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Conserved domains on  [gi|446314994|ref|WP_000392849|]
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F0F1 ATP synthase subunit A [Streptococcus pneumoniae]

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
 5-237 6.62e-56

F0F1 ATP synthase subunit A; Validated


:

Pssm-ID: 235617  Cd Length: 227  Bit Score: 178.06  E-value: 6.62e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994   5 INPIISIGPVIFNL-TMLAMTLLIVGVIFVFIYWASRNMTLKPKGKQNVLEYVYDFVIGFTEPNIGSRYMKdYSLFFLCL 83
Cdd:PRK05815   1 IEHHLIIGFGGFNFdSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKK-FAPLAFTL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  84 FLFMVIANNLGLMTkiqtidgtNWWSSPTANLQYDLTLSFLVILLTHIESVRRRGFKKSIKSF-MSPV-FVIPMNILEEF 161
Cdd:PRK05815  80 FLFILLMNLLGLIP--------YLLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFyLQPHpLLLPIEIISEF 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446314994 162 TNFLSLALRIFGNIFAGEVMTSLLLLLSHQAIYWYPVAFGANLAWTAFSVFISCIQAYVFTLLTSVYLGNKINIEE 237
Cdd:PRK05815 152 SRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEEEH 227
 
Name Accession Description Interval E-value
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 5-237 6.62e-56

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 178.06  E-value: 6.62e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994   5 INPIISIGPVIFNL-TMLAMTLLIVGVIFVFIYWASRNMTLKPKGKQNVLEYVYDFVIGFTEPNIGSRYMKdYSLFFLCL 83
Cdd:PRK05815   1 IEHHLIIGFGGFNFdSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKK-FAPLAFTL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  84 FLFMVIANNLGLMTkiqtidgtNWWSSPTANLQYDLTLSFLVILLTHIESVRRRGFKKSIKSF-MSPV-FVIPMNILEEF 161
Cdd:PRK05815  80 FLFILLMNLLGLIP--------YLLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFyLQPHpLLLPIEIISEF 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446314994 162 TNFLSLALRIFGNIFAGEVMTSLLLLLSHQAIYWYPVAFGANLAWTAFSVFISCIQAYVFTLLTSVYLGNKINIEE 237
Cdd:PRK05815 152 SRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEEEH 227
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 21-234 3.45e-47

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: 155.23  E-value: 3.45e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  21 LAMTLLIVGVIFVFIYWASRNMTLKPKGKQNVLEYVYDFVIGFTEPNIGSRYMKdYSLFFLCLFLFMVIANNLGLMTkiq 100
Cdd:COG0356    3 VLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRK-FAPLLLTLFLFILVSNLLGLIP--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994 101 tidgtnWWSSPTANLQYDLTLSFLVILLTHIESVRRRGFKKSIKS-FMSPV-----FVIPMNILEEFTNFLSLALRIFGN 174
Cdd:COG0356   79 ------GLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHlFFPPFpwlapLMLPIEIISELARPLSLSLRLFGN 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994 175 IFAGEVMTSLLLLLShQAIYWYPVAFGANLAWTAFSVFISCIQAYVFTLLTSVYLGNKIN 234
Cdd:COG0356  153 MFAGHIILLLLAGLA-PFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVE 211
ATP-synt_A pfam00119
ATP synthase A chain;
21-230 4.77e-40

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 136.85  E-value: 4.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994   21 LAMTLLIVGVIFVFIYWASRN-MTLKPKGKQNVLEYVYDFVIGFTEPNIGSRYMKDYSLFFLCLFLFMVIANNLGLMTKI 99
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKtKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIPKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  100 QTIdgtnwwSSPTANLQYDLTLSFLVILLTHIESVRRRGFKKSIKSFMSP-------VFVIPMNILEEFTNFLSLALRIF 172
Cdd:pfam00119  81 PGG------FTVTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKLFVPpvplplvPLLLPIEIISEFARPVSLSLRLF 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446314994  173 GNIFAGEVMTSLLLLL----SHQAIYWYPVAFGANLAWTAFSVFISCIQAYVFTLLTSVYLG 230
Cdd:pfam00119 155 GNMLAGHLLLLLLAGLifalLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 15-233 7.90e-25

