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Conserved domains on  [gi|170026947|gb|ACB06002|]
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ATP synthase F0 subunit 6 (mitochondrion) [Sousa chinensis]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009564)

ATP synthase F0 subunit 6 is part of the mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V), which produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 3.01e-124

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 350.79  E-value: 3.01e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   1 MNENLFASFMIPVMLGVPITTLIIMFPTMLFPTPNRLINNRMIAIQQWLTKLTSKQLMITHSPKGQAWSLMLISLFLFIA 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  81 STNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170026947 161 TANITAGHLLLHLIGSATLALMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 3.01e-124

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 350.79  E-value: 3.01e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   1 MNENLFASFMIPVMLGVPITTLIIMFPTMLFPTPNRLINNRMIAIQQWLTKLTSKQLMITHSPKGQAWSLMLISLFLFIA 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  81 STNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170026947 161 TANITAGHLLLHLIGSATLALMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
6-225 3.68e-50

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: 162.76  E-value: 3.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947    6 FASFMIPVMLGVPITTLIIMFptMLFPTPNRLINNRMIAIQQWLTKLTSKQLMITHSPKGQAWSLMLISLFLFIASTNLL 85
Cdd:TIGR01131  10 ITLFSLTLLSLILLLSLLIFL--ISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   86 GMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALAVRLTANIT 165
Cdd:TIGR01131  88 GLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANIS 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  166 AGHLLLHLIGSATLALMNISLFTalITFIILTLLIILEFAVALIQAYVFTLLVSLYLQDN 225
Cdd:TIGR01131 168 AGHLLLTLLSGLLFSLMSSAIFA--LLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
65-223 1.58e-39

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 133.29  E-value: 1.58e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  65 GQAWSLMLISLFLFIASTNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMI 144
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170026947 145 ETTSLFIQPLALAVRLTANITAGHLLLHLIGSATLALMNISLFtalITFIILTLLIILEFAVALIQAYVFTLLVSLYLQ 223
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGL---LPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
22-223 2.56e-33

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 119.13  E-value: 2.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   22 LIIMFPTMLFPTPNRLINNRMIAIQQWLTKLTSKQLM-ITHSPKGQAWSLMLISLFLFIASTNLLGML---PHSFTPTTQ 97
Cdd:pfam00119  10 ILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTAD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   98 LSMNLGMAIPLWAGTVFIGFRNK-TKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALAVRLTANITAGHLLLHLIGS 176
Cdd:pfam00119  90 INVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAG 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 170026947  177 ATLALMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQ 223
Cdd:pfam00119 170 LIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
71-224 3.52e-22

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: 90.13  E-value: 3.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  71 MLISLFLFIASTNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNK-TKMSLAHLLpLGTPTFLIPMLVMIETTSL 149
Cdd:COG0356   60 LLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLF-FPPFPWLAPLMLPIEIISE 138
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170026947 150 FIQPLALAVRLTANITAGHLLLHLIgsatlALMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQD 224
Cdd:COG0356  139 LARPLSLSLRLFGNMFAGHIILLLL-----AGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 3.01e-124

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 350.79  E-value: 3.01e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   1 MNENLFASFMIPVMLGVPITTLIIMFPTMLFPTPNRLINNRMIAIQQWLTKLTSKQLMITHSPKGQAWSLMLISLFLFIA 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  81 STNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170026947 161 TANITAGHLLLHLIGSATLALMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
1-226 6.02e-86

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 253.98  E-value: 6.02e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   1 MNENLFASFMIPVMLGVPITTLIIMFPTMLFPTP-NRLINNRMIAIQQWLTKLTSKQLMITHSPKGQAWSLMLISLFLFI 79
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPkNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  80 ASTNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALAVR 159
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170026947 160 LTANITAGHLLLHLIGSATLALMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQDNT 226
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
1-226 2.61e-78

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 234.48  E-value: 2.61e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   1 MNENLFASFMIPVMLGVPITTLIIMFPTMLFPTP-NRLINNRMIAIQQWLTKLTSKQLMITHSPKGQAWSLMLISLFLFI 79
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPtNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  80 ASTNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALAVR 159
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170026947 160 LTANITAGHLLLHLIGSATLALMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQDNT 226
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-225 1.58e-77

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 232.46  E-value: 1.58e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   1 MNENLFASFMIPVMLGVPITTLIIMFPTMLFPTP-NRLINNRMIAIQQWLTKLTSKQLMITHSPKGQAWSLMLISLFLFI 79
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPtSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  80 ASTNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALAVR 159
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170026947 160 LTANITAGHLLLHLIGSATLALMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQDN 225
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
1-226 8.64e-68

