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Conserved domains on  [gi|503999423|ref|WP_014233417|]
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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 3.67e-79

F0F1 ATP synthase subunit A; Validated


:

Pssm-ID: 235617  Cd Length: 227  Bit Score: 238.54  E-value: 3.67e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  34 SFWNVHIDSLFFSWFTGLIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMN 113
Cdd:PRK05815   8 GFGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 114 VMDLVPIdflpypaehwlgipyLKVVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELALHPFnhPLMIPfnllIE 193
Cdd:PRK05815  88 LLGLIPY---------------LLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFYLQPH--PLLLP----IE 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503999423 194 VVSLLAKPLSLGMRLFGNMFAGEVVFILC-----AAMLPWYLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLSMAHED 267
Cdd:PRK05815 147 IISEFSRPISLSLRLFGNMLAGELILALIallggAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEE 225
 
Name Accession Description Interval E-value
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
34-267 3.67e-79

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 238.54  E-value: 3.67e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  34 SFWNVHIDSLFFSWFTGLIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMN 113
Cdd:PRK05815   8 GFGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 114 VMDLVPIdflpypaehwlgipyLKVVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELALHPFnhPLMIPfnllIE 193
Cdd:PRK05815  88 LLGLIPY---------------LLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFYLQPH--PLLLP----IE 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503999423 194 VVSLLAKPLSLGMRLFGNMFAGEVVFILC-----AAMLPWYLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLSMAHED 267
Cdd:PRK05815 147 IISEFSRPISLSLRLFGNMLAGELILALIallggAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEE 225
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
41-267 9.96e-75

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: 226.49  E-value: 9.96e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  41 DSLFFSWFTGLIFLGIFYKVAKRTtAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMNVMDLvpi 120
Cdd:COG0356    1 DTVLMSWLAMLLLLLLFLLATRKL-KLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGL--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 121 dflpypaehwlgIPYLKvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELALHPFnhPLMIPFNLLIEVVSLLAK 200
Cdd:COG0356   77 ------------IPGLF-PPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHLFFPPF--PWLAPLMLPIEIISELAR 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503999423 201 PLSLGMRLFGNMFAGEVVFILCAAMLPW----YLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLSMAHED 267
Cdd:COG0356  142 PLSLSLRLFGNMFAGHIILLLLAGLAPFlllgVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVEE 212
ATP-synt_A pfam00119
ATP synthase A chain;
43-262 2.06e-61

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 193.09  E-value: 2.06e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423   43 LFFSWFTGLIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRN-PLIAPLALTIFCWVFLMNVMDLVPId 121
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKKgRKFFPLLLTLFFFILVSNLLGLIPK- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  122 fLPYPAEhwlgipylkvvPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELaLHPFNHPLMIPFNLLIEVVSLLAKP 201
Cdd:pfam00119  80 -SPGGFT-----------VTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKL-FVPPVPLPLVPLLLPIEIISEFARP 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  202 LSLGMRLFGNMFAGEVVFILCAAMLPW---------YLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLS 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 2.82e-37

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: 131.17  E-value: 2.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423   33 TSFWNVHIDSLFFSWFTGLIFLGIFYKVAKRttaGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLM 112
Cdd:TIGR01131   8 SPITLFSLTLLSLILLLSLLIFLISSSLSRW---LIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILIS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  113 NVMDLVPIDFlpypaehwlgipylkvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAkELALHPFNHPLmIPFNLLI 192
Cdd:TIGR01131  85 NLLGLIPYSF----------------TPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLA-HLVPSGTPLPL-IPFLVII 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503999423  193 EVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPW-------YLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLS 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 7.15e-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: 115.19  E-value: 7.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  99 APLALTIFCWVFLMNVMDLVPIDFlpypaehwlgipylkvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELalh 178
Cdd:cd00310    5 LPLLGTLFLFILFSNLLGLIPYSF----------------TPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFL--- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 179 PFNHPL-MIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLQWMGSLPWAI------FHILVITIQAF 251
Cdd:cd00310   66 PPGTPLpLAPLMVPIELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLpvaltlLELFVAFIQAY 145
                        170
                 ....*....|.
gi 503999423 252 VFMMLTIVYLS 262
Cdd:cd00310  146 VFTLLTAVYIS 156
 
