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Conserved domains on  [gi|1896069433|gb|QNJ46872|]
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ATP synthase F0 subunit 6, partial (mitochondrion) [Atractomorpha sp. RINSinlTDFRAAPEI-84]

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 7.46e-99

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 286.29  E-value: 7.46e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433   1 MMTNLFSTFDPSTSlFYYSINWSSTIMGMFLMPSLFWILPSRNNLLWNKLTLKIHQEFKMLIGNKYNGMTLMFISMFIMM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  81 MFNNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069433 161 LTANMIAGHLLLTLLGNSGAMIKLNLLSMVIIAQMLLMVLESGVALIQAYVFSILSTLYASETY 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-224 7.46e-99

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 286.29  E-value: 7.46e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433   1 MMTNLFSTFDPSTSlFYYSINWSSTIMGMFLMPSLFWILPSRNNLLWNKLTLKIHQEFKMLIGNKYNGMTLMFISMFIMM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  81 MFNNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069433 161 LTANMIAGHLLLTLLGNSGAMIKLNLLSMVIIAQMLLMVLESGVALIQAYVFSILSTLYASETY 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 ...
 5-222 9.39e-47

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: 153.90  E-value: 9.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433   5 LFSTFDPSTSLFYYSINWS-----STIMGMFLMPSLFWILPSRNNLLWNKLTLKIHQEFKMLIGNKYNGMTLMFISMFIM 79
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLSlilllSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  80 MMFNNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLAV 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069433 160 RLTANMIAGHLLLTLLGNSG-AMIKLNLLSMVIIAQMLLMVLESGVALIQAYVFSILSTLYASE 222
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLfSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 83-219 7.36e-43

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: 141.77  E-value: 7.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  83 NNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLAVRLT 162
Cdd:cd00310    18 SNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLF 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1896069433 163 ANMIAGHLLLTLLGNSGAMIKLNLLSMVIIAQMLLMVLESGVALIQAYVFSILSTLY 219
Cdd:cd00310    98 ANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVY 154
ATP-synt_A pfam00119
ATP synthase A chain;
83-219 3.19e-26

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 100.64  E-value: 3.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  83 NNFMGLF---PYIFTSTSHMVMTFSIALPMWVSFMLFG-WINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLA 158
Cdd:pfam00119  71 SNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLS 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069433 159 VRLTANMIAGHLLLTLLGNSGAMIKLNLLSMVII---AQMLLMVLESGVALIQAYVFSILSTLY 219
Cdd:pfam00119 151 LRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIpplLGVAWTLFELLVAFIQAYVFTMLTAVY 214
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 83-219 6.97e-24

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: 94.37  E-value: 6.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  83 NNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFG-WINNTKHMLAHLVPQGTPnLLMPFMVLIETISNIIRPGTLAVRL 161
Cdd:COG0356    71 SNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRL 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1896069433 162 TANMIAGHLLLTLLGNSGAMIKLNLLSmvIIAQMLLMVLESGVALIQAYVFSILSTLY 219
Cdd:COG0356   150 FGNMFAGHIILLLLAGLAPFLLLGVLS--LLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-224 7.46e-99

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 286.29  E-value: 7.46e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433   1 MMTNLFSTFDPSTSlFYYSINWSSTIMGMFLMPSLFWILPSRNNLLWNKLTLKIHQEFKMLIGNKYNGMTLMFISMFIMM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  81 MFNNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069433 161 LTANMIAGHLLLTLLGNSGAMIKLNLLSMVIIAQMLLMVLESGVALIQAYVFSILSTLYASETY 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-224 1.42e-50

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 164.05  E-value: 1.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433   1 MMTNLFSTFDPSTSLFY--YSINWSSTIMGMFLMPSLFWILPSRNNLLWNKLTLKIHQEFKMLIGNKYNGMTLMFISMFI 78
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFsmISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  79 MMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLA 158
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1896069433 159 VRLTANMIAGHLLLTLLGNSGA---MIKLNLLSMVIIAQMLLMVLESGVALIQAYVFSILSTLYASETY 224
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWgllPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-222 9.39e-47

