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Conserved domains on  [gi|1904996154|gb|QNS38383|]
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ATP synthase F0 subunit 6 (mitochondrion) [Calyptomena viridis]

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 1.35e-105

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177190  Cd Length: 227  Bit Score: 303.72  E-value: 1.35e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154   1 MNLNLFDQFMSPSILGIPLILISTLFPMLLYPSPKNQWIPNRLSTLQLWFLHLITKQLLMPLNKKGHKWALILTSLMTFL 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  81 LSINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIETTSLLIRPMALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904996154 161 LTANLTAGHLLIQLISTATTTLLPILPAVSILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 1.35e-105

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 303.72  E-value: 1.35e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154   1 MNLNLFDQFMSPSILGIPLILISTLFPMLLYPSPKNQWIPNRLSTLQLWFLHLITKQLLMPLNKKGHKWALILTSLMTFL 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  81 LSINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIETTSLLIRPMALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904996154 161 LTANLTAGHLLIQLISTATTTLLPILPAVSILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQENI 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 ...
 5-227 1.21e-46

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


Pssm-ID: 273458  Cd Length: 226  Bit Score: 153.90  E-value: 1.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154   5 LFDQFMSPS--ILGIPLILISTLFPMLLY---PSPKNQWIPNRLSTLQLWFLHLITKQLLMPLNKKGHKWALILTSLMTF 79
Cdd:TIGR01131   1 LFSQFDISPitLFSLTLLSLILLLSLLIFlisSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  80 LLSINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIETTSLLIRPMALGV 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1904996154 160 RLTANLTAGHLLIQLISTATTTLLPilPAVSILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMS--SAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-224 1.27e-32

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: 115.57  E-value: 1.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  66 GHKWALILTSLMTFLLSINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILI 145
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1904996154 146 ETTSLLIRPMALGVRLTANLTAGHLLIQLISTATTTLLPIlpaVSILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
35-224 6.41e-28

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 105.26  E-value: 6.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  35 KNQWIPNRLSTLQLWFLHLITKQLLMPL-NKKGHKWALILTSLMTFLL---SINLLGLLPYTFTPTTQLSMNMALAFPLW 110
Cdd:pfam00119  22 TKKLVPGRLQNFVEMLVEFVDNIVKDNIgKKKGRKFFPLLLTLFFFILvsnLLGLIPKSPGGFTVTADINVTLALALIVF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154 111 LATLLTGLRNQPSIT-LGHLLPEGTPTPLIPALILIETTSLLIRPMALGVRLTANLTAGHLLIQLISTATTTLLPILPAV 189
Cdd:pfam00119 102 LLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLL 181

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1904996154 190 SILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 182 GVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 35-225 8.43e-17

FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 75.88  E-value: 8.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  35 KNQWIPNRLSTLQLWFLHLITKQLLMPLNKKGHKWALILTSLMTFLLSINLLGLLPYTFTPTTQLSMNMALAFPLWLATL 114
Cdd:COG0356    23 KLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154 115 LTGLRNQPSIT-LGHLLPEGTPtPLIPALILIETTSLLIRPMALGVRLTANLTAGHLLIQLISTATTTLLPILPAVsilt 193
Cdd:COG0356   103 YYGIKKKGLGGyLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSL---- 177

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1904996154 194 tLILILLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:COG0356   178 -LLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 1.35e-105

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 303.72  E-value: 1.35e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154   1 MNLNLFDQFMSPSILGIPLILISTLFPMLLYPSPKNQWIPNRLSTLQLWFLHLITKQLLMPLNKKGHKWALILTSLMTFL 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  81 LSINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIETTSLLIRPMALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904996154 161 LTANLTAGHLLIQLISTATTTLLPILPAVSILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-227 2.27e-104