Name Accession Description Interval E-value
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
34-267 3.67e-79

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 238.54  E-value: 3.67e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  34 SFWNVHIDSLFFSWFTGLIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMN 113
Cdd:PRK05815   8 GFGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 114 VMDLVPIdflpypaehwlgipyLKVVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELALHPFnhPLMIPfnllIE 193
Cdd:PRK05815  88 LLGLIPY---------------LLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFYLQPH--PLLLP----IE 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503999423 194 VVSLLAKPLSLGMRLFGNMFAGEVVFILC-----AAMLPWYLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLSMAHED 267
Cdd:PRK05815 147 IISEFSRPISLSLRLFGNMLAGELILALIallggAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEE 225
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
41-267 9.96e-75

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: 226.49  E-value: 9.96e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  41 DSLFFSWFTGLIFLGIFYKVAKRTtAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMNVMDLvpi 120
Cdd:COG0356    1 DTVLMSWLAMLLLLLLFLLATRKL-KLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGL--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 121 dflpypaehwlgIPYLKvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELALHPFnhPLMIPFNLLIEVVSLLAK 200
Cdd:COG0356   77 ------------IPGLF-PPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHLFFPPF--PWLAPLMLPIEIISELAR 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503999423 201 PLSLGMRLFGNMFAGEVVFILCAAMLPW----YLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLSMAHED 267
Cdd:COG0356  142 PLSLSLRLFGNMFAGHIILLLLAGLAPFlllgVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVEE 212
ATP-synt_A pfam00119
ATP synthase A chain;
43-262 2.06e-61

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 193.09  E-value: 2.06e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423   43 LFFSWFTGLIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRN-PLIAPLALTIFCWVFLMNVMDLVPId 121
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKKgRKFFPLLLTLFFFILVSNLLGLIPK- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  122 fLPYPAEhwlgipylkvvPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELaLHPFNHPLMIPFNLLIEVVSLLAKP 201
Cdd:pfam00119  80 -SPGGFT-----------VTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKL-FVPPVPLPLVPLLLPIEIISEFARP 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  202 LSLGMRLFGNMFAGEVVFILCAAMLPW---------YLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLS 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 2.82e-37

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: 131.17  E-value: 2.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423   33 TSFWNVHIDSLFFSWFTGLIFLGIFYKVAKRttaGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLM 112
Cdd:TIGR01131   8 SPITLFSLTLLSLILLLSLLIFLISSSLSRW---LIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILIS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  113 NVMDLVPIDFlpypaehwlgipylkvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAkELALHPFNHPLmIPFNLLI 192
Cdd:TIGR01131  85 NLLGLIPYSF----------------TPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLA-HLVPSGTPLPL-IPFLVII 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503999423  193 EVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPW-------YLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLS 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 7.15e-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: 115.19  E-value: 7.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  99 APLALTIFCWVFLMNVMDLVPIDFlpypaehwlgipylkvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELalh 178
Cdd:cd00310    5 LPLLGTLFLFILFSNLLGLIPYSF----------------TPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFL--- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 179 PFNHPL-MIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLQWMGSLPWAI------FHILVITIQAF 251
Cdd:cd00310   66 PPGTPLpLAPLMVPIELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLpvaltlLELFVAFIQAY 145
                        170
                 ....*....|.
gi 503999423 252 VFMMLTIVYLS 262
Cdd:cd00310  146 VFTLLTAVYIS 156
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
51-270 2.07e-18

