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Conserved domains on  [gi|1807606641|gb|QHX99915|]
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ATP synthase F0 subunit 6 (mitochondrion) [Tagasta indica]

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 8.38e-97

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 281.29  E-value: 8.38e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641   1 MMTNLFSTFDPSTSlFNLSINWLSTFMGILMIPNMFWFNSSRIQLLWNKLSLNLHNELKTLIGiKSFNGTTLIFISMFIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLG-PKNKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  81 LMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISNIIRPGTLAI 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1807606641 161 RLAANMIAGHLLLTLMGNTGPSMHHNILIILITSQMMLLILESAVALIQAYVFSILSALYSSESY 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 8.38e-97

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 281.29  E-value: 8.38e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641   1 MMTNLFSTFDPSTSlFNLSINWLSTFMGILMIPNMFWFNSSRIQLLWNKLSLNLHNELKTLIGiKSFNGTTLIFISMFIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLG-PKNKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  81 LMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISNIIRPGTLAI 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1807606641 161 RLAANMIAGHLLLTLMGNTGPSMHHNILIILITSQMMLLILESAVALIQAYVFSILSALYSSESY 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 1.27e-44

ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be designated ATP synthase, F0 subunit A; eukaryotic (chloroplast and mitochondrial) forms should be designated ATP synthase, F0 subunit 6. The F1/F0 ATP synthase is a multisubunit, membrane associated enzyme found in bacteria and mitochondria and chloroplast. This enzyme is principally involved in the synthesis of ATP from ADP and inorganic phosphate by coupling the energy derived from the proton electrochemical gradient across the biological membrane. A brief description of this multisubunit enzyme complex: F1 and F0 represent two major clusters of subunits. Individual subunits in each of these clusters are named differently in prokaryotes and in organelles e.g., mitochondria and chloroplast. The bacterial equivalent of subunit 6 is named subunit 'A'. It has been shown that proton is conducted though this subunit. Typically, deprotonation and reprotonation of the acidic amino acid side-chains are implicated in the process. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273458  Cd Length: 226  Bit Score: 148.51  E-value: 1.27e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641   5 LFSTFDPST-SLFNLSINWLSTFMGILMIPNMFWFN----SSRIQLLWNKLSLNLHNELKTLIGIKSFNgTTLIFISMFI 79
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFLISSSLSrwliPSRWQNLMESIYEFVLSIVKSQIGGKKGK-FFPLIFTLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  80 MLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISNIIRPGTLA 159
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1807606641 160 IRLAANMIAGHLLLTLMGNTGPSMHH-NILIILITSQMMLLILESAVALIQAYVFSILSALYSSESY 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 ...
 71-222 1.17e-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: 138.69  E-value: 1.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  71 TLIFISMFIMLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETIS 150
Cdd:cd00310     5 LPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELIS 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1807606641 151 NIIRPGTLAIRLAANMIAGHLLLTLMGNTGPSMHHNILIILITSQMMLLILESAVALIQAYVFSILSALYSS 222
Cdd:cd00310    85 ELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
41-222 2.66e-25

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 98.33  E-value: 2.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  41 SRIQLLWNKLSLNLHNELKTLIGIKSFNGTTLIFISMFIMLMFNNFMGLF---PYIFTSSSHMVMTFSIALPMWLSFMLF 117
Cdd:pfam00119  28 GRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641 118 GWINN-TKHMLAHLVPQGTPMALMSFMVLIETISNIIRPGTLAIRLAANMIAGHLLLTLMGNTGPSMHHN---ILIILIT 193
Cdd:pfam00119 108 GIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAgflLGVIPPL 187

                         170       180
                  ....*....|....*....|....*....
gi 1807606641 194 SQMMLLILESAVALIQAYVFSILSALYSS 222
Cdd:pfam00119 188 LGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 76-220 1.22e-21

FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 88.59  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  76 SMFIMLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFG-WINNTKHMLAHLVPQGTPmALMSFMVLIETISNIIR 154
Cdd:COG0356    63 TLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISELAR 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1807606641 155 PGTLAIRLAANMIAGHLLLTLMGNTGPSMHHNILIILITsqMMLLILESAVALIQAYVFSILSALY 220
Cdd:COG0356   142 PLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLLP--VAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 8.38e-97

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 281.29  E-value: 8.38e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641   1 MMTNLFSTFDPSTSlFNLSINWLSTFMGILMIPNMFWFNSSRIQLLWNKLSLNLHNELKTLIGiKSFNGTTLIFISMFIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLG-PKNKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  81 LMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISNIIRPGTLAI 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1807606641 161 RLAANMIAGHLLLTLMGNTGPSMHHNILIILITSQMMLLILESAVALIQAYVFSILSALYSSESY 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-225 2.64e-50

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 163.28  E-value: 2.64e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641   1 MMTNLFSTFDPSTSLF--NLSINWLSTFMGILMIPNMFWFNSSRIQLLWNKLSlNLHNELKTLIGIKSFNGTTLIFISMF 78
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIfsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFS-TFLPEMILRSNGSYILGSASIIISLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  79 IMLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISNIIRPGTL 158
Cdd:MTH00176   80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641 159 AIRLAANMIAGHLLLTLMGNTGPS---MHHNILIILITSQMMLLILESAVALIQAYVFSILSALYSSESY 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 1.27e-44

ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be designated ATP synthase, F0 subunit A; eukaryotic (chloroplast and mitochondrial) forms should be designated ATP synthase, F0 subunit 6. The F1/F0 ATP synthase is a multisubunit, membrane associated enzyme found in bacteria and mitochondria and chloroplast. This enzyme is principally involved in the synthesis of ATP from ADP and inorganic phosphate by coupling the energy derived from the proton electrochemical gradient across the biological membrane. A brief description of this multisubunit enzyme complex: F1 and F0 represent two major clusters of subunits. Individual subunits in each of these clusters are named differently in prokaryotes and in organelles e.g., mitochondria and chloroplast. The bacterial equivalent of subunit 6 is named subunit 'A'. It has been shown that proton is conducted though this subunit. Typically, deprotonation and reprotonation of the acidic amino acid side-chains are implicated in the process. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273458  Cd Length: 226  Bit Score: 148.51  E-value: 1.27e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641   5 LFSTFDPST-SLFNLSINWLSTFMGILMIPNMFWFN----SSRIQLLWNKLSLNLHNELKTLIGIKSFNgTTLIFISMFI 79
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFLISSSLSrwliPSRWQNLMESIYEFVLSIVKSQIGGKKGK-FFPLIFTLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  80 MLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISNIIRPGTLA 159
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1807606641 160 IRLAANMIAGHLLLTLMGNTGPSMHH-NILIILITSQMMLLILESAVALIQAYVFSILSALYSSESY 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 ...
 71-222 1.17e-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: 138.69  E-value: 1.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  71 TLIFISMFIMLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETIS 150
Cdd:cd00310     5 LPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELIS 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1807606641 151 NIIRPGTLAIRLAANMIAGHLLLTLMGNTGPSMHHNILIILITSQMMLLILESAVALIQAYVFSILSALYSS 222
Cdd:cd00310    85 ELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-223 1.75e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 138.33  E-value: 1.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641   1 MMTNLFSTFDPSTSLFNL----SINWLSTFMGILMIPNMFWFNSSRIQLLWNKLSLNLHNELKTLIGiKSFNGTTLIFIS 76
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFNnlssTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFG-KHLKGFSSLISA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  77 MFIMLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISNIIRPG 156
Cdd:MTH00005   80 LFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641 157 TLAIRLAANMIAGHLLLTLMGN-TGPSMHHNIL--IILITSQMMLLILESAVALIQAYVFSILSALYSSE 223
Cdd:MTH00005  160 TLSFRLAANMSAGHIVLSLIGIyAASALFSSISstILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-224 1.18e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 136.15  E-value: 1.18e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641   1 MMTNLFSTFDPSTSLFNL--SINWLSTFMGILMIPNMFWFNSSRIQLLWNKLSLNLHNELKTLIGiKSFNGTTLIFISMF 78
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSSlsFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSG-LNLGGFSLLLSSLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  79 IMLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISNIIRPGTL 158
Cdd:MTH00173   80 LFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641 159 AIRLAANMIAGHLLLTLMGNTGPS----MHHNILIILITSQMMLLILESAVALIQAYVFSILSALYSSES 224
Cdd:MTH00173  160 TVRLLANISAGHIVLTLIGNYLSSslfsSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDEH 229
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 3-223 3.13e-38

