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Conserved domains on  [gi|803360374|gb|AKA97964|]
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ATPase subunit 6 (mitochondrion) [Dendrocopos assimilis]

Protein Classification

FoF1 ATP synthase subunit a( domain architecture ID 116)

FoF1 ATP synthase subunit a is part of the membrane proton channel (Fo complex) of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane; it plays a direct role in the translocation of protons across the membrane

Gene Ontology:  GO:0045263|GO:0015078|GO:0015986
PubMed:  11533110|12370007|30901262

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP-synt_Fo_a_6 super family cl00413
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 1-227 5.87e-46

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.


The actual alignment was detected with superfamily member MTH00073:

Pssm-ID: 469762  Cd Length: 227  Bit Score: 152.04  E-value: 5.87e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803360374   1 MNLSFFDQFTSPCLLGIPLILLSMLFPALLLPSPGSRWITNRLSTLQSWCIDLITKQLMTPLNKNGHKWALILTSLMILL 80
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803360374  81 LSINLLGLLPYT******************************************************************** 160
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 803360374 161 ***NLTAGHLLIQLISTASTALLTIMPAVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
 
Name Accession Description Interval E-value
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-227 5.87e-46

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 152.04  E-value: 5.87e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803360374   1 MNLSFFDQFTSPCLLGIPLILLSMLFPALLLPSPGSRWITNRLSTLQSWCIDLITKQLMTPLNKNGHKWALILTSLMILL 80
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803360374  81 LSINLLGLLPYT******************************************************************** 160
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 803360374 161 ***NLTAGHLLIQLISTASTALLTIMPAVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 164-227 4.59e-07

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: 48.74  E-value: 4.59e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 803360374  164 NLTAGHLLIQLISTASTALltIMPAVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:TIGR01131 165 NISAGHLLLTLLSGLLFSL--MSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_A pfam00119
ATP synthase A chain;
164-224 6.86e-07

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 48.25  E-value: 6.86e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 803360374  164 NLTAGHLLIQLISTASTALLTIMPAVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 156 NMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 164-224 3.14e-05

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: 42.77  E-value: 3.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 803360374 164 NLTAGHLLIQLISTASTALLTImpaVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310   99 NMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
 
Name Accession Description Interval E-value
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-227 5.87e-46

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 152.04  E-value: 5.87e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803360374   1 MNLSFFDQFTSPCLLGIPLILLSMLFPALLLPSPGSRWITNRLSTLQSWCIDLITKQLMTPLNKNGHKWALILTSLMILL 80
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803360374  81 LSINLLGLLPYT******************************************************************** 160
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 803360374 161 ***NLTAGHLLIQLISTASTALLTIMPAVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-227 4.29e-45

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 149.97  E-value: 4.29e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803360374   1 MNLSFFDQFTSPCLLGIPLILLSMLFPALLLPSPGSRWITNRLSTLQSWCIDLITKQLMTPLNKNGHKWALILTSLMILL 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803360374  81 LSINLLGLLPYT******************************************************************** 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 803360374 161 ***NLTAGHLLIQLISTASTALLTIMPAVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 1.88e-44

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 148.48  E-value: 1.88e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803360374   1 MNLSFFDQFTSPCLLGIPLILLSMLFPALLLPSPGSRWITNRLSTLQSWCIDLITKQLMTPLNKNGHKWALILTSLMILL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803360374  81 LSINLLGLLPYT******************************************************************** 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 803360374 161 ***NLTAGHLLIQLISTASTALLTIMPAVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-226 1.56e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 117.74  E-value: 1.56e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803360374   1 MNLSFFDQFTSPCLLGIPLILLSMLFPALLLPSPGSRWITNRLSTLQSWCIDLITKQLMTPLNKNGHKWALILTSLMILL 80
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803360374  81 LSINLLGLLPYT******************************************************************** 160
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 803360374 161 ***NLTAGHLLIQLISTASTALLTIMPAVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.49e-25

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 99.26  E-value: 1.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803360374   1 MNLSFFDQFTSPCLLGIPLILLSMLFPALLLPSPgSRWITNRLSTLQSWCIDLITKQLMTPLNKNGHKWALILTSLMILL 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTP-NRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 803360374  81 LSINLLGLLPYT******************************************************************** 160
Cdd:MTH00101  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 803360374 161 ***NLTAGHLLIQLISTASTALLTIMPAVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00101 160 LTANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 164-227 6.20e-08

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 51.51  E-value: 6.20e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 803360374 164 NLTAGHLLIQLISTAsTALLTIMPAVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00035 167 NLTAGHLLIFLLSTA-IWELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 164-226 3.96e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 49.26  E-value: 3.96e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 803360374 164 NLTAGHLLIQLISTASTALLTIMPAVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00176 166 NLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 164-227 4.59e-07

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: 48.74  E-value: 4.59e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 803360374  164 NLTAGHLLIQLISTASTALltIMPAVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:TIGR01131 165 NISAGHLLLTLLSGLLFSL--MSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_A pfam00119
ATP synthase A chain;
164-224 6.86e-07

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 48.25  E-value: 6.86e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 803360374  164 NLTAGHLLIQLISTASTALLTIMPAVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 156 NMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 164-225 2.27e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 46.70  E-value: 2.27e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 803360374 164 NLTAGHLLIQLISTASTALLTIMpavSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00157 163 NMIAGHLLLTLLGNTGPSLSSMI---LSILILIQILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 164-224 3.14e-05

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: 42.77  E-value: 3.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 803360374 164 NLTAGHLLIQLISTASTALLTImpaVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310   99 NMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 164-227 5.38e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 42.72  E-value: 5.38e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 803360374 164 NLTAGHLLIQLISTASTALLTIMPAVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00172 166 NLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTI 229
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 164-227 1.22e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 41.92  E-value: 1.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 803360374 164 NLTAGHLLIQLIST-ASTALLTIMPAVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00175 177 NISAGHLLFAILSGfAFNMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGDTI 241
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 164-225 2.73e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 37.92  E-value: 2.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 803360374 164 NLTAGHLLIQLISTASTALLTIMPAVSILTTIILLLL-TILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00173 166 NISAGHIVLTLIGNYLSSSLFSSSVVSLLLVLLIQVGyFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 164-222 8.42e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 36.25  E-value: 8.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 803360374 164 NLTAGHLLIQLISTASTALLTIMPAVSILTTIILLLLTILEVAVAMIQAYVFVLLLSLY 222
Cdd:MTH00005 168 NMSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
 
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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