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Conserved domains on  [gi|1861254776|gb|QKX65243|]
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ATP synthase F0 subunit 6 (mitochondrion) [Acanthogobius stigmothonus]

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 8.70e-140

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177190  Cd Length: 227  Bit Score: 390.39  E-value: 8.70e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776   1 MSLSFFDQFMSPIWLGIPLIALALVLPWVLFPALSPRWMNNRLLTLQNWFINRFASQMFLPMNLGGHKWALMLTALMLYL 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  81 ITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861254776 161 LTANLTAGHLLMQLIATAAFVLLPLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 8.70e-140

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 390.39  E-value: 8.70e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776   1 MSLSFFDQFMSPIWLGIPLIALALVLPWVLFPALSPRWMNNRLLTLQNWFINRFASQMFLPMNLGGHKWALMLTALMLYL 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  81 ITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861254776 161 LTANLTAGHLLMQLIATAAFVLLPLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYLQENV 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 ...
 4-227 4.79e-53

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: 170.46  E-value: 4.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776   4 SFFDQFMSPIWLGIPLIALALVLPWVLFPALSPRWM-NNRLLTLQNWFINRFASQMFLPMNLGGHKWALMLTALMLYLIT 82
Cdd:TIGR01131   4 QFDISPITLFSLTLLSLILLLSLLIFLISSSLSRWLiPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  83 LNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVRLT 162
Cdd:TIGR01131  84 SNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLF 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861254776 163 ANLTAGHLLMQLIATAAFVLlpLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:TIGR01131 164 ANISAGHLLLTLLSGLLFSL--MSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-224 3.24e-40

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: 135.22  E-value: 3.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  66 GHKWALMLTALMLYLITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIII 145
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861254776 146 ETISLFIRPLALGVRLTANLTAGHLLMQLIATAAFVLLPLmpgVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
19-224 1.67e-35

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 124.91  E-value: 1.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  19 LIALALVLPWVLFPALSPRWMNNRLLTLQNWFINRFASQMFLPMNL-GGHKWALMLTALMLYLITLNMLGLL---PYTFT 94
Cdd:pfam00119   6 IVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKkKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  95 PTTQLSMNMGLAVPLWLATVLIGMRNQPTAA-LGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLMQ 173
Cdd:pfam00119  86 VTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLL 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1861254776 174 LIATAAFVLLPLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 166 LLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 66-225 5.91e-25

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: 97.45  E-value: 5.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  66 GHKWALMLTALMLYLITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAA-LGHLLPEGTPvPLIPVLII 144
Cdd:COG0356    54 GRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776 145 IETISLFIRPLALGVRLTANLTAGHLLMQLIATAAFVLLPLMPGVAIAtaailFLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:COG0356   133 IEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLLP-----VAWTAFELLVGFLQAYIFTMLTAVYIS 207


                  .
gi 1861254776 225 E 225
Cdd:COG0356   208 L 208
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 8.70e-140

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 390.39  E-value: 8.70e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776   1 MSLSFFDQFMSPIWLGIPLIALALVLPWVLFPALSPRWMNNRLLTLQNWFINRFASQMFLPMNLGGHKWALMLTALMLYL 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  81 ITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861254776 161 LTANLTAGHLLMQLIATAAFVLLPLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-227 5.27e-118

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 335.40  E-value: 5.27e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776   1 MSLSFFDQFMSPIWLGIPLIALALVLPWVLFPALSPRWMNNRLLTLQNWFINRFASQMFLPMNLGGHKWALMLTALMLYL 80
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  81 ITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861254776 161 LTANLTAGHLLMQLIATAAFVLLPLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-227 3.01e-109

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 312.91  E-value: 3.01e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776   1 MSLSFFDQFMSPIWLGIPLIALALVLPWVLFPALSPRWMNNRLLTLQNWFINRFASQMFLPMNLGGHKWALMLTALMLYL 80
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  81 ITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861254776 161 LTANLTAGHLLMQLIATAAFVLLPLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-227 5.83e-93

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 271.82  E-value: 5.83e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776   1 MSLSFFDQFMSPIWLGIPLIALALVLPWVLFPALSPRWMNNRLLTLQNWFINRFASQMFLPMNLGGHKWALMLTALMLYL 80
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  81 ITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861254776 161 LTANLTAGHLLMQLIATAAFVLLPLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00179  161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.02e-81

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 243.32  E-value: 1.02e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776   1 MSLSFFDQFMSPIWLGIPLIALALVLPWVLFPAlSPRWMNNRLLTLQNWFINRFASQMFLPMNLGGHKWALMLTALMLYL 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPT-PNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  81 ITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00101   80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861254776 161 LTANLTAGHLLMQLIATAAFVLLPLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYLQEN 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 ...
 4-227 4.79e-53