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 83.25  E-value: 2.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  51 LIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNV--KDTFHGRNPLIaPLALTIFCWVFLMNVMDLVPidflpYPAe 128
Cdd:PRK13419 122 VVFLAAGRKYKKMTKSQAPKGLANAMEALVEFIRLDVakSNIGHGYEKFL-PYLLTVFFFILVCNLLGLVP-----YGA- 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 129 hwlgipylkvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKEL--ALHPFNHPLMIPfnllIEVVSLLAKPLSLGM 206
Cdd:PRK13419 195 ----------TATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLtgGTHWSLWIIMIP----IEFIGLFTKPFALTV 260
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503999423 207 RLFGNMFAGEVV-----FILCAAMLPWYLQWMgSLPWAIF----HILVITIQAFVFMMLTIVY--LSMAHEDPDH 270
Cdd:PRK13419 261 RLFANMTAGHIVilsliFISFILKSYIVAVAV-SVPFAIFiyllELFVAFLQAYIFTMLSALFigLATAHEGHDE 334
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
51-270 1.83e-16

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 75.89  E-value: 1.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  51 LIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMNVMDLVPidflpypaehw 130
Cdd:PRK13421  30 MAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRALIGTLFLFVLVANWSSLVP----------- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 131 lGIPylkvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELAlHPfnHPLMIPFNLlievVSLLAKPLSLGMRLFG 210
Cdd:PRK13421  99 -GVE----PPTAHLETDAALALIVFLATIYYGVRARGVRGYLATFA-EP--TWVMIPLNL----VEQLTRTFSLIVRLFG 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503999423 211 NMFAGEVV--FILCAAMLpwylqwMGSLPWAIFHILVITIQAFVFMMLTIVYLSMAHEDPDH 270
Cdd:PRK13421 167 NVMSGVFVigIVLSLAGL------LVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVSDDEA 222
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
41-262 2.68e-14

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 70.16  E-value: 2.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  41 DSLFFSWFTgLIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMNVMDLVPi 120
Cdd:PRK13420  18 ESVLTTWGI-MIVLVLASWLTTRRLSLDPGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFVGTLWIFILVANLIGLIP- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 121 dflpypAEHwlgipylkvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELaLHPFnhPLMIPFNLLIEVVSLLAk 200
Cdd:PRK13420  96 ------GFH---------SPTADLSVTAALALLVFFSVHWFGIRAEGLREYLKHY-LSPS--PFLLPFHLISEITRTLA- 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503999423 201 plsLGMRLFGNM----FAGEVVFILCAAMLPwylqwmgsLPWAIFHILVITIQAFVFMMLTIVYLS 262
Cdd:PRK13420 157 ---LAVRLFGNImsleLAALLVLLVAGFLVP--------VPILMLHIIEALVQAYIFGMLALIYIA 211
atpI CHL00046
ATP synthase CF0 A subunit
38-260 3.58e-10

