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Conserved domains on  [gi|503090581|ref|WP_013325419|]
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F0F1 ATP synthase subunit A [Gloeothece verrucosa]

Protein Classification

ATP synthase subunit a( domain architecture ID 10000050)

ATP synthase subunit a is a component of the Fo complex of FoF1-ATP synthase found in chloroplasts, and which plays a direct role in the translocation of protons across the membrane

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
atpI CHL00046
ATP synthase CF0 A subunit
13-238 2.73e-140

ATP synthase CF0 A subunit


:

Pssm-ID: 176987  Cd Length: 228  Bit Score: 392.76  E-value: 2.73e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  13 FTLASLEVGKHWYWHIGNLKIHGQVFLTSWFVIGLLLIASVAASSSIKRIPSGIQNLMEYVLEFLRDLAKNQLGEKEYRP 92
Cdd:CHL00046   1 YDISGVEVGQHFYWQIGGFQVHGQVLITSWVVIAILLGSALLATRNLQTIPTGGQNFFEYVLEFIRDLAKTQIGEEEYRP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  93 WLPFIGTLFLFIFVSNWSGALIPWKLIEIPESELAAPTNDINTTVALALLTSLAYFYAGFSKKGLGYFANYVQPIPVLLP 172
Cdd:CHL00046  81 WVPFIGTMFLFIFVSNWSGALLPWKLIELPHGELAAPTNDINTTVALALLTSVAYFYAGLSKKGLGYFGKYIQPTPILLP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503090581 173 IKILEDFTKPLSLSFRLFGNILADELVVAVLVFLVPLFVPLPLMALGLFTSAIQALVFATLAGAYI 238
Cdd:CHL00046 161 INILEDFTKPLSLSFRLFGNILADELVVAVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYI 226
 
Name Accession Description Interval E-value
atpI CHL00046
ATP synthase CF0 A subunit
13-238 2.73e-140

ATP synthase CF0 A subunit


Pssm-ID: 176987  Cd Length: 228  Bit Score: 392.76  E-value: 2.73e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  13 FTLASLEVGKHWYWHIGNLKIHGQVFLTSWFVIGLLLIASVAASSSIKRIPSGIQNLMEYVLEFLRDLAKNQLGEKEYRP 92
Cdd:CHL00046   1 YDISGVEVGQHFYWQIGGFQVHGQVLITSWVVIAILLGSALLATRNLQTIPTGGQNFFEYVLEFIRDLAKTQIGEEEYRP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  93 WLPFIGTLFLFIFVSNWSGALIPWKLIEIPESELAAPTNDINTTVALALLTSLAYFYAGFSKKGLGYFANYVQPIPVLLP 172
Cdd:CHL00046  81 WVPFIGTMFLFIFVSNWSGALLPWKLIELPHGELAAPTNDINTTVALALLTSVAYFYAGLSKKGLGYFGKYIQPTPILLP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503090581 173 IKILEDFTKPLSLSFRLFGNILADELVVAVLVFLVPLFVPLPLMALGLFTSAIQALVFATLAGAYI 238
Cdd:CHL00046 161 INILEDFTKPLSLSFRLFGNILADELVVAVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYI 226
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
36-238 2.19e-53

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: 171.41  E-value: 2.19e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  36 QVFLTSWFVIGLLLIASVAASSSIKRIPSGIQNLMEYVLEFLRDLAKNQLGeKEYRPWLPFIGTLFLFIFVSNWSGaLIP 115
Cdd:COG0356    1 DTVLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIG-KKGRKFAPLLLTLFLFILVSNLLG-LIP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581 116 WklieipeseLAAPTNDINTTVALALLTSLAYFYAGFSKKGL-GYFAN-YVQPI----PVLLPIKILEDFTKPLSLSFRL 189
Cdd:COG0356   79 G---------LFPPTADINVTLALALIVFVLVHYYGIKKKGLgGYLKHlFFPPFpwlaPLMLPIEIISELARPLSLSLRL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503090581 190 FGNILADE--------LVVAVLVFLVPLFVPLPLMALGLFTSAIQALVFATLAGAYI 238
Cdd:COG0356  150 FGNMFAGHiillllagLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206
ATP-synt_A pfam00119
ATP synthase A chain;
39-238 5.55e-46