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 300.59  E-value: 2.27e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154   1 MNLNLFDQFMSPSILGIPLILISTLFPMLLYPSPKNQWIPNRLSTLQLWFLHLITKQLLMPLNKKGHKWALILTSLMTFL 80
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  81 LSINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIETTSLLIRPMALGVR 160
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904996154 161 LTANLTAGHLLIQLISTATTTLLPILPAVSILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-227 3.30e-102

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 295.34  E-value: 3.30e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154   1 MNLNLFDQFMSPSILGIPLILISTLFPMLLYPSPKNQWIPNRLSTLQLWFLHLITKQLLMPLNKKGHKWALILTSLMTFL 80
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  81 LSINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIETTSLLIRPMALGVR 160
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904996154 161 LTANLTAGHLLIQLISTATTTLLPILPAVSILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-226 1.13e-78

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 235.61  E-value: 1.13e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154   1 MNLNLFDQFMSPSILGIPLILISTLFPMLLYPSPKNQWIPNRLSTLQLWFLHLITKQLLMPLNKKGHKWALILTSLMTFL 80
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  81 LSINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIETTSLLIRPMALGVR 160
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1904996154 161 LTANLTAGHLLIQLISTATTTLLPILPAVSILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00179  161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 4.66e-78

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 234.08  E-value: 4.66e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154   1 MNLNLFDQFMSPSILGIPLILISTLFPMLLYPSPKNqWIPNRLSTLQLWFLHLITKQLLMPLNKKGHKWALILTSLMTFL 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNR-LINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  81 LSINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIETTSLLIRPMALGVR 160
Cdd:MTH00101   80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1904996154 161 LTANLTAGHLLIQLISTATTTLLPILPAVSILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00101  160 LTANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-227 1.21e-46

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


Pssm-ID: 273458  Cd Length: 226  Bit Score: 153.90  E-value: 1.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154   5 LFDQFMSPS--ILGIPLILISTLFPMLLY---PSPKNQWIPNRLSTLQLWFLHLITKQLLMPLNKKGHKWALILTSLMTF 79
Cdd:TIGR01131   1 LFSQFDISPitLFSLTLLSLILLLSLLIFlisSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  80 LLSINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIETTSLLIRPMALGV 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1904996154 160 RLTANLTAGHLLIQLISTATTTLLPilPAVSILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMS--SAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-227 2.46e-45

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 150.51  E-value: 2.46e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154   1 MNLNLFDQFMSPSILGIPLILISTLFPML-LYPSPKNQWIPNRLSTLQLWFLHLITKQLLMPLNKKGHKWALILTSLMTF 79
Cdd:MTH00035    3 INNSIFGQFSPDTILFIPLTLLSSVIALSwLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  80 LLSINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIETTSLLIRPMALGV 159
Cdd:MTH00035   83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1904996154 160 RLTANLTAGHLLIQLISTATTTLLPiLPAVSILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00035  163 RLAANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 1.89e-42

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 143.00  E-value: 1.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154   1 MNLNLFDQFMSPSILGIPLILISTLFPMLLYPSpkNQW-IPNRLSTLQLWFLHLITKQLLMPLNKKGHKWALILTSLMTF 79
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPS--SFWlIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  80 LLSINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIETTSLLIRPMALGV 159
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1904996154 160 RLTANLTAGHLLIQLISTATTTLLPILpavSILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMI---LSILILIQILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 2.99e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 132.46  E-value: 2.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154   1 MNLNLFDQFMSPSILGIPLILISTLFPML-LYPSPKNQWI-PNRLSTLQLWFLHLITKQLLMPLNKKGHKWALILTSLMT 78
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFSMISLSWITLLLfLLLMPSSVWFcPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  79 FLLSINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIETTSLLIRPMALG 158
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1904996154 159 VRLTANLTAGHLLIQLISTATTTLLPILPAVSILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 6-225 1.33e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 125.75  E-value: 1.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154   6 FDQFMSPSILGIPLILISTLFPMLLYPSPKnQWIPNRLSTLQLWFLHLITKQLLMPLNKKGHKWALILTSLMTFLLSINL 85
Cdd:MTH00173    9 FDDHNSSFSSLSFLMWLLSLMSLFFFSSSV-WVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  86 LGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIETTSLLIRPMALGVRLTANL 165
Cdd:MTH00173   88 SGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANI 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1904996154 166 TAGHLLIQLISTATTTLLPILPAVSILTTLILILL-TILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00173  168 SAGHIVLTLIGNYLSSSLFSSSVVSLLLVLLIQVGyFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-224 1.27e-32

