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Conserved domains on  [gi|408904976|gb|AFU97036|]
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AtpI, partial (chloroplast) [Passiflora ciliata]

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
24-250 1.32e-151

ATP synthase CF0 A subunit


:

Pssm-ID: 176987  Cd Length: 228  Bit Score: 421.65  E-value: 1.32e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976  24 YDISGVEVGQHFYLKLGGFQVHAQVLITSWVVIAILLGSAIVAVRNPQTIPSDGQNFFEYVLEFIRDVSKTQIGE-EYGP 102
Cdd:CHL00046   1 YDISGVEVGQHFYWQIGGFQVHGQVLITSWVVIAILLGSALLATRNLQTIPTGGQNFFEYVLEFIRDLAKTQIGEeEYRP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976 103 WVPFIGTMFLFIFVSNWSGALLPWKIIQLPHGELAAPTNDINTTVALALLTSIAYFYAGLSKKGLGYFVKYIQPTPILLP 182
Cdd:CHL00046  81 WVPFIGTMFLFIFVSNWSGALLPWKLIELPHGELAAPTNDINTTVALALLTSVAYFYAGLSKKGLGYFGKYIQPTPILLP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408904976 183 INILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPSVVPIPVMLLGLFTSGIQALIFATLAAAYIGE 250
Cdd:CHL00046 161 INILEDFTKPLSLSFRLFGNILADELVVAVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGE 228
 
Name Accession Description Interval E-value
atpI CHL00046
ATP synthase CF0 A subunit
24-250 1.32e-151

ATP synthase CF0 A subunit


Pssm-ID: 176987  Cd Length: 228  Bit Score: 421.65  E-value: 1.32e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976  24 YDISGVEVGQHFYLKLGGFQVHAQVLITSWVVIAILLGSAIVAVRNPQTIPSDGQNFFEYVLEFIRDVSKTQIGE-EYGP 102
Cdd:CHL00046   1 YDISGVEVGQHFYWQIGGFQVHGQVLITSWVVIAILLGSALLATRNLQTIPTGGQNFFEYVLEFIRDLAKTQIGEeEYRP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976 103 WVPFIGTMFLFIFVSNWSGALLPWKIIQLPHGELAAPTNDINTTVALALLTSIAYFYAGLSKKGLGYFVKYIQPTPILLP 182
Cdd:CHL00046  81 WVPFIGTMFLFIFVSNWSGALLPWKLIELPHGELAAPTNDINTTVALALLTSVAYFYAGLSKKGLGYFGKYIQPTPILLP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408904976 183 INILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPSVVPIPVMLLGLFTSGIQALIFATLAAAYIGE 250
Cdd:CHL00046 161 INILEDFTKPLSLSFRLFGNILADELVVAVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGE 228
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
47-253 3.86e-56

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: 178.73  E-value: 3.86e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976  47 QVLITSWVVIAILLGSAIVAVRNPQTIPSDGQNFFEYVLEFIRDVSKTQIGEEYGPWVPFIGTMFLFIFVSNWSGaLLPW 126
Cdd:COG0356    1 DTVLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLG-LIPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976 127 kiiqlphgeLAAPTNDINTTVALALLTSIAYFYAGLSKKGLGYFVK--YIQPT----PILLPINILEDFTKPLSLSFRLF 200
Cdd:COG0356   80 ---------LFPPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKhlFFPPFpwlaPLMLPIEIISELARPLSLSLRLF 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 408904976 201 GNILADE--------LVVVVLVSLVPSVVPIPVMLLGLFTSGIQALIFATLAAAYIGESME 253
Cdd:COG0356  151 GNMFAGHiillllagLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVE 211
ATP-synt_A pfam00119
ATP synthase A chain;
49-249 1.66e-43

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 146.48  E-value: 1.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976   49 LITSWVVIAILLGSAIVAVRN-PQTIPSDGQNFFEYVLEFIRDVSKTQIG-EEYGPWVPFIGTMFLFIFVSNWSGAllpw 126
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKtKKLVPGRLQNFVEMLVEFVDNIVKDNIGkKKGRKFFPLLLTLFFFILVSNLLGL---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976  127 kIIQLPHGelAAPTNDINTTVALALLTSIAYFYAGLSKKGL-GYFVKYIQP------TPILLPINILEDFTKPLSLSFRL 199
Cdd:pfam00119  77 -IPKSPGG--FTVTADINVTLALALIVFLLVHYYGIKKHGLgGYFKKLFVPpvplplVPLLLPIEIISEFARPVSLSLRL 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 408904976  200 FGNILADE-------------LVVVVLVSLVPSVVPIPVMLLGLFTSGIQALIFATLAAAYIG 249
Cdd:pfam00119 154 FGNMLAGHllllllaglifalLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
100-249 8.03e-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: 117.12  E-value: 8.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976 100 YGPWVPFIGTMFLFIFVSNWSGaLLPWkiiqlphgeLAAPTNDINTTVALALLTSIAYFYAGLSKKGLGYFVK------Y 173
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLG-LIPY---------SFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHflppgtP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976 174 IQPTPILLPINILEDFTKPLSLSFRLFGNILADE----------LVVVVLVSLVPSVVPIPVMLLGLFTSGIQALIFATL 243
Cdd:cd00310   71 LPLAPLMVPIELISELIRPLSLSVRLFANMFAGHlllallsglvPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLL 150