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 152.64  E-value: 5.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581   39 LTSWFVIGLLLI-ASVAASSSIKRIPSGIQNLMEYVLEFLRDLAKNQLGEKEYRPWLPFIGTLFLFIFVSNWSGaLIPwk 117
Cdd:pfam00119   2 LMSLIVALILLLfLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLG-LIP-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  118 liEIPESelAAPTNDINTTVALALLTSLAYFYAGFSKKGL-GYFANYVQP------IPVLLPIKILEDFTKPLSLSFRLF 190
Cdd:pfam00119  79 --KSPGG--FTVTADINVTLALALIVFLLVHYYGIKKHGLgGYFKKLFVPpvplplVPLLLPIEIISEFARPVSLSLRLF 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503090581  191 GNILADE-------------LVVAVLVFLVPLFVPLPLMALGLFTSAIQALVFATLAGAYI 238
Cdd:pfam00119 155 GNMLAGHllllllaglifalLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYI 215
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
90-238 2.12e-33

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: 118.27  E-value: 2.12e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  90 YRPWLPFIGTLFLFIFVSNWSGaLIPWklieipeseLAAPTNDINTTVALALLTSLAYFYAGFSKKGLGYFAN------Y 163
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLG-LIPY---------SFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHflppgtP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581 164 VQPIPVLLPIKILEDFTKPLSLSFRLFGNILADE----------LVVAVLVFLVPLFVPLPLMALGLFTSAIQALVFATL 233
Cdd:cd00310   71 LPLAPLMVPIELISELIRPLSLSVRLFANMFAGHlllallsglvPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLL 150

                 ....*
gi 503090581 234 AGAYI 238
Cdd:cd00310  151 TAVYI 155
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
39-238 8.51e-33

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: 118.85  E-value: 8.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581   39 LTSWFVIGLLLIASVAASSSIKRIPSGIQNLMEYVLEFLRDLAKNQLGEKEYrPWLPFIGTLFLFIFVSNWSGaLIPWkl 118
Cdd:TIGR01131  17 LLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKG-KFFPLIFTLFLFILISNLLG-LIPY-- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  119 ieipeseLAAPTNDINTTVALALLTSLAYFYAGFSKKGLG---YFANYVQP---IPVLLPIKILEDFTKPLSLSFRLFGN 192
Cdd:TIGR01131  93 -------SFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGflaHLVPSGTPlplIPFLVIIETISYLARPISLSVRLFAN 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 503090581  193 ILADE-----------LVVAVLVFLVPLFVPLPLMALGLFTSAIQALVFATLAGAYI 238
Cdd:TIGR01131 166 ISAGHllltllsgllfSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYL 222
 
Name Accession Description Interval E-value
atpI CHL00046
ATP synthase CF0 A subunit
13-238 2.73e-140

ATP synthase CF0 A subunit


Pssm-ID: 176987  Cd Length: 228  Bit Score: 392.76  E-value: 2.73e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  13 FTLASLEVGKHWYWHIGNLKIHGQVFLTSWFVIGLLLIASVAASSSIKRIPSGIQNLMEYVLEFLRDLAKNQLGEKEYRP 92
Cdd:CHL00046   1 YDISGVEVGQHFYWQIGGFQVHGQVLITSWVVIAILLGSALLATRNLQTIPTGGQNFFEYVLEFIRDLAKTQIGEEEYRP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  93 WLPFIGTLFLFIFVSNWSGALIPWKLIEIPESELAAPTNDINTTVALALLTSLAYFYAGFSKKGLGYFANYVQPIPVLLP 172
Cdd:CHL00046  81 WVPFIGTMFLFIFVSNWSGALLPWKLIELPHGELAAPTNDINTTVALALLTSVAYFYAGLSKKGLGYFGKYIQPTPILLP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503090581 173 IKILEDFTKPLSLSFRLFGNILADELVVAVLVFLVPLFVPLPLMALGLFTSAIQALVFATLAGAYI 238
Cdd:CHL00046 161 INILEDFTKPLSLSFRLFGNILADELVVAVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYI 226
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
20-238 7.05e-57

