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Conserved domains on  [gi|2070647616|gb|QXT45725|]
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ATP synthase F0 subunit 6 (mitochondrion) [Epeorus dayongensis]

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 8.02e-120

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 339.45  E-value: 8.02e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616   1 MTNLFSVFDPSSSiMNLSLNWVSTFLGLLLLPSAYWLMPSRYSLIWNKVTSTLHQEFNTLLGPTgHPGSTFLFISLFSLI 80
Cdd:MTH00157    2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  81 VFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070647616 161 LAANMIAGHLLMTLLGNTGPSLSLTLLSFLVIGQIALLVLESAVAIIQSYVFAVLSTLYSSEVN 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-224 8.02e-120

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 339.45  E-value: 8.02e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616   1 MTNLFSVFDPSSSiMNLSLNWVSTFLGLLLLPSAYWLMPSRYSLIWNKVTSTLHQEFNTLLGPTgHPGSTFLFISLFSLI 80
Cdd:MTH00157    2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  81 VFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070647616 161 LAANMIAGHLLMTLLGNTGPSLSLTLLSFLVIGQIALLVLESAVAIIQSYVFAVLSTLYSSEVN 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 1.80e-53

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: 171.24  E-value: 1.80e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616   4 LFSVFDPSSSIM-NLSLNWVSTFLGLLLL----PSAYWLMPSRYSLIWNKVTSTLHQEFNTLLGPTGHPgSTFLFISLFS 78
Cdd:TIGR01131   1 LFSQFDISPITLfSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGK-FFPLIFTLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  79 LIVFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLA 158
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070647616 159 VRLAANMIAGHLLMTLLGNTGPSLSLTLLSFLVI-GQIALLVLESAVAIIQSYVFAVLSTLYSSEVN 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 3.27e-47

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: 152.94  E-value: 3.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  72 LFISLFSLIVFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNV 151
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616 152 IRPGTLAVRLAANMIAGHLLMTLLGNTGPSLSLTLLSFLVIGQIALLVLESAVAIIQSYVFAVLSTLYSS 221
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
21-221 2.56e-32

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 116.44  E-value: 2.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  21 WVSTFLGLLLLPSAYW----LMPSRYSLIWNKVTSTLHQEFNTLLGPTGHPGSTFLFISLFSLIVFNNFLGLF---PYIF 93
Cdd:pfam00119   5 LIVALILLLFLLLATRktkkLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  94 TSSSHLTFTLTLALPLWMSFMLYGWINH-TQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLAVRLAANMIAGHLLM 172
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2070647616 173 TLLGNTGPSLSLTLLSFLVI---GQIALLVLESAVAIIQSYVFAVLSTLYSS 221
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVIpplLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 72-219 6.90e-25

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: 97.07  E-value: 6.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  72 LFISLFSLIVFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINH-TQHMFAHLVPQGTPPvLMPFMVCIETISN 150
Cdd:COG0356    60 LLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPW-LAPLMLPIEIISE 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070647616 151 VIRPGTLAVRLAANMIAGHLLMTLLGNTGPslSLTLLSFLVIGQIALLVLESAVAIIQSYVFAVLSTLY 219
Cdd:COG0356   139 LARPLSLSLRLFGNMFAGHIILLLLAGLAP--FLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-224 8.02e-120

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 339.45  E-value: 8.02e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616   1 MTNLFSVFDPSSSiMNLSLNWVSTFLGLLLLPSAYWLMPSRYSLIWNKVTSTLHQEFNTLLGPTgHPGSTFLFISLFSLI 80
Cdd:MTH00157    2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  81 VFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2070647616 161 LAANMIAGHLLMTLLGNTGPSLSLTLLSFLVIGQIALLVLESAVAIIQSYVFAVLSTLYSSEVN 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 1.80e-53

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: 171.24  E-value: 1.80e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616   4 LFSVFDPSSSIM-NLSLNWVSTFLGLLLL----PSAYWLMPSRYSLIWNKVTSTLHQEFNTLLGPTGHPgSTFLFISLFS 78
Cdd:TIGR01131   1 LFSQFDISPITLfSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGK-FFPLIFTLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  79 LIVFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLA 158
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070647616 159 VRLAANMIAGHLLMTLLGNTGPSLSLTLLSFLVI-GQIALLVLESAVAIIQSYVFAVLSTLYSSEVN 224
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFSLMSSAIFALLLlILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-223 1.19e-52

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 169.44  E-value: 1.19e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616   1 MTNLFSVFDPSSSIM--NLSLNWVSTFLGLLLLPSAYWLMPSRYSLIWNKVtSTLHQEFNTLLGPTGHPGSTFLFISLFS 78
Cdd:MTH00176    2 LVDLFSSFDPPNKNIfsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMF-STFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  79 LIVFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLA 158
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2070647616 159 VRLAANMIAGHLLMTLLGNTGPSLSLTLLSFLV---IGQIALLVLESAVAIIQSYVFAVLSTLYSSEV 223
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFlllIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 72-221 3.27e-47

