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Conserved domains on  [gi|446652535|ref|WP_000729881|]
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MULTISPECIES: F0F1 ATP synthase subunit A [Vibrio]

Protein Classification

FoF1 ATP synthase subunit a( domain architecture ID 10012597)

FoF1 ATP synthase subunit a is part of the membrane proton channel of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane; it plays a direct role in the translocation of protons across the membrane

Gene Ontology:  GO:0045263|GO:0046933|GO:0005886
PubMed:  28001127

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 34-267 8.61e-80

F0F1 ATP synthase subunit A; Validated


:

Pssm-ID: 235617  Cd Length: 227  Bit Score: 240.08  E-value: 8.61e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  34 SFWNVHIDSLFFSVLTGLIFLGVFRAVARKATAGVPGKLQCAVEMVVEFVDKNVKDTFHGRNPLIAPLALTIFCWVFLMN 113
Cdd:PRK05815   8 GFGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 114 LMDLVPIdflpypaqhwlgipyLKVVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELALHPFnhWIMIPfnllIE 193
Cdd:PRK05815  88 LLGLIPY---------------LLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFYLQPH--PLLLP----IE 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446652535 194 VVSLLAKPLSLGMRLFGNMFAGEVVFILC-----AAMLPWYLQWMGSLPWAIFHILVILIQSFVFMMLTIVYMSMAHED 267
Cdd:PRK05815 147 IISEFSRPISLSLRLFGNMLAGELILALIallggAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEE 225
 
Name Accession Description Interval E-value
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 34-267 8.61e-80

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 240.08  E-value: 8.61e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  34 SFWNVHIDSLFFSVLTGLIFLGVFRAVARKATAGVPGKLQCAVEMVVEFVDKNVKDTFHGRNPLIAPLALTIFCWVFLMN 113
Cdd:PRK05815   8 GFGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 114 LMDLVPIdflpypaqhwlgipyLKVVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELALHPFnhWIMIPfnllIE 193
Cdd:PRK05815  88 LLGLIPY---------------LLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFYLQPH--PLLLP----IE 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446652535 194 VVSLLAKPLSLGMRLFGNMFAGEVVFILC-----AAMLPWYLQWMGSLPWAIFHILVILIQSFVFMMLTIVYMSMAHED 267
Cdd:PRK05815 147 IISEFSRPISLSLRLFGNMLAGELILALIallggAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEE 225
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 41-267 1.99e-76

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: 231.12  E-value: 1.99e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  41 DSLFFSVLTGLIFLGVFRAVARKAtAGVPGKLQCAVEMVVEFVDKNVKDTFHGRNPLIAPLALTIFCWVFLMNLMDLvpi 120
Cdd:COG0356    1 DTVLMSWLAMLLLLLLFLLATRKL-KLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGL--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 121 dflpypaqhwlgIPYLKvVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELALHPFnhWIMIPFNLLIEVVSLLAK 200
Cdd:COG0356   77 ------------IPGLF-PPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHLFFPPF--PWLAPLMLPIEIISELAR 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446652535 201 PLSLGMRLFGNMFAGEVVFILCAAMLPW----YLQWMGSLPWAIFHILVILIQSFVFMMLTIVYMSMAHED 267
Cdd:COG0356  142 PLSLSLRLFGNMFAGHIILLLLAGLAPFlllgVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVEE 212
ATP-synt_A pfam00119
ATP synthase A chain;
43-262 1.28e-62

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 196.17  E-value: 1.28e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535   43 LFFSVLTGLIFLGVFRAVARKATAGVPGKLQCAVEMVVEFVDKNVKDTFHGRN-PLIAPLALTIFCWVFLMNLMDLVPId 121
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKKgRKFFPLLLTLFFFILVSNLLGLIPK- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  122 fLPYPAQhwlgipylkvvPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELaLHPFNHWIMIPFNLLIEVVSLLAKP 201
Cdd:pfam00119  80 -SPGGFT-----------VTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKL-FVPPVPLPLVPLLLPIEIISEFARP 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  202 LSLGMRLFGNMFAGEVVFILCAAMLPW---------YLQWMGSLPWAIFHILVILIQSFVFMMLTIVYMS 262
Cdd:pfam00119 147 VSLSLRLFGNMLAGHLLLLLLAGLIFAllsagfllgVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 33-262 1.89e-36

