLSNGLIILSLFPMLIMIF----ITLLEMAVAVIQAYVFCLLTTIYLGDT 240
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 72-220 1.46e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 88.94  E-value: 1.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  72 SMLIMLLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETISNLIRP 151
Cdd:MTH00172   77 SLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRA 156

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896069427 152 GTLSIRLAANMIAGHLLMTLL---GNNGPSTSMNLISILIFSQMMLLILESAVTIIQAYVFSVLSILYSSET 220
Cdd:MTH00172  157 ISLGVRLAANLSAGHLLFAILagfGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADT 228
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 69-216 3.10e-20

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: 84.74  E-value: 3.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  69 MFTSMLIMLLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTIN-TKKMFTHLVPMGTPSMImPFMVIIETISN 147
Cdd:COG0356    60 LLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPWLA-PLMLPIEIISE 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1896069427 148 LIRPGTLSIRLAANMIAGHLLMTLLGNNGPSTSMNLISILIfsQMMLLILESAVTIIQAYVFSVLSILY 216
Cdd:COG0356   139 LARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 45-216 6.30e-17

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 76.37  E-value: 6.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  45 MIWNKMNNSIKNEFKSISKKSNMLMFTsMLIMLLTNNFMGLFP-YIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMF 123
Cdd:PRK05815   52 MIVEFVRGQVKDNIGGKGKKFAPLAFT-LFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGY 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427 124 THLVPMGtpsmIMPFMVIIETISNLIRPGTLSIRLAANMIAGHLLMTLLGNNGPSTSMNLISILIFSqMMLLILESAVTI 203
Cdd:PRK05815  131 LKEFYLQ----PHPLLLPIEIISEFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILP-VAWTIFEIFVGT 205

                         170
                  ....*....|...
gi 1896069427 204 IQAYVFSVLSILY 216
Cdd:PRK05815  206 LQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 62-220 2.28e-16

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 75.36  E-value: 2.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  62 SKKSNMLMFT-SMLIMLLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMV 140
Cdd:MTH00174   85 NKGGNYLAFVlSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLT 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427 141 IIETISNLIRPGTLSIRLAANMIAGHLLMTLLGNNGPSTSMNLISILIFSQMMLL----ILESAVTIIQAYVFSVLSILY 216
Cdd:MTH00174  165 IIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSFVPFAILifvtILEMAVAIIQAYVFTLLTIVY 244


                  ....
gi 1896069427 217 SSET 220
Cdd:MTH00174  245 LRDT 248
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 44-174 1.29e-08

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 52.58  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  44 MMIWNkmNNSIKNEFKSISKKSNMLMFTSMLIMLLTNNFMGL-FPYIFTSTSHMLMTFSIAMPMWTSFMLFGWTINTKKM 122
Cdd:MTH00050    1 MFVND--FSSLFSLIYKLILGGSVSYYYSVVLFIVLFLFLLYrLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEF 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1896069427 123 FTHLVPMGTPSMIMPFMVIIETISNLIRPGTLSIRLAANMIAGHLLMTLLGN 174
Cdd:MTH00050   79 FSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGCFGGVALGN 130
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 73-216 4.33e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 52.44  E-value: 4.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  73 MLIMLLtnNFMGLFPYIFTSTSHMLMTfsIAMPMWTSFMLFGWTINT---KKMFTHLVPmGTPSMIMPFMVIIETISNLI 149
Cdd:PRK13419  179 FFILVC--NLLGLVPYGATATGNINVT--LTLAVFTFFITQYAAIKAhgiKGYLAHLTG-GTHWSLWIIMIPIEFIGLFT 253

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1896069427 150 RPGTLSIRLAANMIAGHL-LMTLLGNN----------GPSTSMnliSILIFsqmmllILESAVTIIQAYVFSVLSILY 216
Cdd:PRK13419  254 KPFALTVRLFANMTAGHIvILSLIFISfilksyivavAVSVPF---AIFIY------LLELFVAFLQAYIFTMLSALF 322
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 70-219 7.16e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 50.75  E-value: 7.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  70 FTSMLIMLLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFgwTINTKKMFTHLVPMGTPSMIMPF-MVIIETISNL 148
Cdd:MTH00087   55 SFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLS--FLSKSEKFSVYLSKGSDSFLKTFsMLFVEIVSEL 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896069427 149 IRPGTLSIRLAANMIAGHLLMTLLGNNGPSTSMNLISILIFsqmmllilESAVTIIQAYVFSVLSILYSSE 219
Cdd:MTH00087  133 SRPLALTLRLTVNLMVGHLISSLLNFLGEKYVWLSILAIMM--------ECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 91-216 3.34e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 49.89  E-value: 3.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  91 TSTSHMLMTFSIAMPMWTSFMLFGWTINTKKMFTHLVPMGTPSMIMPFMVIIETI-SNLIRPGTLSIRLAANMIAGH-LL 168
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHvII 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1896069427 169 MTLLGNNGPSTSMNLISILIFSQMMLLILESAVTIIQAYVFSVLSILY 216
Cdd:PRK13417  297 LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 72-216 9.91e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 35.87  E-value: 9.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069427  72 SMLIMLLTNNFMGLFPYIFTSTSHMLMTFSIAMPMWTSFMLFGwtINTKKMFTHLVPMGTPSmimPFMVIIETISNLIRP 151
Cdd:PRK13420   80 TLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFG--IRAEGLREYLKHYLSPS---PFLLPFHLISEITRT 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896069427 152 GTLSIRLAANMIAGHLLMTLLgnngpstsmnLISILIFSQMMLLILESAVTIIQAYVFSVLSILY 216
Cdd:PRK13420  155 LALAVRLFGNIMSLELAALLV----------LLVAGFLVPVPILMLHIIEALVQAYIFGMLALIY 209
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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