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Conserved domains on  [gi|159106858|ref|YP_001531277|]
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ATP synthase CF0 subunit IV (chloroplast) [Lolium perenne]

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
15-241 6.21e-152

ATP synthase CF0 A subunit


:

Pssm-ID: 176987  Cd Length: 228  Bit Score: 422.03  E-value: 6.21e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  15 YDISGVEVGQHFYWQIGSFQIHAQVLITSWVVITILLGSVVIAVRNPQTVPMDGQNFFEYVLEFIRDLSKTQIGE-EYGP 93
Cdd:CHL00046   1 YDISGVEVGQHFYWQIGGFQVHGQVLITSWVVIAILLGSALLATRNLQTIPTGGQNFFEYVLEFIRDLAKTQIGEeEYRP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  94 WVPFIGTMFLFIFVSNWSGALLPWKIIELPHGELAAPTNDINTTVALALLTSAAYFYAGLSKKGLSYFEKYIKPTPILLP 173
Cdd:CHL00046  81 WVPFIGTMFLFIFVSNWSGALLPWKLIELPHGELAAPTNDINTTVALALLTSVAYFYAGLSKKGLGYFGKYIQPTPILLP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 159106858 174 INILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGE 241
Cdd:CHL00046 161 INILEDFTKPLSLSFRLFGNILADELVVAVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGE 228
 
Name Accession Description Interval E-value
atpI CHL00046
ATP synthase CF0 A subunit
15-241 6.21e-152

ATP synthase CF0 A subunit


Pssm-ID: 176987  Cd Length: 228  Bit Score: 422.03  E-value: 6.21e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  15 YDISGVEVGQHFYWQIGSFQIHAQVLITSWVVITILLGSVVIAVRNPQTVPMDGQNFFEYVLEFIRDLSKTQIGE-EYGP 93
Cdd:CHL00046   1 YDISGVEVGQHFYWQIGGFQVHGQVLITSWVVIAILLGSALLATRNLQTIPTGGQNFFEYVLEFIRDLAKTQIGEeEYRP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  94 WVPFIGTMFLFIFVSNWSGALLPWKIIELPHGELAAPTNDINTTVALALLTSAAYFYAGLSKKGLSYFEKYIKPTPILLP 173
Cdd:CHL00046  81 WVPFIGTMFLFIFVSNWSGALLPWKLIELPHGELAAPTNDINTTVALALLTSVAYFYAGLSKKGLGYFGKYIQPTPILLP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 159106858 174 INILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGE 241
Cdd:CHL00046 161 INILEDFTKPLSLSFRLFGNILADELVVAVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGE 228
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
38-244 1.17e-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: 172.18  E-value: 1.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  38 QVLITSWVVITILLGSVVIAVRNPQTVPMDGQNFFEYVLEFIRDLSKTQIGEEYGPWVPFIGTMFLFIFVSNWSGaLLPW 117
Cdd:COG0356    1 DTVLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLG-LIPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858 118 kiielphgeLAAPTNDINTTVALALLTSAAYFYAGLSKKGLSYF--EKYIKPT----PILLPINILEDFTKPLSLSFRLF 191
Cdd:COG0356   80 ---------LFPPTADINVTLALALIVFVLVHYYGIKKKGLGGYlkHLFFPPFpwlaPLMLPIEIISELARPLSLSLRLF 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 159106858 192 GNILADE--------LVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGESME 244
Cdd:COG0356  151 GNMFAGHiillllagLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVE 211
ATP-synt_A pfam00119
ATP synthase A chain;
40-240 6.99e-42

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 142.24  E-value: 6.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858   40 LITSWVVITILLGSVVIAVRN-PQTVPMDGQNFFEYVLEFIRDLSKTQIG-EEYGPWVPFIGTMFLFIFVSNWSGAllpw 117
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKtKKLVPGRLQNFVEMLVEFVDNIVKDNIGkKKGRKFFPLLLTLFFFILVSNLLGL---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  118 kIIELPHGelAAPTNDINTTVALALLTSAAYFYAGLSKKGLS-YFEKYIKP------TPILLPINILEDFTKPLSLSFRL 190
Cdd:pfam00119  77 -IPKSPGG--FTVTADINVTLALALIVFLLVHYYGIKKHGLGgYFKKLFVPpvplplVPLLLPIEIISEFARPVSLSLRL 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 159106858  191 FGNILADE-------------LVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIG 240
Cdd:pfam00119 154 FGNMLAGHllllllaglifalLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
91-240 1.92e-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: 115.96  E-value: 1.92e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  91 YGPWVPFIGTMFLFIFVSNWSGaLLPWkiielphgeLAAPTNDINTTVALALLTSAAYFYAGLSKKGLSYFEK------Y 164
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLG-LIPY---------SFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHflppgtP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858 165 IKPTPILLPINILEDFTKPLSLSFRLFGNILADE----------LVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATL 234
Cdd:cd00310   71 LPLAPLMVPIELISELIRPLSLSVRLFANMFAGHlllallsglvPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLL 150

