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Conserved domains on  [gi|671759929|gb|AII98551|]
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ATP synthase F0 subunit 6 (mitochondrion) [Eulemur rubriventer]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009564)

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 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.32e-130

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 366.97  E-value: 1.32e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929   1 MNENLFASFITPTIVGIPIVIFIIMIPSILFPSPTRLINNRLTSLQQWLIQLILKQLMLIHNIKGRTWSLMLISLILFIG 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 671759929 161 TANITAGHLLMHLIGGATLVLSSISPATASITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.32e-130

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 366.97  E-value: 1.32e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929   1 MNENLFASFITPTIVGIPIVIFIIMIPSILFPSPTRLINNRLTSLQQWLIQLILKQLMLIHNIKGRTWSLMLISLILFIG 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 671759929 161 TANITAGHLLMHLIGGATLVLSSISPATASITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 29-225 5.82e-53

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


Pssm-ID: 273458  Cd Length: 226  Bit Score: 170.08  E-value: 5.82e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929   29 ILFPSPTRLINNRLTSLQQWLIQLILKQLMLIHNIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL 108
Cdd:TIGR01131  31 ISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  109 WAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGatLVLSSISPAT 188
Cdd:TIGR01131 111 WLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSG--LLFSLMSSAI 188

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 671759929  189 ASITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 189 FALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 7.44e-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: 136.76  E-value: 7.44e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  65 GRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVII 144
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 671759929 145 ETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLSSISpatASITFIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSV---GLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
35-223 2.31e-37

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 129.53  E-value: 2.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929   35 TRLINNRLTSLQQWLIQLILKQLM-LIHNIKGRTWSLMLISLILFIGSTNLLGLL---PHSFTPTTQLSMNLGMAIPLWA 110
Cdd:pfam00119  23 KKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  111 AAVIKGFR-HKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLSSISPATA 189
Cdd:pfam00119 103 LVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLG 182

                         170       180       190
                  ....*....|....*....|....*....|....
gi 671759929  190 SITFIILILLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 183 VIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 64-224 4.71e-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: 95.14  E-value: 4.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  64 KGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFRHK-TKTSLAHFLPQGTPiPLIPMLV 142
Cdd:COG0356   53 KGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLML 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929 143 IIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLSSispatASITFIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:COG0356  132 PIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206


                 ..
gi 671759929 223 HD 224
Cdd:COG0356  207 SL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.32e-130

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 366.97  E-value: 1.32e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929   1 MNENLFASFITPTIVGIPIVIFIIMIPSILFPSPTRLINNRLTSLQQWLIQLILKQLMLIHNIKGRTWSLMLISLILFIG 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 671759929 161 TANITAGHLLMHLIGGATLVLSSISPATASITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-226 1.10e-83

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 248.20  E-value: 1.10e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929   1 MNENLFASFITPTIVGIPIVIFIIMIPSILFPSPT-RLINNRLTSLQQWLIQLILKQLMLIHNIKGRTWSLMLISLILFI 79
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKnRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 671759929 160 LTANITAGHLLMHLIGGATLVLSSISPATASITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-226 1.37e-80

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 240.25  E-value: 1.37e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929   1 MNENLFASFITPTIVGIPIVIFIIMIPSILFPSPT-RLINNRLTSLQQWLIQLILKQLMLIHNIKGRTWSLMLISLILFI 79
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTnKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 671759929 160 LTANITAGHLLMHLIGGATLVLSSISPATASITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-225 4.64e-79

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 236.69  E-value: 4.64e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929   1 MNENLFASFITPTIVGIPIVIFIIMIPSILFPSPT-RLINNRLTSLQQWLIQLILKQLMLIHNIKGRTWSLMLISLILFI 79
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTsRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 671759929 160 LTANITAGHLLMHLIGGATLVLSSISPATASITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-226 1.32e-69

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 212.50  E-value: 1.32e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929   1 MNENLFASFITPTIVGIPIVIFIIMIPSILFPSPT-RLINNRLTSLQQWLIQLILKQLMLIHNIKGRTWSLMLISLILFI 79
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTnRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 671759929 160 LTANITAGHLLMHLIGGATLVLSSISPATASITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 29-225 5.82e-53

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


Pssm-ID: 273458  Cd Length: 226  Bit Score: 170.08  E-value: 5.82e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929   29 ILFPSPTRLINNRLTSLQQWLIQLILKQLMLIHNIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL 108
Cdd:TIGR01131  31 ISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  109 WAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGatLVLSSISPAT 188
Cdd:TIGR01131 111 WLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSG--LLFSLMSSAI 188

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 671759929  189 ASITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 189 FALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-221 5.69e-46

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 151.86  E-value: 5.69e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929   1 MNENLFASFITPTIVGIPIVIFIIMIPSILFPSPTRLINNRLTSLQQWLIQLILKQLMLIHNIKGRTWSLMLISLILFIG 80
Cdd:MTH00157   1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00157  81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 671759929 161 TANITAGHLLMHLIGGATLVLSSIspaTASITFIILILLTILEFAVALIQAYVFTLLVSLY 221
Cdd:MTH00157 161 AANMIAGHLLLTLLGNTGPSLSSM---ILSILILIQILLLILESAVAIIQSYVFSVLSTLY 218
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 29-225 7.41e-45

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 149.35  E-value: 7.41e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  29 ILFPSPTRLINNRLTSLQQWLIQLILKQLMLIHNIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL 108
Cdd:MTH00035  33 LFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILILSINVLGLFPYAFTSTSHISLTYSLGIPL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929 109 WAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLSSiSPAT 188
Cdd:MTH00035 113 WMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRLAANLTAGHLLIFLLSTAIWELSN-SPLI 191

