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Conserved domains on  [gi|2505717300|gb|WHI93297|]
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ATP synthase F0 subunit 6 (mitochondrion) [Mussismilia hispida]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009609)

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 MTH00172
ATP synthase F0 subunit 6; Provisional
2-225 1.21e-98

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214447  Cd Length: 232  Bit Score: 286.55  E-value: 1.21e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300   2 SGSSYFEQFNVVWLFGLTNSAIMMFLVIFVVLLFLKGVDLIPKRWQSFFELVCFHFYYVAKENLGVEGLKFFPFILSLFF 81
Cdd:MTH00172    1 MSSSYFDQFNIVWLIGLTNSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  82 FLVFLNIFGLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIETVSYFSRAISLG 161
Cdd:MTH00172   81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2505717300 162 VRLAANLSAGHLLFAILAGFGVIFKSA--------IVIMVFITLLEIAVAIIQAYVFCLLTTIYLADTLVLH 225
Cdd:MTH00172  161 VRLAANLSAGHLLFAILAGFGFNMLCAsgflslfpLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTIVLH 232
 
Name Accession Description Interval E-value
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
2-225 1.21e-98

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 286.55  E-value: 1.21e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300   2 SGSSYFEQFNVVWLFGLTNSAIMMFLVIFVVLLFLKGVDLIPKRWQSFFELVCFHFYYVAKENLGVEGLKFFPFILSLFF 81
Cdd:MTH00172    1 MSSSYFDQFNIVWLIGLTNSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  82 FLVFLNIFGLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIETVSYFSRAISLG 161
Cdd:MTH00172   81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2505717300 162 VRLAANLSAGHLLFAILAGFGVIFKSA--------IVIMVFITLLEIAVAIIQAYVFCLLTTIYLADTLVLH 225
Cdd:MTH00172  161 VRLAANLSAGHLLFAILAGFGFNMLCAsgflslfpLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTIVLH 232
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
7-220 3.32e-44

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: 147.74  E-value: 3.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300   7 FEQFN--VVWLFGLTNSAIMMFLVIFVVLLFLKGVD-LIPKRWQSFFELVCFHFYYVAKENLGVEGLKFFPFILSLFFFL 83
Cdd:TIGR01131   2 FSQFDisPITLFSLTLLSLILLLSLLIFLISSSLSRwLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  84 VFLNIFGLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIETVSYFSRAISLGVR 163
Cdd:TIGR01131  82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2505717300 164 LAANLSAGHLLFAILAGF------GVIFKSAIVIMVFITLLEIAVAIIQAYVFCLLTTIYLAD 220
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLlfslmsSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
69-219 5.01e-32

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: 114.03  E-value: 5.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  69 GLKFFPFILSLFFFLVFLNIFGLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLI 148
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2505717300 149 ETVSYFSRAISLGVRLAANLSAGHLLFAILAGFGVIFKS-----AIVIMVFITLLEIAVAIIQAYVFCLLTTIYLA 219
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSsvgllPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
23-219 1.46e-28

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 106.81  E-value: 1.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  23 IMMFLVIFVVLLFL-----KGVDLIPKRWQSFFELVCFHFYYVAKENLGVEGLKFFPFILSLFFFLVFLN----IFGLCP 93
Cdd:pfam00119   2 LMSLIVALILLLFLllatrKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSnllgLIPKSP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  94 YVFTPTTHIIVTLGFSFSIIIGITLSGLLR--FKKDFFSILMPSgAPLILAPLLVLIETVSYFSRAISLGVRLAANLSAG 171
Cdd:pfam00119  82 GGFTVTADINVTLALALIVFLLVHYYGIKKhgLGGYFKKLFVPP-VPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2505717300 172 HLLFAILAGFGVIFKSA--------IVIMVFITLLEIAVAIIQAYVFCLLTTIYLA 219
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAgfllgvipPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
21-220 2.26e-28