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 207.88  E-value: 8.64e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   1 MNENLFASFMIPVMLGVPITTLIIMFPTMLFPTP-NRLINNRMIAIQQWLTKLTSKQLMITHSPKGQAWSLMLISLFLFI 79
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLtNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  80 ASTNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALAVR 159
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170026947 160 LTANITAGHLLLHLIGSATLALMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQDNT 226
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
6-225 3.68e-50

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: 162.76  E-value: 3.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947    6 FASFMIPVMLGVPITTLIIMFptMLFPTPNRLINNRMIAIQQWLTKLTSKQLMITHSPKGQAWSLMLISLFLFIASTNLL 85
Cdd:TIGR01131  10 ITLFSLTLLSLILLLSLLIFL--ISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   86 GMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALAVRLTANIT 165
Cdd:TIGR01131  88 GLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANIS 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  166 AGHLLLHLIGSATLALMNISLFTalITFIILTLLIILEFAVALIQAYVFTLLVSLYLQDN 225
Cdd:TIGR01131 168 AGHLLLTLLSGLLFSLMSSAIFA--LLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-224 1.99e-47

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 155.71  E-value: 1.99e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   1 MNENLFASFMIPVMLGVPITTLIIMFPTMLFPTPNRLINNRMIAIQQWLTKLTSKQLMITHSPKGQAWSLMLISLFLFIA 80
Cdd:MTH00157   1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  81 STNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALAVRL 160
Cdd:MTH00157  81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170026947 161 TANITAGHLLLHLIGSATLALMNISLFTaliTFIILTLLIILEFAVALIQAYVFTLLVSLYLQD 224
Cdd:MTH00157 161 AANMIAGHLLLTLLGNTGPSLSSMILSI---LILIQILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
1-225 8.83e-43

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 143.96  E-value: 8.83e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   1 MNENLFASFMIPVMLGVPITTLIIMFPT--MLFPTPNRLINNRMIAIQQWLTKLTSKQLMITHSPKGQAWSLMLISLFLF 78
Cdd:MTH00035   3 INNSIFGQFSPDTILFIPLTLLSSVIALswLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  79 IASTNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALAV 158
Cdd:MTH00035  83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170026947 159 RLTANITAGHLLLHLIGSATLALMNiSLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQDN 225
Cdd:MTH00035 163 RLAANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
65-223 1.58e-39

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 133.29  E-value: 1.58e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  65 GQAWSLMLISLFLFIASTNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMI 144
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170026947 145 ETTSLFIQPLALAVRLTANITAGHLLLHLIGSATLALMNISLFtalITFIILTLLIILEFAVALIQAYVFTLLVSLYLQ 223
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGL---LPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
5-224 2.31e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 132.68  E-value: 2.31e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   5 LFASFMIPVMLGVPITTLIIMFPTM---LFPTPNRLINNRMIAIQQWLTKLTSKQLMITHSPKGQAWSLMLISLFLFIAS 81
Cdd:MTH00173   5 LFSSFDDHNSSFSSLSFLMWLLSLMslfFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLIS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  82 TNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALAVRLT 161
Cdd:MTH00173  85 LNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLL 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170026947 162 ANITAGHLLLHLIGSATLA-LMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQD 224
Cdd:MTH00173 165 ANISAGHIVLTLIGNYLSSsLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
1-226 2.14e-37

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 130.15  E-value: 2.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   1 MNENLFASFMIPVMLGVPITTLI---IMFPTMLFPTPNRLINNRMIAIQQWLTKLTSKQLMITHSPKGQAWSLMLISLFL 77
Cdd:MTH00176   1 MLVDLFSSFDPPNKNIFSMISLSwitLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  78 FIASTNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALA 157
Cdd:MTH00176  81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170026947 158 VRLTANITAGHLLLHLIGSATLALMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQDNT 226
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP-synt_A pfam00119
ATP synthase A chain;
22-223 2.56e-33

