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Conserved domains on  [gi|1812385333|gb|QID48462|]
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ATP synthase F0 subunit 6 [Systolederus spicupennis]

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
 1-222 3.77e-87

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 256.63  E-value: 3.77e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333   1 MMTNLFSSFDPSTNYFMSMNWLSMIIFMLIIPSTFWMNNSRSNILSKMMNMKLFQEF-NILMNNTKGGEMIFIATFTIIM 79
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFkTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  80 CYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIRPGTLAIRL 159
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1812385333 160 TANMIAGHLLLTLMGNSGNKIHEILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLYSSEIN 222
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-222 3.77e-87

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 256.63  E-value: 3.77e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333   1 MMTNLFSSFDPSTNYFMSMNWLSMIIFMLIIPSTFWMNNSRSNILSKMMNMKLFQEF-NILMNNTKGGEMIFIATFTIIM 79
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFkTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  80 CYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIRPGTLAIRL 159
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1812385333 160 TANMIAGHLLLTLMGNSGNKIHEILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLYSSEIN 222
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-222 1.01e-42

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: 143.50  E-value: 1.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333   5 LFSSFDPSTNYFMSMNWLSMIIFMLIIPSTFWMNNSRSNILSKMMNMK---LFQEFNILMNNTKGGEMIFIATFTIIMCY 81
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLSLILLLSLLIFLISSSLSRWLIPSRWQNLMesiYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  82 ----NFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIRPGTLAI 157
Cdd:TIGR01131  81 ilisNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1812385333 158 RLTANMIAGHLLLTLMGNSGNKIHEILLMSMLLMQMALLML-ESAVAIIQGYVFSVLMTLYSSEIN 222
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIFALLLLILVALIIlEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 70-219 2.22e-39

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: 132.91  E-value: 2.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  70 IFIATFTIIMCYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSL 149
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333 150 IRPGTLAIRLTANMIAGHLLLTLMGNSGNKIHEILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLYSS 219
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
75-219 3.81e-23

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 92.55  E-value: 3.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  75 FTIIMCYNFMGLF---PYIFTSTSHMAMTLSLALPMWLGINLFGWIKK--TNHMFEHLVPlGTPKLLMPFMVCIETISSL 149
Cdd:pfam00119  65 FFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIKKHglGGYFKKLFVP-PVPLPLVPLLLPIEIISEF 143

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1812385333 150 IRPGTLAIRLTANMIAGHLLLTLMGNSGNKIHEILLMSMLLMQMALLML---ESAVAIIQGYVFSVLMTLYSS 219
Cdd:pfam00119 144 ARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWtlfELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 71-217 4.25e-17

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: 76.27  E-value: 4.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  71 FIAT-FTIIMCYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFG-WIKKTNHMFEHLVpLGTPKLLMPFMVCIETISS 148
Cdd:COG0356    60 LLLTlFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLF-FPPFPWLAPLMLPIEIISE 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1812385333 149 LIRPGTLAIRLTANMIAGHLLLTLMGNSGNKIheILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLY 217
Cdd:COG0356   139 LARPLSLSLRLFGNMFAGHIILLLLAGLAPFL--LLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-222 3.77e-87

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 256.63  E-value: 3.77e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333   1 MMTNLFSSFDPSTNYFMSMNWLSMIIFMLIIPSTFWMNNSRSNILSKMMNMKLFQEF-NILMNNTKGGEMIFIATFTIIM 79
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFkTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  80 CYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIRPGTLAIRL 159
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1812385333 160 TANMIAGHLLLTLMGNSGNKIHEILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLYSSEIN 222
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-220 2.60e-46

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 152.88  E-value: 2.60e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333   1 MMTNLFSSFDPSTNY---FMSMNWLSMIIFMLIIPSTFWMNNSRSNILSKMMNMKLFQEFNILMNNTKGG-EMIFIATFT 76
Cdd:MTH00176    1 MLVDLFSSFDPPNKNifsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGsASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  77 IIMCYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIRPGTLA 156
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1812385333 157 IRLTANMIAGHLLLTLMGNSGNK---IHEILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLYSSE 220
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGllpVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDE 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-222 1.01e-42

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: 143.50  E-value: 1.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333   5 LFSSFDPSTNYFMSMNWLSMIIFMLIIPSTFWMNNSRSNILSKMMNMK---LFQEFNILMNNTKGGEMIFIATFTIIMCY 81
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLSLILLLSLLIFLISSSLSRWLIPSRWQNLMesiYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  82 ----NFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIRPGTLAI 157
Cdd:TIGR01131  81 ilisNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1812385333 158 RLTANMIAGHLLLTLMGNSGNKIHEILLMSMLLMQMALLML-ESAVAIIQGYVFSVLMTLYSSEIN 222
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIFALLLLILVALIIlEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-221 1.42e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 135.76  E-value: 1.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333   1 MMTNLFSSFDPSTNYFMSMN---WLSMIIFMLIIPSTFWMNNSRSNILSKMMNMKLFQEFNILMNNTKGGEMIFIAT-FT 76
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSSLSflmWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSlFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  77 IIMCYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIRPGTLA 156
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1812385333 157 IRLTANMIAGHLLLTLMGNSGNK----IHEILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLYSSEI 221
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYLSSslfsSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDEH 229
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 70-219 2.22e-39