                 ....*.
gi 408904976 244 AAAYIG 249
Cdd:cd00310  151 TAVYIS 156
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
52-251 2.89e-29

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: 109.99  E-value: 2.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976   52 SWVVIAILLGSAIVAVRNPQTIPSDGQNFFEYVLEFIRDVSKTQIGEEYGPWVPFIGTMFLFIFVSNWSGaLLPWkiiql 131
Cdd:TIGR01131  19 SLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLG-LIPY----- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976  132 phgeLAAPTNDINTTVALALLTSIAYFYAGLSKKGLG---YFVKYIQPT---PILLPINILEDFTKPLSLSFRLFGNILA 205
Cdd:TIGR01131  93 ----SFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGflaHLVPSGTPLpliPFLVIIETISYLARPISLSVRLFANISA 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 408904976  206 DE-------LVVVVLVSLVPSVVPIPVML----LGLFTSGIQALIFATLAAAYIGES 251
Cdd:TIGR01131 169 GHllltllsGLLFSLMSSAIFALLLLILValiiLEIFVAFIQAYVFTLLTCLYLNDA 225
 
Name Accession Description Interval E-value
atpI CHL00046
ATP synthase CF0 A subunit
24-250 1.32e-151

ATP synthase CF0 A subunit


Pssm-ID: 176987  Cd Length: 228  Bit Score: 421.65  E-value: 1.32e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976  24 YDISGVEVGQHFYLKLGGFQVHAQVLITSWVVIAILLGSAIVAVRNPQTIPSDGQNFFEYVLEFIRDVSKTQIGE-EYGP 102
Cdd:CHL00046   1 YDISGVEVGQHFYWQIGGFQVHGQVLITSWVVIAILLGSALLATRNLQTIPTGGQNFFEYVLEFIRDLAKTQIGEeEYRP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976 103 WVPFIGTMFLFIFVSNWSGALLPWKIIQLPHGELAAPTNDINTTVALALLTSIAYFYAGLSKKGLGYFVKYIQPTPILLP 182
Cdd:CHL00046  81 WVPFIGTMFLFIFVSNWSGALLPWKLIELPHGELAAPTNDINTTVALALLTSVAYFYAGLSKKGLGYFGKYIQPTPILLP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408904976 183 INILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPSVVPIPVMLLGLFTSGIQALIFATLAAAYIGE 250
Cdd:CHL00046 161 INILEDFTKPLSLSFRLFGNILADELVVAVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGE 228
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
31-256 1.21e-58

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 185.77  E-value: 1.21e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976  31 VGQHFYLKLGGFQVHAQVLITsWVVIAILLGSAIVAVRNPQTIPSDGQNFFEYVLEFIRDVSKTQIGEEYGPWVPFIGTM 110
Cdd:PRK05815   1 IEHHLIIGFGGFNFDSLLLSV-LLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976 111 FLFIFVSNWSGaLLPWkiiqlphgELAAPTNDINTTVALALLTSIAYFYAGLSKKGLGYFVK--YIQPTPILLPINILED 188
Cdd:PRK05815  80 FLFILLMNLLG-LIPY--------LLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKefYLQPHPLLLPIEIISE 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 408904976 189 FTKPLSLSFRLFGNILADE---------LVVVVLVSLVPSVVPIPVMLLGLFTSGIQALIFATLAAAYIGESMEGHH 256
Cdd:PRK05815 151 FSRPISLSLRLFGNMLAGElilaliallGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEEEH 227
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
47-253 3.86e-56

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: 178.73  E-value: 3.86e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976  47 QVLITSWVVIAILLGSAIVAVRNPQTIPSDGQNFFEYVLEFIRDVSKTQIGEEYGPWVPFIGTMFLFIFVSNWSGaLLPW 126
Cdd:COG0356    1 DTVLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLG-LIPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976 127 kiiqlphgeLAAPTNDINTTVALALLTSIAYFYAGLSKKGLGYFVK--YIQPT----PILLPINILEDFTKPLSLSFRLF 200
Cdd:COG0356   80 ---------LFPPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKhlFFPPFpwlaPLMLPIEIISELARPLSLSLRLF 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 408904976 201 GNILADE--------LVVVVLVSLVPSVVPIPVMLLGLFTSGIQALIFATLAAAYIGESME 253
Cdd:COG0356  151 GNMFAGHiillllagLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVE 211
ATP-synt_A pfam00119
ATP synthase A chain;
49-249 1.66e-43