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: 129.25  E-value: 1.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535   33 SSFWNVHIDSLFFSVLTGLIFLGVFRAVARKAtagVPGKLQCAVEMVVEFVDKNVKDTFHGRNPLIAPLALTIFCWVFLM 112
Cdd:TIGR01131   8 SPITLFSLTLLSLILLLSLLIFLISSSLSRWL---IPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILIS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  113 NLMDLVPIDFlpypaqhwlgipylkvVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAkELALHPFNHWImIPFNLLI 192
Cdd:TIGR01131  85 NLLGLIPYSF----------------TPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLA-HLVPSGTPLPL-IPFLVII 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446652535  193 EVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPW-------YLQWMGSLPWAIFHILVILIQSFVFMMLTIVYMS 262
Cdd:TIGR01131 147 ETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSlmssaifALLLLILVALIILEIFVAFIQAYVFTLLTCLYLN 223
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 99-262 3.82e-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: 3.82e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  99 APLALTIFCWVFLMNLMDLVPIDFlpypaqhwlgipylkvVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELALH 178
Cdd:cd00310    5 LPLLGTLFLFILFSNLLGLIPYSF----------------TPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 179 PFnhWIMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLQWMGSLPWAI------FHILVILIQSFV 252
Cdd:cd00310   69 TP--LPLAPLMVPIELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLpvaltlLELFVAFIQAYV 146

                        170
                 ....*....|
gi 446652535 253 FMMLTIVYMS 262
Cdd:cd00310  147 FTLLTAVYIS 156
 
Name Accession Description Interval E-value
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 34-267 8.61e-80

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 240.08  E-value: 8.61e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  34 SFWNVHIDSLFFSVLTGLIFLGVFRAVARKATAGVPGKLQCAVEMVVEFVDKNVKDTFHGRNPLIAPLALTIFCWVFLMN 113
Cdd:PRK05815   8 GFGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 114 LMDLVPIdflpypaqhwlgipyLKVVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELALHPFnhWIMIPfnllIE 193
Cdd:PRK05815  88 LLGLIPY---------------LLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFYLQPH--PLLLP----IE 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446652535 194 VVSLLAKPLSLGMRLFGNMFAGEVVFILC-----AAMLPWYLQWMGSLPWAIFHILVILIQSFVFMMLTIVYMSMAHED 267
Cdd:PRK05815 147 IISEFSRPISLSLRLFGNMLAGELILALIallggAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEE 225
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 41-267 1.99e-76

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: 231.12  E-value: 1.99e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  41 DSLFFSVLTGLIFLGVFRAVARKAtAGVPGKLQCAVEMVVEFVDKNVKDTFHGRNPLIAPLALTIFCWVFLMNLMDLvpi 120
Cdd:COG0356    1 DTVLMSWLAMLLLLLLFLLATRKL-KLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGL--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 121 dflpypaqhwlgIPYLKvVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELALHPFnhWIMIPFNLLIEVVSLLAK 200
Cdd:COG0356   77 ------------IPGLF-PPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHLFFPPF--PWLAPLMLPIEIISELAR 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446652535 201 PLSLGMRLFGNMFAGEVVFILCAAMLPW----YLQWMGSLPWAIFHILVILIQSFVFMMLTIVYMSMAHED 267
Cdd:COG0356  142 PLSLSLRLFGNMFAGHIILLLLAGLAPFlllgVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVEE 212
ATP-synt_A pfam00119
ATP synthase A chain;
43-262 1.28e-62

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 196.17  E-value: 1.28e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535   43 LFFSVLTGLIFLGVFRAVARKATAGVPGKLQCAVEMVVEFVDKNVKDTFHGRN-PLIAPLALTIFCWVFLMNLMDLVPId 121
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKKgRKFFPLLLTLFFFILVSNLLGLIPK- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  122 fLPYPAQhwlgipylkvvPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELaLHPFNHWIMIPFNLLIEVVSLLAKP 201
Cdd:pfam00119  80 -SPGGFT-----------VTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKL-FVPPVPLPLVPLLLPIEIISEFARP 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  202 LSLGMRLFGNMFAGEVVFILCAAMLPW---------YLQWMGSLPWAIFHILVILIQSFVFMMLTIVYMS 262
Cdd:pfam00119 147 VSLSLRLFGNMLAGHLLLLLLAGLIFAllsagfllgVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 33-262 1.89e-36