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 181.15  E-value: 7.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  20 VGKHWYWHIGNLKIHgQVFLTSWFVIGLLLIASVAASSSIKRIPSGIQNLMEYVLEFLRDLAKNQLGEKEyRPWLPFIGT 99
Cdd:PRK05815   1 IEHHLIIGFGGFNFD-SLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKG-KKFAPLAFT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581 100 LFLFIFVSNWSGaLIPWklieipesELAAPTNDINTTVALALLTSLAYFYAGFSKKGLGYFAN--YVQPIPVLLPIKILE 177
Cdd:PRK05815  79 LFLFILLMNLLG-LIPY--------LLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKefYLQPHPLLLPIEIIS 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581 178 DFTKPLSLSFRLFGNILADE---------LVVAVLVFLVPLFVPLPLMALGLFTSAIQALVFATLAGAYI 238
Cdd:PRK05815 150 EFSRPISLSLRLFGNMLAGElilaliallGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYI 219
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
36-238 2.19e-53

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: 171.41  E-value: 2.19e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  36 QVFLTSWFVIGLLLIASVAASSSIKRIPSGIQNLMEYVLEFLRDLAKNQLGeKEYRPWLPFIGTLFLFIFVSNWSGaLIP 115
Cdd:COG0356    1 DTVLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIG-KKGRKFAPLLLTLFLFILVSNLLG-LIP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581 116 WklieipeseLAAPTNDINTTVALALLTSLAYFYAGFSKKGL-GYFAN-YVQPI----PVLLPIKILEDFTKPLSLSFRL 189
Cdd:COG0356   79 G---------LFPPTADINVTLALALIVFVLVHYYGIKKKGLgGYLKHlFFPPFpwlaPLMLPIEIISELARPLSLSLRL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503090581 190 FGNILADE--------LVVAVLVFLVPLFVPLPLMALGLFTSAIQALVFATLAGAYI 238
Cdd:COG0356  150 FGNMFAGHiillllagLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206
ATP-synt_A pfam00119
ATP synthase A chain;
39-238 5.55e-46

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 152.64  E-value: 5.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581   39 LTSWFVIGLLLI-ASVAASSSIKRIPSGIQNLMEYVLEFLRDLAKNQLGEKEYRPWLPFIGTLFLFIFVSNWSGaLIPwk 117
Cdd:pfam00119   2 LMSLIVALILLLfLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLG-LIP-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  118 liEIPESelAAPTNDINTTVALALLTSLAYFYAGFSKKGL-GYFANYVQP------IPVLLPIKILEDFTKPLSLSFRLF 190
Cdd:pfam00119  79 --KSPGG--FTVTADINVTLALALIVFLLVHYYGIKKHGLgGYFKKLFVPpvplplVPLLLPIEIISEFARPVSLSLRLF 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503090581  191 GNILADE-------------LVVAVLVFLVPLFVPLPLMALGLFTSAIQALVFATLAGAYI 238
Cdd:pfam00119 155 GNMLAGHllllllaglifalLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYI 215
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
27-238 1.17e-36

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 129.05  E-value: 1.17e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  27 HIGNLKIHGQVfLTSWFVIGLLLIASVAASSSIKRIPSGIQNLMEYVLEFLRDLAKNQLgEKEYRPWLPFIGTLFLFIFV 106
Cdd:PRK13421  13 SLGPVPISAPV-VVTWAIMAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTM-QTDPAPYRALIGTLFLFVLV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581 107 SNWSGaLIPwklieipesELAAPTNDINTTVALALLTSLAYFYAGFSKKGL-GYFANYVQPIPVLLPIKILEDFTKPLSL 185
Cdd:PRK13421  91 ANWSS-LVP---------GVEPPTAHLETDAALALIVFLATIYYGVRARGVrGYLATFAEPTWVMIPLNLVEQLTRTFSL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503090581 186 SFRLFGNILADELVVAVLVFLVPLFVPLPLMALGLFTSAIQALVFATLAGAYI 238
Cdd:PRK13421 161 IVRLFGNVMSGVFVIGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFI 213
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
90-238 2.12e-33

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: 118.27  E-value: 2.12e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  90 YRPWLPFIGTLFLFIFVSNWSGaLIPWklieipeseLAAPTNDINTTVALALLTSLAYFYAGFSKKGLGYFAN------Y 163
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLG-LIPY---------SFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHflppgtP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581 164 VQPIPVLLPIKILEDFTKPLSLSFRLFGNILADE----------LVVAVLVFLVPLFVPLPLMALGLFTSAIQALVFATL 233
Cdd:cd00310   71 LPLAPLMVPIELISELIRPLSLSVRLFANMFAGHlllallsglvPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLL 150

                 ....*
gi 503090581 234 AGAYI 238
Cdd:cd00310  151 TAVYI 155
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
23-238 6.82e-33

