NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2201038922|gb|UMB50546|]
View 

ATP synthase F0 subunit 6 [Synodontis cf. brichardi FDBS-2022]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 2.12e-113

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177190  Cd Length: 227  Bit Score: 323.75  E-value: 2.12e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922   1 MALNLFDQFMSPTYLGIPLIAIALTLPWILIPTPTNRYQTNRLVSLQNWFIKTFTQQLLTPLNKGGHKWATILASLMIFI 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  81 LMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIIIETISLFIRPLALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201038922 161 LTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 2.12e-113

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 323.75  E-value: 2.12e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922   1 MALNLFDQFMSPTYLGIPLIAIALTLPWILIPTPTNRYQTNRLVSLQNWFIKTFTQQLLTPLNKGGHKWATILASLMIFI 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  81 LMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIIIETISLFIRPLALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201038922 161 LTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 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 1.17e-40

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: 138.49  E-value: 1.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922   5 LFDQFMSPTY----LGIPLIAIALTLPWILIPTPTNRY-QTNRLVSLQNWFIKTFTQQLLTPLNKGGHKWATILASLMIF 79
Cdd:TIGR01131   1 LFSQFDISPItlfsLTLLSLILLLSLLIFLISSSLSRWlIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  80 ILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIIIETISLFIRPLALGV 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201038922 160 RLTANLTAGHLLIQLISTATITLLPMMttVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 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 9.52e-30

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: 108.26  E-value: 9.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  66 GHKWATILASLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIII 145
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2201038922 146 ETISLFIRPLALGVRLTANLTAGHLLIQLISTATITllpMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQ 224
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPS---LLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
19-224 7.89e-26

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 99.87  E-value: 7.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  19 LIAIALTLPWILIPTP-TNRYQTNRLVSLQNWFIKTFTQQLLTPL-NKGGHKWATILASLMIFILMLNILGLL---PYTF 93
Cdd:pfam00119   5 LIVALILLLFLLLATRkTKKLVPGRLQNFVEMLVEFVDNIVKDNIgKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  94 TPTTQLSLNMGLAVPLWLATVIIGLRNQPTAA-LGHLLPEGTPTPLIPILIIIETISLFIRPLALGVRLTANLTAGHLLI 172
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2201038922 173 QLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 49-225 4.83e-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: 76.27  E-value: 4.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  49 WFIKTFTQQLLTPLNKGGHKWATILASLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAA-LG 127
Cdd:COG0356    37 MLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922 128 HLLPEGTPTPLIPILIIIETiSLFIRPLALGVRLTANLTAGHLLIqlistATITLLPMMTTVATLTAILLVLLTLLEVAV 207
Cdd:COG0356   117 HLFFPPFPWLAPLMLPIEII-SELARPLSLSLRLFGNMFAGHIIL-----LLLAGLAPFLLLGVLSLLLPVAWTAFELLV 190

                         170
                  ....*....|....*...
gi 2201038922 208 AIIQAYVFVLLLSLYLQE 225
Cdd:COG0356   191 GFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 2.12e-113

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 323.75  E-value: 2.12e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922   1 MALNLFDQFMSPTYLGIPLIAIALTLPWILIPTPTNRYQTNRLVSLQNWFIKTFTQQLLTPLNKGGHKWATILASLMIFI 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  81 LMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIIIETISLFIRPLALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201038922 161 LTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-227 3.10e-100

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 290.33  E-value: 3.10e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922   1 MALNLFDQFMSPTYLGIPLIAIALTLPWILIPTPTNRYQTNRLVSLQNWFIKTFTQQLLTPLNKGGHKWATILASLMIFI 80
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  81 LMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIIIETISLFIRPLALGVR 160
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201038922 161 LTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-227 1.74e-91

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 268.23  E-value: 1.74e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922   1 MALNLFDQFMSPTYLGIPLIAIALTLPWILIPTPTNRYQTNRLVSLQNWFIKTFTQQLLTPLNKGGHKWATILASLMIFI 80
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  81 LMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIIIETISLFIRPLALGVR 160
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201038922 161 LTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-227 3.72e-79

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 236.77  E-value: 3.72e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922   1 MALNLFDQFMSPTYLGIPLIAIALTLPWILIPTPTNRYQTNRLVSLQNWFIKTFTQQLLTPLNKGGHKWATILASLMIFI 80
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  81 LMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIIIETISLFIRPLALGVR 160
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201038922 161 LTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00179  161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 6.82e-64

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 197.87  E-value: 6.82e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922   1 MALNLFDQFMSPTYLGIPLIAIALTLPWILIPTPtNRYQTNRLVSLQNWFIKTFTQQLLTPLNKGGHKWATILASLMIFI 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTP-NRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  81 LMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIIIETISLFIRPLALGVR 160
Cdd:MTH00101   80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201038922 161 LTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQEN 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 1.17e-40

