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Conserved domains on  [gi|2201039006|gb|UMB50624|]
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ATP synthase F0 subunit 6 [Synodontis khartoumensis]

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 1.96e-125

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177190  Cd Length: 227  Bit Score: 354.18  E-value: 1.96e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006   1 MALNLFDQFMSPTHLGIPLIAIALTLPWILVPSPTNRYQTNRLISLQNWFIKTFTQQLLTPLNKGGHKWAMILTSLMIFI 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  81 LMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETISLFIRPLALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201039006 161 LTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQENV 227
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 1.96e-125

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 354.18  E-value: 1.96e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006   1 MALNLFDQFMSPTHLGIPLIAIALTLPWILVPSPTNRYQTNRLISLQNWFIKTFTQQLLTPLNKGGHKWAMILTSLMIFI 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  81 LMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETISLFIRPLALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201039006 161 LTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQENV 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 8.79e-49

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: 159.29  E-value: 8.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006   5 LFDQFMSP----THLGIPLIAIALTLPWILVPSPTNRY-QTNRLISLQNWFIKTFTQQLLTPLNKGGHKWAMILTSLMIF 79
Cdd:TIGR01131   1 LFSQFDISpitlFSLTLLSLILLLSLLIFLISSSLSRWlIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  80 ILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETISLFIRPLALGV 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201039006 160 RLTANLTAGHLLIQLISTATITLLPMMttVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQENV 227
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-224 1.27e-38

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: 130.98  E-value: 1.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  66 GHKWAMILTSLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVI 145
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2201039006 146 ETISLFIRPLALGVRLTANLTAGHLLIQLISTATITllpMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQ 224
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPS---LLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
19-224 1.38e-33

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 119.90  E-value: 1.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  19 LIAIALTLPWILVPSPTNRYQTNRLISLQNWFIKTFTQQLLTPL-NKGGHKWAMILTSLMIFILMLNILGLL---PYTFT 94
Cdd:pfam00119   6 IVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIgKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  95 PTTQLSLNMGLAVPLWLATVIIGLRNQPTAA-LGHLLPEGTPAPLIPILIVIETISLFIRPLALGVRLTANLTAGHLLIQ 173
Cdd:pfam00119  86 VTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLL 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2201039006 174 LISTATITLLPMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 166 LLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 49-225 7.21e-24

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


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 94.37  E-value: 7.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  49 WFIKTFTQQLLTPLNKGGHKWAMILTSLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAA-LG 127
Cdd:COG0356    37 MLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006 128 HLLPEGTPaPLIPILIVIETISLFIRPLALGVRLTANLTAGHLLIqlistATITLLPMMTTVATLTAILLVLLTLLEVAV 207
Cdd:COG0356   117 HLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIIL-----LLLAGLAPFLLLGVLSLLLPVAWTAFELLV 190

                         170
                  ....*....|....*...
gi 2201039006 208 AVIQAYVFVLLLSLYLQE 225
Cdd:COG0356   191 GFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 1.96e-125

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 354.18  E-value: 1.96e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006   1 MALNLFDQFMSPTHLGIPLIAIALTLPWILVPSPTNRYQTNRLISLQNWFIKTFTQQLLTPLNKGGHKWAMILTSLMIFI 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  81 LMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETISLFIRPLALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201039006 161 LTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQENV 227
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-227 2.40e-111

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 318.45  E-value: 2.40e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006   1 MALNLFDQFMSPTHLGIPLIAIALTLPWILVPSPTNRYQTNRLISLQNWFIKTFTQQLLTPLNKGGHKWAMILTSLMIFI 80
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  81 LMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETISLFIRPLALGVR 160
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201039006 161 LTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQENV 227
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-227 1.43e-103

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 298.66  E-value: 1.43e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006   1 MALNLFDQFMSPTHLGIPLIAIALTLPWILVPSPTNRYQTNRLISLQNWFIKTFTQQLLTPLNKGGHKWAMILTSLMIFI 80
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  81 LMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETISLFIRPLALGVR 160
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201039006 161 LTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQENV 227
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-227 5.30e-90