ATP synthase CF0 A subunit


Pssm-ID: 176987  Cd Length: 228  Bit Score: 58.41  E-value: 3.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  38 VHIDSLFFSWFTGLIFLGIFYkVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLI-APLALTIFCWVFLMN-VM 115
Cdd:CHL00046  21 VHGQVLITSWVVIAILLGSAL-LATRNLQTIPTGGQNFFEYVLEFIRDLAKTQIGEEEYRPwVPFIGTMFLFIFVSNwSG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 116 DLVPIDFLPYPaEHWLGipylkvVPSADVNITMAMALGVfALMIFYS-IKVKGLGGFAKelALHPFnhPLMIPFNLLIEv 194
Cdd:CHL00046 100 ALLPWKLIELP-HGELA------APTNDINTTVALALLT-SVAYFYAgLSKKGLGYFGK--YIQPT--PILLPINILED- 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503999423 195 vslLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLqwmgSLPWAIFHILVITIQAFVFMMLTIVY 260
Cdd:CHL00046 167 ---FTKPLSLSFRLFGNILADELVVAVLVSLVPLVV----PIPVMFLGLFTSGIQALIFATLAAAY 225
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
68-262 2.11e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 50.78  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  68 VPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMNVMDLVPIDFlpypaehwlgipylkvVPSADVNIT 147
Cdd:MTH00175  52 IPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVF----------------TPTAHIIIT 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 148 MAMALGvfalmIFYSIKVKGLGGFAKEL--ALHPFNHPLMI-PFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAA 224
Cdd:MTH00175 116 FGLSLS-----IIIAVTLLGFLTFKWNFlsILMPGGAPLVLaPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSG 190
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 503999423 225 ----MLPWYLQWMGSLPW------AIFHILVITIQAFVFMMLTIVYLS 262
Cdd:MTH00175 191 fafnMLSNGLIILSLFPMlimifiTLLEMAVAVIQAYVFCLLTTIYLG 238
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
68-261 2.62e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 50.04  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  68 VPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMNVMDLVPIDFLPypaehwlgipylkvvpsaDVNIT 147
Cdd:MTH00172  41 IPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTP------------------TTHIV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 148 MAMALGVFalmIFYSIKVKGLGGFAKELA--LHPFNHPLMI-PFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVF----- 219
Cdd:MTH00172 103 VTLGLSFS---IIIGVTLAGFWRFKWDFFsiLMPSGAPLGLaPLLVLIETVSYISRAISLGVRLAANLSAGHLLFailag 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 503999423 220 ----ILCAAMLPWYLQWMGSLPWAIFHILVITIQAFVFMMLTIVYL 261
Cdd:MTH00172 180 fgfnMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYL 225
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
183-262 4.78e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 49.26  E-value: 4.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 183 PLMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLpWYLQWMGSLPWA----------IFHILVITIQAFV 252
Cdd:MTH00176 138 PLLNPFLVLIELVSLLIRPLTLAVRLAANLSAGHLLLGLLGAAM-WGLLPVSPLIGFlllivqilyfMFEIAVCMIQAYV 216
                         90
                 ....*....|
gi 503999423 253 FMMLTIVYLS 262
Cdd:MTH00176 217 FTLLLSLYLD 226
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
33-262 1.84e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 47.47  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  33 TSFWNVHIDslFFSWFTGLIFLGIFYKVakrttagVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLM 112
Cdd:MTH00157  12 STSFNLSLN--WLSTFLGLLFIPSSFWL-------IPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFILFN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 113 NVMDLVPIDFlpypaehwlgipylkvVPSADVNITMAMALGV-FALMIFYSIKvkglggFAKELALH--PFNHPLM-IPF 188
Cdd:MTH00157  83 NFLGLFPYIF----------------TSTSHLSLTLSLALPLwLSFMLFGWIN------NTNHMFAHlvPQGTPPIlMPF 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 189 NLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFIL---CAAMLPWYLQWMGSLPWAIFHIL---VITIQAFVFMMLTIVYLS 262
Cdd:MTH00157 141 MVLIETISNLIRPGTLAVRLAANMIAGHLLLTLlgnTGPSLSSMILSILILIQILLLILesaVAIIQSYVFSVLSTLYSS 220
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
47-264 7.49e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 46.42  E-value: 7.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  47 WFTGLIFLGIFYKVAK---RTTAGVPGKLQCAVEMIVEFVADNVKD-TFHGRNPLIAPLALTIFCWVFLMNVMDLVP--- 119
Cdd:PRK13417 102 WIVAFFLFLIFIPAANiiaKNPLKVQSRFANTVEVFVNFLRKDIVDeSMHGHGHSYYHYIFTLFFFILFCNLMGLVPsvg 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 120 -----------------IDFLPYpAEHWLGIPYLKVVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKEL--ALHPF 180
Cdd:PRK13417 182 eltvvasdygglvalgvMDHTPH-ALPTFAKVWSGITVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVpnGVPLL 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 181 NHPLMIPFNLlieVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLQW-------MGSLPWAIFHILVITIQAFVF 253
Cdd:PRK13417 261 LYPIMWPLEF---IVSPMAKTFALTVRLLANMTAGHVIILALMGFIFQFQSWgivpvsvIGSGLIYVLEIFVAFLQAYIF 337
                        250
                 ....*....|.
gi 503999423 254 MMLTIVYLSMA 264
Cdd:PRK13417 338 VLLTSLFVGLS 348
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
183-262 8.09e-06