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: 106.31  E-value: 2.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  21 SAIMMFLVIFVVLLFLKGVDLIPKRWQSFFELVCFHFYYVAKENLGVEGLKFFPFILSLFFFLVFLNIFGLCPYVFTPTT 100
Cdd:COG0356     6 SWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300 101 HIIVTLGFSFSIIIGITLSGLLR--FKKDFFSILMPSGAPliLAPLLVLIETVSYFSRAISLGVRLAANLSAGHLLFAIL 178
Cdd:COG0356    86 DINVTLALALIVFVLVHYYGIKKkgLGGYLKHLFFPPFPW--LAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLL 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2505717300 179 AGFGVIFKSAIV---IMVFITLLEIAVAIIQAYVFCLLTTIYLAD 220
Cdd:COG0356   164 AGLAPFLLLGVLsllLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
2-225 1.21e-98

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 286.55  E-value: 1.21e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300   2 SGSSYFEQFNVVWLFGLTNSAIMMFLVIFVVLLFLKGVDLIPKRWQSFFELVCFHFYYVAKENLGVEGLKFFPFILSLFF 81
Cdd:MTH00172    1 MSSSYFDQFNIVWLIGLTNSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  82 FLVFLNIFGLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIETVSYFSRAISLG 161
Cdd:MTH00172   81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2505717300 162 VRLAANLSAGHLLFAILAGFGVIFKSA--------IVIMVFITLLEIAVAIIQAYVFCLLTTIYLADTLVLH 225
Cdd:MTH00172  161 VRLAANLSAGHLLFAILAGFGFNMLCAsgflslfpLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTIVLH 232
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
4-225 6.57e-79

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 236.83  E-value: 6.57e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300   4 SSYFEQFNVV-----------WLFGLTNSAIMMFLVIFVVLLFLKGVDLIPKRWQSFFELVCFHFYYVAKENLGVEGLKF 72
Cdd:MTH00175    3 AAYFDQFNIIrlitiqaflgdWLVTFTNSSMMMVLAVIIFWLLLKGDKLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  73 FPFILSLFFFLVFLNIFGLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIETVS 152
Cdd:MTH00175   83 FPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300 153 YFSRAISLGVRLAANLSAGHLLFAILAGF-------GVIFKS--AIVIMVFITLLEIAVAIIQAYVFCLLTTIYLADTLV 223
Cdd:MTH00175  163 YLIRAISLGVRLAANISAGHLLFAILSGFafnmlsnGLIILSlfPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGDTIA 242

                  ..
gi 2505717300 224 LH 225
Cdd:MTH00175  243 LH 244
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
7-220 3.32e-44

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: 147.74  E-value: 3.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300   7 FEQFN--VVWLFGLTNSAIMMFLVIFVVLLFLKGVD-LIPKRWQSFFELVCFHFYYVAKENLGVEGLKFFPFILSLFFFL 83
Cdd:TIGR01131   2 FSQFDisPITLFSLTLLSLILLLSLLIFLISSSLSRwLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  84 VFLNIFGLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIETVSYFSRAISLGVR 163
Cdd:TIGR01131  82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2505717300 164 LAANLSAGHLLFAILAGF------GVIFKSAIVIMVFITLLEIAVAIIQAYVFCLLTTIYLAD 220
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLlfslmsSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
4-225 1.86e-43

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 146.62  E-value: 1.86e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300   4 SSYFEQFNVV-----WLFGL-----------TNSAIMM-FLVIFVVLLFLKGVD--LIPKRWQSFFELVCFHFYYVAKEN 64
Cdd:MTH00174    3 AAYFDQFNIIpifsiWVYFLsfwingeffcfTNTFFMMsFAVFLFYTIGAKGNNntLVPNRILVGLELIYSHFYTVLKDN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  65 LGVEGLKFFPFILSLFFFLVFLNIFGLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPL 144
Cdd:MTH00174   83 LGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300 145 LVLIETVSYFSRAISLGVRLAANLSAGHLLFAILAGF-------GVIFKSAI--VIMVFITLLEIAVAIIQAYVFCLLTT 215
Cdd:MTH00174  163 LTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFawkmintGILIGSFVpfAILIFVTILEMAVAIIQAYVFTLLTI 242
                         250
                  ....*....|
gi 2505717300 216 IYLADTLVLH 225
Cdd:MTH00174  243 VYLRDTVELH 252
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
4-221 1.76e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 122.58  E-value: 1.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300   4 SSYFEQFNVVWLFGLTNSAIMMFLVIFVVLLFLKgvdLIPKRWQSFFELVCFHFYYVAKENLGVEGLKFFPFILSLFFFL 83
Cdd:MTH00157    3 TNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFW---LIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  84 VFLNIFGLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIETVSYFSRAISLGVR 163
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2505717300 164 LAANLSAGHLLFAILAGFGVIFKSAIVIMVFIT-----LLEIAVAIIQAYVFCLLTTIYLADT 221
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIqilllILESAVAIIQSYVFSVLSTLYSSEV 222
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
69-219 5.01e-32