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 132.40  E-value: 3.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641   3 TNLFSTFDPSTSLFnLSINWLSTFMGI---LMIPNMFWFNSsRIQLLWNKLSLNLHNELKTLIGIKSFNGTTLIFiSMFI 79
Cdd:MTH00035    5 NSIFGQFSPDTILF-IPLTLLSSVIALswlFFINPTNWLPS-RSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLT-TVFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  80 MLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISNIIRPGTLA 159
Cdd:MTH00035   82 LILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALG 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1807606641 160 IRLAANMIAGHLLLTLMGNT--GPSMHHNILIILITSQMMLLILESAVALIQAYVFSILSALYSSE 223
Cdd:MTH00035  162 LRLAANLTAGHLLIFLLSTAiwELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-223 1.73e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 125.06  E-value: 1.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641   1 MMTNLFSTFDpSTSLFNLSINWLSTFMGILMIP--NMFWFNSsRIQLLWNKLSLNLHNELKTLIGIKSFNGTtLIFISMF 78
Cdd:MTH00179    1 MMLSMFDQFE-SPSLLGIPLLALALLLPWLLFPslTNRWLNN-RLSTLQSWFFGSFTFQLMQPINKKGHKWA-VLFLSLM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  79 IMLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISNIIRPGTL 158
Cdd:MTH00179   78 LFLLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLAL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1807606641 159 AIRLAANMIAGHLLLTLMGNTGPSMHHNILIILITSQ---MMLLILESAVALIQAYVFSILSALYSSE 223
Cdd:MTH00179  158 GVRLTANITAGHLLMHLISSAVFVLMNFMGMVALLTLlvlFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-223 9.17e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 118.00  E-value: 9.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641   1 MMTNLFSTFDPSTSLFnlsinwLSTFMGILMIPNMFWFNSSRiQLLWNKLS----LNLHNELKTLIGIKSFNGT--TLIF 74
Cdd:MTH00120    1 MNLNFFDQFSSPELLG------IPLILLAMLIPALLIPSPKN-RLLTNRLTtlqlWLIKLITKQLMLPLNKKGHkwALIL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  75 ISMFIMLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISNIIR 154
Cdd:MTH00120   74 TSLMLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1807606641 155 PGTLAIRLAANMIAGHLLLTLMG-------NTGPSMHHNILIILitsqMMLLILESAVALIQAYVFSILSALYSSE 223
Cdd:MTH00120  154 PLALGVRLTANLTAGHLLIQLIStatlnllPTMPTLSLLTLIIL----LLLTILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-220 1.15e-30