                 ....*.
gi 159106858 235 AAAYIG 240
Cdd:cd00310  151 TAVYIS 156
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
30-242 1.86e-28

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: 107.68  E-value: 1.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858   30 IGSFQIHAQVLIT----SWVVITILLGSVVIAVRNPQTVPMDGQNFFEYVLEFIRDLSKTQIGEEYGPWVPFIGTMFLFI 105
Cdd:TIGR01131   2 FSQFDISPITLFSltllSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  106 FVSNWSGaLLPWkiielphgeLAAPTNDINTTVALALLTSAAYFYAGLSKKGLSYFeKYIKPT-------PILLPINILE 178
Cdd:TIGR01131  82 LISNLLG-LIPY---------SFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFL-AHLVPSgtplpliPFLVIIETIS 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 159106858  179 DFTKPLSLSFRLFGNILADE-----------LVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGES 242
Cdd:TIGR01131 151 YLARPISLSVRLFANISAGHllltllsgllfSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
 
Name Accession Description Interval E-value
atpI CHL00046
ATP synthase CF0 A subunit
15-241 6.21e-152

ATP synthase CF0 A subunit


Pssm-ID: 176987  Cd Length: 228  Bit Score: 422.03  E-value: 6.21e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  15 YDISGVEVGQHFYWQIGSFQIHAQVLITSWVVITILLGSVVIAVRNPQTVPMDGQNFFEYVLEFIRDLSKTQIGE-EYGP 93
Cdd:CHL00046   1 YDISGVEVGQHFYWQIGGFQVHGQVLITSWVVIAILLGSALLATRNLQTIPTGGQNFFEYVLEFIRDLAKTQIGEeEYRP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  94 WVPFIGTMFLFIFVSNWSGALLPWKIIELPHGELAAPTNDINTTVALALLTSAAYFYAGLSKKGLSYFEKYIKPTPILLP 173
Cdd:CHL00046  81 WVPFIGTMFLFIFVSNWSGALLPWKLIELPHGELAAPTNDINTTVALALLTSVAYFYAGLSKKGLGYFGKYIQPTPILLP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 159106858 174 INILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGE 241
Cdd:CHL00046 161 INILEDFTKPLSLSFRLFGNILADELVVAVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGE 228
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
22-247 2.15e-57

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 182.30  E-value: 2.15e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  22 VGQHFYWQIGSFQIHAQVLITsWVVITILLGSVVIAVRNPQTVPMDGQNFFEYVLEFIRDLSKTQIGEEYGPWVPFIGTM 101
Cdd:PRK05815   1 IEHHLIIGFGGFNFDSLLLSV-LLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858 102 FLFIFVSNWSGaLLPWkiielphgELAAPTNDINTTVALALLTSAAYFYAGLSKKGLSYF--EKYIKPTPILLPINILED 179
Cdd:PRK05815  80 FLFILLMNLLG-LIPY--------LLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYlkEFYLQPHPLLLPIEIISE 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 159106858 180 FTKPLSLSFRLFGNILADE---------LVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGESMEGHH 247
Cdd:PRK05815 151 FSRPISLSLRLFGNMLAGElilaliallGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEEEH 227
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
38-244 1.17e-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: 172.18  E-value: 1.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  38 QVLITSWVVITILLGSVVIAVRNPQTVPMDGQNFFEYVLEFIRDLSKTQIGEEYGPWVPFIGTMFLFIFVSNWSGaLLPW 117
Cdd:COG0356    1 DTVLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLG-LIPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858 118 kiielphgeLAAPTNDINTTVALALLTSAAYFYAGLSKKGLSYF--EKYIKPT----PILLPINILEDFTKPLSLSFRLF 191
Cdd:COG0356   80 ---------LFPPTADINVTLALALIVFVLVHYYGIKKKGLGGYlkHLFFPPFpwlaPLMLPIEIISELARPLSLSLRLF 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 159106858 192 GNILADE--------LVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGESME 244
Cdd:COG0356  151 GNMFAGHiillllagLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVE 211
ATP-synt_A pfam00119
ATP synthase A chain;
40-240 6.99e-42