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: 114.03  E-value: 5.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  69 GLKFFPFILSLFFFLVFLNIFGLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLI 148
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2505717300 149 ETVSYFSRAISLGVRLAANLSAGHLLFAILAGFGVIFKS-----AIVIMVFITLLEIAVAIIQAYVFCLLTTIYLA 219
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSsvgllPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
23-219 1.46e-28

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 106.81  E-value: 1.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  23 IMMFLVIFVVLLFL-----KGVDLIPKRWQSFFELVCFHFYYVAKENLGVEGLKFFPFILSLFFFLVFLN----IFGLCP 93
Cdd:pfam00119   2 LMSLIVALILLLFLllatrKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSnllgLIPKSP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  94 YVFTPTTHIIVTLGFSFSIIIGITLSGLLR--FKKDFFSILMPSgAPLILAPLLVLIETVSYFSRAISLGVRLAANLSAG 171
Cdd:pfam00119  82 GGFTVTADINVTLALALIVFLLVHYYGIKKhgLGGYFKKLFVPP-VPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2505717300 172 HLLFAILAGFGVIFKSA--------IVIMVFITLLEIAVAIIQAYVFCLLTTIYLA 219
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAgfllgvipPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
21-220 2.26e-28

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: 106.31  E-value: 2.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  21 SAIMMFLVIFVVLLFLKGVDLIPKRWQSFFELVCFHFYYVAKENLGVEGLKFFPFILSLFFFLVFLNIFGLCPYVFTPTT 100
Cdd:COG0356     6 SWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300 101 HIIVTLGFSFSIIIGITLSGLLR--FKKDFFSILMPSGAPliLAPLLVLIETVSYFSRAISLGVRLAANLSAGHLLFAIL 178
Cdd:COG0356    86 DINVTLALALIVFVLVHYYGIKKkgLGGYLKHLFFPPFPW--LAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLL 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2505717300 179 AGFGVIFKSAIV---IMVFITLLEIAVAIIQAYVFCLLTTIYLAD 220
Cdd:COG0356   164 AGLAPFLLLGVLsllLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
90-218 2.67e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 101.10  E-value: 2.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  90 GLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIETVSYFSRAISLGVRLAANLS 169
Cdd:MTH00132   87 GLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLT 166
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2505717300 170 AGHLLFAIL--AGFGVIFKSAIV------IMVFITLLEIAVAIIQAYVFCLLTTIYL 218
Cdd:MTH00132  167 AGHLLIQLIatAAFVLLPLMPTVailtatLLFLLTLLEVAVAMIQAYVFVLLLSLYL 223
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
5-222 3.78e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 100.79  E-value: 3.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300   5 SYFEQFNVVWLFGLTNSAIMMFLVIFVVLLFLKGvdLIPKRWQSFFELVCFHFYYVAKENLGVEGLKFFPFILSLFFFLV 84
Cdd:MTH00179    4 SMFDQFESPSLLGIPLLALALLLPWLLFPSLTNR--WLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  85 FLNIFGLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIETVSYFSRAISLGVRL 164
Cdd:MTH00179   82 TLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVRL 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2505717300 165 AANLSAGHLL--------FAILAGFGVIFKSAIVIMVFITLLEIAVAIIQAYVFCLLTTIYLADTL 222
Cdd:MTH00179  162 TANITAGHLLmhlissavFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
90-218 4.02e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 100.81  E-value: 4.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  90 GLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIETVSYFSRAISLGVRLAANLS 169
Cdd:MTH00073   87 GLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVRLTANLT 166
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2505717300 170 AGHLL--------FAILAGFGVIFKSAIVIMVFITLLEIAVAIIQAYVFCLLTTIYL 218
Cdd:MTH00073  167 AGHLLiqlistatLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYL 223
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
90-218 1.35e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 99.51  E-value: 1.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  90 GLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIETVSYFSRAISLGVRLAANLS 169
Cdd:MTH00120   87 GLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVRLTANLT 166
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2505717300 170 AGHLL--------FAILAGFGVIFKSAIVIMVFITLLEIAVAIIQAYVFCLLTTIYL 218
Cdd:MTH00120  167 AGHLLiqlistatLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYL 223
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
90-220 1.80e-25