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 112.74  E-value: 1.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641   1 MMTNLFSTFDPSTsLFNLSINWLSTFMGILMIPNMFWFNSSRIQLLWNKLslnLHNELKTLIGIKSFNGTT--LIFISMF 78
Cdd:MTH00101    1 MNENLFASFITPT-ILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWL---IQLTSKQMMTIHNTKGQTwsLMLMSLI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  79 IMLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISNIIRPGTL 158
Cdd:MTH00101   77 LFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMAL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1807606641 159 AIRLAANMIAGHLLLTLMGN-TGPSMHHNILIILITSQMMLL--ILESAVALIQAYVFSILSALY 220
Cdd:MTH00101  157 AVRLTANITAGHLLIHLIGGaTLALMSISTTTALITFIILILltILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 72-224 4.31e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 111.12  E-value: 4.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  72 LIFISMFIMLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISN 151
Cdd:MTH00132   71 LLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISL 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1807606641 152 IIRPGTLAIRLAANMIAGHLLLTLMGNTG---PSMHHNILIILITSQMMLLILESAVALIQAYVFSILSALYSSES 224
Cdd:MTH00132  151 FIRPLALGVRLTANLTAGHLLIQLIATAAfvlLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-223 1.24e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 104.66  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641   1 MMTNLFSTFdPSTSLFNLSINWLSTFMGILMIPNMF--WFNSsRIQLLWNKLSLNLHNELKTLIGIKSFNgTTLIFISMF 78
Cdd:MTH00073    1 MNLSFFDQF-LSPTLLGIPLIMLAMLLPWLLFPTPTnkWLNN-RLSTLQIWFLQNFTKQLMLPLNTPGHK-WALILTSLM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  79 IMLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISNIIRPGTL 158
Cdd:MTH00073   78 VFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLAL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1807606641 159 AIRLAANMIAGHLLLTLMGNTGPSMHHNILIILITSQMMLL---ILESAVALIQAYVFSILSALYSSE 223
Cdd:MTH00073  158 GVRLTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFlltLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 75-225 6.84e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 100.47  E-value: 6.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  75 ISMFIMLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISNIIR 154
Cdd:MTH00175   87 LSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIR 166

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1807606641 155 PGTLAIRLAANMIAGHLLLTLMGNTGPSMHHNILIILITSQMMLLI----LESAVALIQAYVFSILSALYSSESY 225
Cdd:MTH00175  167 AISLGVRLAANISAGHLLFAILSGFAFNMLSNGLIILSLFPMLIMIfitlLEMAVAVIQAYVFCLLTTIYLGDTI 241
ATP-synt_A pfam00119
ATP synthase A chain;
41-222 2.66e-25

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 98.33  E-value: 2.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  41 SRIQLLWNKLSLNLHNELKTLIGIKSFNGTTLIFISMFIMLMFNNFMGLF---PYIFTSSSHMVMTFSIALPMWLSFMLF 117
Cdd:pfam00119  28 GRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641 118 GWINN-TKHMLAHLVPQGTPMALMSFMVLIETISNIIRPGTLAIRLAANMIAGHLLLTLMGNTGPSMHHN---ILIILIT 193
Cdd:pfam00119 108 GIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAgflLGVIPPL 187

                         170       180
                  ....*....|....*....|....*....
gi 1807606641 194 SQMMLLILESAVALIQAYVFSILSALYSS 222
Cdd:pfam00119 188 LGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 15-220 3.30e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 98.57  E-value: 3.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  15 LFNLSINWLSTFMGILMIPNMFWFNSSRIQLLWNKLSLNLHNELKTLIGIKSFNGTTLIfISMFIMLMFNNFMGLFPYIF 94
Cdd:MTH00172   17 LTNSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFI-ISLFFFIVFLNLLGLFPYVF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  95 TSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISNIIRPGTLAIRLAANMIAGHLLLT 174
Cdd:MTH00172   96 TPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFA 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1807606641 175 LMGNTGPSMHHNILIILITSQMMLL---ILESAVALIQAYVFSILSALY 220
Cdd:MTH00172  176 ILAGFGFNMLCASGFLSLFPLLIMVfitLLEIAVAVIQAYVFCLLTTIY 224
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 76-220 1.22e-21

FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 88.59  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  76 SMFIMLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFG-WINNTKHMLAHLVPQGTPmALMSFMVLIETISNIIR 154
Cdd:COG0356    63 TLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISELAR 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1807606641 155 PGTLAIRLAANMIAGHLLLTLMGNTGPSMHHNILIILITsqMMLLILESAVALIQAYVFSILSALY 220
Cdd:COG0356   142 PLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLLP--VAWTAFELLVGFLQAYIFTMLTAVY 205
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 75-220 8.09e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 79.21  E-value: 8.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  75 ISMFIMLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETISNIIR 154
Cdd:MTH00174   95 LSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISR 174