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 142.24  E-value: 6.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858   40 LITSWVVITILLGSVVIAVRN-PQTVPMDGQNFFEYVLEFIRDLSKTQIG-EEYGPWVPFIGTMFLFIFVSNWSGAllpw 117
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKtKKLVPGRLQNFVEMLVEFVDNIVKDNIGkKKGRKFFPLLLTLFFFILVSNLLGL---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  118 kIIELPHGelAAPTNDINTTVALALLTSAAYFYAGLSKKGLS-YFEKYIKP------TPILLPINILEDFTKPLSLSFRL 190
Cdd:pfam00119  77 -IPKSPGG--FTVTADINVTLALALIVFLLVHYYGIKKHGLGgYFKKLFVPpvplplVPLLLPIEIISEFARPVSLSLRL 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 159106858  191 FGNILADE-------------LVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIG 240
Cdd:pfam00119 154 FGNMLAGHllllllaglifalLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
29-240 5.55e-34

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 121.73  E-value: 5.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  29 QIGSFQIHAQVLITsWVVITILLGSVVIAVRNPQTVPMDGQNFFEYVLEFIRDLSKTQIGEEYGPWVPFIGTMFLFIFVS 108
Cdd:PRK13421  13 SLGPVPISAPVVVT-WAIMAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRALIGTLFLFVLVA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858 109 NWSGaLLPwkiielphgELAAPTNDINTTVALALLTSAAYFYAGLSKKGLS-YFEKYIKPTPILLPINILEDFTKPLSLS 187
Cdd:PRK13421  92 NWSS-LVP---------GVEPPTAHLETDAALALIVFLATIYYGVRARGVRgYLATFAEPTWVMIPLNLVEQLTRTFSLI 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 159106858 188 FRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIG 240
Cdd:PRK13421 162 VRLFGNVMSGVFVIGIVLSLAGLLVPIPLMALDLLTGAVQAYIFAVLAMVFIG 214
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
91-240 1.92e-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: 115.96  E-value: 1.92e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  91 YGPWVPFIGTMFLFIFVSNWSGaLLPWkiielphgeLAAPTNDINTTVALALLTSAAYFYAGLSKKGLSYFEK------Y 164
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLG-LIPY---------SFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHflppgtP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858 165 IKPTPILLPINILEDFTKPLSLSFRLFGNILADE----------LVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATL 234
Cdd:cd00310   71 LPLAPLMVPIELISELIRPLSLSVRLFANMFAGHlllallsglvPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLL 150

                 ....*.
gi 159106858 235 AAAYIG 240
Cdd:cd00310  151 TAVYIS 156
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
25-246 2.26e-31

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 115.22  E-value: 2.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  25 HFYWQIGSFQIHAQVLiTSWVVITILLGSVVIAVRNPQTVPMDGQNFFEYVLEFIRDLSKTQIGEEYGPWVPFIGTMFLF 104
Cdd:PRK13420   6 HVLFHIGPLPITESVL-TTWGIMIVLVLASWLTTRRLSLDPGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFVGTLWIF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858 105 IFVSNWSGaLLPwkiielphgELAAPTNDINTTVALALLTSAAYFYAGLSKKGLS-YFEKYIKPTPILLPINILEDFTKP 183
Cdd:PRK13420  85 ILVANLIG-LIP---------GFHSPTADLSVTAALALLVFFSVHWFGIRAEGLReYLKHYLSPSPFLLPFHLISEITRT 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 159106858 184 LSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGESMEGH 246
Cdd:PRK13420 155 LALAVRLFGNIMSLELAALLVLLVAGFLVPVPILMLHIIEALVQAYIFGMLALIYIAGGIQAH 217
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
30-242 1.86e-28

