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Conserved domains on  [gi|1331215852|ref|YP_009454602|]
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ATP synthase F0 subunit 6 (mitochondrion) [Caryanda elegans]

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
1-225 1.37e-101

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 293.61  E-value: 1.37e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852   1 MMSNLFSTFDPSTNiFNLSLNWTSTMLGLILIPCLFWLMPSRINILWNKLNITLHNEFKTLLGSSsFNGTTFIFISIFIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  81 MLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISNVIRPGTLAV 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331215852 161 RLAANMIAGHLLLTLLGNTGPSMAMNLISLLIIGQMLLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-225 1.37e-101

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 293.61  E-value: 1.37e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852   1 MMSNLFSTFDPSTNiFNLSLNWTSTMLGLILIPCLFWLMPSRINILWNKLNITLHNEFKTLLGSSsFNGTTFIFISIFIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  81 MLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISNVIRPGTLAV 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331215852 161 RLAANMIAGHLLLTLLGNTGPSMAMNLISLLIIGQMLLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
5-225 6.10e-46

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: 151.98  E-value: 6.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852   5 LFSTFDPST-NIFNLSLNWTSTMLGLILI----PCLFWLMPSRINILWNKLNITLHNEFKTLLGSSSFNGTTFIFiSIFI 79
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  80 MMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISNVIRPGTLA 159
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331215852 160 VRLAANMIAGHLLLTLLGNTGPS-MAMNLISLLIIGQMLLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFSlMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
73-222 2.87e-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: 137.92  E-value: 2.87e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  73 IFISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISNV 152
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852 153 IRPGTLAVRLAANMIAGHLLLTLLGNTGPSMAMNLISLLIIGQMLLLILESAVAMIQAYVFSILSTLYSS 222
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
38-222 2.93e-25

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 98.33  E-value: 2.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  38 LMPSRINILWNKLNITLHNEFKTLLGSSSFNGTTFIFISIFIMMLFNNFMGLF---PYIFTSTSHLALTFAIALPMWLSF 114
Cdd:pfam00119  25 LVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852 115 MLFGWINH-TNHMFSHLVPQGTPPALMSFMVLIETISNVIRPGTLAVRLAANMIAGHLLLTLLGNTGPSMAMNLISLLII 193
Cdd:pfam00119 105 HYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVI 184
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1331215852 194 ---GQMLLLILESAVAMIQAYVFSILSTLYSS 222
Cdd:pfam00119 185 pplLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
76-220 7.16e-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: 89.36  E-value: 7.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  76 SIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINH-TNHMFSHLVPQGTPPaLMSFMVLIETISNVIR 154
Cdd:COG0356    63 TLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPW-LAPLMLPIEIISELAR 141
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331215852 155 PGTLAVRLAANMIAGHLLLTLLGNTGPSMAMNLISLLIigQMLLLILESAVAMIQAYVFSILSTLY 220
Cdd:COG0356   142 PLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-225 1.37e-101

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 293.61  E-value: 1.37e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852   1 MMSNLFSTFDPSTNiFNLSLNWTSTMLGLILIPCLFWLMPSRINILWNKLNITLHNEFKTLLGSSsFNGTTFIFISIFIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  81 MLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISNVIRPGTLAV 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331215852 161 RLAANMIAGHLLLTLLGNTGPSMAMNLISLLIIGQMLLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
1-225 5.72e-53

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 170.21  E-value: 5.72e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852   1 MMSNLFSTFDP-STNIFN-LSLNWTSTMLGLILIPCLFWLMPSRINILWNKLNiTLHNEFKTLLGSSSFNGTTFIFISIF 78
Cdd:MTH00176    1 MLVDLFSSFDPpNKNIFSmISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFS-TFLPEMILRSNGSYILGSASIIISLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  79 IMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISNVIRPGTL 158
Cdd:MTH00176   80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852 159 AVRLAANMIAGHLLLTLLGNTGPSMAMNLI---SLLIIGQMLLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:MTH00176  160 AVRLAANLSAGHLLLGLLGAAMWGLLPVSPligFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
5-225 6.10e-46