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 45.73  E-value: 8.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 183 PLMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLpWYLqwMGSLPWA-----------IFHILVITIQAF 251
Cdd:MTH00035 139 SFLIPLMVWIETLSLFAQPIALGLRLAANLTAGHLLIFLLSTAI-WEL--SNSPLISiitliiffllfILEIGVACIQAY 215
                         90
                 ....*....|.
gi 503999423 252 VFMMLTIVYLS 262
Cdd:MTH00035 216 VFTALVHFYLE 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
184-261 3.02e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 44.04  E-value: 3.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 184 LMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCA----AMLPWYLQwMGSLPWAIFHIL------VITIQAFVF 253
Cdd:MTH00120 137 PLIPALILIETISLLIRPLALGVRLTANLTAGHLLIQLIStatlNLLPTMPT-LSLLTLIILLLLtilelaVAMIQAYVF 215

                 ....*...
gi 503999423 254 MMLTIVYL 261
Cdd:MTH00120 216 VLLLSLYL 223
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
34-260 3.40e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 44.09  E-value: 3.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423  34 SFWNVHIDSLFFSWFTGLIFLGIFYKVakrtTAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMN 113
Cdd:MTH00173  11 DHNSSFSSLSFLMWLLSLMSLFFFSSS----VWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 114 VMDLVPIDFlpypaehwlgipylkvVPSADVNITMAMALGVFALMIFYSIkVKGLGGFAKELAlhPFNHPLM-IPFNLLI 192
Cdd:MTH00173  87 LSGLLPFVF----------------SVTSHLAFTFSLALPLWLSLILSGL-FYNPSKSLAGLV--PAGAPAGlNPFLVLI 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503999423 193 EVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLP---WYLQWMGSLP-------WAIFHILVITIQAFVFMMLTIVY 260
Cdd:MTH00173 148 ETVSILIRPLTLTVRLLANISAGHIVLTLIGNYLSsslFSSSVVSLLLvlliqvgYFIFEVAVMLIQAYIFTLLIKLY 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
184-261 1.16e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 42.26  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 184 LMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCA----AMLPW-----YLQWMGSLPWAIFHILVITIQAFVFM 254
Cdd:MTH00073 137 LLIPILIIIETISLFIRPLALGVRLTANLTAGHLLIQLIStatlVLLPLmptvsILTMIVLFLLTLLEIAVAMIQAYVFV 216

                 ....*..
gi 503999423 255 MLTIVYL 261
Cdd:MTH00073 217 LLLSLYL 223
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
101-261 2.60e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 41.09  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 101 LALTIFCWVFLMNVMDLVPIDFlpypaehwlgipylkvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELalhPF 180
Cdd:MTH00179  72 LFLSLMLFLLTLNLLGLLPYTF----------------TPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLL---PE 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 181 NHP-LMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLQWMGSLPWAIFHIL---------VITIQA 250
Cdd:MTH00179 133 GTPtPLIPMLVWIETISLLIRPLALGVRLTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLflltllevaVAMIQA 212
                        170
                 ....*....|.
gi 503999423 251 FVFMMLTIVYL 261
Cdd:MTH00179 213 YVFVLLLSLYL 223
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
183-261 4.00e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 40.63  E-value: 4.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 183 PLMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCA----AMLP-----WYLQWMGSLPWAIFHILVITIQAFVF 253
Cdd:MTH00132 136 TPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIAtaafVLLPlmptvAILTATLLFLLTLLEVAVAMIQAYVF 215

                 ....*...
gi 503999423 254 MMLTIVYL 261
Cdd:MTH00132 216 VLLLSLYL 223
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
187-260 6.43e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 37.02  E-value: 6.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 187 PFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCA--AMLPWYLQWMGSLPWAIFHILVI-------TIQAFVFMMLT 257
Cdd:MTH00005 144 PFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGiyAASALFSSISSTILLILTQMGYIlfevgicLIQAYIFCLLL 223

                 ...
gi 503999423 258 IVY 260
Cdd:MTH00005 224 SLY 226
 
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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