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641 155 PGTLAIRLAANMIAGHLLLTLMGNTGPSMHHNILIILITSQMMLL----ILESAVALIQAYVFSILSALY 220
Cdd:MTH00174  175 AISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSFVPFAILifvtILEMAVAIIQAYVFTLLTIVY 244
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 73-225 5.65e-17

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 76.37  E-value: 5.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  73 IFISMFIMLMFNNFMGLFP-YIFTSSSHMVMTFSIALPMWLSFMLFG-WINNTKHMLAHLVPQGTPmalmsFMVLIETIS 150
Cdd:PRK05815   75 LAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQPHP-----LLLPIEIIS 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1807606641 151 NIIRPGTLAIRLAANMIAGHLLLTLMGNTGPSMHHNILIILITSqMMLLILESAVALIQAYVFSILSALYSSESY 225
Cdd:PRK05815  150 EFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILP-VAWTIFEIFVGTLQAYIFMMLTIVYISMAV 223
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 75-220 1.97e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 59.37  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  75 ISMFIMLMFNNFMGLFPYIFTSSSHMVMTFSIALpmwLSFMLFGW----INNTKHMLAHLVpQGTPMALMSFMVLIETIS 150
Cdd:PRK13419  175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLAV---FTFFITQYaaikAHGIKGYLAHLT-GGTHWSLWIIMIPIEFIG 250

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1807606641 151 NIIRPGTLAIRLAANMIAGHL-LLTLMGNTGpSMHHNILIILITSQMMLLI--LESAVALIQAYVFSILSALY 220
Cdd:PRK13419  251 LFTKPFALTVRLFANMTAGHIvILSLIFISF-ILKSYIVAVAVSVPFAIFIylLELFVAFLQAYIFTMLSALF 322
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 95-220 2.06e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 53.36  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  95 TSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLAHLVPQGTPMALMSFMVLIETI-SNIIRPGTLAIRLAANMIAGH-LL 172
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHvII 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1807606641 173 LTLMGNTGPSMHHNILIILITSQMMLLILESAVALIQAYVFSILSALY 220
Cdd:PRK13417  297 LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 73-223 4.08e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 48.82  E-value: 4.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  73 IFISMFIMLMFNNFMGLFPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKhmLAHLVPQGTPMALMSF-MVLIETISN 151
Cdd:MTH00087   54 ISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEK--FSVYLSKGSDSFLKTFsMLFVEIVSE 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1807606641 152 IIRPGTLAIRLAANMIAGHLLLTLMGntgpSMHHNILIILITSQMMllilESAVALIQAYVFSILSALYSSE 223
Cdd:MTH00087  132 LSRPLALTLRLTVNLMVGHLISSLLN----FLGEKYVWLSILAIMM----ECFVAFIQSYIFSRLIYLYLNE 195
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 50-217 4.05e-06

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 45.65  E-value: 4.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641  50 LSLNLHNELKTLIGIKSFNGTTLIFISMFIMLMFNNFMGL-FPYIFTSSSHMVMTFSIALPMWLSFMLFGWINNTKHMLA 128
Cdd:MTH00050    1 MFVNDFSSLFSLIYKLILGGSVSYYYSVVLFIVLFLFLLYrLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1807606641 129 HLVPQGTPMALMSFMVLIETISNIIRPGTLAIRLAANMIAGHLLLTLMGNTGPSMHHNILIILItsqmmLLILESAVALI 208
Cdd:MTH00050   81 SFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGCFGGVALGNLCFISYWWFLVLFF-----LFFYEVFVALV 155

                         170
                  ....*....|
gi 1807606641 209 QAY-VFSILS 217
Cdd:MTH00050  156 HWFiVSSILS 165
 
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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