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: 151.98  E-value: 6.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852   5 LFSTFDPST-NIFNLSLNWTSTMLGLILI----PCLFWLMPSRINILWNKLNITLHNEFKTLLGSSSFNGTTFIFiSIFI 79
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  80 MMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISNVIRPGTLA 159
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331215852 160 VRLAANMIAGHLLLTLLGNTGPS-MAMNLISLLIIGQMLLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFSlMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
73-222 2.87e-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: 137.92  E-value: 2.87e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  73 IFISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISNV 152
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852 153 IRPGTLAVRLAANMIAGHLLLTLLGNTGPSMAMNLISLLIIGQMLLLILESAVAMIQAYVFSILSTLYSS 222
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
1-223 5.70e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 134.48  E-value: 5.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852   1 MMSNLFSTFDPSTNIFNLSLN----WTSTMLGLILIPCLFWLMPSRINILWNKLNITLHNEFKTLLGSSsFNGTTFIFIS 76
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFNNLSstafWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKH-LKGFSSLISA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  77 IFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISNVIRPG 156
Cdd:MTH00005   80 LFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPI 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852 157 TLAVRLAANMIAGHLLLTLLGNTGPSMAMNLIS---LLIIGQMLLLILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00005  160 TLSFRLAANMSAGHIVLSLIGIYAASALFSSISstiLLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
3-223 3.62e-37

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 129.71  E-value: 3.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852   3 SNLFSTFDPSTnIFNLSLNWTSTMLGLILIPCLF---WLmPSRINILWNKLNITLhneFKTLLGSSSFNGTTFI--FISI 77
Cdd:MTH00035    5 NSIFGQFSPDT-ILFIPLTLLSSVIALSWLFFINptnWL-PSRSQSIWLTFRQEI---LKLIFQNTNPNTAPWAglLTTV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  78 FIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISNVIRPGT 157
Cdd:MTH00035   80 FILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331215852 158 LAVRLAANMIAGHLLLTLLGNTGPSMAMNLI--SLLIIGQMLLLILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00035  160 LGLRLAANLTAGHLLIFLLSTAIWELSNSPLisIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
1-223 1.01e-36

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 128.44  E-value: 1.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852   1 MMSNLFSTFDPSTNIFNL--SLNWTSTMLGLILIPCLFWLMPSRINILWNKLNITLHNeFKTLLGSSSFNGTTFIFISIF 78
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSSlsFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSS-QVTRSSGLNLGGFSLLLSSLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  79 IMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISNVIRPGTL 158
Cdd:MTH00173   80 LFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331215852 159 AVRLAANMIAGHLLLTLLGNTGPSMAMNLIS----LLIIGQMLLLILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00173  160 TVRLLANISAGHIVLTLIGNYLSSSLFSSSVvsllLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
73-223 1.80e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 117.23  E-value: 1.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  73 IFISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISNV 152
Cdd:MTH00120   72 ILTSLMLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLL 151
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331215852 153 IRPGTLAVRLAANMIAGH-------LLLTLLGNTGPSMAMNLISLLiigqMLLLILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00120  152 IRPLALGVRLTANLTAGHlliqlisTATLNLLPTMPTLSLLTLIIL----LLLTILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
1-223 3.07e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 116.59  E-value: 3.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852   1 MMSNLFSTFDpSTNIFNLSLNWTSTMLGLILIPCLFWLMP-SRINILWNKLNITLHNEFKTLLGSSSFNGTtFIFISIFI 79
Cdd:MTH00179    1 MMLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLTNRWLnNRLSTLQSWFFGSFTFQLMQPINKKGHKWA-VLFLSLML 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  80 MMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISNVIRPGTLA 159
Cdd:MTH00179   79 FLLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331215852 160 VRLAANMIAGHLLLTLLGNTGPSMA--MNLISLLI-IGQMLLLILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00179  159 VRLTANITAGHLLMHLISSAVFVLMnfMGMVALLTlLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
73-223 5.94e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 113.43  E-value: 5.94e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  73 IFISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISNV 152
Cdd:MTH00132   72 LLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLF 151
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331215852 153 IRPGTLAVRLAANMIAGHLLLTLLGNTGPSMA--MNLISLLIIGQMLLL-ILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00132  152 IRPLALGVRLTANLTAGHLLIQLIATAAFVLLplMPTVAILTATLLFLLtLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
72-223 1.11e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 107.36  E-value: 1.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  72 FIFISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISN 151
Cdd:MTH00073   71 LILTSLMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISL 150
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331215852 152 VIRPGTLAVRLAANMIAGHLLLTLLGNTGPSMA--MNLISLLIIGQMLLL-ILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00073  151 FIRPLALGVRLTANLTAGHLLIQLISTATLVLLplMPTVSILTMIVLFLLtLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-220 1.26e-28