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: 129.25  E-value: 1.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535   33 SSFWNVHIDSLFFSVLTGLIFLGVFRAVARKAtagVPGKLQCAVEMVVEFVDKNVKDTFHGRNPLIAPLALTIFCWVFLM 112
Cdd:TIGR01131   8 SPITLFSLTLLSLILLLSLLIFLISSSLSRWL---IPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILIS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  113 NLMDLVPIDFlpypaqhwlgipylkvVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAkELALHPFNHWImIPFNLLI 192
Cdd:TIGR01131  85 NLLGLIPYSF----------------TPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLA-HLVPSGTPLPL-IPFLVII 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446652535  193 EVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPW-------YLQWMGSLPWAIFHILVILIQSFVFMMLTIVYMS 262
Cdd:TIGR01131 147 ETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSlmssaifALLLLILVALIILEIFVAFIQAYVFTLLTCLYLN 223
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 99-262 3.82e-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: 3.82e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  99 APLALTIFCWVFLMNLMDLVPIDFlpypaqhwlgipylkvVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELALH 178
Cdd:cd00310    5 LPLLGTLFLFILFSNLLGLIPYSF----------------TPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 179 PFnhWIMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLQWMGSLPWAI------FHILVILIQSFV 252
Cdd:cd00310   69 TP--LPLAPLMVPIELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLpvaltlLELFVAFIQAYV 146

                        170
                 ....*....|
gi 446652535 253 FMMLTIVYMS 262
Cdd:cd00310  147 FTLLTAVYIS 156
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 46-270 2.09e-20

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 89.03  E-value: 2.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  46 SVLTGLIFLGVFRAVARKATAGVPGKLQCAVEMVVEFV--DKNVKDTFHGRNPLIaPLALTIFCWVFLMNLMDLVPidfl 123
Cdd:PRK13419 117 SAILLVVFLAAGRKYKKMTKSQAPKGLANAMEALVEFIrlDVAKSNIGHGYEKFL-PYLLTVFFFILVCNLLGLVP---- 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 124 pYPAqhwlgipylkvVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKEL--ALHPFNHWIMIPfnllIEVVSLLAKP 201
Cdd:PRK13419 192 -YGA-----------TATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLtgGTHWSLWIIMIP----IEFIGLFTKP 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 202 LSLGMRLFGNMFAGEVV-----FILCAAMLPWYLQWMgSLPWAIF----HILVILIQSFVFMMLTIVY--MSMAHEDNDH 270
Cdd:PRK13419 256 FALTVRLFANMTAGHIVilsliFISFILKSYIVAVAV-SVPFAIFiyllELFVAFLQAYIFTMLSALFigLATAHEGHDE 334
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
 51-270 7.66e-18

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 79.74  E-value: 7.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  51 LIFLGVFRAVARKATAGVPGKLQCAVEMVVEFVDKNVKDTFHGRNPLIAPLALTIFCWVFLMNLMDLVPidflpypaqhw 130
Cdd:PRK13421  30 MAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRALIGTLFLFVLVANWSSLVP----------- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 131 lGIPylkvVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELAlHPfnHWIMIPFNLlievVSLLAKPLSLGMRLFG 210
Cdd:PRK13421  99 -GVE----PPTAHLETDAALALIVFLATIYYGVRARGVRGYLATFA-EP--TWVMIPLNL----VEQLTRTFSLIVRLFG 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446652535 211 NMFAGEVV--FILCAAMLpwylqwMGSLPWAIFHILVILIQSFVFMMLTIVYMSMAHEDNDH 270
Cdd:PRK13421 167 NVMSGVFVigIVLSLAGL------LVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVSDDEA 222
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 46-262 3.64e-14

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 69.77  E-value: 3.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  46 SVLTGLIFLGVFRAVARKATAGV---PGKLQCAVEMVVEFVDKNVKDTFHGRNPLIAPLALTIFCWVFLMNLMDLVPidf 122
Cdd:PRK13420  19 SVLTTWGIMIVLVLASWLTTRRLsldPGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFVGTLWIFILVANLIGLIP--- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 123 lpypAQHwlgipylkvVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELaLHPFNhwIMIPFNLLIEVVSLLAkpl 202
Cdd:PRK13420  96 ----GFH---------SPTADLSVTAALALLVFFSVHWFGIRAEGLREYLKHY-LSPSP--FLLPFHLISEITRTLA--- 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446652535 203 sLGMRLFGNMFAGE----VVFILCAAMLPwylqwmgsLPWAIFHILVILIQSFVFMMLTIVYMS 262
Cdd:PRK13420 157 -LAVRLFGNIMSLElaalLVLLVAGFLVP--------VPILMLHIIEALVQAYIFGMLALIYIA 211
atpI CHL00046
ATP synthase CF0 A subunit
 140-218 1.38e-07

