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Conserved domains on  [gi|555946313|gb|AGZ19475|]
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ATP synthase F0 subunit 6 (mitochondrion) [Anas chathamica]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009577)

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 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 2.13e-107

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177190  Cd Length: 227  Bit Score: 308.34  E-value: 2.13e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   1 MNLSFFDQFSSPYLLGIPLILLSLLFPALLFPSP*NRWINNRLSTIQLWLLHLITKQLMIPLNKNGHKWALMLTSLMTML 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  81 LTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILIETTSLLIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 555946313 161 LTANLTAGHLLIQLISTASIALMP*LPAVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 2.13e-107

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 308.34  E-value: 2.13e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   1 MNLSFFDQFSSPYLLGIPLILLSLLFPALLFPSP*NRWINNRLSTIQLWLLHLITKQLMIPLNKNGHKWALMLTSLMTML 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  81 LTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILIETTSLLIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 555946313 161 LTANLTAGHLLIQLISTASIALMP*LPAVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 19-227 2.09e-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: 155.83  E-value: 2.09e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   19 LILLSLLFPALLFPSP*NRWINNRLSTIQLWLLHLITKQLMIPLNKNGHKWALMLTSLMTMLLTINLLGLLPYTFTPTTQ 98
Cdd:TIGR01131  20 LILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   99 LSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILIETTSLLIRPLALGVRLTANLTAGHLLIQLISTA 178
Cdd:TIGR01131 100 LSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 555946313  179 SIALMP*lPAVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:TIGR01131 180 LFSLMS--SAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-224 1.53e-36

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: 125.59  E-value: 1.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  66 GHKWALMLTSLMTMLLTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILI 145
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 555946313 146 ETTSLLIRPLALGVRLTANLTAGHLLIQLISTASIALMp*lPAVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLL---SSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
63-224 4.22e-30

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 111.04  E-value: 4.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   63 NKNGHKWALMLTSLMTMLL---TINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSAS-LAHLLPEGTPTPL 138
Cdd:pfam00119  51 KKKGRKFFPLLLTLFFFILvsnLLGLIPKSPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  139 IPALILIETTSLLIRPLALGVRLTANLTAGHLLIQLISTASIALMP*LPAVSILTMAILLLLTILEVAVAMIQAYVFVLL 218
Cdd:pfam00119 131 VPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTML 210


                  ....*.
gi 555946313  219 LSLYLQ 224
Cdd:pfam00119 211 TAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 49-225 4.68e-20

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: 84.35  E-value: 4.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  49 WLLHLITKQLMIPLNKNGHKWALMLTSLMTMLLTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNK-PSASLA 127
Cdd:COG0356   37 MLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLK 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313 128 HLLPEGTPtPLIPALILIETTSLLIRPLALGVRLTANLTAGHLLIqlistASIALMP*LPAVSILTMAILLLLTILEVAV 207
Cdd:COG0356  117 HLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIIL-----LLLAGLAPFLLLGVLSLLLPVAWTAFELLV 190

                        170
                 ....*....|....*...
gi 555946313 208 AMIQAYVFVLLLSLYLQE 225
Cdd:COG0356  191 GFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 2.13e-107

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 308.34  E-value: 2.13e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   1 MNLSFFDQFSSPYLLGIPLILLSLLFPALLFPSP*NRWINNRLSTIQLWLLHLITKQLMIPLNKNGHKWALMLTSLMTML 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  81 LTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILIETTSLLIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 555946313 161 LTANLTAGHLLIQLISTASIALMP*LPAVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-227 2.30e-107

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 308.29  E-value: 2.30e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   1 MNLSFFDQFSSPYLLGIPLILLSLLFPALLFPSP*NRWINNRLSTIQLWLLHLITKQLMIPLNKNGHKWALMLTSLMTML 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  81 LTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILIETTSLLIRPLALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 555946313 161 LTANLTAGHLLIQLISTASIALMP*LPAVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-227 2.03e-103

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 298.42  E-value: 2.03e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   1 MNLSFFDQFSSPYLLGIPLILLSLLFPALLFPSP*NRWINNRLSTIQLWLLHLITKQLMIPLNKNGHKWALMLTSLMTML 80
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  81 LTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILIETTSLLIRPLALGVR 160
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 555946313 161 LTANLTAGHLLIQLISTASIALMP*LPAVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-226 4.86e-82

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 244.09  E-value: 4.86e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   1 MNLSFFDQFSSPYLLGIPLILLSLLFPALLFPSP*NRWINNRLSTIQLWLLHLITKQLMIPLNKNGHKWALMLTSLMTML 80
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  81 LTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILIETTSLLIRPLALGVR 160
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 555946313 161 LTANLTAGHLLIQLISTASIALMP*LPAVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 4.55e-81

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 241.78  E-value: 4.55e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   1 MNLSFFDQFSSPYLLGIPLILLSLLFPALLFPSP*NRWINNRLSTIQLWLLHLITKQLMIPLNKNGHKWALMLTSLMTML 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTP-NRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  81 LTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILIETTSLLIRPLALGVR 160
Cdd:MTH00101  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 555946313 161 LTANLTAGHLLIQLISTASIALMP*LPAVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00101 160 LTANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-227 1.36e-47