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: 152.94  E-value: 3.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  72 LFISLFSLIVFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNV 151
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616 152 IRPGTLAVRLAANMIAGHLLMTLLGNTGPSLSLTLLSFLVIGQIALLVLESAVAIIQSYVFAVLSTLYSS 221
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-222 7.26e-43

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 144.49  E-value: 7.26e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616   1 MTNLFSVFDPSSSIMNLSLN----WVSTFLGLLLLPSAYWLMPSRYSLIWNKVTSTLHQEFNTLLGpTGHPGSTFLFISL 76
Cdd:MTH00005    2 LTDIFSSFDPATNSLFNNLSstafWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFG-KHLKGFSSLISAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  77 FSLIVFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGT 156
Cdd:MTH00005   81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070647616 157 LAVRLAANMIAGHLLMTLLG---NTGPSLSLTLLSFLVIGQIALLVLESAVAIIQSYVFAVLSTLYSSE 222
Cdd:MTH00005  161 LSFRLAANMSAGHIVLSLIGiyaASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-222 2.50e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 134.99  E-value: 2.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616   1 MTNLFSVFDPSSSIMNL--SLNWVSTFLGLLLLPSAYWLMPSRYSLIWNKVTSTLHQEFNTLLGPTGHPGSTFLFiSLFS 78
Cdd:MTH00173    2 MVDLFSSFDDHNSSFSSlsFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLS-SLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  79 LIVFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLA 158
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2070647616 159 VRLAANMIAGHLLMTLLGNTGPSLSLTLLSFLV----IGQIALLVLESAVAIIQSYVFAVLSTLYSSE 222
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYLSSSLFSSSVVSLllvlLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-222 6.56e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 133.92  E-value: 6.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616   1 MTNLFSVFDpSSSIMNLSLNWVSTFLGLLLLPSAYWLMP-SRYSLIWNKVTSTLHQEFNTLLGPTGHPGStFLFISLFSL 79
Cdd:MTH00179    2 MLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLTNRWLnNRLSTLQSWFFGSFTFQLMQPINKKGHKWA-VLFLSLMLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  80 IVFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLAV 159
Cdd:MTH00179   80 LLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070647616 160 RLAANMIAGHLLMTLLGNTGPSLSLTLLSFLVIGQ---IALLVLESAVAIIQSYVFAVLSTLYSSE 222
Cdd:MTH00179  160 RLTANITAGHLLMHLISSAVFVLMNFMGMVALLTLlvlFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 2-222 1.63e-36

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 127.78  E-value: 1.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616   2 TNLFSVFDPSSsIMNLSLNWVSTFLGL---LLLPSAYWLmPSRYSLIWNKVTSTLHQEFNTLLGPTGHPGSTFLFiSLFS 78
Cdd:MTH00035    5 NSIFGQFSPDT-ILFIPLTLLSSVIALswlFFINPTNWL-PSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLT-TVFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  79 LIVFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLA 158
Cdd:MTH00035   82 LILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALG 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070647616 159 VRLAANMIAGHLLMTLLGNT--GPSLSLTLLSFLVIGQIALLVLESAVAIIQSYVFAVLSTLYSSE 222
Cdd:MTH00035  162 LRLAANLTAGHLLIFLLSTAiwELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-222 2.90e-36

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 127.25  E-value: 2.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616   1 MTNLFSVFDpSSSIMNLSLNWVSTFLGLLLLPSA-YWLMPSRYSLIWNKVTSTLHQEFNTLLGPTGHPGSTFLfISLFSL 79
Cdd:MTH00120    2 NLNFFDQFS-SPELLGIPLILLAMLIPALLIPSPkNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALIL-TSLMLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  80 IVFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLAV 159
Cdd:MTH00120   80 LLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2070647616 160 RLAANMIAGHLLMTLLGNTGPSLSLTLLSFLVIGQIALL---VLESAVAIIQSYVFAVLSTLYSSE 222
Cdd:MTH00120  160 RLTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLlltILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 3-219 5.37e-34

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 121.21  E-value: 5.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616   3 NLFSVFDpSSSIMNLSLNWVSTFLGLLLLPSAYWLMPSRYSLIWNKVTSTLHQEFNTLLGPTGHPGSTFLfISLFSLIVF 82
Cdd:MTH00101    4 NLFASFI-TPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLML-MSLILFIGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  83 NNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLAVRLA 162
Cdd:MTH00101   82 TNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLT 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616 163 ANMIAGHLLMTLLGNTGPSLSLTLLSFLVIGQIALL---VLESAVAIIQSYVFAVLSTLY 219
Cdd:MTH00101  162 ANITAGHLLIHLIGGATLALMSISTTTALITFIILIlltILEFAVALIQAYVFTLLVSLY 221
ATP-synt_A pfam00119
ATP synthase A chain;
21-221 2.56e-32