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 99.26  E-value: 1.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  90 GLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLlRFK-KDFFSILMPSGAPLILAPLLVLIETVSYFSRAISLGVRLAANL 168
Cdd:MTH00101   86 GLLPHSFTPTTQLSMNLGMAIPLWAGTVITGF-RNKtKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANI 164
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300 169 SAGHLLFAILAGFGVIFKS--------AIVIMVFITLLEIAVAIIQAYVFCLLTTIYLAD 220
Cdd:MTH00101  165 TAGHLLIHLIGGATLALMSistttaliTFIILILLTILEFAVALIQAYVFTLLVSLYLHD 224
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
90-223 7.39e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 97.63  E-value: 7.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  90 GLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIETVSYFSRAISLGVRLAANLS 169
Cdd:MTH00173   89 GLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANIS 168
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2505717300 170 AGHLLFAILAGFGVIF---------KSAIVIMVFITLLEIAVAIIQAYVFCLLTTIYLADTLV 223
Cdd:MTH00173  169 AGHIVLTLIGNYLSSSlfsssvvslLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDEHPV 231
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
90-220 8.42e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 97.50  E-value: 8.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  90 GLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIETVSYFSRAISLGVRLAANLS 169
Cdd:MTH00005   91 GLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMS 170
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2505717300 170 AGHLLFAIL------AGFGVIFKSA--IVIMVFITLLEIAVAIIQAYVFCLLTTIYLAD 220
Cdd:MTH00005  171 AGHIVLSLIgiyaasALFSSISSTIllILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
27-220 3.54e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 95.87  E-value: 3.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  27 LVIFVVLLFLKGVDLIPKRWQSFFELVCFHFYYVAKENLGVEGLKFFPFILSLFFFLVFLNIFGLCPYVFTPTTHIIVTL 106
Cdd:MTH00176   26 TLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFILVMSLNLSGLIPYVFTSTSHLVITL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300 107 GFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIETVSYFSRAISLGVRLAANLSAGHLLFAILAGFG---- 182
Cdd:MTH00176  106 SLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLAVRLAANLSAGHLLLGLLGAAMwgll 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2505717300 183 ----VIFKSAIVIMVFITLLEIAVAIIQAYVFCLLTTIYLAD 220
Cdd:MTH00176  186 pvspLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDE 227
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
13-220 3.42e-23

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 92.94  E-value: 3.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  13 VWLFGLTNSAIMMFLVIFVVLLFL----KGVDLIPKRWQSFFELVCFHFYYVAKENLGVEGLKFFPFILSLFFFLVFLNI 88
Cdd:PRK05815    9 FGGFNFDSLLLSVLLGVLILLLFAlvatRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  89 FGLCP-YVFTPTTHIIVTLGFSFSIIIGITLSGLLRFK-KDFFSILMPSGAPLILApllvlIETVSYFSRAISLGVRLAA 166
Cdd:PRK05815   89 LGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKKGlGGYLKEFYLQPHPLLLP-----IEIISEFSRPISLSLRLFG 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2505717300 167 NLSAGHLLFAILAGFG----VIFKSAIVIMVFITLLEIAVAIIQAYVFCLLTTIYLAD 220
Cdd:PRK05815  164 NMLAGELILALIALLGgaglLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
90-222 2.72e-22

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 90.80  E-value: 2.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  90 GLCPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIETVSYFSRAISLGVRLAANLS 169
Cdd:MTH00035   90 GLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRLAANLT 169
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300 170 AGHLL-------FAILAGFGVIFKSAIVIMVFITLLEIAVAIIQAYVFCLLTTIYLADTL 222
Cdd:MTH00035  170 AGHLLifllstaIWELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
18-225 8.36e-12