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 107.35  E-value: 1.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852   1 MMSNLFSTFDpstnifnlslnwTSTMLGL------ILIPCLFWLMPSR-INILWNKLNITL-HNEFKTLLGSSSFNGTTF 72
Cdd:MTH00101    1 MNENLFASFI------------TPTILGLpivtliIMFPSLLFPTPNRlINNRLISIQQWLiQLTSKQMMTIHNTKGQTW 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  73 --IFISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETIS 150
Cdd:MTH00101   69 slMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETIS 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331215852 151 NVIRPGTLAVRLAANMIAGHLLLTLLGN-----TGPSMAMNLISLLIIgqMLLLILESAVAMIQAYVFSILSTLY 220
Cdd:MTH00101  149 LFIQPMALAVRLTANITAGHLLIHLIGGatlalMSISTTTALITFIIL--ILLTILEFAVALIQAYVFTLLVSLY 221
ATP-synt_A pfam00119
ATP synthase A chain;
38-222 2.93e-25

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 98.33  E-value: 2.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  38 LMPSRINILWNKLNITLHNEFKTLLGSSSFNGTTFIFISIFIMMLFNNFMGLF---PYIFTSTSHLALTFAIALPMWLSF 114
Cdd:pfam00119  25 LVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852 115 MLFGWINH-TNHMFSHLVPQGTPPALMSFMVLIETISNVIRPGTLAVRLAANMIAGHLLLTLLGNTGPSMAMNLISLLII 193
Cdd:pfam00119 105 HYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVI 184
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1331215852 194 ---GQMLLLILESAVAMIQAYVFSILSTLYSS 222
Cdd:pfam00119 185 pplLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
15-220 3.23e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 98.57  E-value: 3.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  15 IFNLSLNWTSTMLGLILIPCLFWLMPSRINILWNKLNITLHNEFKTLLGSSSFNGTTFIfISIFIMMLFNNFMGLFPYIF 94
Cdd:MTH00172   17 LTNSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFI-ISLFFFIVFLNLLGLFPYVF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  95 TSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISNVIRPGTLAVRLAANMIAGHLLLT 174
Cdd:MTH00172   96 TPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFA 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1331215852 175 LLGNTGPSMAM-----NLISLLIIgqMLLLILESAVAMIQAYVFSILSTLY 220
Cdd:MTH00172  176 ILAGFGFNMLCasgflSLFPLLIM--VFITLLEIAVAVIQAYVFCLLTTIY 224
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
23-220 3.88e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 98.54  E-value: 3.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  23 TSTMLGLILIpcLFWLM-------PSRINILWNKLNITLHNEFKTLLGSSSFNGTTFIFiSIFIMMLFNNFMGLFPYIFT 95
Cdd:MTH00175   31 SSMMMVLAVI--IFWLLlkgdkliPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFIL-SLFLFIAILNILGLFPYVFT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  96 STSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVLIETISNVIRPGTLAVRLAANMIAGHLLLTL 175
Cdd:MTH00175  108 PTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAI 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1331215852 176 LGNTGPSMAMNLISLLIIGQMLLLI----LESAVAMIQAYVFSILSTLY 220
Cdd:MTH00175  188 LSGFAFNMLSNGLIILSLFPMLIMIfitlLEMAVAVIQAYVFCLLTTIY 236
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
76-220 7.16e-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: 89.36  E-value: 7.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  76 SIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINH-TNHMFSHLVPQGTPPaLMSFMVLIETISNVIR 154
Cdd:COG0356    63 TLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPW-LAPLMLPIEIISELAR 141
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331215852 155 PGTLAVRLAANMIAGHLLLTLLGNTGPSMAMNLISLLIigQMLLLILESAVAMIQAYVFSILSTLY 220
Cdd:COG0356   142 PLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
73-220 9.44e-18

