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Conserved domains on  [gi|313666483|ref|YP_004061416|]
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ATP synthase F0 subunit 6 (mitochondrion) [Protopterus aethiopicus]

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 1.79e-123

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177190  Cd Length: 227  Bit Score: 349.17  E-value: 1.79e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTSPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313666483 161 LTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-227 1.79e-123

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 349.17  E-value: 1.79e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTSPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313666483 161 LTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 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 ...
6-227 8.48e-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: 161.99  E-value: 8.48e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483    6 FDQFLSP--TILGIPLIMLSLILP--WLLYPTSPNRWL-SNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:TIGR01131   2 FSQFDISpiTLFSLTLLSLILLLSllIFLISSSLSRWLiPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:TIGR01131  82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313666483  161 LTANLTAGHLLMQLIATAVFFLASVMptIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
66-224 2.33e-37

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: 127.90  E-value: 2.33e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  66 GHKWAAILTSLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVI 145
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313666483 146 ETISLFIRPLALGVRLTANLTAGHLLMQLIATAVFFLASVmptIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQ 224
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
66-224 4.67e-32

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 116.05  E-value: 4.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   66 GHKWAAILTSLMILLISINLLGLL---PYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTS-IGHLLPE*TPNLLIPA 141
Cdd:pfam00119  54 GRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  142 LVVIETISLFIRPLALGVRLTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTL 221
Cdd:pfam00119 134 LLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAV 213

                  ...
gi 313666483  222 YLQ 224
Cdd:pfam00119 214 YIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
61-225 8.63e-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: 8.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  61 PINQQGHKWAAILTSLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTS-IGHLLPE*TPnLLI 139
Cdd:COG0356   49 TIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 140 PALVVIETISLFIRPLALGVRLTANLTAGHLLMQLIATAVFFLASVMPTIALltytvLFLLTILELAVAMIQAYVFVLLL 219
Cdd:COG0356  128 PLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL-----PVAWTAFELLVGFLQAYIFTMLT 202

                 ....*.
gi 313666483 220 TLYLQE 225
Cdd:COG0356  203 AVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-227 1.79e-123

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 349.17  E-value: 1.79e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTSPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313666483 161 LTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
1-227 5.62e-113

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 322.69  E-value: 5.62e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTSPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313666483 161 LTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
1-227 2.44e-106

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 305.60  E-value: 2.44e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTSPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313666483 161 LTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
1-226 6.26e-89

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 261.81  E-value: 6.26e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTSPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313666483 161 LTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQEN 226
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 5.99e-80

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 238.70  E-value: 5.99e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTsPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPT-PNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:MTH00101  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313666483 161 LTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQEN 226
Cdd:MTH00101 160 LTANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
4-227 1.46e-51

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 166.69  E-value: 1.46e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   4 SFFDQFLSPTILGIPLIMLSLI--LPWLLYPTSPNrWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILLI 81
Cdd:MTH00035   6 SIFGQFSPDTILFIPLTLLSSViaLSWLFFINPTN-WLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILIL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  82 SINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVRL 161
Cdd:MTH00035  85 SINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRL 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313666483 162 TANLTAGHLLMQLIATAVFFLASVmPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:MTH00035 165 AANLTAGHLLIFLLSTAIWELSNS-PLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
6-227 8.48e-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: 161.99  E-value: 8.48e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483    6 FDQFLSP--TILGIPLIMLSLILP--WLLYPTSPNRWL-SNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:TIGR01131   2 FSQFDISpiTLFSLTLLSLILLLSllIFLISSSLSRWLiPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:TIGR01131  82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313666483  161 LTANLTAGHLLMQLIATAVFFLASVMptIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-225 4.74e-42