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: 170.46  E-value: 4.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776   4 SFFDQFMSPIWLGIPLIALALVLPWVLFPALSPRWM-NNRLLTLQNWFINRFASQMFLPMNLGGHKWALMLTALMLYLIT 82
Cdd:TIGR01131   4 QFDISPITLFSLTLLSLILLLSLLIFLISSSLSRWLiPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  83 LNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVRLT 162
Cdd:TIGR01131  84 SNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLF 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861254776 163 ANLTAGHLLMQLIATAAFVLlpLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:TIGR01131 164 ANISAGHLLLTLLSGLLFSL--MSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 4-227 1.64e-50

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 163.99  E-value: 1.64e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776   4 SFFDQFMSPIWLGIPL--IALALVLPWVLFpALSPRWMNNRLLTLQNWFINRFASQMFLPMNLGGHKWALMLTALMLYLI 81
Cdd:MTH00035    6 SIFGQFSPDTILFIPLtlLSSVIALSWLFF-INPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  82 TLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVRL 161
Cdd:MTH00035   85 SINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861254776 162 TANLTAGHLLMQLIATAAFVLLPLmPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00035  165 AANLTAGHLLIFLLSTAIWELSNS-PLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 39-225 1.12e-42

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 143.77  E-value: 1.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  39 MNNRLLTLQNWFINRFASQMFLPMNLGGHKWALMLTALMLYLITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGM 118
Cdd:MTH00157   38 IPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGW 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776 119 RNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLMQLIATAAFVLLPLMPGVAIataAILF 198
Cdd:MTH00157  118 INNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSSMILSILI---LIQI 194

                         170       180
                  ....*....|....*....|....*..
gi 1861254776 199 LLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00157  195 LLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-225 6.99e-42

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 141.93  E-value: 6.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776   1 MSLSFFDQFMSPIWLGIPLIALALVLP-WVLFPALSPRWMN-NRLLTLQNWFINRFASQMFLPMNLGGHKWALMLTALML 78
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSSLSFLMWLLSlMSLFFFSSSVWVSsSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  79 YLITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALG 158
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861254776 159 VRLTANLTAGHLLMQLIA-TAAFVLLPLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGnYLSSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-224 3.24e-40

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: 135.22  E-value: 3.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  66 GHKWALMLTALMLYLITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIII 145
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861254776 146 ETISLFIRPLALGVRLTANLTAGHLLMQLIATAAFVLLPLmpgVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 5.54e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 134.39  E-value: 5.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776   1 MSLSFFDQFMSPIWLGIPLIALALVLPWVLFPALSPRW--MNNRLLTLQNWFINRFASQMFLPMNLGGHKWALMLTALML 78
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFSMISLSWITLLLFLLLMPSSVwfCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  79 YLITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALG 158
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861254776 159 VRLTANLTAGHLLMQLIATAAFVLLPLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP-synt_A pfam00119
ATP synthase A chain;
19-224 1.67e-35

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 124.91  E-value: 1.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  19 LIALALVLPWVLFPALSPRWMNNRLLTLQNWFINRFASQMFLPMNL-GGHKWALMLTALMLYLITLNMLGLL---PYTFT 94
Cdd:pfam00119   6 IVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKkKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  95 PTTQLSMNMGLAVPLWLATVLIGMRNQPTAA-LGHLLPEGTPVPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLMQ 173
Cdd:pfam00119  86 VTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLL 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1861254776 174 LIATAAFVLLPLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 166 LLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 1-223 3.45e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 116.68  E-value: 3.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776   1 MSLSFFDQF--MSPIWLGIPLIALALVLPWVLFPALSPRWMNNRLLTLQNWFINRFASQMFLPMNLGGHKWALMLTALML 78
Cdd:MTH00172    1 MSSSYFDQFniVWLIGLTNSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  79 YLITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLFIRPLALG 158
Cdd:MTH00172   81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861254776 159 VRLTANLTAGHLLMQLIATAAFVLLPLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYL 223
Cdd:MTH00172  161 VRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYL 225
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 72-222 2.83e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 114.44  E-value: 2.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  72 MLTALMLYLITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLF 151
Cdd:MTH00005   76 LISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISIL 155

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861254776 152 IRPLALGVRLTANLTAGHLLMQLIATAAFVLLPLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLY 222
Cdd:MTH00005  156 VRPITLSFRLAANMSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 63-227 8.33e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 105.86  E-value: 8.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  63 NLG--GHKWALMLTALMLYLITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIP 140
Cdd:MTH00175   74 NLGksGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAP 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776 141 VLIIIETISLFIRPLALGVRLTANLTAGHLLMQLIATAAF-VLLPLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLL 219
Cdd:MTH00175  154 FLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFnMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLT 233