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 156.29  E-value: 1.36e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   1 MNLSFFDQFSSPYLLGIPL-ILLSLLFPALLFPSP*NRWINNRLSTIQLWLLHLITKQLMIPLNKNGHKWALMLTSLMTM 79
Cdd:MTH00035   3 INNSIFGQFSPDTILFIPLtLLSSVIALSWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  80 LLTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILIETTSLLIRPLALGV 159
Cdd:MTH00035  83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 555946313 160 RLTANLTAGHLLIQLISTAsIALMP*LPAVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00035 163 RLAANLTAGHLLIFLLSTA-IWELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 19-227 2.09e-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: 155.83  E-value: 2.09e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   19 LILLSLLFPALLFPSP*NRWINNRLSTIQLWLLHLITKQLMIPLNKNGHKWALMLTSLMTMLLTINLLGLLPYTFTPTTQ 98
Cdd:TIGR01131  20 LILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   99 LSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILIETTSLLIRPLALGVRLTANLTAGHLLIQLISTA 178
Cdd:TIGR01131 100 LSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 555946313  179 SIALMP*lPAVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:TIGR01131 180 LFSLMS--SAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 39-225 1.78e-42

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 143.00  E-value: 1.78e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  39 INNRLSTIQLWLLHLITKQLMIPLNKNGHKWALMLTSLMTMLLTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGL 118
Cdd:MTH00157  38 IPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGW 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313 119 RNKPSASLAHLLPEGTPTPLIPALILIETTSLLIRPLALGVRLTANLTAGHLLIQLISTASIALMP*LPAVSILTMAILL 198
Cdd:MTH00157 118 INNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLL 197

                        170       180
                 ....*....|....*....|....*..
gi 555946313 199 lltILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00157 198 ---ILESAVAIIQSYVFSVLSTLYSSE 221
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 4-225 5.00e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 131.91  E-value: 5.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   4 SFFDQFSSPYLLGIPLILLSLLFPALLFPSP*nrWIN-NRLSTIQLWLLHLITKQLMIPLNKNGHKWALMLTSLMTMLLT 82
Cdd:MTH00173   7 SSFDDHNSSFSSLSFLMWLLSLMSLFFFSSSV--WVSsSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLIS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  83 INLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILIETTSLLIRPLALGVRLT 162
Cdd:MTH00173  85 LNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 555946313 163 ANLTAGHLLIQLISTASIALMP*LPAVSIL-TMAILLLLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00173 165 ANISAGHIVLTLIGNYLSSSLFSSSVVSLLlVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-224 1.53e-36

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: 125.59  E-value: 1.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  66 GHKWALMLTSLMTMLLTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILI 145
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 555946313 146 ETTSLLIRPLALGVRLTANLTAGHLLIQLISTASIALMp*lPAVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLL---SSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 6.68e-36

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 126.30  E-value: 6.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   1 MNLSFFDQFSSPYLLGIPLILLS-LLFPALLFPSP*NRWI-NNRLSTIQLWLLHLITKQLMIPLNKNGHKWALMLTSLMT 78
Cdd:MTH00176   1 MLVDLFSSFDPPNKNIFSMISLSwITLLLFLLLMPSSVWFcPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  79 MLLTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILIETTSLLIRPLALG 158
Cdd:MTH00176  81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 555946313 159 VRLTANLTAGHLLIQLISTASIALMP*LPAVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 40-222 1.90e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 120.22  E-value: 1.90e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  40 NNRLSTIQLWLLHLITKQLMIPLNKNGHKWALMLTSLMTMLLTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLR 119
Cdd:MTH00005  44 PNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVT 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313 120 NKPSASLAHLLPEGTPTPLIPALILIETTSLLIRPLALGVRLTANLTAGHLLIQLISTASIALMP*LPAVSILTMAILLL 199
Cdd:MTH00005 124 FSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGIYAASALFSSISSTILLILTQMG 203

                        170       180
                 ....*....|....*....|...
gi 555946313 200 LTILEVAVAMIQAYVFVLLLSLY 222
Cdd:MTH00005 204 YILFEVGICLIQAYIFCLLLSLY 226
ATP-synt_A pfam00119
ATP synthase A chain;
63-224 4.22e-30

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 111.04  E-value: 4.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   63 NKNGHKWALMLTSLMTMLL---TINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSAS-LAHLLPEGTPTPL 138
Cdd:pfam00119  51 KKKGRKFFPLLLTLFFFILvsnLLGLIPKSPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  139 IPALILIETTSLLIRPLALGVRLTANLTAGHLLIQLISTASIALMP*LPAVSILTMAILLLLTILEVAVAMIQAYVFVLL 218
Cdd:pfam00119 131 VPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTML 210