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: 132.91  E-value: 2.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  70 IFIATFTIIMCYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSL 149
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333 150 IRPGTLAIRLTANMIAGHLLLTLMGNSGNKIHEILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLYSS 219
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-220 1.25e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 133.15  E-value: 1.25e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333   1 MMTNLFSSFDPSTNYFMSMNWLSMIIFMLIIPSTF--WMNNSRSNILSKMMNMKLFQEFNILMNNTKGGEMIFIATFTII 78
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTnrWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  79 MCYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIRPGTLAIR 158
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812385333 159 LTANMIAGHLLLTLMGN---SGNKIHEILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLYSSE 220
Cdd:MTH00179  161 LTANITAGHLLMHLISSavfVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-220 5.95e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 131.78  E-value: 5.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333   1 MMTNLFSSFDPSTNYFM-----SMNWLSMIIFMLIIPSTFWMNNSR-SNILSKMMNMKLFQEFNILMNNTKGGEMIFIAT 74
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFnnlssTAFWAFNFSIILLLSSSFWITPNRlSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  75 FTIIMCYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIRPGT 154
Cdd:MTH00005   81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1812385333 155 LAIRLTANMIAGHLLLTLMG---NSGNKIHEILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLYSSE 220
Cdd:MTH00005  161 LSFRLAANMSAGHIVLSLIGiyaASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-220 7.59e-37

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 128.40  E-value: 7.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333   1 MMTNLFSSFDPSTNYFMSMNWLSMIIFMLIIPST--FWMNNSRSNILSKMMNMKLFQEFNILMNNTKGGEMIFIATFTII 78
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPknRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  79 MCYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIRPGTLAIR 158
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812385333 159 LTANMIAGHLLLTLMGNSGN---KIHEILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLYSSE 220
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLnllPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 3-220 9.04e-37

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 128.55  E-value: 9.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333   3 TNLFSSFDPSTNYFMSMNWLSMII---FMLIIPSTFWMNNSRSNILSKMMNMKLFQEFNILMNNTKGGEMIFIATFTIIM 79
Cdd:MTH00035    5 NSIFGQFSPDTILFIPLTLLSSVIalsWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  80 CYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIRPGTLAIRL 159
Cdd:MTH00035   85 SINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1812385333 160 TANMIAGHLLLTLMGNSgnkIHEILLMSMLLMQMALLML-----ESAVAIIQGYVFSVLMTLYSSE 220
Cdd:MTH00035  165 AANLTAGHLLIFLLSTA---IWELSNSPLISIITLIIFFllfilEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-220 5.37e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 116.22  E-value: 5.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333   1 MMTNLFSSFDPSTNYFMSMNWLSMIIFMLII--PSTFWMNNSRSNILSKMMNMKLFQEFNILMNNTKGGEMIFIATFTII 78
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFptPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  79 MCYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIRPGTLAIR 158
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812385333 159 LTANMIAGHLLLTLMGNSGNKIHEILLMSMLLMQMALL---MLESAVAIIQGYVFSVLMTLYSSE 220
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFlltLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-217 7.87e-31

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 113.12  E-value: 7.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333   1 MMTNLFSSFDPSTnyFMSMNWLSMIIF---MLIIPSTFWMNNSRSNILSKMMNMKLFQEfnILMNNTKGG--EMIFIATF 75
Cdd:MTH00101    1 MNENLFASFITPT--ILGLPIVTLIIMfpsLLFPTPNRLINNRLISIQQWLIQLTSKQM--MTIHNTKGQtwSLMLMSLI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  76 TIIMCYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIRPGTL 155
Cdd:MTH00101   77 LFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMAL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812385333 156 AIRLTANMIAGHLLLTLMGNSG---NKIHEILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLY 217
Cdd:MTH00101  157 AVRLTANITAGHLLIHLIGGATlalMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 32-220 6.77e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 108.04  E-value: 6.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  32 PSTFWMNNSRSNILSKMMNMKLFQefnILMNNTKGGE---MIFIATFTIIMCYNFMGLFPYIFTSTSHMAMTLSLALPMW 108
Cdd:MTH00132   34 PTSRWLNNRLLTLQGWFINRFTQQ---LLLPLNVGGHkwaLLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLW 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333 109 LGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIRPGTLAIRLTANMIAGHLLLTLMGNSGNKIHEIL---L 185
Cdd:MTH00132  111 LATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAAFVLLPLMptvA 190

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1812385333 186 MSMLLMQMALLMLESAVAIIQGYVFSVLMTLYSSE 220
Cdd:MTH00132  191 ILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP-synt_A pfam00119
ATP synthase A chain;
75-219 3.81e-23

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 92.55  E-value: 3.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  75 FTIIMCYNFMGLF---PYIFTSTSHMAMTLSLALPMWLGINLFGWIKK--TNHMFEHLVPlGTPKLLMPFMVCIETISSL 149
Cdd:pfam00119  65 FFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIKKHglGGYFKKLFVP-PVPLPLVPLLLPIEIISEF 143