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 146.48  E-value: 1.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976   49 LITSWVVIAILLGSAIVAVRN-PQTIPSDGQNFFEYVLEFIRDVSKTQIG-EEYGPWVPFIGTMFLFIFVSNWSGAllpw 126
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKtKKLVPGRLQNFVEMLVEFVDNIVKDNIGkKKGRKFFPLLLTLFFFILVSNLLGL---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976  127 kIIQLPHGelAAPTNDINTTVALALLTSIAYFYAGLSKKGL-GYFVKYIQP------TPILLPINILEDFTKPLSLSFRL 199
Cdd:pfam00119  77 -IPKSPGG--FTVTADINVTLALALIVFLLVHYYGIKKHGLgGYFKKLFVPpvplplVPLLLPIEIISEFARPVSLSLRL 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 408904976  200 FGNILADE-------------LVVVVLVSLVPSVVPIPVMLLGLFTSGIQALIFATLAAAYIG 249
Cdd:pfam00119 154 FGNMLAGHllllllaglifalLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
37-249 1.76e-35

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 125.96  E-value: 1.76e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976  37 LKLGGFQVHAQVLITsWVVIAILLGSAIVAVRNPQTIPSDGQNFFEYVLEFIRDVSKTQIGEEYGPWVPFIGTMFLFIFV 116
Cdd:PRK13421  12 FSLGPVPISAPVVVT-WAIMAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRALIGTLFLFVLV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976 117 SNWSGaLLPwkiiqlphgELAAPTNDINTTVALALLTSIAYFYAGLSKKGL-GYFVKYIQPTPILLPINILEDFTKPLSL 195
Cdd:PRK13421  91 ANWSS-LVP---------GVEPPTAHLETDAALALIVFLATIYYGVRARGVrGYLATFAEPTWVMIPLNLVEQLTRTFSL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 408904976 196 SFRLFGNILADELVVVVLVSLVPSVVPIPVMLLGLFTSGIQALIFATLAAAYIG 249
Cdd:PRK13421 161 IVRLFGNVMSGVFVIGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIG 214
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
100-249 8.03e-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: 117.12  E-value: 8.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976 100 YGPWVPFIGTMFLFIFVSNWSGaLLPWkiiqlphgeLAAPTNDINTTVALALLTSIAYFYAGLSKKGLGYFVK------Y 173
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLG-LIPY---------SFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHflppgtP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976 174 IQPTPILLPINILEDFTKPLSLSFRLFGNILADE----------LVVVVLVSLVPSVVPIPVMLLGLFTSGIQALIFATL 243
Cdd:cd00310   71 LPLAPLMVPIELISELIRPLSLSVRLFANMFAGHlllallsglvPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLL 150

                 ....*.
gi 408904976 244 AAAYIG 249
Cdd:cd00310  151 TAVYIS 156
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
34-255 3.67e-32

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 117.54  E-value: 3.67e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976  34 HFYLKLGGFQVHAQVLiTSWVVIAILLGSAIVAVRNPQTIPSDGQNFFEYVLEFIRDVSKTQIGEEYGPWVPFIGTMFLF 113
Cdd:PRK13420   6 HVLFHIGPLPITESVL-TTWGIMIVLVLASWLTTRRLSLDPGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFVGTLWIF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976 114 IFVSNWSGaLLPwkiiqlphgELAAPTNDINTTVALALLTSIAYFYAGLSKKGL-GYFVKYIQPTPILLPINILEDFTKP 192
Cdd:PRK13420  85 ILVANLIG-LIP---------GFHSPTADLSVTAALALLVFFSVHWFGIRAEGLrEYLKHYLSPSPFLLPFHLISEITRT 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 408904976 193 LSLSFRLFGNILADELVVVVLVSLVPSVVPIPVMLLGLFTSGIQALIFATLAAAYIGESMEGH 255
Cdd:PRK13420 155 LALAVRLFGNIMSLELAALLVLLVAGFLVPVPILMLHIIEALVQAYIFGMLALIYIAGGIQAH 217
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
52-251 2.89e-29

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: 109.99  E-value: 2.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976   52 SWVVIAILLGSAIVAVRNPQTIPSDGQNFFEYVLEFIRDVSKTQIGEEYGPWVPFIGTMFLFIFVSNWSGaLLPWkiiql 131
Cdd:TIGR01131  19 SLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLG-LIPY----- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976  132 phgeLAAPTNDINTTVALALLTSIAYFYAGLSKKGLG---YFVKYIQPT---PILLPINILEDFTKPLSLSFRLFGNILA 205
Cdd:TIGR01131  93 ----SFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGflaHLVPSGTPLpliPFLVIIETISYLARPISLSVRLFANISA 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 408904976  206 DE-------LVVVVLVSLVPSVVPIPVML----LGLFTSGIQALIFATLAAAYIGES 251
Cdd:TIGR01131 169 GHllltllsGLLFSLMSSAIFALLLLILValiiLEIFVAFIQAYVFTLLTCLYLNDA 225
altF1_A TIGR03306
alternate F1F0 ATPase, F0 subunit A; A small number of taxonomically diverse prokaryotic ...
49-249 3.90e-25

alternate F1F0 ATPase, F0 subunit A; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F0 subunit A of this apparent second ATP synthase.