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: 153.90  E-value: 9.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433   5 LFSTFDPSTSLFYYSINWS-----STIMGMFLMPSLFWILPSRNNLLWNKLTLKIHQEFKMLIGNKYNGMTLMFISMFIM 79
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLSlilllSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  80 MMFNNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLAV 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069433 160 RLTANMIAGHLLLTLLGNSG-AMIKLNLLSMVIIAQMLLMVLESGVALIQAYVFSILSTLYASE 222
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLfSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-222 1.25e-43

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 146.42  E-value: 1.25e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433   1 MMTNLFSTFDPSTSLFYY----SINWSSTIMGMFLMPSLFWILPSRNNLLWNKLTLKIHQEFKMLIGNKYNGMTLMFISM 76
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFNnlssTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  77 FIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGT 156
Cdd:MTH00005   81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1896069433 157 LAVRLTANMIAGHLLLTLLG---NSGAMIKLNLLSMVIIAQMLLMVLESGVALIQAYVFSILSTLYASE 222
Cdd:MTH00005  161 LSFRLAANMSAGHIVLSLIGiyaASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 83-219 7.36e-43

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: 141.77  E-value: 7.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  83 NNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLAVRLT 162
Cdd:cd00310    18 SNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLF 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1896069433 163 ANMIAGHLLLTLLGNSGAMIKLNLLSMVIIAQMLLMVLESGVALIQAYVFSILSTLY 219
Cdd:cd00310    98 ANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVY 154
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-223 1.48e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 135.76  E-value: 1.48e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433   1 MMTNLFSTFDPSTSLFY--YSINWSSTIMGMFLMPSLFWILPSRNNLLWNKLTLKIHQEFKMLIGNKYNGMTLMFISMFI 78
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSslSFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  79 MMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLA 158
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1896069433 159 VRLTANMIAGHLLLTLLGN----SGAMIKLNLLSMVIIAQMLLMVLESGVALIQAYVFSILSTLYASET 223
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNylssSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDEH 229
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 3-222 3.52e-38

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 132.02  E-value: 3.52e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433   3 TNLFSTFDPSTSLFYysinwSSTIMGMFLMPSLFWI------LPSRNNLLWNKLTLKIhqeFKMLIGN---KYNGMTLMF 73
Cdd:MTH00035    5 NSIFGQFSPDTILFI-----PLTLLSSVIALSWLFFinptnwLPSRSQSIWLTFRQEI---LKLIFQNtnpNTAPWAGLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  74 ISMFIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIR 153
Cdd:MTH00035   77 TTVFILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQ 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896069433 154 PGTLAVRLTANMIAGHLLLTLLGNSGAMIKLNLL--SMVIIAQMLLMVLESGVALIQAYVFSILSTLYASE 222
Cdd:MTH00035  157 PIALGLRLAANLTAGHLLIFLLSTAIWELSNSPLisIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-222 9.33e-36

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 125.83  E-value: 9.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433   1 MMTNLFSTFDpSTSLFYYSINWSSTIMGMFLMPSL-FWILPSRNNLLWNKLTLKIHQEFKMLIGNKYNGMTLMFISMFIM 79
Cdd:MTH00179    1 MMLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLtNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  80 MMFNNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLAV 159
Cdd:MTH00179   80 LLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896069433 160 RLTANMIAGHLLLTLLGnSGAMIKLNLLSMVIIAQ----MLLMVLESGVALIQAYVFSILSTLYASE 222
Cdd:MTH00179  160 RLTANITAGHLLMHLIS-SAVFVLMNFMGMVALLTllvlFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-222 3.49e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 124.17  E-value: 3.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433   1 MMTNLFSTFDPSTSLFYysinwsSTIMGMFLMPSLFWILPSrNNLLWNKLTLKIHQEFKMLIGNKYNGMT-------LMF 73
Cdd:MTH00120    1 MNLNFFDQFSSPELLGI------PLILLAMLIPALLIPSPK-NRLLTNRLTTLQLWLIKLITKQLMLPLNkkghkwaLIL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  74 ISMFIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIR 153
Cdd:MTH00120   74 TSLMLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069433 154 PGTLAVRLTANMIAGHLLLTLLGNSG-----AMIKLNLLSMVIIaqMLLMVLESGVALIQAYVFSILSTLYASE 222
Cdd:MTH00120  154 PLALGVRLTANLTAGHLLIQLISTATlnllpTMPTLSLLTLIIL--LLLTILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-219 1.55e-33