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 119.13  E-value: 2.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   22 LIIMFPTMLFPTPNRLINNRMIAIQQWLTKLTSKQLM-ITHSPKGQAWSLMLISLFLFIASTNLLGML---PHSFTPTTQ 97
Cdd:pfam00119  10 ILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTAD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   98 LSMNLGMAIPLWAGTVFIGFRNK-TKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALAVRLTANITAGHLLLHLIGS 176
Cdd:pfam00119  90 INVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAG 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 170026947  177 ATLALMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQ 223
Cdd:pfam00119 170 LIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
4-226 1.44e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 117.91  E-value: 1.44e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   4 NLFASFMIPVMLGVPITTLIIMFPTMLFPTPNRLInnrmiAIQQWLTKLTSKQLMITHSPKGQAWSLMLISLFLFIASTN 83
Cdd:MTH00005  14 NSLFNNLSSTAFWAFNFSIILLLSSSFWITPNRLS-----SIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  84 LLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALAVRLTAN 163
Cdd:MTH00005  89 LSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAAN 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 170026947 164 ITAGHLLLHLIGSATLALMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQDNT 226
Cdd:MTH00005 169 MSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
1-224 1.21e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 110.13  E-value: 1.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947   1 MNENLFASFMIPVMLGV---PITTLIIMFPTMLFPTPNRLINNRMIAIQQWLTKLTSKQLMITHSPKGQAWSLMLISLFL 77
Cdd:MTH00172   1 MSSSYFDQFNIVWLIGLtnsSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  78 FIASTNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALA 157
Cdd:MTH00172  81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170026947 158 VRLTANITAGHLLLHLIGSATLALMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQD 224
Cdd:MTH00172 161 VRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
22-224 2.81e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 98.93  E-value: 2.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  22 LIIMFPTMLFPTpNRLINNRMIAIQQWLTKLTSKQLMITHSPKGQAWSLMLISLFLFIASTNLLGMLPHSFTPTTQLSMN 101
Cdd:MTH00175  37 LAVIIFWLLLKG-DKLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIIT 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947 102 LGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIETTSLFIQPLALAVRLTANITAGHLLLHLI-GSATLA 180
Cdd:MTH00175 116 FGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILsGFAFNM 195
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 170026947 181 LMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQD 224
Cdd:MTH00175 196 LSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
71-224 3.52e-22

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: 90.13  E-value: 3.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  71 MLISLFLFIASTNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNK-TKMSLAHLLpLGTPTFLIPMLVMIETTSL 149
Cdd:COG0356   60 LLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLF-FPPFPWLAPLMLPIEIISE 138
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170026947 150 FIQPLALAVRLTANITAGHLLLHLIgsatlALMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYLQD 224
Cdd:COG0356  139 LARPLSLSLRLFGNMFAGHIILLLL-----AGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
64-224 2.91e-19

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 82.53  E-value: 2.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  64 KGQAWSLMLISLFLFIASTNLLGMLP-HSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPmlv 142
Cdd:PRK05815  68 KGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFYLQPHPLLLP--- 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947 143 mIETTSLFIQPLALAVRLTANITAGHLLLHLIGSatlaLMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK05815 145 -IEIISEFSRPISLSLRLFGNMLAGELILALIAL----LGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYI 219

                 ..
gi 170026947 223 QD 224
Cdd:PRK05815 220 SM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
64-224 1.71e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 78.44  E-value: 1.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  64 KGQAWSLMLISLFLFIASTNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVM 143
Cdd:MTH00174  86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947 144 IETTSLFIQPLALAVRLTANITAGHLLLHLIGSATLALMNIS-LFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00174 166 IETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGiLIGSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245

                 ..
gi 170026947 223 QD 224
Cdd:MTH00174 246 RD 247
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
72-222 1.13e-14

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 71.70  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  72 LISLFLFIASTNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFR-NKTKMSLAHLLPlGTPTFLIPMLVMIETTSLF 150
Cdd:PRK13419 174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAHLTG-GTHWSLWIIMIPIEFIGLF 252
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170026947 151 IQPLALAVRLTANITAGHLLLhligsatLALMNIS------LFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13419 253 TKPFALTVRLFANMTAGHIVI-------LSLIFISfilksyIVAVAVSVPFAIFIYLLELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
74-222 1.17e-11

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 61.53  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  74 SLFLFIASTNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSlaHLLPLGTPTFLIPM-LVMIETTSLFIQ 152
Cdd:MTH00087  57 FTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTFsMLFVEIVSELSR 134
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947 153 PLALAVRLTANITAGHLLLHLIGSATLALMNISLFtalitfiiltlLIILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00087 135 PLALTLRLTVNLMVGHLISSLLNFLGEKYVWLSIL-----------AIMMECFVAFIQSYIFSRLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
93-222 1.41e-05

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 45.27  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  93 TPTTQLSMNLGMAIPLWAGTVFIGFRNKTKMSLAHLLPLGTPTFLIPMLVMIE-TTSLFIQPLALAVRLTANITAGH-LL 170
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEfIVSPMAKTFALTVRLLANMTAGHvII 296
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 170026947 171 LHLIGsatLALMNISLFTALITFIILTLLIILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13417 297 LALMG---FIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
74-217 7.37e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 36.60  E-value: 7.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170026947  74 SLFLFIASTNLLGMLPHSFTPTTQLSMNLGMAIPLWAGTVFIGFRnkTKMSLAHLLPLGTPTFL-IPMLVMIETTSLFiq 152
Cdd:PRK13421  83 TLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVR--ARGVRGYLATFAEPTWVmIPLNLVEQLTRTF-- 158
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170026947 153 plALAVRLTANITAGHLLLHLIGSATLALMNISLftalitfiiltllIILEFAVALIQAYVFTLL 217
Cdd:PRK13421 159 --SLIVRLFGNVMSGVFVIGIVLSLAGLLVPIPL-------------MALDLLTGAVQAYIFAVL 208
 
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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