                  ....*...
gi 1861254776 220 SLYLQENV 227
Cdd:MTH00175  234 TIYLGDTI 241
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 66-225 5.91e-25

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: 97.45  E-value: 5.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  66 GHKWALMLTALMLYLITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAA-LGHLLPEGTPvPLIPVLII 144
Cdd:COG0356    54 GRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776 145 IETISLFIRPLALGVRLTANLTAGHLLMQLIATAAFVLLPLMPGVAIAtaailFLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:COG0356   133 IEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLLP-----VAWTAFELLVGFLQAYIFTMLTAVYIS 207


                  .
gi 1861254776 225 E 225
Cdd:COG0356   208 L 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 66-225 4.78e-22

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 90.24  E-value: 4.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  66 GHKWALMLTALMLYLITLNMLGLLP-YTFTPTTQLSMNMGLAVPLWLATVLIGMRNQptaALGHLLPEGTPVPlIPVLII 144
Cdd:PRK05815   69 GKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLP 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776 145 IETISLFIRPLALGVRLTANLTAGHLLMQLIATAAFVLLPLMPGVAIATAAilflLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:PRK05815  145 IEIISEFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILPVA----WTIFEIFVGTLQAYIFMMLTIVYIS 220


                  .
gi 1861254776 225 E 225
Cdd:PRK05815  221 M 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 63-227 5.69e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 87.69  E-value: 5.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  63 NLGGHKWALMLTALMLYLITlNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVL 142
Cdd:MTH00174   85 NKGGNYLAFVLSLFILILFG-NGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLL 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776 143 IIIETISLFIRPLALGVRLTANLTAGHLLMQLIATAAFVLLPLMPGV-AIATAAILFLLTILEVAVAMIQAYVFVLLLSL 221
Cdd:MTH00174  164 TIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPFAILIFVTILEMAVAIIQAYVFTLLTIV 243


                  ....*.
gi 1861254776 222 YLQENV 227
Cdd:MTH00174  244 YLRDTV 249
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 72-223 7.65e-16

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 75.16  E-value: 7.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  72 MLTALMLYLItLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETISLF 151
Cdd:PRK13419  174 LLTVFFFILV-CNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGTHWSLWIIMIPIEFIGLF 252

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861254776 152 IRPLALGVRLTANLTAGHLLMQLIATAAFVLLPLMPGVAIATAAILFLLtILEVAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13419  253 TKPFALTVRLFANMTAGHIVILSLIFISFILKSYIVAVAVSVPFAIFIY-LLELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 76-225 1.23e-12

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 64.23  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  76 LMLYLITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQptAALGHLLPEGTPVPLIP-VLIIIETISLFIRP 154
Cdd:MTH00087   58 TFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKS--EKFSVYLSKGSDSFLKTfSMLFVEIVSELSRP 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861254776 155 LALGVRLTANLTAGHLLMQLIATAAFVLLplmpgvaiataaILFLLTIL-EVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00087  136 LALTLRLTVNLMVGHLISSLLNFLGEKYV------------WLSILAIMmECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 94-223 9.39e-11

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 60.29  E-value: 9.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  94 TPTTQLSMNMGLAVPLWLATVLIGMRNQPTAALGHLLPEGTPVPLIPVLIIIETI-SLFIRPLALGVRLTANLTAGHLLm 172
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVI- 295

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1861254776 173 qLIATAAFVLLPLMPGVAIATAAILFLLTILEVAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13417  296 -ILALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 76-223 8.20e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 39.34  E-value: 8.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  76 LMLYLITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQP-TAALGHLLPEGtpvpliPVLIIIETISLFIRP 154
Cdd:PRK13420   81 LWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEGlREYLKHYLSPS------PFLLPFHLISEITRT 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861254776 155 LALGVRLTANLTAghllMQLIAtaafvLLPLMPGVAIATAAILflltILEVAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13420  155 LALAVRLFGNIMS----LELAA-----LLVLLVAGFLVPVPIL----MLHIIEALVQAYIFGMLALIYI 210
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
 76-218 8.35e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 39.29  E-value: 8.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254776  76 LMLYLITLNMLGLLPYTFTPTTQLSMNMGLAVPLWLATVLIGMRNQptAALGHLLPEGTPVPLIPVLIIIETISlfiRPL 155
Cdd:PRK13421   84 LFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVRAR--GVRGYLATFAEPTWVMIPLNLVEQLT---RTF 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861254776 156 ALGVRLTANLTAGHLLMQLIATAA--FVLLPLMPgvaiataailflltiLEVAVAMIQAYVFVLL 218
Cdd:PRK13421  159 SLIVRLFGNVMSGVFVIGIVLSLAglLVPIPLMA---------------LDLLTGAVQAYIFAVL 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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