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 120.06  E-value: 1.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433   1 MMTNLFSTFDPSTSLFYysinwsSTIMGMFLMPSLfwILPSRNNLLWNK-------LTLKIHQEFKMLIGNKYNGMTLMF 73
Cdd:MTH00101    1 MNENLFASFITPTILGL------PIVTLIIMFPSL--LFPTPNRLINNRlisiqqwLIQLTSKQMMTIHNTKGQTWSLML 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  74 ISMFIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIR 153
Cdd:MTH00101   73 MSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQ 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1896069433 154 PGTLAVRLTANMIAGHLLLTLLGNSG-AMIKLNLLSMVI--IAQMLLMVLESGVALIQAYVFSILSTLY 219
Cdd:MTH00101  153 PMALAVRLTANITAGHLLIHLIGGATlALMSISTTTALItfIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 84-222 3.20e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 116.51  E-value: 3.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  84 NFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLAVRLTA 163
Cdd:MTH00132   84 NMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTA 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896069433 164 NMIAGHLLLTLLGnSGAMIKLNLLSMVIIAQM----LLMVLESGVALIQAYVFSILSTLYASE 222
Cdd:MTH00132  164 NLTAGHLLIQLIA-TAAFVLLPLMPTVAILTAtllfLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 84-222 1.02e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 110.06  E-value: 1.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  84 NFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLAVRLTA 163
Cdd:MTH00073   84 NLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVRLTA 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896069433 164 NMIAGHLLLTLLgNSGAMIKLNLLSMVIIAQM----LLMVLESGVALIQAYVFSILSTLYASE 222
Cdd:MTH00073  164 NLTAGHLLIQLI-STATLVLLPLMPTVSILTMivlfLLTLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 84-224 3.33e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 103.93  E-value: 3.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  84 NFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLAVRLTA 163
Cdd:MTH00175   97 NILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAA 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896069433 164 NMIAGHLLLTLLGN------SGAMIKLNLLSMVIIaqMLLMVLESGVALIQAYVFSILSTLYASETY 224
Cdd:MTH00175  177 NISAGHLLFAILSGfafnmlSNGLIILSLFPMLIM--IFITLLEMAVAVIQAYVFCLLTTIYLGDTI 241
ATP-synt_A pfam00119
ATP synthase A chain;
83-219 3.19e-26

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 100.64  E-value: 3.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  83 NNFMGLF---PYIFTSTSHMVMTFSIALPMWVSFMLFG-WINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLA 158
Cdd:pfam00119  71 SNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLS 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069433 159 VRLTANMIAGHLLLTLLGNSGAMIKLNLLSMVII---AQMLLMVLESGVALIQAYVFSILSTLY 219
Cdd:pfam00119 151 LRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIpplLGVAWTLFELLVAFIQAYVFTMLTAVY 214
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 84-223 3.50e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 98.57  E-value: 3.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  84 NFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLAVRLTA 163
Cdd:MTH00172   86 NLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAA 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896069433 164 NMIAGHLLLTLLGNSGAMIK-----LNLLSMVIIAQMLLmvLESGVALIQAYVFSILSTLYASET 223
Cdd:MTH00172  166 NLSAGHLLFAILAGFGFNMLcasgfLSLFPLLIMVFITL--LEIAVAVIQAYVFCLLTTIYLADT 228
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 83-219 6.97e-24

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: 94.37  E-value: 6.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  83 NNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFG-WINNTKHMLAHLVPQGTPnLLMPFMVLIETISNIIRPGTLAVRL 161
Cdd:COG0356    71 SNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRL 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1896069433 162 TANMIAGHLLLTLLGNSGAMIKLNLLSmvIIAQMLLMVLESGVALIQAYVFSILSTLY 219
Cdd:COG0356   150 FGNMFAGHIILLLLAGLAPFLLLGVLS--LLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 84-219 6.91e-19