Pssm-ID: 132349  Cd Length: 217  Bit Score: 99.04  E-value: 3.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976   49 LITSWVVIAILLGSAIVAVRNPQT--IPSDGQNFFEY----VLEFIRDVSKTQIGeeygPWVPFIGTMFLFIFVSNWsga 122
Cdd:TIGR03306  20 IAFTWLLMLLLVIGSWLITRRLSTglERSRWQNLLEVlvtgIQEQISDVGLAKPR----KYLPFLGTLFLFIAVANL--- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976  123 llpwkIIQLPHGElaAPTNDINTTVALALLTSIAYFYAGLSKKGL-GYFVKYIQPTPILLPINILEDFTKPLSLSFRLFG 201
Cdd:TIGR03306  93 -----LSVIPGYE--PPTGSLSTTAALALCVFVAVPLFGIAERGLsGYLKSYLKPTPFMLPFNIIGELSRTLALAVRLFG 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 408904976  202 NILADELVVVVLVSLVPSVVPIPVMLLGLFTSGIQALIFATLAAAYIG 249
Cdd:TIGR03306 166 NMMSGSMILAILLSISPLIFPVLMQVLGLLTGMVQAYIFSVLATVYIA 213
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
37-256 1.22e-21

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 92.11  E-value: 1.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976  37 LKLGGFQVH-AQVLITSWVVIAILLGSAIVAVRNPQTI-----PSDGQNFFEYVLEFIR-DVSKTQIGEEYGPWVPFIGT 109
Cdd:PRK13419  97 LVVGGFDISiTKHVVMMWIASAILLVVFLAAGRKYKKMtksqaPKGLANAMEALVEFIRlDVAKSNIGHGYEKFLPYLLT 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976 110 MFLFIFVSNWSGaLLPWKiiqlphgelAAPTNDINTTVALALLTSIAYFYAGLSKKGL-GYFVKYIQPTP-----ILLPI 183
Cdd:PRK13419 177 VFFFILVCNLLG-LVPYG---------ATATGNINVTLTLAVFTFFITQYAAIKAHGIkGYLAHLTGGTHwslwiIMIPI 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976 184 NILEDFTKPLSLSFRLFGNILADELVVVVLV------------SLVPSVVPIPVMLLGLFTSGIQALIFATLAAAYIG-- 249
Cdd:PRK13419 247 EFIGLFTKPFALTVRLFANMTAGHIVILSLIfisfilksyivaVAVSVPFAIFIYLLELFVAFLQAYIFTMLSALFIGla 326
                        250
                 ....*....|
gi 408904976 250 ---ESMEGHH 256
Cdd:PRK13419 327 tahEGHDEEH 336
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
30-255 7.25e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 40.26  E-value: 7.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976  30 EVGQHFYLkLGGFQVHAQVLITS-WVV----IAILLGSAIVAVRNPQTIPSDGQNFFEYVLEFIR-DVSKTQIGEEYGPW 103
Cdd:PRK13417  79 ETGKRFHY-VGGFDMHITKRVTMmWIVafflFLIFIPAANIIAKNPLKVQSRFANTVEVFVNFLRkDIVDESMHGHGHSY 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976 104 VPFIGTMFLFIFVSNWSG----------------ALLPWKIIQLPHGELA---------APTNDINTTVALALLTSIAYF 158
Cdd:PRK13417 158 YHYIFTLFFFILFCNLMGlvpsvgeltvvasdygGLVALGVMDHTPHALPtfakvwsgiTVTGDISVTMTLALLTMFLIY 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408904976 159 YAGLSKKGLGyFVKYIQPT-------PILLPIN-ILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPSV---VPIPVML 227
Cdd:PRK13417 238 GAGFSYQGPK-FIWHSVPNgvplllyPIMWPLEfIVSPMAKTFALTVRLLANMTAGHVIILALMGFIFQFqswGIVPVSV 316
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 408904976 228 LG--------LFTSGIQALIFATLAAAYIGESMEGH 255
Cdd:PRK13417 317 IGsgliyvleIFVAFLQAYIFVLLTSLFVGLSMHRH 352
 
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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