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 63.61  E-value: 8.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  18 LTNSAIMMFLVIFVVLLFLKGV---------DLIPKRWQSFFE-LVCFHFYYVAKENLGVEGLKFFPFILSLFFFLVFLN 87
Cdd:PRK13419  106 ITKHVVMMWIASAILLVVFLAAgrkykkmtkSQAPKGLANAMEaLVEFIRLDVAKSNIGHGYEKFLPYLLTVFFFILVCN 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  88 IFGLCPYVFTPTTHIIVTLG---FSFSI--IIGITLSGLlrfkKDFFSILMpSGAPLILAPLLVLIETVSYFSRAISLGV 162
Cdd:PRK13419  186 LLGLVPYGATATGNINVTLTlavFTFFItqYAAIKAHGI----KGYLAHLT-GGTHWSLWIIMIPIEFIGLFTKPFALTV 260
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300 163 RLAANLSAGHLLFAILAGFGVIFKSAIVIMV-------FITLLEIAVAIIQAYVFCLLTTIYLADTLVLH 225
Cdd:PRK13419  261 RLFANMTAGHIVILSLIFISFILKSYIVAVAvsvpfaiFIYLLELFVAFLQAYIFTMLSALFIGLATAHE 330
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
97-225 7.23e-11

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 60.67  E-value: 7.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  97 TPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIE-TVSYFSRAISLGVRLAANLSAGHLLF 175
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEfIVSPMAKTFALTVRLLANMTAGHVII 296
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2505717300 176 AILAGFGVIFKSAIVIMV------FITLLEIAVAIIQAYVFCLLTTIYLADTLVLH 225
Cdd:PRK13417  297 LALMGFIFQFQSWGIVPVsvigsgLIYVLEIFVAFLQAYIFVLLTSLFVGLSMHRH 352
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
90-218 4.63e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 48.44  E-value: 4.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  90 GLCPYVFTPTTHIIVTlgFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPL-LVLIETVSYFSRAISLGVRLAANL 168
Cdd:MTH00087   69 GLFPYSFSPCGMVEFT--FLYALVAWLSTFLSFLSKSEKFSVYLSKGSDSFLKTFsMLFVEIVSELSRPLALTLRLTVNL 146
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2505717300 169 SAGHLLFAILAGFGVIFksaIVIMVFITLLEIAVAIIQAYVFCLLTTIYL 218
Cdd:MTH00087  147 MVGHLISSLLNFLGEKY---VWLSILAIMMECFVAFIQSYIFSRLIYLYL 193
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
92-211 3.78e-06

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 45.65  E-value: 3.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  92 CPYVFTPTTHIIVTLGFSFSIIIGITLSGLLRFKKDFFSILMPSGAPLILAPLLVLIETVSYFSRAISLGVRLAANLSAG 171
Cdd:MTH00050   42 LPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLG 121
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2505717300 172 HLLFAILAGFGVIFKSAIVIMVFITLLEIAVAIIQAYVFC 211
Cdd:MTH00050  122 CFGGVALGNLCFISYWWFLVLFFLFFYEVFVALVHWFIVS 161
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
18-219 2.79e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 40.88  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  18 LTNSAIMMFLVIFVVLLfLKGVDLIPKRWQSFFELVCFHFYYVAKENLGVEGLKFFPFILSLFFFLVFLNIFGLCPYVFT 97
Cdd:PRK13420   21 LTTWGIMIVLVLASWLT-TRRLSLDPGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFVGTLWIFILVANLIGLIPGFHS 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2505717300  98 PTTHIIVTLGFSFSIII-----GITLSGLLRFKKDFFSilmPSgaplilaPLLVLIETVSYFSRAISLGVRLAANLSA-- 170
Cdd:PRK13420  100 PTADLSVTAALALLVFFsvhwfGIRAEGLREYLKHYLS---PS-------PFLLPFHLISEITRTLALAVRLFGNIMSle 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2505717300 171 -GHLLFAILAGFgvifksaiVIMVFITLLEIAVAIIQAYVFCLLTTIYLA 219
Cdd:PRK13420  170 lAALLVLLVAGF--------LVPVPILMLHIIEALVQAYIFGMLALIYIA 211
 
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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