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 81.76  E-value: 6.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  84 NFMGLFP-YIFTSTSHMVMTFSIALPMWVSFMLFG-WINNTKHMLAHLVPQgtpnlLMPFMVLIETISNIIRPGTLAVRL 161
Cdd:PRK05815   87 NLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQ-----PHPLLLPIEIISEFSRPISLSLRL 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1896069433 162 TANMIAGHLLLTLLGNSGAMIKLNLLSMVIIAqMLLMVLESGVALIQAYVFSILSTLY 219
Cdd:PRK05815  162 FGNMLAGELILALIALLGGAGLLLALAPLILP-VAWTIFEIFVGTLQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 62-223 1.63e-15

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 73.05  E-value: 1.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  62 IGNKYNGMTLMFISMFIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPF 141
Cdd:MTH00174   83 LGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPL 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433 142 MVLIETISNIIRPGTLAVRLTANMIAGHLLLTLLGN-SGAMIKLNLLSMVIIAQMLLM---VLESGVALIQAYVFSILST 217
Cdd:MTH00174  163 LTIIETLSYISRAISLGVRLAANISSGHLLFSIIASfAWKMINTGILIGSFVPFAILIfvtILEMAVAIIQAYVFTLLTI 242


                  ....*.
gi 1896069433 218 LYASET 223
Cdd:MTH00174  243 VYLRDT 248
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 84-219 2.31e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 59.37  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  84 NFMGLFPYIFTSTSHMVMTFSIALPMWV-----SFMLFGwinnTKHMLAHLVpQGTPNLLMPFMVLIETISNIIRPGTLA 158
Cdd:PRK13419  185 NLLGLVPYGATATGNINVTLTLAVFTFFitqyaAIKAHG----IKGYLAHLT-GGTHWSLWIIMIPIEFIGLFTKPFALT 259

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069433 159 VRLTANMIAGHL-LLTLLGNSGAMiKLNLLSMVIIAQMLLMV--LESGVALIQAYVFSILSTLY 219
Cdd:PRK13419  260 VRLFANMTAGHIvILSLIFISFIL-KSYIVAVAVSVPFAIFIylLELFVAFLQAYIFTMLSALF 322
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 94-219 7.68e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 57.59  E-value: 7.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  94 TSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETI-SNIIRPGTLAVRLTANMIAGH-LL 171
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHvII 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1896069433 172 LTLLGNSGAMIKLNLLSMVIIAQMLLMVLESGVALIQAYVFSILSTLY 219
Cdd:PRK13417  297 LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 84-222 2.91e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 51.90  E-value: 2.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  84 NFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKhmLAHLVPQGTPNLLMPF-MVLIETISNIIRPGTLAVRLT 162
Cdd:MTH00087   66 CFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEK--FSVYLSKGSDSFLKTFsMLFVEIVSELSRPLALTLRLT 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433 163 ANMIAGHLLLTLLGNSGamiklnllSMVIIAQMLLMVLESGVALIQAYVFSILSTLYASE 222
Cdd:MTH00087  144 VNLMVGHLISSLLNFLG--------EKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 89-216 1.61e-06

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 46.42  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  89 FPYIFTSTSHMVMTFSIALPMWVSFMLFGWINNTKHMLAHLVPQGTPNLLMPFMVLIETISNIIRPGTLAVRLTANMIAG 168
Cdd:MTH00050   42 LPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLG 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1896069433 169 HLLLTLLGNsgamikLNLLSMVIIAQM-LLMVLESGVALIQAY-VFSILS 216
Cdd:MTH00050  122 CFGGVALGN------LCFISYWWFLVLfFLFFYEVFVALVHWFiVSSILS 165
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 38-219 5.76e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 39.73  E-value: 5.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433  38 ILPSRNNLLWNKLTLKIHQEFKMLIGNKYNGMTLMFISMFIMMMFNNFMGLFPYIFTSTSHMVMTFSIALPMWVSFMLFG 117
Cdd:PRK13420   43 LDPGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFVGTLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069433 118 -----WINNTKHMLahlvpqgTPN-LLMPFMVlietISNIIRPGTLAVRLTANM----IAGHLLLTLLGnsgamiklnll 187
Cdd:PRK13420  123 iraegLREYLKHYL-------SPSpFLLPFHL----ISEITRTLALAVRLFGNImsleLAALLVLLVAG----------- 180

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1896069433 188 SMVIIAQMLLMVLEsgvALIQAYVFSILSTLY 219
Cdd:PRK13420  181 FLVPVPILMLHIIE---ALVQAYIFGMLALIY 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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