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 141.84  E-value: 4.74e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTSpnRWLS-NRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMIL 79
Cdd:MTH00157   1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSS--FWLIpSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  80 LISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGV 159
Cdd:MTH00157  79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313666483 160 RLTANLTAGHLLMQLIATAVFFLASVMPTIALLTytvLFLLTILELAVAMIQAYVFVLLLTLYLQE 225
Cdd:MTH00157 159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILI---QILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
1-226 7.41e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 136.70  E-value: 7.41e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTSPNRW--LSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMI 78
Cdd:MTH00176   1 MLVDLFSSFDPPNKNIFSMISLSWITLLLFLLLMPSSVwfCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  79 LLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALG 158
Cdd:MTH00176  81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313666483 159 VRLTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQEN 226
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
4-225 9.47e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 136.53  E-value: 9.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   4 SFFDQFLSPTILGIPLIMLSLILPWLLYPtSPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILLISI 83
Cdd:MTH00173   7 SSFDDHNSSFSSLSFLMWLLSLMSLFFFS-SSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  84 NLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVRLTA 163
Cdd:MTH00173  86 NLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLA 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313666483 164 NLTAGHLLMQLIATAV-FFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQE 225
Cdd:MTH00173 166 NISAGHIVLTLIGNYLsSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
66-224 2.33e-37

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: 127.90  E-value: 2.33e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  66 GHKWAAILTSLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVI 145
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313666483 146 ETISLFIRPLALGVRLTANLTAGHLLMQLIATAVFFLASVmptIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQ 224
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
66-224 4.67e-32

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 116.05  E-value: 4.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   66 GHKWAAILTSLMILLISINLLGLL---PYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTS-IGHLLPE*TPNLLIPA 141
Cdd:pfam00119  54 GRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  142 LVVIETISLFIRPLALGVRLTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTL 221
Cdd:pfam00119 134 LLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAV 213

                  ...
gi 313666483  222 YLQ 224
Cdd:pfam00119 214 YIS 216
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
70-222 7.55e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 113.29  E-value: 7.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  70 AAILTSLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETIS 149
Cdd:MTH00005  74 SSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETIS 153
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313666483 150 LFIRPLALGVRLTANLTAGHLLMQLIA--TAVFFLASVMPTIALLTYTVLFLLtiLELAVAMIQAYVFVLLLTLY 222
Cdd:MTH00005 154 ILVRPITLSFRLAANMSAGHIVLSLIGiyAASALFSSISSTILLILTQMGYIL--FEVGICLIQAYIFCLLLSLY 226
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
1-227 3.32e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 111.67  E-value: 3.32e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   1 MTLSFFDQFLSPTILGI--PLIMLSLILPWLLYPTSPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMI 78
Cdd:MTH00172   1 MSSSYFDQFNIVWLIGLtnSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  79 LLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALG 158
Cdd:MTH00172  81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313666483 159 VRLTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:MTH00172 161 VRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTI 229
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
1-227 6.79e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 108.56  E-value: 6.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483   1 MTLSFFDQFLSPTILGIP---------------LIMLSLILPWLLYPTS---PNRWLSNRLLTLENwfifrttAQLMVPI 62
Cdd:MTH00175   1 MLAAYFDQFNIIRLITIQaflgdwlvtftnssmMMVLAVIIFWLLLKGDkliPNRWQSIMELIYLN-------IRSVVHD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  63 N--QQGHKWAAILTSLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIP 140
Cdd:MTH00175  74 NlgKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 141 ALVVIETISLFIRPLALGVRLTANLTAGHLLMQLIATAVF-FLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLL 219
Cdd:MTH00175 154 FLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFnMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLT 233

                 ....*...
gi 313666483 220 TLYLQENI 227
Cdd:MTH00175 234 TIYLGDTI 241
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
61-225 8.63e-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: 8.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  61 PINQQGHKWAAILTSLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTS-IGHLLPE*TPnLLI 139
Cdd:COG0356   49 TIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 140 PALVVIETISLFIRPLALGVRLTANLTAGHLLMQLIATAVFFLASVMPTIALltytvLFLLTILELAVAMIQAYVFVLLL 219
Cdd:COG0356  128 PLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL-----PVAWTAFELLVGFLQAYIFTMLT 202