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 264.50  E-value: 5.30e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006   1 MALNLFDQFMSPTHLGIPLIAIALTLPWILVPSPTNRYQTNRLISLQNWFIKTFTQQLLTPLNKGGHKWAMILTSLMIFI 80
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  81 LMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETISLFIRPLALGVR 160
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201039006 161 LTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQENV 227
Cdd:MTH00179  161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 4.67e-75

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 226.37  E-value: 4.67e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006   1 MALNLFDQFMSPTHLGIPLIAIALTLPWILVPSPtNRYQTNRLISLQNWFIKTFTQQLLTPLNKGGHKWAMILTSLMIFI 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTP-NRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  81 LMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETISLFIRPLALGVR 160
Cdd:MTH00101   80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201039006 161 LTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQEN 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 8.79e-49

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: 159.29  E-value: 8.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006   5 LFDQFMSP----THLGIPLIAIALTLPWILVPSPTNRY-QTNRLISLQNWFIKTFTQQLLTPLNKGGHKWAMILTSLMIF 79
Cdd:TIGR01131   1 LFSQFDISpitlFSLTLLSLILLLSLLIFLISSSLSRWlIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  80 ILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETISLFIRPLALGV 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201039006 160 RLTANLTAGHLLIQLISTATITLLPMMttVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQENV 227
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 4-227 1.39e-47

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 156.29  E-value: 1.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006   4 NLFDQFMSPTHLGIPL--IAIALTLPWILVPSPTNRYQTnRLISLQNWFIKTFTQQLLTPLNKGGHKWAMILTSLMIFIL 81
Cdd:MTH00035    6 SIFGQFSPDTILFIPLtlLSSVIALSWLFFINPTNWLPS-RSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  82 MLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETISLFIRPLALGVRL 161
Cdd:MTH00035   85 SINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201039006 162 TANLTAGHLLIQLISTAtITLLPMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQENV 227
Cdd:MTH00035  165 AANLTAGHLLIFLLSTA-IWELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 2.47e-44

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 148.01  E-value: 2.47e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006   1 MALNLFDQFMSPTHLGIPLIAIALTLPWILVPSPTNrYQTNRLISLQNWFIKTFTQQLLTPLNKGGHKWAMILTSLMIFI 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFW-LIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  81 LMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETISLFIRPLALGVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201039006 161 LTANLTAGHLLIQLISTATITLLPMMTTVatlTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQE 225
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSI---LILIQILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 2.58e-41

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 140.17  E-value: 2.58e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006   1 MALNLFDQFMSPTHLGIPLIAIALTLPWI--LVPSPTNRYQTNRLISLQNWFIKTFTQQLLTPLNKGGHKWAMILTSLMI 78
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFSMISLSWITLLLflLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  79 FILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETISLFIRPLALG 158
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201039006 159 VRLTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQEN 226
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-224 1.27e-38

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: 130.98  E-value: 1.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  66 GHKWAMILTSLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVI 145
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2201039006 146 ETISLFIRPLALGVRLTANLTAGHLLIQLISTATITllpMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQ 224
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPS---LLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 6-225 3.02e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 132.30  E-value: 3.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006   6 FDQFMSPTHLGIPLIAIALTLPWILVPSPTnRYQTNRLISLQNWFIKTFTQQLLTPLNKGGHKWAMILTSLMIFILMLNI 85
Cdd:MTH00173    9 FDDHNSSFSSLSFLMWLLSLMSLFFFSSSV-WVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  86 LGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETISLFIRPLALGVRLTANL 165
Cdd:MTH00173   88 SGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANI 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201039006 166 TAGHLLIQLI-STATITLLPMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQE 225
Cdd:MTH00173  168 SAGHIVLTLIgNYLSSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_A pfam00119
ATP synthase A chain;
19-224 1.38e-33