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 671759929 189 ASITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00035 192 SIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 7.44e-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: 136.76  E-value: 7.44e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  65 GRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVII 144
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 671759929 145 ETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLSSISpatASITFIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSV---GLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 29-224 2.36e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 135.38  E-value: 2.36e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  29 ILFPSPTRLINNRLTSLQQWLIQLILKQLMLIHNIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL 108
Cdd:MTH00173  32 FFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSLALPL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929 109 WAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLSSISPAT 188
Cdd:MTH00173 112 WLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYLSSSLFSSSVV 191

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 671759929 189 ASITFIILILL-TILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00173 192 SLLLVLLIQVGyFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 1.62e-37

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 130.54  E-value: 1.62e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929   1 MNENLFASFITPTIV---GIPIVIFIIMIPSILFPSPTRLINNRLTSLQQWLIQLILKQLMLIHNIKGRTWSLMLISLIL 77
Cdd:MTH00176   1 MLVDLFSSFDPPNKNifsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  78 FIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALA 157
Cdd:MTH00176  81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 671759929 158 VRLTANITAGHLLMHLIGGATLVLSSISPATASITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP-synt_A pfam00119
ATP synthase A chain;
35-223 2.31e-37

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 129.53  E-value: 2.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929   35 TRLINNRLTSLQQWLIQLILKQLM-LIHNIKGRTWSLMLISLILFIGSTNLLGLL---PHSFTPTTQLSMNLGMAIPLWA 110
Cdd:pfam00119  23 KKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  111 AAVIKGFR-HKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLSSISPATA 189
Cdd:pfam00119 103 LVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLG 182

                         170       180       190
                  ....*....|....*....|....*....|....
gi 671759929  190 SITFIILILLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 183 VIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 39-226 9.47e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 112.90  E-value: 9.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  39 NNRLTSLQQWLIQLILKQLMLIHNIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFR 118
Cdd:MTH00005  44 PNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVT 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929 119 HKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLSSISPATASITFIILIL 198
Cdd:MTH00005 124 FSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGIYAASALFSSISSTILLILTQMG 203

                        170       180
                 ....*....|....*....|....*...
gi 671759929 199 LTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00005 204 YILFEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 29-224 6.05e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 105.89  E-value: 6.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  29 ILFPSPTRLINNRLTSLQQWLIQLILKQLMLIHNIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL 108
Cdd:MTH00172  32 LLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSI 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929 109 WAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLSSISPAT 188
Cdd:MTH00172 112 IIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNMLCASGFL 191

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 671759929 189 ASITFIILILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00172 192 SLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 36-224 1.18e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 102.78  E-value: 1.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  36 RLINNRLTSLQQwLIQLILKQLMLIH-NIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVI 114
Cdd:MTH00175  50 KLIPNRWQSIME-LIYLNIRSVVHDNlGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929 115 KGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATL-VLSSISPATASITF 193
Cdd:MTH00175 129 LGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFnMLSNGLIILSLFPM 208

                        170       180       190
                 ....*....|....*....|....*....|.
gi 671759929 194 IILILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00175 209 LIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 64-224 4.71e-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: 95.14  E-value: 4.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  64 KGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFRHK-TKTSLAHFLPQGTPiPLIPMLV 142
Cdd:COG0356   53 KGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLML 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929 143 IIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLSSispatASITFIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:COG0356  132 PIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206


                 ..
gi 671759929 223 HD 224
Cdd:COG0356  207 SL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 35-224 3.80e-20

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 84.85  E-value: 3.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  35 TRLINNRLTSLQQWLIQLILKQLMLIHNIKGRTWSLMLISLILFIGSTNLLGLLP-HSFTPTTQLSMNLGMAIPLWAAAV 113
Cdd:PRK05815  39 LSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVI 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929 114 IKGFRHKtktSLAHFLPQGTPIPlIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGatlvLSSISPATASITF 193
Cdd:PRK05815 119 YYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGELILALIAL----LGGAGLLLALAPL 190

                        170       180       190
                 ....*....|....*....|....*....|.
gi 671759929 194 IILILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:PRK05815 191 ILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 64-224 5.03e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 77.29  E-value: 5.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  64 KGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVI 143
Cdd:MTH00174  86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929 144 IETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLSSISPATASIT-FIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00174 166 IETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSFVpFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245


                 ..
gi 671759929 223 HD 224
Cdd:MTH00174 246 RD 247
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 72-222 1.20e-15

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 74.39  E-value: 1.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  72 LISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFR-HKTKTSLAHfLPQGTPIPLIPMLVIIETISLF 150
Cdd:PRK13419 174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAH-LTGGTHWSLWIIMIPIEFIGLF 252

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 671759929 151 IQPMALAVRLTANITAGHLLMHLIGGATLVLSSISPATAsITFIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13419 253 TKPFALTVRLFANMTAGHIVILSLIFISFILKSYIVAVA-VSVPFAIFIYLLELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 71-222 3.66e-10

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 57.30  E-value: 3.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  71 MLISLILFigstNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVIKGFRHKTKTSlaHFLPQGTPIPLIPM-LVIIETISL 149
Cdd:MTH00087  58 TFIVLLLF----CFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTFsMLFVEIVSE 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 671759929 150 FIQPMALAVRLTANITAGHLLMHLIGGATLVLSSISpatasitfiilILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00087 132 LSRPLALTLRLTVNLMVGHLISSLLNFLGEKYVWLS-----------ILAIMMECFVAFIQSYIFSRLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 93-222 2.30e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 53.36  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671759929  93 TPTTQLSMNLGMAIPLWAAAVIKGFRHKTKTSLAHFLPQGTPIPLIPMLVIIETI-SLFIQPMALAVRLTANITAGHLLM 171
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 671759929 172 HLIGGatLVLSSISPATASITFIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13417 297 LALMG--FIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
 
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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