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 116.44  E-value: 2.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  21 WVSTFLGLLLLPSAYW----LMPSRYSLIWNKVTSTLHQEFNTLLGPTGHPGSTFLFISLFSLIVFNNFLGLF---PYIF 93
Cdd:pfam00119   5 LIVALILLLFLLLATRktkkLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  94 TSSSHLTFTLTLALPLWMSFMLYGWINH-TQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLAVRLAANMIAGHLLM 172
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2070647616 173 TLLGNTGPSLSLTLLSFLVI---GQIALLVLESAVAIIQSYVFAVLSTLYSS 221
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVIpplLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 17-222 9.02e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 115.36  E-value: 9.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  17 LSLNWVstflgLLLLPSAYWLMpSRYSLIWNKVTSTLHQEFNTLLGPTGHPGSTfLFISLFSLIVFNNFLGLFPYIFTSS 96
Cdd:MTH00132   24 LTLPWI-----LFPTPTSRWLN-NRLLTLQGWFINRFTQQLLLPLNVGGHKWAL-LLTSLMLFLITLNMLGLLPYTFTPT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  97 SHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLAVRLAANMIAGHLLMTLLG 176
Cdd:MTH00132   97 TQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIA 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2070647616 177 NTGPSLSLTLLSFLVIGQIALL---VLESAVAIIQSYVFAVLSTLYSSE 222
Cdd:MTH00132  177 TAAFVLLPLMPTVAILTATLLFlltLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-222 1.55e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 115.06  E-value: 1.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616   1 MTNLFSVFdPSSSIMNLSLNWVSTFLGLLLL--PSAYWLmPSRYSLIWNKVTSTLHQEFNTLLGPTGHPGStFLFISLFS 78
Cdd:MTH00073    2 NLSFFDQF-LSPTLLGIPLIMLAMLLPWLLFptPTNKWL-NNRLSTLQIWFLQNFTKQLMLPLNTPGHKWA-LILTSLMV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  79 LIVFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLA 158
Cdd:MTH00073   79 FLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070647616 159 VRLAANMIAGHLLMTLLGNTGPSLSLTLLSFLVIGQIALL---VLESAVAIIQSYVFAVLSTLYSSE 222
Cdd:MTH00073  159 VRLTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFlltLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 14-219 3.03e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 106.66  E-value: 3.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  14 IMNLSLNWVSTFLGLLLLPSAYWLMPSRYSLIWNKVTSTLHQEFNTLLGPTGHPGSTFLfISLFSLIVFNNFLGLFPYIF 93
Cdd:MTH00172   17 LTNSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFI-ISLFFFIVFLNLLGLFPYVF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  94 TSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLAVRLAANMIAGHLLMT 173
Cdd:MTH00172   96 TPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFA 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2070647616 174 LLGNTG---PSLSLTLLSFLVIGQIALLVLESAVAIIQSYVFAVLSTLY 219
Cdd:MTH00172  176 ILAGFGfnmLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIY 224
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 9-219 2.61e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 101.62  E-value: 2.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616   9 DPSSSIMNLSLNWVSTFLGLLLLPSAYWLMPSRYSLIWNKVTSTLHQEFNTLLGPTGHPGSTFLFiSLFSLIVFNNFLGL 88
Cdd:MTH00175   23 DWLVTFTNSSMMMVLAVIIFWLLLKGDKLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFIL-SLFLFIAILNILGL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  89 FPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTLAVRLAANMIAG 168
Cdd:MTH00175  102 FPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAG 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2070647616 169 HLLMTLLgnTGPSLSLTLLSFLVIGQIALL------VLESAVAIIQSYVFAVLSTLY 219
Cdd:MTH00175  182 HLLFAIL--SGFAFNMLSNGLIILSLFPMLimifitLLEMAVAVIQAYVFCLLTTIY 236
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 72-219 6.90e-25

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: 97.07  E-value: 6.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  72 LFISLFSLIVFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINH-TQHMFAHLVPQGTPPvLMPFMVCIETISN 150
Cdd:COG0356    60 LLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPW-LAPLMLPIEIISE 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2070647616 151 VIRPGTLAVRLAANMIAGHLLMTLLGNTGPslSLTLLSFLVIGQIALLVLESAVAIIQSYVFAVLSTLY 219
Cdd:COG0356   139 LARPLSLSLRLFGNMFAGHIILLLLAGLAP--FLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 72-219 7.07e-21