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: 115.57  E-value: 1.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  66 GHKWALILTSLMTFLLSINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILI 145
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1904996154 146 ETTSLLIRPMALGVRLTANLTAGHLLIQLISTATTTLLPIlpaVSILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 18-222 7.28e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 110.98  E-value: 7.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  18 PLILISTLFPMLLYPSPKNQWIPNRLSTLQLWFLHLITKQLLMPLNKKGHKWALILTSLMTFLLSINLLGLLPYTFTPTT 97
Cdd:MTH00005   22 STAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  98 QLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIETTSLLIRPMALGVRLTANLTAGHLLIQLIST 177
Cdd:MTH00005  102 HLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGI 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1904996154 178 ATTTLLPILPAVSILTTLILILLTILEVAVAMIQAYVFVLLLSLY 222
Cdd:MTH00005  182 YAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP-synt_A pfam00119
ATP synthase A chain;
35-224 6.41e-28

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 105.26  E-value: 6.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  35 KNQWIPNRLSTLQLWFLHLITKQLLMPL-NKKGHKWALILTSLMTFLL---SINLLGLLPYTFTPTTQLSMNMALAFPLW 110
Cdd:pfam00119  22 TKKLVPGRLQNFVEMLVEFVDNIVKDNIgKKKGRKFFPLLLTLFFFILvsnLLGLIPKSPGGFTVTADINVTLALALIVF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154 111 LATLLTGLRNQPSIT-LGHLLPEGTPTPLIPALILIETTSLLIRPMALGVRLTANLTAGHLLIQLISTATTTLLPILPAV 189
Cdd:pfam00119 102 LLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLL 181

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1904996154 190 SILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 182 GVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 1-227 4.05e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 103.58  E-value: 4.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154   1 MNLNLFDQFMSPSILGI---PLILISTLFPMLLYpSPKNQWIPNRLSTLQ---LWFLHLITKQLLMPlnkKGHKWALILT 74
Cdd:MTH00172    1 MSSSYFDQFNIVWLIGLtnsSIMMILVIIVVLLL-FKGIKLIPKRWQSIIeiiYNHFHGVVKDNLGN---EGLKYFPFII 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  75 SLMTFLLSINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIETTSLLIRP 154
Cdd:MTH00172   77 SLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1904996154 155 MALGVRLTANLTAGHLLIQLISTATTTLLPILPAVSILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00172  157 ISLGVRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTI 229
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 1-227 4.91e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 95.84  E-value: 4.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154   1 MNLNLFDQFMSPSILGIP----------------LILISTLFPMLLYpspKNQWIPNRLSTLqLWFLHLITKQLLMP-LN 63
Cdd:MTH00175    1 MLAAYFDQFNIIRLITIQaflgdwlvtftnssmmMVLAVIIFWLLLK---GDKLIPNRWQSI-MELIYLNIRSVVHDnLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  64 KKGHKWALILTSLMTFLLSINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALI 143
Cdd:MTH00175   77 KSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154 144 LIETTSLLIRPMALGVRLTANLTAGHLLIQLIST-ATTTLLPILPAVSILTTLILILLTILEVAVAMIQAYVFVLLLSLY 222
Cdd:MTH00175  157 LIETLSYLIRAISLGVRLAANISAGHLLFAILSGfAFNMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIY 236