                  ....*.
gi 555946313  219 LSLYLQ 224
Cdd:pfam00119 211 TAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 1-227 1.35e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 110.13  E-value: 1.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   1 MNLSFFDQFSSPYLLGI--PLILLSLLFPALLFPSP*NRWINNRLSTIQLWL---LHLITKQlmiPLNKNGHKWALMLTS 75
Cdd:MTH00172   1 MSSSYFDQFNIVWLIGLtnSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIynhFHGVVKD---NLGNEGLKYFPFIIS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  76 LMTMLLTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILIETTSLLIRPL 155
Cdd:MTH00172  78 LFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAI 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 555946313 156 ALGVRLTANLTAGHLLIQLISTASIALMP*LPAVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00172 158 SLGVRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTI 229
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 1-227 3.15e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 104.32  E-value: 3.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313   1 MNLSFFDQFSSPYLLGIPL-------------ILLSLLFPALLFPSP*NRWINNRLSTIqLWLLHLITKQLMIP-LNKNG 66
Cdd:MTH00175   1 MLAAYFDQFNIIRLITIQAflgdwlvtftnssMMMVLAVIIFWLLLKGDKLIPNRWQSI-MELIYLNIRSVVHDnLGKSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  67 HKWALMLTSLMTMLLTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILIE 146
Cdd:MTH00175  80 QKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313 147 TTSLLIRPLALGVRLTANLTAGHLLIQLISTASI-ALMP*LPAVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00175 160 TLSYLIRAISLGVRLAANISAGHLLFAILSGFAFnMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239


                 ..
gi 555946313 226 NI 227
Cdd:MTH00175 240 TI 241
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 49-225 4.68e-20

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: 84.35  E-value: 4.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  49 WLLHLITKQLMIPLNKNGHKWALMLTSLMTMLLTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNK-PSASLA 127
Cdd:COG0356   37 MLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLK 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313 128 HLLPEGTPtPLIPALILIETTSLLIRPLALGVRLTANLTAGHLLIqlistASIALMP*LPAVSILTMAILLLLTILEVAV 207
Cdd:COG0356  117 HLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIIL-----LLLAGLAPFLLLGVLSLLLPVAWTAFELLV 190

                        170
                 ....*....|....*...
gi 555946313 208 AMIQAYVFVLLLSLYLQE 225
Cdd:COG0356  191 GFLQAYIFTMLTAVYISL 208
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 63-227 1.52e-19

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 84.22  E-value: 1.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  63 NKNGHKWALMLtSLMTMLLTINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPAL 142
Cdd:MTH00174  85 NKGGNYLAFVL-SLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLL 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313 143 ILIETTSLLIRPLALGVRLTANLTAGHLLIQLISTASIALMP*LPAV-SILTMAILLLLTILEVAVAMIQAYVFVLLLSL 221
Cdd:MTH00174 164 TIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPFAILIFVTILEMAVAIIQAYVFTLLTIV 243


                 ....*.
gi 555946313 222 YLQENI 227
Cdd:MTH00174 244 YLRDTV 249
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 91-225 2.57e-17

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 77.53  E-value: 2.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  91 YTFTPTTQLSMNMALAFPLWLATLLTGLRNKpsaSLAHLLPEGTPTPlIPALILIETTSLLIRPLALGVRLTANLTAGHL 170
Cdd:PRK05815  95 LLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGEL 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 555946313 171 LIQLISTASIALMP*LPAVSILTMAilllLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:PRK05815 171 ILALIALLGGAGLLLALAPLILPVA----WTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 90-225 4.14e-12

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 62.69  E-value: 4.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNkpSASLAHLLPEGTPTPLIP-ALILIETTSLLIRPLALGVRLTANLTAG 168
Cdd:MTH00087  72 PYSFSPCGMVEFTFLYALVAWLSTFLSFLSK--SEKFSVYLSKGSDSFLKTfSMLFVEIVSELSRPLALTLRLTVNLMVG 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 555946313 169 HLLIQLISTasialmp*lpaVSILTMAILLLLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00087 150 HLISSLLNF-----------LGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 90-223 2.12e-11

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 62.45  E-value: 2.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  90 PYTFTPTTQLSMNMALAFPLWLATLLTGLR-NKPSASLAHLlPEGTPTPLIPALILIETTSLLIRPLALGVRLTANLTAG 168
Cdd:PRK13419 191 PYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAHL-TGGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAG 269

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 555946313 169 HLLI-QLISTASIALMP*LPAVSILTMAILLLLtiLEVAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13419 270 HIVIlSLIFISFILKSYIVAVAVSVPFAIFIYL--LELFVAFLQAYIFTMLSALFI 323
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 94-223 6.81e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 57.98  E-value: 6.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555946313  94 TPTTQLSMNMALAFPLWLATLLTGLRNKPSASLAHLLPEGTPTPLIPALILIE-TTSLLIRPLALGVRLTANLTAGHLLI 172
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEfIVSPMAKTFALTVRLLANMTAGHVII 296

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 555946313 173 qlisTASIALMP*LPAVSILTMAIL--LLLTILEVAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13417 297 ----LALMGFIFQFQSWGIVPVSVIgsGLIYVLEIFVAFLQAYIFVLLTSLFV 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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