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 86.77  E-value: 7.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  72 LFISLFSLIVFNNFLGLFP-YIFTSSSHLTFTLTLALPLWMSFMLYG-WINHTQHMFAHLVPQgtppvLMPFMVCIETIS 149
Cdd:PRK05815   75 LAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQ-----PHPLLLPIEIIS 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616 150 NVIRPGTLAVRLAANMIAGHLLMTLLGNTGPSLSLTLLSFLVIGqIALLVLESAVAIIQSYVFAVLSTLY 219
Cdd:PRK05815  150 EFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILP-VAWTIFEIFVGTLQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 74-219 8.56e-19

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 81.91  E-value: 8.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  74 ISLFSLIVFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIR 153
Cdd:MTH00174   95 LSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISR 174

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616 154 PGTLAVRLAANMIAGHLLMTLLGNTGPSLSLTLLSFLVIGQIALL----VLESAVAIIQSYVFAVLSTLY 219
Cdd:MTH00174  175 AISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSFVPFAILifvtILEMAVAIIQAYVFTLLTIVY 244
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 74-219 4.04e-11

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 61.30  E-value: 4.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  74 ISLFSLIVFNNFLGLFPYIFTSSSHLTFTLTLALplwMSFMLYGWINHTQH----MFAHLVpQGTPPVLMPFMVCIETIS 149
Cdd:PRK13419  175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLAV---FTFFITQYAAIKAHgikgYLAHLT-GGTHWSLWIIMIPIEFIG 250

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2070647616 150 NVIRPGTLAVRLAANMIAGHL-LMTLLGNTGPS-LSLTLLSFLVIGQIALLVLESAVAIIQSYVFAVLSTLY 219
Cdd:PRK13419  251 LFTKPFALTVRLFANMTAGHIvILSLIFISFILkSYIVAVAVSVPFAIFIYLLELFVAFLQAYIFTMLSALF 322
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 67-222 4.70e-10

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 56.91  E-value: 4.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  67 PGSTFLFISLFSLIVFNNFLGLFPYIFTSSSHLTFTLTLALPLWMSFMLYGWINhtQHMFAHLVPQGTPPVLMPF-MVCI 145
Cdd:MTH00087   49 PLSSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSK--SEKFSVYLSKGSDSFLKTFsMLFV 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2070647616 146 ETISNVIRPGTLAVRLAANMIAGHLLMTLLGNTGpslsltllSFLVIGQIALLVLESAVAIIQSYVFAVLSTLYSSE 222
Cdd:MTH00087  127 EIVSELSRPLALTLRLTVNLMVGHLISSLLNFLG--------EKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 94-219 5.03e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 55.28  E-value: 5.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  94 TSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETI-SNVIRPGTLAVRLAANMIAGH-LL 171
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHvII 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2070647616 172 MTLLGNTGPSLSLTLLSFLVIGQIALLVLESAVAIIQSYVFAVLSTLY 219
Cdd:PRK13417  297 LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 22-219 5.75e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 48.59  E-value: 5.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  22 VSTFLGLLLLPSAYWLMPSRYSLIWNKVTSTLHQEFNTLLgpTGHPGSTFLFI-SLFSLIVFNNFLGLFPYIFTSSSHLT 100
Cdd:PRK13420   28 IVLVLASWLTTRRLSLDPGRFQVALEGVVSTIEDAIKEVL--PRHARLVLPFVgTLWIFILVANLIGLIPGFHSPTADLS 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616 101 FTLTLALPLWMSFMLYG-----WINHTQHmfaHLVPQgtpPVLMPFMVcietISNVIRPGTLAVRLAANM----IAGHLL 171
Cdd:PRK13420  106 VTAALALLVFFSVHWFGiraegLREYLKH---YLSPS---PFLLPFHL----ISEITRTLALAVRLFGNImsleLAALLV 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2070647616 172 MTLLGNTGPslsltllsflvigqIALLVLESAVAIIQSYVFAVLSTLY 219
Cdd:PRK13420  176 LLVAGFLVP--------------VPILMLHIIEALVQAYIFGMLALIY 209
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 79-177 2.15e-06

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 46.42  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2070647616  79 LIVFNNFLGL-FPYIFTSSSHLTFTLTLALPLWMSFMLYGWINHTQHMFAHLVPQGTPPVLMPFMVCIETISNVIRPGTL 157
Cdd:MTH00050   31 FIVLFLFLLYrLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVL 110

                          90       100
                  ....*....|....*....|
gi 2070647616 158 AVRLAANMIAGHLLMTLLGN 177
Cdd:MTH00050  111 ILRPFINISLGCFGGVALGN 130
 
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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