ATP synthase CF0 A subunit


Pssm-ID: 176987  Cd Length: 228  Bit Score: 51.09  E-value: 1.38e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446652535 140 PSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELALHPfnhwIMIPFNLLIEvvslLAKPLSLGMRLFGNMFAGEVV 218
Cdd:CHL00046 117 PTNDINTTVALALLTSVAYFYAGLSKKGLGYFGKYIQPTP----ILLPINILED----FTKPLSLSFRLFGNILADELV 187
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 183-262 5.01e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 49.26  E-value: 5.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 183 WIMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLpWYLQWMGSLPWA----------IFHILVILIQSFV 252
Cdd:MTH00176 138 PLLNPFLVLIELVSLLIRPLTLAVRLAANLSAGHLLLGLLGAAM-WGLLPVSPLIGFlllivqilyfMFEIAVCMIQAYV 216

                         90
                 ....*....|
gi 446652535 253 FMMLTIVYMS 262
Cdd:MTH00176 217 FTLLLSLYLD 226
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 51-264 4.08e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 47.19  E-value: 4.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  51 LIFLGVFRAVARKATAgVPGKLQCAVEMVVEFVDKNVKD-TFHGRNPLIAPLALTIFCWVFLMNLMDLVP---------- 119
Cdd:PRK13417 110 LIFIPAANIIAKNPLK-VQSRFANTVEVFVNFLRKDIVDeSMHGHGHSYYHYIFTLFFFILFCNLMGLVPsvgeltvvas 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 120 ----------IDFLPYpAQHWLGIPYLKVVPSADVNITMAMALGVFALMIYYSIKVKGLGGFAKELALH-PFNHW-IMIP 187
Cdd:PRK13417 189 dygglvalgvMDHTPH-ALPTFAKVWSGITVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGvPLLLYpIMWP 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 188 FNLlieVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLQW-------MGSLPWAIFHILVILIQSFVFMMLTIVY 260
Cdd:PRK13417 268 LEF---IVSPMAKTFALTVRLLANMTAGHVIILALMGFIFQFQSWgivpvsvIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344


                 ....
gi 446652535 261 MSMA 264
Cdd:PRK13417 345 VGLS 348
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 182-262 4.82e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 46.40  E-value: 4.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 182 HWIMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLP---WYLQWMGSLP-------WAIFHILVILIQSF 251
Cdd:MTH00173 137 PAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYLSsslFSSSVVSLLLvlliqvgYFIFEVAVMLIQAY 216

                         90
                 ....*....|.
gi 446652535 252 VFMMLTIVYMS 262
Cdd:MTH00173 217 IFTLLIKLYSD 227
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 68-262 5.65e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 46.31  E-value: 5.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  68 VPGKLQCAVEMVVEFVDKNVKDTFHGRNPLIAPLALTIFCWVFLMNLMDLVPIDFlpypaqhwlgipylkvVPSADVNIT 147
Cdd:MTH00157  38 IPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFILFNNFLGLFPYIF----------------TSTSHLSLT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 148 MAMALGV-FALMIYYSIKVKglggfakelaLHPFNHWI-------MIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVF 219
Cdd:MTH00157 102 LSLALPLwLSFMLFGWINNT----------NHMFAHLVpqgtppiLMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLL 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446652535 220 ILCAAMLPWYLQWMGSLPWAIFHILVIL------IQSFVFMMLTIVYMS 262
Cdd:MTH00157 172 TLLGNTGPSLSSMILSILILIQILLLILesavaiIQSYVFSVLSTLYSS 220
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 184-262 2.25e-05

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 44.58  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 184 IMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLpWYLqwMGSLPWA-----IFHILVIL------IQSFV 252
Cdd:MTH00035 140 FLIPLMVWIETLSLFAQPIALGLRLAANLTAGHLLIFLLSTAI-WEL--SNSPLISiitliIFFLLFILeigvacIQAYV 216