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: 138.49  E-value: 1.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922   5 LFDQFMSPTY----LGIPLIAIALTLPWILIPTPTNRY-QTNRLVSLQNWFIKTFTQQLLTPLNKGGHKWATILASLMIF 79
Cdd:TIGR01131   1 LFSQFDISPItlfsLTLLSLILLLSLLIFLISSSLSRWlIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  80 ILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIIIETISLFIRPLALGV 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201038922 160 RLTANLTAGHLLIQLISTATITLLPMMttVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 227
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 4-227 1.82e-38

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 133.17  E-value: 1.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922   4 NLFDQFMSPTYLGIPL--IAIALTLPWILIPTPTNRYQTnRLVSLQNWFIKTFTQQLLTPLNKGGHKWATILASLMIFIL 81
Cdd:MTH00035    6 SIFGQFSPDTILFIPLtlLSSVIALSWLFFINPTNWLPS-RSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  82 MLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIIIETISLFIRPLALGVRL 161
Cdd:MTH00035   85 SINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201038922 162 TANLTAGHLLIQLISTAtITLLPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00035  165 AANLTAGHLLIFLLSTA-IWELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 1.95e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 122.45  E-value: 1.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922   1 MALNLFDQFMSPTYLGIPLIAIALTLPWI-LIPTPTNRY-QTNRLVSLQNWFIKTFTQQLLTPLNKGGHKWATILASLMI 78
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFSMISLSWITLLLfLLLMPSSVWfCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  79 FILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIIIETISLFIRPLALG 158
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201038922 159 VRLTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQEN 226
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 3.90e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 121.43  E-value: 3.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922   1 MALNLFDQFMSPTYLGIPLIAIALTLPWILIPTPTNrYQTNRLVSLQNWFIKTFTQQLLTPLNKGGHKWATILASLMIFI 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFW-LIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  81 LMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIIIETISLFIRPLALGVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201038922 161 LTANLTAGHLLIQLISTATITLLPMMTTVatlTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQE 225
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSI---LILIQILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-224 9.52e-30

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: 108.26  E-value: 9.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  66 GHKWATILASLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIII 145
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2201038922 146 ETISLFIRPLALGVRLTANLTAGHLLIQLISTATITllpMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQ 224
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPS---LLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 6-225 5.21e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 105.72  E-value: 5.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922   6 FDQFMSPTYLGIPLIAIALTLPWILIPTPTnRYQTNRLVSLQNWFIKTFTQQLLTPLNKGGHKWATILASLMIFILMLNI 85
Cdd:MTH00173    9 FDDHNSSFSSLSFLMWLLSLMSLFFFSSSV-WVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  86 LGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIIIETISLFIRPLALGVRLTANL 165
Cdd:MTH00173   88 SGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANI 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201038922 166 TAGHLLIQLI-STATITLLPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQE 225
Cdd:MTH00173  168 SAGHIVLTLIgNYLSSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_A pfam00119
ATP synthase A chain;
19-224 7.89e-26

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 99.87  E-value: 7.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  19 LIAIALTLPWILIPTP-TNRYQTNRLVSLQNWFIKTFTQQLLTPL-NKGGHKWATILASLMIFILMLNILGLL---PYTF 93
Cdd:pfam00119   5 LIVALILLLFLLLATRkTKKLVPGRLQNFVEMLVEFVDNIVKDNIgKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  94 TPTTQLSLNMGLAVPLWLATVIIGLRNQPTAA-LGHLLPEGTPTPLIPILIIIETISLFIRPLALGVRLTANLTAGHLLI 172
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2201038922 173 QLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 6-222 2.72e-22

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 90.95  E-value: 2.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922   6 FDQFMSPTYLGI-PLIAIALTLPWILIPTPTNRYQTNRLVSLQNWFIKTFTQQLLTPLNKGGHKWATILASLMIFILMLN 84
Cdd:MTH00005    9 FDPATNSLFNNLsSTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  85 ILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIIIETISLFIRPLALGVRLTAN 164
Cdd:MTH00005   89 LSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAAN 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2201038922 165 LTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLY 222
Cdd:MTH00005  169 MSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 1-223 6.42e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 87.40  E-value: 6.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922   1 MALNLFDQFMSPTYLGIPLIAIALTLPWILIPTPTNRYQT--NRLVSLQNWFIKTFTQQLLTPLNKGGHKWATILASLMI 78
Cdd:MTH00172    1 MSSSYFDQFNIVWLIGLTNSSIMMILVIIVVLLLFKGIKLipKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  79 FILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILIIIETISLFIRPLALG 158
Cdd:MTH00172   81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201038922 159 VRLTANLTAGHLLIQLISTATITLLPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYL 223
Cdd:MTH00172  161 VRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYL 225
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 62-227 3.81e-20