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 119.90  E-value: 1.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  19 LIAIALTLPWILVPSPTNRYQTNRLISLQNWFIKTFTQQLLTPL-NKGGHKWAMILTSLMIFILMLNILGLL---PYTFT 94
Cdd:pfam00119   6 IVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIgKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  95 PTTQLSLNMGLAVPLWLATVIIGLRNQPTAA-LGHLLPEGTPAPLIPILIVIETISLFIRPLALGVRLTANLTAGHLLIQ 173
Cdd:pfam00119  86 VTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLL 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2201039006 174 LISTATITLLPMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 166 LLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 18-222 4.02e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 108.67  E-value: 4.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  18 PLIAIALTLPWILVPSPTNRYQTNRLISLQNWFIKTFTQQLLTPLNKGGHKWAMILTSLMIFILMLNILGLLPYTFTPTT 97
Cdd:MTH00005   22 STAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  98 QLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETISLFIRPLALGVRLTANLTAGHLLIQLIST 177
Cdd:MTH00005  102 HLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGI 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2201039006 178 ATITLLPMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLY 222
Cdd:MTH00005  182 YAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 62-227 5.63e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 103.55  E-value: 5.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  62 LNKGGHKWAMILTSLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPI 141
Cdd:MTH00175   75 LGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPF 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006 142 LIVIETISLFIRPLALGVRLTANLTAGHLLIQLISTATITLLPM-MTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLS 220
Cdd:MTH00175  155 LVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNgLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTT 234


                  ....*..
gi 2201039006 221 LYLQENV 227
Cdd:MTH00175  235 IYLGDTI 241
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 1-223 5.86e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 103.20  E-value: 5.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006   1 MALNLFDQFMSPTHLGIPLIAIALTLPW--ILVPSPTNRYQTNRLISLQNWFIKTFTQQLLTPLNKGGHKWAMILTSLMI 78
Cdd:MTH00172    1 MSSSYFDQFNIVWLIGLTNSSIMMILVIivVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  79 FILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETISLFIRPLALG 158
Cdd:MTH00172   81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201039006 159 VRLTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYL 223
Cdd:MTH00172  161 VRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYL 225
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 49-225 7.21e-24

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


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 94.37  E-value: 7.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  49 WFIKTFTQQLLTPLNKGGHKWAMILTSLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAA-LG 127
Cdd:COG0356    37 MLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006 128 HLLPEGTPaPLIPILIVIETISLFIRPLALGVRLTANLTAGHLLIqlistATITLLPMMTTVATLTAILLVLLTLLEVAV 207
Cdd:COG0356   117 HLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIIL-----LLLAGLAPFLLLGVLSLLLPVAWTAFELLV 190

                         170
                  ....*....|....*...
gi 2201039006 208 AVIQAYVFVLLLSLYLQE 225
Cdd:COG0356   191 GFLQAYIFTMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 64-225 6.77e-21

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 87.16  E-value: 6.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  64 KGGHKWAMILTSLMIFILMLNILGLLP-YTFTPTTQLSLNMGLAVPLWLATVIIGLRNQptaALGHLLPEGTPAPlIPIL 142
Cdd:PRK05815   67 GKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLL 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006 143 IVIETISLFIRPLALGVRLTANLTAGHLLIQLIStatiTLLPMMTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLY 222
Cdd:PRK05815  143 LPIEIISEFSRPISLSLRLFGNMLAGELILALIA----LLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVY 218


                  ...
gi 2201039006 223 LQE 225
Cdd:PRK05815  219 ISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 63-227 2.40e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 80.75  E-value: 2.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  63 NKGGHKWAMILtSLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPIL 142
Cdd:MTH00174   85 NKGGNYLAFVL-SLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLL 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006 143 IVIETISLFIRPLALGVRLTANLTAGHLLIQLISTATITLLPMMTTV-ATLTAILLVLLTLLEVAVAVIQAYVFVLLLSL 221
Cdd:MTH00174  164 TIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPFAILIFVTILEMAVAIIQAYVFTLLTIV 243