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: 107.68  E-value: 1.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858   30 IGSFQIHAQVLIT----SWVVITILLGSVVIAVRNPQTVPMDGQNFFEYVLEFIRDLSKTQIGEEYGPWVPFIGTMFLFI 105
Cdd:TIGR01131   2 FSQFDISPITLFSltllSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  106 FVSNWSGaLLPWkiielphgeLAAPTNDINTTVALALLTSAAYFYAGLSKKGLSYFeKYIKPT-------PILLPINILE 178
Cdd:TIGR01131  82 LISNLLG-LIPY---------SFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFL-AHLVPSgtplpliPFLVIIETIS 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 159106858  179 DFTKPLSLSFRLFGNILADE-----------LVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGES 242
Cdd:TIGR01131 151 YLARPISLSVRLFANISAGHllltllsgllfSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
altF1_A TIGR03306
alternate F1F0 ATPase, F0 subunit A; A small number of taxonomically diverse prokaryotic ...
27-240 7.35e-26

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: 100.58  E-value: 7.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858   27 YWQIGSFQIHAQVLITSWVVITILLGSVVIAVRNPQTVPMDG-QNFFEYVLEFIRDLSKTQIGEEYGPWVPFIGTMFLFI 105
Cdd:TIGR03306   8 YWQYGFVKINATIAFTWLLMLLLVIGSWLITRRLSTGLERSRwQNLLEVLVTGIQEQISDVGLAKPRKYLPFLGTLFLFI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  106 FVSNWsgallpwkIIELPHGElaAPTNDINTTVALALLTSAAYFYAGLSKKGLS-YFEKYIKPTPILLPINILEDFTKPL 184
Cdd:TIGR03306  88 AVANL--------LSVIPGYE--PPTGSLSTTAALALCVFVAVPLFGIAERGLSgYLKSYLKPTPFMLPFNIIGELSRTL 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 159106858  185 SLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIG 240
Cdd:TIGR03306 158 ALAVRLFGNMMSGSMILAILLSISPLIFPVLMQVLGLLTGMVQAYIFSVLATVYIA 213
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
44-247 8.62e-19

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 84.02  E-value: 8.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  44 WVVITILLGSVVIAVR-----NPQTVPMDGQNFFEYVLEFIR-DLSKTQIGEEYGPWVPFIGTMFLFIFVSNWSGaLLPW 117
Cdd:PRK13419 114 WIASAILLVVFLAAGRkykkmTKSQAPKGLANAMEALVEFIRlDVAKSNIGHGYEKFLPYLLTVFFFILVCNLLG-LVPY 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858 118 KiielphgelAAPTNDINTTVALALLTSAAYFYAGLSKKGLS-YFEKYIKPTP-----ILLPINILEDFTKPLSLSFRLF 191
Cdd:PRK13419 193 G---------ATATGNINVTLTLAVFTFFITQYAAIKAHGIKgYLAHLTGGTHwslwiIMIPIEFIGLFTKPFALTVRLF 263
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 159106858 192 GNILADELVVVVLV------------SLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIG-----ESMEGHH 247
Cdd:PRK13419 264 ANMTAGHIVILSLIfisfilksyivaVAVSVPFAIFIYLLELFVAFLQAYIFTMLSALFIGlatahEGHDEEH 336
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
21-246 9.06e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 36.79  E-value: 9.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  21 EVGQHFYWqIGSFQIHAQVLITS-WVV----ITILLGSVVIAVRNPQTVPMDGQNFFEYVLEFIR-DLSKTQIGEEYGPW 94
Cdd:PRK13417  79 ETGKRFHY-VGGFDMHITKRVTMmWIVafflFLIFIPAANIIAKNPLKVQSRFANTVEVFVNFLRkDIVDESMHGHGHSY 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858  95 VPFIGTMFLFIFVSNWSG----------------ALLPWKIIELPHGELA---------APTNDINTTVALALLTSAAYF 149
Cdd:PRK13417 158 YHYIFTLFFFILFCNLMGlvpsvgeltvvasdygGLVALGVMDHTPHALPtfakvwsgiTVTGDISVTMTLALLTMFLIY 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159106858 150 YAGLSKKGLSYFEKYI-KPTPILLPI------NILEDFTKPLSLSFRLFGNILADELVVVV-----------LVSLVPLV 211
Cdd:PRK13417 238 GAGFSYQGPKFIWHSVpNGVPLLLYPimwpleFIVSPMAKTFALTVRLLANMTAGHVIILAlmgfifqfqswGIVPVSVI 317
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 159106858 212 VPIPVMFLGLFTSGIQALIFATLAAAYIGESMEGH 246
Cdd:PRK13417 318 GSGLIYVLEIFVAFLQAYIFVLLTSLFVGLSMHRH 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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