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: 97.66  E-value: 7.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994   15 IFNLTMLAMTLLIVGVIFVFIYWASRNMtlKPKGKQNVLEYVYDFVIGFTEPNIGSRYMKdYSLFFLCLFLFMVIANNLG 94
Cdd:TIGR01131  12 LFSLTLLSLILLLSLLIFLISSSLSRWL--IPSRWQNLMESIYEFVLSIVKSQIGGKKGK-FFPLIFTLFLFILISNLLG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994   95 LMTkiqtidgtnWWSSPTANLQYDLTLSFLVILLTHIESVRRR--GFKKSIKSFMSPV----FVIPMNILEEFTNFLSLA 168
Cdd:TIGR01131  89 LIP---------YSFTPTSHLSFTLGLALPLWLGLTISGFRKHpkGFLAHLVPSGTPLplipFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446314994  169 LRIFGNIFAGEVMTSLL--LLLSHQAIYWYPVAFGANLAWTAFSVFISCIQAYVFTLLTSVYLGNKI 233
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLsgLLFSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 107-230 2.80e-24

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: 94.39  E-value: 2.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994 107 WWSSPTANLQYDLTLSFLVILLTHIESVRRRGFKKSIKSFMSPV------FVIPMNILEEFTNFLSLALRIFGNIFAGEV 180
Cdd:cd00310   26 YSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTplplapLMVPIELISELIRPLSLSVRLFANMFAGHL 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446314994 181 MTSLLLLLSHQAIYW-YPVAFGANLAWTAFSVFISCIQAYVFTLLTSVYLG 230
Cdd:cd00310  106 LLALLSGLVPSLLSSvGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
 
Name Accession Description Interval E-value
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 5-237 6.62e-56

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 178.06  E-value: 6.62e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994   5 INPIISIGPVIFNL-TMLAMTLLIVGVIFVFIYWASRNMTLKPKGKQNVLEYVYDFVIGFTEPNIGSRYMKdYSLFFLCL 83
Cdd:PRK05815   1 IEHHLIIGFGGFNFdSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKK-FAPLAFTL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  84 FLFMVIANNLGLMTkiqtidgtNWWSSPTANLQYDLTLSFLVILLTHIESVRRRGFKKSIKSF-MSPV-FVIPMNILEEF 161
Cdd:PRK05815  80 FLFILLMNLLGLIP--------YLLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFyLQPHpLLLPIEIISEF 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446314994 162 TNFLSLALRIFGNIFAGEVMTSLLLLLSHQAIYWYPVAFGANLAWTAFSVFISCIQAYVFTLLTSVYLGNKINIEE 237
Cdd:PRK05815 152 SRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEEEH 227
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 21-234 3.45e-47

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: 155.23  E-value: 3.45e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  21 LAMTLLIVGVIFVFIYWASRNMTLKPKGKQNVLEYVYDFVIGFTEPNIGSRYMKdYSLFFLCLFLFMVIANNLGLMTkiq 100
Cdd:COG0356    3 VLMSWLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRK-FAPLLLTLFLFILVSNLLGLIP--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994 101 tidgtnWWSSPTANLQYDLTLSFLVILLTHIESVRRRGFKKSIKS-FMSPV-----FVIPMNILEEFTNFLSLALRIFGN 174
Cdd:COG0356   79 ------GLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHlFFPPFpwlapLMLPIEIISELARPLSLSLRLFGN 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994 175 IFAGEVMTSLLLLLShQAIYWYPVAFGANLAWTAFSVFISCIQAYVFTLLTSVYLGNKIN 234
Cdd:COG0356  153 MFAGHIILLLLAGLA-PFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVE 211
ATP-synt_A pfam00119
ATP synthase A chain;
21-230 4.77e-40

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 136.85  E-value: 4.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994   21 LAMTLLIVGVIFVFIYWASRN-MTLKPKGKQNVLEYVYDFVIGFTEPNIGSRYMKDYSLFFLCLFLFMVIANNLGLMTKI 99
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKtKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIPKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  100 QTIdgtnwwSSPTANLQYDLTLSFLVILLTHIESVRRRGFKKSIKSFMSP-------VFVIPMNILEEFTNFLSLALRIF 172
Cdd:pfam00119  81 PGG------FTVTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKLFVPpvplplvPLLLPIEIISEFARPVSLSLRLF 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446314994  173 GNIFAGEVMTSLLLLL----SHQAIYWYPVAFGANLAWTAFSVFISCIQAYVFTLLTSVYLG 230
Cdd:pfam00119 155 GNMLAGHLLLLLLAGLifalLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 15-233 7.90e-25

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: 97.66  E-value: 7.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994   15 IFNLTMLAMTLLIVGVIFVFIYWASRNMtlKPKGKQNVLEYVYDFVIGFTEPNIGSRYMKdYSLFFLCLFLFMVIANNLG 94
Cdd:TIGR01131  12 LFSLTLLSLILLLSLLIFLISSSLSRWL--IPSRWQNLMESIYEFVLSIVKSQIGGKKGK-FFPLIFTLFLFILISNLLG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994   95 LMTkiqtidgtnWWSSPTANLQYDLTLSFLVILLTHIESVRRR--GFKKSIKSFMSPV----FVIPMNILEEFTNFLSLA 168
Cdd:TIGR01131  89 LIP---------YSFTPTSHLSFTLGLALPLWLGLTISGFRKHpkGFLAHLVPSGTPLplipFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446314994  169 LRIFGNIFAGEVMTSLL--LLLSHQAIYWYPVAFGANLAWTAFSVFISCIQAYVFTLLTSVYLGNKI 233
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLsgLLFSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 107-230 2.80e-24

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: 94.39  E-value: 2.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994 107 WWSSPTANLQYDLTLSFLVILLTHIESVRRRGFKKSIKSFMSPV------FVIPMNILEEFTNFLSLALRIFGNIFAGEV 180
Cdd:cd00310   26 YSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTplplapLMVPIELISELIRPLSLSVRLFANMFAGHL 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446314994 181 MTSLLLLLSHQAIYW-YPVAFGANLAWTAFSVFISCIQAYVFTLLTSVYLG 230
Cdd:cd00310  106 LLALLSGLVPSLLSSvGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
 4-234 2.16e-17

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 77.81  E-value: 2.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994   4 SINPIISIGPVIFNLTMLAmTLLIVGVIFVFIYWASRNMTLKPKGKQNVLEYVYDFVIG------FTEPnigsrymKDYS 77
Cdd:PRK13421   7 STVPLFSLGPVPISAPVVV-TWAIMAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAqirdtmQTDP-------APYR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  78 LFFLCLFLFMVIANNLGLMTKIQtidgtnwwsSPTANLQYDLTLSFLVILLTHIESVRRRGFKKSIKSFMSPVFV-IPMN 156
Cdd:PRK13421  79 ALIGTLFLFVLVANWSSLVPGVE---------PPTAHLETDAALALIVFLATIYYGVRARGVRGYLATFAEPTWVmIPLN 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446314994 157 ILEEFTNFLSLALRIFGNIFAGEVMTSLLLLLshqAIYWYPVAFganlawTAFSVFISCIQAYVFTLLTSVYLGNKIN 234
Cdd:PRK13421 150 LVEQLTRTFSLIVRLFGNVMSGVFVIGIVLSL---AGLLVPIPL------MALDLLTGAVQAYIFAVLAMVFIGAAVS 218
atpI CHL00046
ATP synthase CF0 A subunit
 11-230 1.59e-15

ATP synthase CF0 A subunit


Pssm-ID: 176987  Cd Length: 228  Bit Score: 73.04  E-value: 1.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  11 IGPVIFNLTMLAMTLLIVGVIFVFIYWASRNMTLKPKGKQNVLEYVYDFVIGFTEPNIGSRYMKDYSLFFLCLFLFMVIA 90
Cdd:CHL00046  16 IGGFQVHGQVLITSWVVIAILLGSALLATRNLQTIPTGGQNFFEYVLEFIRDLAKTQIGEEEYRPWVPFIGTMFLFIFVS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  91 NNLGLMTKIQTIDGTNW-WSSPTANLQYDLTLSFLVILLTHIESVRRRG---FKKSIKSfmSPVFvIPMNILEEFTNFLS 166
Cdd:CHL00046  96 NWSGALLPWKLIELPHGeLAAPTNDINTTVALALLTSVAYFYAGLSKKGlgyFGKYIQP--TPIL-LPINILEDFTKPLS 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446314994 167 LALRIFGNIFAGEVMTSLLLLLshqaiywypVAFGANLAWTAFSVFISCIQAYVFTLLTSVYLG 230
Cdd:CHL00046 173 LSFRLFGNILADELVVAVLVSL---------VPLVVPIPVMFLGLFTSGIQALIFATLAAAYIG 227
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 10-233 1.44e-12

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 64.76  E-value: 1.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  10 SIGPVIFNLTMLAmTLLIVGVIFVFIYWASRNMTLKPKGKQNVLEYVYDFVIGFTEpNIGSRYMKDYSLFFLCLFLFMVI 89
Cdd:PRK13420  10 HIGPLPITESVLT-TWGIMIVLVLASWLTTRRLSLDPGRFQVALEGVVSTIEDAIK-EVLPRHARLVLPFVGTLWIFILV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  90 ANNLGLMTKIQtidgtnwwsSPTANLQYDLTLSFLVILLTHIESVRRRGFKKSIKSFMSPV-FVIPMNILEEFTNFLSLA 168
Cdd:PRK13420  88 ANLIGLIPGFH---------SPTADLSVTAALALLVFFSVHWFGIRAEGLREYLKHYLSPSpFLLPFHLISEITRTLALA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446314994 169 LRIFGNIFAGEvMTSLLLLLShqAIYWYPVAFganlawTAFSVFISCIQAYVFTLLTSVYLGNKI 233
Cdd:PRK13420 159 VRLFGNIMSLE-LAALLVLLV--AGFLVPVPI------LMLHIIEALVQAYIFGMLALIYIAGGI 214
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 20-230 5.34e-12

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 64.38  E-value: 5.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  20 MLAMTLLIVGVIFVFIYWASRNMT--LKPKGKQNVLEYVYDFV-IGFTEPNIGSRYMKdYSLFFLCLFLFMVIANNLGLM 96
Cdd:PRK13419 112 MMWIASAILLVVFLAAGRKYKKMTksQAPKGLANAMEALVEFIrLDVAKSNIGHGYEK-FLPYLLTVFFFILVCNLLGLV 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  97 TkiqtidgtnWWSSPTANLQYDLTLSFLVILLTHIESVRRRGFKKSIKSFMSPV------FVIPMNILEEFTNFLSLALR 170
Cdd:PRK13419 191 P---------YGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGThwslwiIMIPIEFIGLFTKPFALTVR 261

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446314994 171 IFGNIFAGE-VMTSLLLLLSHQAIYWypVAFGANLAWTAF----SVFISCIQAYVFTLLTSVYLG 230
Cdd:PRK13419 262 LFANMTAGHiVILSLIFISFILKSYI--VAVAVSVPFAIFiyllELFVAFLQAYIFTMLSALFIG 324
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 15-235 1.30e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 45.03  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  15 IFNLTMLAMTLLIVgVIFVFIywASRNMTLKPKGKQNVLEYVYDFVIGFTEPNIGSRYMKdYSLFFLCLFLFMVIANNLG 94
Cdd:MTH00172  14 LIGLTNSSIMMILV-IIVVLL--LFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLK-YFPFIISLFFFIVFLNLLG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  95 LMTKIQTidgtnwwssPTANLQYDLTLSFLVILlthieSVRRRGFKKSIKSFMS-------PVFVIPMNILEEFTNFLS- 166
Cdd:MTH00172  90 LFPYVFT---------PTTHIVVTLGLSFSIII-----GVTLAGFWRFKWDFFSilmpsgaPLGLAPLLVLIETVSYISr 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446314994 167 ---LALRIFGNIFAGEVmtsLLLLLSHQAIYWYPVAFGANLAWTAFSVFIS-------CIQAYVFTLLTSVYLGNKINI 235
Cdd:MTH00172 156 aisLGVRLAANLSAGHL---LFAILAGFGFNMLCASGFLSLFPLLIMVFITlleiavaVIQAYVFCLLTTIYLADTIVL 231
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 148-229 1.55e-04

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 41.48  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994 148 SPVFVIPMNILEE----FTNFLSLALRIFGNIFAGEVMTSLL----LLLSHQAIYWYPVAFGANLAWTAFSVFISCIQAY 219
Cdd:MTH00101 133 TPTPLIPMLVIIEtislFIQPMALAVRLTANITAGHLLIHLIggatLALMSISTTTALITFIILILLTILEFAVALIQAY 212

                         90
                 ....*....|
gi 446314994 220 VFTLLTSVYL 229
Cdd:MTH00101 213 VFTLLVSLYL 222
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 17-229 7.25e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 39.63  E-value: 7.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  17 NLTMLAMTLLIVGVIFVFIYWASRNMTLKPKGKQNVLEYVYDFVIGFTEpNIGSRYMKDYSLFFLCLFLFMVIANNLGLM 96
Cdd:MTH00176  13 NKNIFSMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMIL-RSNGSYILGSASIIISLFILVMSLNLSGLI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994  97 TKIqtidgtnwwSSPTANLQYDLTLSFLVILLTHIESVRR--RGFKKSIKSFMSPVFVIPMNILEEFTNFL----SLALR 170
Cdd:MTH00176  92 PYV---------FTSTSHLVITLSLALPLWLGVILSGFINnfYSRLSHLVPQGTPPLLNPFLVLIELVSLLirplTLAVR 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446314994 171 IFGNIFAGEVMTSLL-----LLLSHQAIYWYPVAFGAnLAWTAFSVFISCIQAYVFTLLTSVYL 229
Cdd:MTH00176 163 LAANLSAGHLLLGLLgaamwGLLPVSPLIGFLLLIVQ-ILYFMFEIAVCMIQAYVFTLLLSLYL 225
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 148-229 6.50e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 36.73  E-value: 6.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994 148 SPVFVIPMNILEEFTNFL----SLALRIFGNIFAGEV------MTSLLLLLSHQAIYwyPVAFGANLAWTAFSVFISCIQ 217
Cdd:MTH00120 134 TPTPLIPALILIETISLLirplALGVRLTANLTAGHLliqlisTATLNLLPTMPTLS--LLTLIILLLLTILELAVAMIQ 211

                         90
                 ....*....|..
gi 446314994 218 AYVFTLLTSVYL 229
Cdd:MTH00120 212 AYVFVLLLSLYL 223
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 108-230 9.63e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 36.79  E-value: 9.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446314994 108 WS--SPTANLQYDLTLSFLVILLTHIESVRRRGFK-------KSIKSFMSPVFVIPMNILEEFTNFLSLALRIFGNIFAG 178
Cdd:PRK13417 213 WSgiTVTGDISVTMTLALLTMFLIYGAGFSYQGPKfiwhsvpNGVPLLLYPIMWPLEFIVSPMAKTFALTVRLLANMTAG 292

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446314994 179 EVMTSLLLLLSHQAIYW--YPVAFGANLAWTAFSVFISCIQAYVFTLLTSVYLG 230
Cdd:PRK13417 293 HVIILALMGFIFQFQSWgiVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFVG 346
 
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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