                 ....*.
gi 313666483 220 TLYLQE 225
Cdd:COG0356  203 AVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
62-225 2.54e-20

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 85.62  E-value: 2.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  62 INQQGHKWAAILTSLMILLISINLLGLLP-YTFTPTTQLSMNMGFAVPMWLATVLIGLRNQpttSIGHLLPE*TPNLlIP 140
Cdd:PRK05815  65 IGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HP 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 141 ALVVIETISLFIRPLALGVRLTANLTAGHLLMQLIATAVFFLASVMPTIALLTytvlFLLTILELAVAMIQAYVFVLLLT 220
Cdd:PRK05815 141 LLLPIEIISEFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILP----VAWTIFEIFVGTLQAYIFMMLTI 216

                 ....*
gi 313666483 221 LYLQE 225
Cdd:PRK05815 217 VYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
36-227 3.13e-20

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 85.76  E-value: 3.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  36 NRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVL 115
Cdd:MTH00174  57 NTLVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTL 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 116 IGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVRLTANLTAGHLLMQLIATAVFFLASVMPTI-ALLTY 194
Cdd:MTH00174 137 AGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPF 216
                        170       180       190
                 ....*....|....*....|....*....|...
gi 313666483 195 TVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:MTH00174 217 AILIFVTILEMAVAIIQAYVFTLLTIVYLRDTV 249
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
72-223 6.44e-14

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 69.39  E-value: 6.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  72 ILTSLMILLIsINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLF 151
Cdd:PRK13419 174 LLTVFFFILV-CNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGTHWSLWIIMIPIEFIGLF 252
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313666483 152 IRPLALGVRLTANLTAGHLLMQLIATAVFFLASVMPTIALltyTVLFLLTI--LELAVAMIQAYVFVLLLTLYL 223
Cdd:PRK13419 253 TKPFALTVRLFANMTAGHIVILSLIFISFILKSYIVAVAV---SVPFAIFIylLELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
75-225 1.91e-11

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 60.76  E-value: 1.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  75 SLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSigHLLPE*TPNLLIP-ALVVIETISLFIR 153
Cdd:MTH00087  57 FTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTfSMLFVEIVSELSR 134
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313666483 154 PLALGVRLTANLTAGHLLMQLIATAVFFlasvmptialltYTVLFLLTIL-ELAVAMIQAYVFVLLLTLYLQE 225
Cdd:MTH00087 135 PLALTLRLTVNLMVGHLISSLLNFLGEK------------YVWLSILAIMmECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
94-223 4.80e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 55.28  E-value: 4.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  94 TPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETI-SLFIRPLALGVRLTANLTAGHLLM 172
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 313666483 173 QLIATAVFFLASVMptIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYL 223
Cdd:PRK13417 297 LALMGFIFQFQSWG--IVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
75-223 2.71e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 40.88  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  75 SLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTsiGHLLPE*TPNlliPALVVIETISLFIRP 154
Cdd:PRK13420  80 TLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEGLR--EYLKHYLSPS---PFLLPFHLISEITRT 154
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313666483 155 LALGVRLTANLTAghllMQLIATAVFFLASVMPTIALLtytvlfLLTILElavAMIQAYVFVLLLTLYL 223
Cdd:PRK13420 155 LALAVRLFGNIMS----LELAALLVLLVAGFLVPVPIL------MLHIIE---ALVQAYIFGMLALIYI 210
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
71-218 3.51e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 37.37  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483  71 AILTSLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTsiGHLLPE*TPNLLIPALVVIETISl 150
Cdd:PRK13421  79 ALIGTLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVRARGVR--GYLATFAEPTWVMIPLNLVEQLT- 155
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313666483 151 fiRPLALGVRLTANLTAGhllmqliataVFFLASVMPTIALLtytVLFLLTILELAVAMIQAYVFVLL 218
Cdd:PRK13421 156 --RTFSLIVRLFGNVMSG----------VFVIGIVLSLAGLL---VPIPLMALDLLTGAVQAYIFAVL 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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