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1812385333 150 IRPGTLAIRLTANMIAGHLLLTLMGNSGNKIHEILLMSMLLMQMALLML---ESAVAIIQGYVFSVLMTLYSS 219
Cdd:pfam00119 144 ARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWtlfELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 72-217 4.25e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 87.40  E-value: 4.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  72 IATFTIIMCYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIR 151
Cdd:MTH00172   76 ISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISR 155

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1812385333 152 PGTLAIRLTANMIAGHLLLTLMGNSGNKI---HEILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLY 217
Cdd:MTH00172  156 AISLGVRLAANLSAGHLLFAILAGFGFNMlcaSGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIY 224
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 75-217 2.78e-20

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 85.83  E-value: 2.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  75 FTIIMCYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIRPGT 154
Cdd:MTH00175   90 FLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAIS 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1812385333 155 LAIRLTANMIAGHLLLTLM-GNSGNKIHE---ILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLY 217
Cdd:MTH00175  170 LGVRLAANISAGHLLFAILsGFAFNMLSNgliILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIY 236
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 71-217 4.25e-17

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: 76.27  E-value: 4.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  71 FIAT-FTIIMCYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFG-WIKKTNHMFEHLVpLGTPKLLMPFMVCIETISS 148
Cdd:COG0356    60 LLLTlFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLF-FPPFPWLAPLMLPIEIISE 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1812385333 149 LIRPGTLAIRLTANMIAGHLLLTLMGNSGNKIheILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLY 217
Cdd:COG0356   139 LARPLSLSLRLFGNMFAGHIILLLLAGLAPFL--LLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 72-217 2.18e-15

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 72.66  E-value: 2.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  72 IATFTIIMCYNFMGLFPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIR 151
Cdd:MTH00174   95 LSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISR 174

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333 152 PGTLAIRLTANMIAGHLLLTLMGNSGNKIHE----ILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLY 217
Cdd:MTH00174  175 AISLGVRLAANISSGHLLFSIIASFAWKMINtgilIGSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVY 244
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 75-217 2.10e-14

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 69.44  E-value: 2.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  75 FTIIMCYNFMGLFP-YIFTSTSHMAMTLSLALPMWLGINLFG-WIKKTNHMFEHLVPLgtpklLMPFMVCIETISSLIRP 152
Cdd:PRK05815   80 FLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQ-----PHPLLLPIEIISEFSRP 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812385333 153 GTLAIRLTANMIAGHLLLTLMGNSGNkIHEILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLY 217
Cdd:PRK05815  155 ISLSLRLFGNMLAGELILALIALLGG-AGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVY 218
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 75-217 7.76e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 54.75  E-value: 7.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  75 FTIIMCYNFMGLFPYIFTSTSHMAMTLSLALPMWLgINLFGWIKK--TNHMFEHLVPlGTPKLLMPFMVCIETISSLIRP 152
Cdd:PRK13419  178 FFFILVCNLLGLVPYGATATGNINVTLTLAVFTFF-ITQYAAIKAhgIKGYLAHLTG-GTHWSLWIIMIPIEFIGLFTKP 255

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1812385333 153 GTLAIRLTANMIAGHL-LLTLMGNS-GNKIHEILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLY 217
Cdd:PRK13419  256 FALTVRLFANMTAGHIvILSLIFISfILKSYIVAVAVSVPFAIFIYLLELFVAFLQAYIFTMLSALF 322
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 22-220 8.31e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 50.75  E-value: 8.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  22 LSMIIFMLIIPSTFWMNNSRSNILSKMMNMKLFQEFNILMNNTKGGEMIFIATFTIIMCyNFMGLFPYIFTSTSHMAMTL 101
Cdd:MTH00087    7 LDVFMFVFLLQYLLYFKESMLNVLVKKFFGLLIIVFSYSNKLPLSSVISFFTFIVLLLF-CFGGLFPYSFSPCGMVEFTF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333 102 SLALPMWLGINLFGWIKKTnhMFEHLVPLGTPKLLMPF-MVCIETISSLIRPGTLAIRLTANMIAGHLLLTLMGNSGNKi 180
Cdd:MTH00087   86 LYALVAWLSTFLSFLSKSE--KFSVYLSKGSDSFLKTFsMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLLNFLGEK- 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1812385333 181 heillmsMLLMQMALLMLESAVAIIQGYVFSVLMTLYSSE 220
Cdd:MTH00087  163 -------YVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 92-217 1.58e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 47.96  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  92 TSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETI-SSLIRPGTLAIRLTANMIAGH-LL 169
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHvII 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1812385333 170 LTLMGNSGNKIHEILLMSMLLMQMALLMLESAVAIIQGYVFSVLMTLY 217
Cdd:PRK13417  297 LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 87-166 2.97e-04

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 39.87  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385333  87 FPYIFTSTSHMAMTLSLALPMWLGINLFGWIKKTNHMFEHLVPLGTPKLLMPFMVCIETISSLIRPGTLAIRLTANMIAG 166
Cdd:MTH00050   42 LPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLG 121
 
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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