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 119.46  E-value: 6.82e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  23 HWYWHIGNLKIHGQVfLTSWFVIGLLLIASVAASSSIKRIPSGIQNLMEYVLEFLRDLAKNQLgEKEYRPWLPFIGTLFL 102
Cdd:PRK13420   6 HVLFHIGPLPITESV-LTTWGIMIVLVLASWLTTRRLSLDPGRFQVALEGVVSTIEDAIKEVL-PRHARLVLPFVGTLWI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581 103 FIFVSNWSGaLIPwklieipesELAAPTNDINTTVALALLTSLAYFYAGFSKKGL-GYFANYVQPIPVLLPIKILEDFTK 181
Cdd:PRK13420  84 FILVANLIG-LIP---------GFHSPTADLSVTAALALLVFFSVHWFGIRAEGLrEYLKHYLSPSPFLLPFHLISEITR 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503090581 182 PLSLSFRLFGNILADELVVAVLVFLVPLFVPLPLMALGLFTSAIQALVFATLAGAYI 238
Cdd:PRK13420 154 TLALAVRLFGNIMSLELAALLVLLVAGFLVPVPILMLHIIEALVQAYIFGMLALIYI 210
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
39-238 8.51e-33

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: 118.85  E-value: 8.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581   39 LTSWFVIGLLLIASVAASSSIKRIPSGIQNLMEYVLEFLRDLAKNQLGEKEYrPWLPFIGTLFLFIFVSNWSGaLIPWkl 118
Cdd:TIGR01131  17 LLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKG-KFFPLIFTLFLFILISNLLG-LIPY-- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  119 ieipeseLAAPTNDINTTVALALLTSLAYFYAGFSKKGLG---YFANYVQP---IPVLLPIKILEDFTKPLSLSFRLFGN 192
Cdd:TIGR01131  93 -------SFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGflaHLVPSGTPlplIPFLVIIETISYLARPISLSVRLFAN 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 503090581  193 ILADE-----------LVVAVLVFLVPLFVPLPLMALGLFTSAIQALVFATLAGAYI 238
Cdd:TIGR01131 166 ISAGHllltllsgllfSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYL 222
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
42-238 4.88e-19

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 84.79  E-value: 4.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  42 WFVIGLLLIASVAASSSIKRI-----PSGIQNLMEYVLEFLR-DLAKNQLGeKEYRPWLPFIGTLFLFIFVSNWSGaLIP 115
Cdd:PRK13419 114 WIASAILLVVFLAAGRKYKKMtksqaPKGLANAMEALVEFIRlDVAKSNIG-HGYEKFLPYLLTVFFFILVCNLLG-LVP 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581 116 WKlieipeselAAPTNDINTTVALALLTSLAYFYAGFSKKGL-GYFANYVQPIP-----VLLPIKILEDFTKPLSLSFRL 189
Cdd:PRK13419 192 YG---------ATATGNINVTLTLAVFTFFITQYAAIKAHGIkGYLAHLTGGTHwslwiIMIPIEFIGLFTKPFALTVRL 262
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503090581 190 FGNILADELVVAVLVFLVPLF----------VPLPLMA--LGLFTSAIQALVFATLAGAYI 238
Cdd:PRK13419 263 FANMTAGHIVILSLIFISFILksyivavavsVPFAIFIylLELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
47-238 6.45e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 36.94  E-value: 6.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581  47 LLLIASVAASSSIKRIPSGIQNLMEYVLEFLRDLAKNQLGEKEYRpWLPFIGTLFLFIFVSNWSGaLIPWKLieipesel 126
Cdd:MTH00172  26 LVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLK-YFPFIISLFFFIVFLNLLG-LFPYVF-------- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503090581 127 aAPTNDINTTVALALLTSLAYFYAGFSKKGLGYFANYV---QPI---PVLLPIKILEDFTKPLSLSFRLFGN-------- 192
Cdd:MTH00172  96 -TPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMpsgAPLglaPLLVLIETVSYISRAISLGVRLAANlsaghllf 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 503090581 193 -ILADELVVAVLVFLVPLFVPLPLMA----LGLFTSAIQALVFATLAGAYI 238
Cdd:MTH00172 175 aILAGFGFNMLCASGFLSLFPLLIMVfitlLEIAVAVIQAYVFCLLTTIYL 225
 
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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