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 78.68  E-value: 9.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  73 IFISIFIMMLFNNFMGLFP-YIFTSTSHLALTFAIALPMWLSFMLFG-WINHTNHMFSHLVPQGTPpalmsFMVLIETIS 150
Cdd:PRK05815   75 LAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQPHP-----LLLPIEIIS 149
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852 151 NVIRPGTLAVRLAANMIAGHLLLTLLGNTGPSMAMNLISLLIIGqMLLLILESAVAMIQAYVFSILSTLY 220
Cdd:PRK05815  150 EFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILP-VAWTIFEIFVGTLQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
38-220 4.87e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 77.29  E-value: 4.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  38 LMPSRINILWNKLNITLHNEFKTLLGSSSFNGTTFIfISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLF 117
Cdd:MTH00174   59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFV-LSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852 118 GWINHTNHMFSHLVPQGTPPALMSFMVLIETISNVIRPGTLAVRLAANMIAGHLLLTLLGNTGPSMAMN--LISLLIIGQ 195
Cdd:MTH00174  138 GLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTgiLIGSFVPFA 217
                         170       180
                  ....*....|....*....|....*..
gi 1331215852 196 MLLL--ILESAVAMIQAYVFSILSTLY 220
Cdd:MTH00174  218 ILIFvtILEMAVAIIQAYVFTLLTIVY 244
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
75-220 1.44e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 59.76  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  75 ISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALpmwLSFMLFGWINHTNH----MFSHLVpQGTPPALMSFMVLIETIS 150
Cdd:PRK13419  175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLAV---FTFFITQYAAIKAHgikgYLAHLT-GGTHWSLWIIMIPIEFIG 250
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331215852 151 NVIRPGTLAVRLAANMIAGHLLLTLLgnTGPSMAMN--LISLLIIGQMLLLI--LESAVAMIQAYVFSILSTLY 220
Cdd:PRK13419  251 LFTKPFALTVRLFANMTAGHIVILSL--IFISFILKsyIVAVAVSVPFAIFIylLELFVAFLQAYIFTMLSALF 322
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
64-223 3.41e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 51.90  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  64 SSSFNGTTFIFISIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFMLFGWINhtNHMFSHLVPQGTPPALMSF- 142
Cdd:MTH00087   45 SNKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSK--SEKFSVYLSKGSDSFLKTFs 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852 143 MVLIETISNVIRPGTLAVRLAANMIAGHLLLtllgntgpSMAMNLISLLIIGQMLLLILESAVAMIQAYVFSILSTLYSS 222
Cdd:MTH00087  123 MLFVEIVSELSRPLALTLRLTVNLMVGHLIS--------SLLNFLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLN 194

                  .
gi 1331215852 223 E 223
Cdd:MTH00087  195 E 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
75-220 3.01e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 47.19  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  75 ISIFIMMLFNNFMGLFPYI-----------------------------------FTSTSHLALTFAIALPMWLSFMLFGW 119
Cdd:PRK13417  162 FTLFFFILFCNLMGLVPSVgeltvvasdygglvalgvmdhtphalptfakvwsgITVTGDISVTMTLALLTMFLIYGAGF 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852 120 INHTNHMFSHLVPQGTPPALMSFMVLIETI-SNVIRPGTLAVRLAANMIAGHLLLT-LLGNTGPSMAMNLISLLIIGQML 197
Cdd:PRK13417  242 SYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVIILaLMGFIFQFQSWGIVPVSVIGSGL 321
                         170       180
                  ....*....|....*....|...
gi 1331215852 198 LLILESAVAMIQAYVFSILSTLY 220
Cdd:PRK13417  322 IYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
67-169 6.27e-05

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 42.18  E-value: 6.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  67 FNGTTFIFISIFIMMLFNNFMGL-FPYIFTSTSHLALTFAIALPMWLSFMLFGWINHTNHMFSHLVPQGTPPALMSFMVL 145
Cdd:MTH00050   18 LGGSVSYYYSVVLFIVLFLFLLYrLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCI 97
                          90       100
                  ....*....|....*....|....
gi 1331215852 146 IETISNVIRPGTLAVRLAANMIAG 169
Cdd:MTH00050   98 AETISYIIRPVVLILRPFINISLG 121
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
38-220 7.20e-05

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 42.42  E-value: 7.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852  38 LMPSRINILWNKLNITLHNEFKTLLgsSSFNGTTFIFI-SIFIMMLFNNFMGLFPYIFTSTSHLALTFAIALPMWLSFML 116
Cdd:PRK13420   43 LDPGRFQVALEGVVSTIEDAIKEVL--PRHARLVLPFVgTLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHW 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331215852 117 FG-----WINHTNHMFShlvpqgTPPALMSFMVlietISNVIRPGTLAVRLAANMIaghllltllgntgpSMAMNLISLL 191
Cdd:PRK13420  121 FGiraegLREYLKHYLS------PSPFLLPFHL----ISEITRTLALAVRLFGNIM--------------SLELAALLVL 176
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1331215852 192 IIGQML----LLILESAVAMIQAYVFSILSTLY 220
Cdd:PRK13420  177 LVAGFLvpvpILMLHIIEALVQAYIFGMLALIY 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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