                  ....*
gi 1904996154 223 LQENI 227
Cdd:MTH00175  237 LGDTI 241
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 25-227 6.49e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 76.90  E-value: 6.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  25 LFPMLLYPSPKNQWIPNR-LSTLQLWFLHLITkQLLMPLNKKGHKWALILTSLMTFLLSINLLGLLPYTFTPTTQLSMNM 103
Cdd:MTH00174   46 LFYTIGAKGNNNTLVPNRiLVGLELIYSHFYT-VLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154 104 ALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIETTSLLIRPMALGVRLTANLTAGHLLIQLISTATTTLL 183
Cdd:MTH00174  125 GLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMI 204

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1904996154 184 PILPAV-SILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00174  205 NTGILIgSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYLRDTV 249
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 35-225 8.43e-17

FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 75.88  E-value: 8.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  35 KNQWIPNRLSTLQLWFLHLITKQLLMPLNKKGHKWALILTSLMTFLLSINLLGLLPYTFTPTTQLSMNMALAFPLWLATL 114
Cdd:COG0356    23 KLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154 115 LTGLRNQPSIT-LGHLLPEGTPtPLIPALILIETTSLLIRPMALGVRLTANLTAGHLLIQLISTATTTLLPILPAVsilt 193
Cdd:COG0356   103 YYGIKKKGLGGyLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSL---- 177

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1904996154 194 tLILILLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:COG0356   178 -LLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 62-225 7.37e-15

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 70.59  E-value: 7.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  62 LNKKGHKWALILTSLMTFLLSINLLGLLP-YTFTPTTQLSMNMALAFPLWLATLLTGLRNQPsitLGHLLPEGTPTPlIP 140
Cdd:PRK05815   65 IGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKKG---LGGYLKEFYLQP-HP 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154 141 ALILIETTSLLIRPMALGVRLTANLTAGHLLIQLISTATTTLLPILPAvsilTTLILILLTILEVAVAMIQAYVFVLLLS 220
Cdd:PRK05815  141 LLLPIEIISEFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALA----PLILPVAWTIFEIFVGTLQAYIFMMLTI 216


                  ....*
gi 1904996154 221 LYLQE 225
Cdd:PRK05815  217 VYISM 221
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 90-225 8.42e-11

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 59.22  E-value: 8.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNqpSITLGHLLPEGTPTPLIP-ALILIETTSLLIRPMALGVRLTANLTAG 168
Cdd:MTH00087   72 PYSFSPCGMVEFTFLYALVAWLSTFLSFLSK--SEKFSVYLSKGSDSFLKTfSMLFVEIVSELSRPLALTLRLTVNLMVG 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1904996154 169 HLLIQLISTatttllpilpaVSILTTLILILLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00087  150 HLISSLLNF-----------LGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 94-223 2.46e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 50.27  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  94 TPTTQLSMNMALAFPLWLATLLTGLRNQPSITLGHLLPEGTPTPLIPALILIE-TTSLLIRPMALGVRLTANLTAGHLLI 172
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEfIVSPMAKTFALTVRLLANMTAGHVII 296

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1904996154 173 ----QLISTATTTLLPILPAVSILTTLILilltilEVAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13417  297 lalmGFIFQFQSWGIVPVSVIGSGLIYVL------EIFVAFLQAYIFVLLTSLFV 345
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 90-223 3.95e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 49.74  E-value: 3.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904996154  90 PYTFTPTTQLSMNMALAFPLWLATLLTGLRNQPsiTLGHL--LPEGTPTPLIPALILIETTSLLIRPMALGVRLTANLTA 167
Cdd:PRK13419  191 PYGATATGNINVTLTLAVFTFFITQYAAIKAHG--IKGYLahLTGGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTA 268

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1904996154 168 GHLLIQ---LISTATTTLLpILPAVSiltTLILILLTILEVAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13419  269 GHIVILsliFISFILKSYI-VAVAVS---VPFAIFIYLLELFVAFLQAYIFTMLSALFI 323
 
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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