                         90
                 ....*....|
gi 446652535 253 FMMLTIVYMS 262
Cdd:MTH00035 217 FTALVHFYLE 226
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 51-261 4.03e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 43.88  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  51 LIFLGVFRAVARKATAGVPGKLQCAVEMVVEFVDKNVKDTFHGRNPLIAPLALTIFCWVFLMNLMDLVPIDFLPypaqhw 130
Cdd:MTH00172  24 MILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTP------ 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 131 lgipylkvvpsaDVNITMAMALGVFalmIYYSIKVKGLGGFAKELA--LHPFNH-WIMIPFNLLIEVVSLLAKPLSLGMR 207
Cdd:MTH00172  98 ------------TTHIVVTLGLSFS---IIIGVTLAGFWRFKWDFFsiLMPSGApLGLAPLLVLIETVSYISRAISLGVR 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446652535 208 LFGNMFAGEVVF---------ILCAAMLPWYLQWMGSLPWAIFHILVILIQSFVFMMLTIVYM 261
Cdd:MTH00172 163 LAANLSAGHLLFailagfgfnMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYL 225
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 185-261 6.38e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 43.01  E-value: 6.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 185 MIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLQWMGSLPWAIFHILVIL---------IQSFVFMM 255
Cdd:MTH00179 138 LIPMLVWIETISLLIRPLALGVRLTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLtllevavamIQAYVFVL 217


                 ....*.
gi 446652535 256 LTIVYM 261
Cdd:MTH00179 218 LLSLYL 223
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 184-262 9.31e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 42.69  E-value: 9.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 184 IMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAA----MLPWYLQWMGSLPW------AIFHILVILIQSFVF 253
Cdd:MTH00175 150 VLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGfafnMLSNGLIILSLFPMlimifiTLLEMAVAVIQAYVF 229


                 ....*....
gi 446652535 254 MMLTIVYMS 262
Cdd:MTH00175 230 CLLTTIYLG 238
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 186-260 2.17e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 41.35  E-value: 2.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 186 IPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCA----AMLPWYLQwMGSLPWAIFHILVIL------IQSFVFMM 255
Cdd:MTH00120 139 IPALILIETISLLIRPLALGVRLTANLTAGHLLIQLIStatlNLLPTMPT-LSLLTLIILLLLTILelavamIQAYVFVL 217


                 ....*
gi 446652535 256 LTIVY 260
Cdd:MTH00120 218 LLSLY 222
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 99-260 2.57e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 41.26  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535  99 APLALTIFCWVFLMNLMDLVPIDFlpypaqhwlgipylkvVPSADVNITMAMALGVFALMIYYSIK---VKGLGGFAKEL 175
Cdd:MTH00005  74 SSLISALFTMIILMNLSGLLPYVF----------------STSSHLIFTLTLGLPLWLSLIMSSVTfspKKFAAHLLPGG 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 176 ALHPFNhwimiPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCA--AMLPWYLQWMGSLPWAIFHILVI------- 246
Cdd:MTH00005 138 APDWLN-----PFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGiyAASALFSSISSTILLILTQMGYIlfevgic 212

                        170
                 ....*....|....
gi 446652535 247 LIQSFVFMMLTIVY 260
Cdd:MTH00005 213 LIQAYIFCLLLSLY 226
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 185-261 2.68e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 38.02  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 185 MIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCA----AMLPW-----YLQWMGSLPWAIFHILVILIQSFVFMM 255
Cdd:MTH00073 138 LIPILIIIETISLFIRPLALGVRLTANLTAGHLLIQLIStatlVLLPLmptvsILTMIVLFLLTLLEIAVAMIQAYVFVL 217


                 ....*.
gi 446652535 256 LTIVYM 261
Cdd:MTH00073 218 LLSLYL 223
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 185-261 8.99e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 36.77  E-value: 8.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446652535 185 MIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCA----AMLP-----WYLQWMGSLPWAIFHILVILIQSFVFMM 255
Cdd:MTH00132 138 LIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIAtaafVLLPlmptvAILTATLLFLLTLLEVAVAMIQAYVFVL 217


                 ....*.
gi 446652535 256 LTIVYM 261
Cdd:MTH00132 218 LLSLYL 223
 
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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