                  ....*.
gi 2201039006 222 YLQENV 227
Cdd:MTH00174  244 YLRDTV 249
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 64-223 3.52e-15

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 73.24  E-value: 3.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  64 KGGHKWAMILTSLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILI 143
Cdd:PRK13419  165 HGYEKFLPYLLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGTHWSLWIIMI 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006 144 VIETISLFIRPLALGVRLTANLTAGHLLI-QLISTATITLLPMMTtvATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLY 222
Cdd:PRK13419  245 PIEFIGLFTKPFALTVRLFANMTAGHIVIlSLIFISFILKSYIVA--VAVSVPFAIFIYLLELFVAFLQAYIFTMLSALF 322


                  .
gi 2201039006 223 L 223
Cdd:PRK13419  323 I 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 71-225 2.50e-12

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 63.46  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  71 MILTSLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQptAALGHLLPEGTPAPLIP-ILIVIETIS 149
Cdd:MTH00087   53 VISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKS--EKFSVYLSKGSDSFLKTfSMLFVEIVS 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201039006 150 LFIRPLALGVRLTANLTAGHLLIQLISTATITLLPMMttvatltaillVLLTLLEVAVAVIQAYVFVLLLSLYLQE 225
Cdd:MTH00087  131 ELSRPLALTLRLTVNLMVGHLISSLLNFLGEKYVWLS-----------ILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 62-223 1.11e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 51.43  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  62 LNKGGHKWAMILTSLMIFILMLNILGLLPYT-----------------------------------FTPTTQLSLNMGLA 106
Cdd:PRK13417  150 MHGHGHSYYHYIFTLFFFILFCNLMGLVPSVgeltvvasdygglvalgvmdhtphalptfakvwsgITVTGDISVTMTLA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006 107 VPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETI-SLFIRPLALGVRLTANLTAGHLLIqlISTATITLLPM 185
Cdd:PRK13417  230 LLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII--LALMGFIFQFQ 307

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2201039006 186 MTTVATLTAILLVLLTLLEVAVAVIQAYVFVLLLSLYL 223
Cdd:PRK13417  308 SWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
 42-175 7.20e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 39.29  E-value: 7.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  42 RLISLQNWFIKTFTQQLLTPLNKGGHKWAMILTSLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQ 121
Cdd:PRK13421   50 RLQSVLELVVTTIDAQIRDTMQTDPAPYRALIGTLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVRAR 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2201039006 122 ptAALGHLLPEGTPAPLIPILIVIETISlfiRPLALGVRLTANLTAGHLLIQLI 175
Cdd:PRK13421  130 --GVRGYLATFAEPTWVMIPLNLVEQLT---RTFSLIVRLFGNVMSGVFVIGIV 178
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 75-168 1.56e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 37.94  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  75 SLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPAPLIPILIVIETISLFIRP 154
Cdd:MTH00050   28 VVLFIVLFLFLLYRLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRP 107

                          90
                  ....*....|....
gi 2201039006 155 LALGVRLTANLTAG 168
Cdd:MTH00050  108 VVLILRPFINISLG 121
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 75-223 1.61e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 38.57  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006  75 SLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQP-TAALGHLLpegTPApliPILIVIETISLFIR 153
Cdd:PRK13420   80 TLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEGlREYLKHYL---SPS---PFLLPFHLISEITR 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201039006 154 PLALGVRLTANLTAGHLLIQLISTATITLLPMmttvatltaillvLLTLLEVAVAVIQAYVFVLLLSLYL 223
Cdd:PRK13420  154 TLALAVRLFGNIMSLELAALLVLLVAGFLVPV-------------PILMLHIIEALVQAYIFGMLALIYI 210
 
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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