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 85.44  E-value: 3.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  62 LNKGGHKWATILASLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPI 141
Cdd:MTH00175   75 LGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPF 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922 142 LIIIETISLFIRPLALGVRLTANLTAGHLLIQLISTATITLLPM-MTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLS 220
Cdd:MTH00175  155 LVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNgLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTT 234


                  ....*..
gi 2201038922 221 LYLQENV 227
Cdd:MTH00175  235 IYLGDTI 241
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 49-225 4.83e-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: 76.27  E-value: 4.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  49 WFIKTFTQQLLTPLNKGGHKWATILASLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAA-LG 127
Cdd:COG0356    37 MLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922 128 HLLPEGTPTPLIPILIIIETiSLFIRPLALGVRLTANLTAGHLLIqlistATITLLPMMTTVATLTAILLVLLTLLEVAV 207
Cdd:COG0356   117 HLFFPPFPWLAPLMLPIEII-SELARPLSLSLRLFGNMFAGHIIL-----LLLAGLAPFLLLGVLSLLLPVAWTAFELLV 190

                         170
                  ....*....|....*...
gi 2201038922 208 AIIQAYVFVLLLSLYLQE 225
Cdd:COG0356   191 GFLQAYIFTMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 64-225 3.69e-14

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 69.05  E-value: 3.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  64 KGGHKWATILASLMIFILMLNILGLLP-YTFTPTTQLSLNMGLAVPLWLATVIIGLRNQptaALGHLLPEgTPTPLIPIL 142
Cdd:PRK05815   67 GKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKE-FYLQPHPLL 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922 143 IIIETISLFIRPLALGVRLTANLTAGHLLIQLIStatiTLLPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLY 222
Cdd:PRK05815  143 LPIEIISEFSRPISLSLRLFGNMLAGELILALIA----LLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVY 218


                  ...
gi 2201038922 223 LQE 225
Cdd:PRK05815  219 ISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 63-227 3.08e-13

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 66.89  E-value: 3.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  63 NKGGHKWATILaSLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPIL 142
Cdd:MTH00174   85 NKGGNYLAFVL-SLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLL 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922 143 IIIETISLFIRPLALGVRLTANLTAGHLLIQLISTATITLLPMMTTV-ATLTAILLVLLTLLEVAVAIIQAYVFVLLLSL 221
Cdd:MTH00174  164 TIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPFAILIFVTILEMAVAIIQAYVFTLLTIV 243


                  ....*.
gi 2201038922 222 YLQENV 227
Cdd:MTH00174  244 YLRDTV 249
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 64-223 1.32e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 57.06  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  64 KGGHKWATILASLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPILI 143
Cdd:PRK13419  165 HGYEKFLPYLLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGTHWSLWIIMI 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922 144 IIETISLFIRPLALGVRLTANLTAGHLLI-QLISTATITLLPMMTtvATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLY 222
Cdd:PRK13419  245 PIEFIGLFTKPFALTVRLFANMTAGHIVIlSLIFISFILKSYIVA--VAVSVPFAIFIYLLELFVAFLQAYIFTMLSALF 322


                  .
gi 2201038922 223 L 223
Cdd:PRK13419  323 I 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 75-225 3.48e-09

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 54.60  E-value: 3.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  75 SLMIFILMLNILGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQptAALGHLLP-EGTPTPLIPILIIIETISLFIR 153
Cdd:MTH00087   57 FTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKS--EKFSVYLSkGSDSFLKTFSMLFVEIVSELSR 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2201038922 154 PLALGVRLTANLTAGHLLIQLISTATITLLPMMttvatltaillVLLTLLEVAVAIIQAYVFVLLLSLYLQE 225
Cdd:MTH00087  135 PLALTLRLTVNLMVGHLISSLLNFLGEKYVWLS-----------ILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 62-223 2.78e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 38.33  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922  62 LNKGGHKWATILASLMIFILMLNILGLLPYT-----------------------------------FTPTTQLSLNMGLA 106
Cdd:PRK13417  150 MHGHGHSYYHYIFTLFFFILFCNLMGLVPSVgeltvvasdygglvalgvmdhtphalptfakvwsgITVTGDISVTMTLA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201038922 107 VPLWLATVIIGLRNQPTAALGHLLPEGTPTPLIPIL-IIIETISLFIRPLALGVRLTANLTAGHLLIqlISTATITLLPM 185
Cdd:PRK13417  230 LLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMwPLEFIVSPMAKTFALTVRLLANMTAGHVII--LALMGFIFQFQ 307

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2201038922 186 MTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYL 223
Cdd:PRK13417  308 SWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH