NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15600753|ref|NP_254247|]
View 

ATP synthase subunit A [Pseudomonas aeruginosa PAO1]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 38-289 5.57e-75

F0F1 ATP synthase subunit A; Validated


:

Pssm-ID: 235617  Cd Length: 227  Bit Score: 228.53  E-value: 5.57e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753   38 EMGFWAFHVDTLGWSVLLGVVFLFIFRLAAKKATSGQPGGLQNFVEVMVEFVDTSVKDTFHGRNPLIAPLALTVFVWIFL 117
Cdd:PRK05815   6 IIGFGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  118 LNLIDLVPVdylpmlaakitgdehlfFRAVATTDPNATLGLSISVFALIVFYSIKVKGIGGFLGELTLHPFssknivvqI 197
Cdd:PRK05815  86 MNLLGLIPY-----------------LLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFYLQPH--------P 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  198 LLIPvnflLEFVTLIAKPVSLALRLFGNMYAGELIFILIAvMFGSGMFLLSALGVALNWAWAVFHILIITLQAFIFMMLT 277
Cdd:PRK05815 141 LLLP----IEIISEFSRPISLSLRLFGNMLAGELILALIA-LLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLT 215

                        250
                 ....*....|..
gi 15600753  278 IVYLSMAHEDNH 289
Cdd:PRK05815 216 IVYISMAVEEEH 227
 
Name Accession Description Interval E-value
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 38-289 5.57e-75

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 228.53  E-value: 5.57e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753   38 EMGFWAFHVDTLGWSVLLGVVFLFIFRLAAKKATSGQPGGLQNFVEVMVEFVDTSVKDTFHGRNPLIAPLALTVFVWIFL 117
Cdd:PRK05815   6 IIGFGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  118 LNLIDLVPVdylpmlaakitgdehlfFRAVATTDPNATLGLSISVFALIVFYSIKVKGIGGFLGELTLHPFssknivvqI 197
Cdd:PRK05815  86 MNLLGLIPY-----------------LLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFYLQPH--------P 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  198 LLIPvnflLEFVTLIAKPVSLALRLFGNMYAGELIFILIAvMFGSGMFLLSALGVALNWAWAVFHILIITLQAFIFMMLT 277
Cdd:PRK05815 141 LLLP----IEIISEFSRPISLSLRLFGNMLAGELILALIA-LLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLT 215

                        250
                 ....*....|..
gi 15600753  278 IVYLSMAHEDNH 289
Cdd:PRK05815 216 IVYISMAVEEEH 227
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 47-287 1.18e-68

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: 211.86  E-value: 1.18e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  47 DTLGWSVLLGVVFLFIFRLAAKKAtSGQPGGLQNFVEVMVEFVDTSVKDTFHGRNPLIAPLALTVFVWIFLLNLIDLVPv 126
Cdd:COG0356   1 DTVLMSWLAMLLLLLLFLLATRKL-KLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIP- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753 127 dylpmlaakitgdehlfFRAVATTDPNATLGLSISVFALIVFYSIKVKGIGGFLGELTLHPFssknivvqILLIPVNFLL 206
Cdd:COG0356  79 -----------------GLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHLFFPPF--------PWLAPLMLPI 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753 207 EFVTLIAKPVSLALRLFGNMYAGELIFILIAVMFgsGMFLLSALGVALNWAWAVFHILIITLQAFIFMMLTIVYLSMAHE 286
Cdd:COG0356 134 EIISELARPLSLSLRLFGNMFAGHIILLLLAGLA--PFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVE 211


                .
gi 15600753 287 D 287
Cdd:COG0356 212 E 212
ATP-synt_A pfam00119
ATP synthase A chain;
51-282 5.68e-57

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 182.30  E-value: 5.68e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753    51 WSVLLGVVFLFIFRLAAKKATSGQPGGLQNFVEVMVEFVDTSVKDTFHGRN-PLIAPLALTVFVWIFLLNLIDLVPVdyl 129
Cdd:pfam00119   3 MSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKKgRKFFPLLLTLFFFILVSNLLGLIPK--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753   130 pmlaakitgdehLFFRAVATTDPNATLGLSISVFALIVFYSIKVKGIGGFLGELTLHPfssknivVQILLIPVNFLLEFV 209
Cdd:pfam00119  80 ------------SPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKLFVPP-------VPLPLVPLLLPIEII 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600753   210 TLIAKPVSLALRLFGNMYAGELIFILIAVM---FGSGMFLLSALGVALNWAWAVFHILIITLQAFIFMMLTIVYLS 282
Cdd:pfam00119 141 SEFARPVSLSLRLFGNMLAGHLLLLLLAGLifaLLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 41-282 1.40e-32

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: 119.62  E-value: 1.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753    41 FWAFHVDTLGWSVLLGVVFLFIFRLAAKKATsgqPGGLQNFVEVMVEFVDTSVKDTFHGRNPLIAPLALTVFVWIFLLNL 120
Cdd:TIGR01131  10 ITLFSLTLLSLILLLSLLIFLISSSLSRWLI---PSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753   121 IDLVPvdylpmlaakitgdehlfFRAVATTDPNATLGLSISVFALIVFYSIKVKGIGgFLGELTLHPFSsknivvqILLI 200
Cdd:TIGR01131  87 LGLIP------------------YSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKG-FLAHLVPSGTP-------LPLI 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753   201 PVNFLLEFVTLIAKPVSLALRLFGNMYAGELIFILIAVM-FGSGMFLLSALGVALNWAWAVFHILIITLQAFIFMMLTIV 279
Cdd:TIGR01131 141 PFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGLlFSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCL 220


                  ...
gi 15600753   280 YLS 282
Cdd:TIGR01131 221 YLN 223
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 105-282 2.95e-28

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: 105.94  E-value: 2.95e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753 105 APLALTVFVWIFLLNLIDLVPvdylpmlaakitgdehlfFRAVATTDPNATLGLSISVFALIVFYSIKVKGIGGFLGELT 184
Cdd:cd00310   5 LPLLGTLFLFILFSNLLGLIP------------------YSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLP 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753 185 LHPFssknivvqILLIPVNFLLEFVTLIAKPVSLALRLFGNMYAGELIFILIAVMFGSGMFLLSALGVALNWAWAVFHIL 264
Cdd:cd00310  67 PGTP--------LPLAPLMVPIELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELF 138

                       170
                ....*....|....*...
gi 15600753 265 IITLQAFIFMMLTIVYLS 282
Cdd:cd00310 139 VAFIQAYVFTLLTAVYIS 156
 
Name Accession Description Interval E-value
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 38-289 5.57e-75

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 228.53  E-value: 5.57e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753   38 EMGFWAFHVDTLGWSVLLGVVFLFIFRLAAKKATSGQPGGLQNFVEVMVEFVDTSVKDTFHGRNPLIAPLALTVFVWIFL 117
Cdd:PRK05815   6 IIGFGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  118 LNLIDLVPVdylpmlaakitgdehlfFRAVATTDPNATLGLSISVFALIVFYSIKVKGIGGFLGELTLHPFssknivvqI 197
Cdd:PRK05815  86 MNLLGLIPY-----------------LLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFYLQPH--------P 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  198 LLIPvnflLEFVTLIAKPVSLALRLFGNMYAGELIFILIAvMFGSGMFLLSALGVALNWAWAVFHILIITLQAFIFMMLT 277
Cdd:PRK05815 141 LLLP----IEIISEFSRPISLSLRLFGNMLAGELILALIA-LLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLT 215

                        250
                 ....*....|..
gi 15600753  278 IVYLSMAHEDNH 289
Cdd:PRK05815 216 IVYISMAVEEEH 227
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 47-287 1.18e-68

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: 211.86  E-value: 1.18e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  47 DTLGWSVLLGVVFLFIFRLAAKKAtSGQPGGLQNFVEVMVEFVDTSVKDTFHGRNPLIAPLALTVFVWIFLLNLIDLVPv 126
Cdd:COG0356   1 DTVLMSWLAMLLLLLLFLLATRKL-KLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIP- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753 127 dylpmlaakitgdehlfFRAVATTDPNATLGLSISVFALIVFYSIKVKGIGGFLGELTLHPFssknivvqILLIPVNFLL 206
Cdd:COG0356  79 -----------------GLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHLFFPPF--------PWLAPLMLPI 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753 207 EFVTLIAKPVSLALRLFGNMYAGELIFILIAVMFgsGMFLLSALGVALNWAWAVFHILIITLQAFIFMMLTIVYLSMAHE 286
Cdd:COG0356 134 EIISELARPLSLSLRLFGNMFAGHIILLLLAGLA--PFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVE 211


                .
gi 15600753 287 D 287
Cdd:COG0356 212 E 212
ATP-synt_A pfam00119
ATP synthase A chain;
51-282 5.68e-57

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 182.30  E-value: 5.68e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753    51 WSVLLGVVFLFIFRLAAKKATSGQPGGLQNFVEVMVEFVDTSVKDTFHGRN-PLIAPLALTVFVWIFLLNLIDLVPVdyl 129
Cdd:pfam00119   3 MSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKKgRKFFPLLLTLFFFILVSNLLGLIPK--- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753   130 pmlaakitgdehLFFRAVATTDPNATLGLSISVFALIVFYSIKVKGIGGFLGELTLHPfssknivVQILLIPVNFLLEFV 209
Cdd:pfam00119  80 ------------SPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKLFVPP-------VPLPLVPLLLPIEII 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600753   210 TLIAKPVSLALRLFGNMYAGELIFILIAVM---FGSGMFLLSALGVALNWAWAVFHILIITLQAFIFMMLTIVYLS 282
Cdd:pfam00119 141 SEFARPVSLSLRLFGNMLAGHLLLLLLAGLifaLLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 41-282 1.40e-32

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: 119.62  E-value: 1.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753    41 FWAFHVDTLGWSVLLGVVFLFIFRLAAKKATsgqPGGLQNFVEVMVEFVDTSVKDTFHGRNPLIAPLALTVFVWIFLLNL 120
Cdd:TIGR01131  10 ITLFSLTLLSLILLLSLLIFLISSSLSRWLI---PSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753   121 IDLVPvdylpmlaakitgdehlfFRAVATTDPNATLGLSISVFALIVFYSIKVKGIGgFLGELTLHPFSsknivvqILLI 200
Cdd:TIGR01131  87 LGLIP------------------YSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKG-FLAHLVPSGTP-------LPLI 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753   201 PVNFLLEFVTLIAKPVSLALRLFGNMYAGELIFILIAVM-FGSGMFLLSALGVALNWAWAVFHILIITLQAFIFMMLTIV 279
Cdd:TIGR01131 141 PFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGLlFSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCL 220


                  ...
gi 15600753   280 YLS 282
Cdd:TIGR01131 221 YLN 223
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 105-282 2.95e-28

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: 105.94  E-value: 2.95e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753 105 APLALTVFVWIFLLNLIDLVPvdylpmlaakitgdehlfFRAVATTDPNATLGLSISVFALIVFYSIKVKGIGGFLGELT 184
Cdd:cd00310   5 LPLLGTLFLFILFSNLLGLIP------------------YSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLP 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753 185 LHPFssknivvqILLIPVNFLLEFVTLIAKPVSLALRLFGNMYAGELIFILIAVMFGSGMFLLSALGVALNWAWAVFHIL 264
Cdd:cd00310  67 PGTP--------LPLAPLMVPIELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELF 138

                       170
                ....*....|....*...
gi 15600753 265 IITLQAFIFMMLTIVYLS 282
Cdd:cd00310 139 VAFIQAYVFTLLTAVYIS 156
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 52-289 3.39e-24

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 99.82  E-value: 3.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753   52 SVLLGVVFLFIFRLAAKKATSGQPGGLQNFVEVMVEFV--DTSVKDTFHGRNPLIaPLALTVFVWIFLLNLIDLVPvdyl 129
Cdd:PRK13419 117 SAILLVVFLAAGRKYKKMTKSQAPKGLANAMEALVEFIrlDVAKSNIGHGYEKFL-PYLLTVFFFILVCNLLGLVP---- 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  130 pmlaakitgdehlfFRAVATTDPNATLGLSISVFALIVFYSIKVKGIGGFLGELT--LHPfsskniVVQILLIPVnfllE 207
Cdd:PRK13419 192 --------------YGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTggTHW------SLWIIMIPI----E 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  208 FVTLIAKPVSLALRLFGNMYAGEliFILIAVMFGSGMFLLSALGVALNWAWAVF----HILIITLQAFIFMMLTIVYLSM 283
Cdd:PRK13419 248 FIGLFTKPFALTVRLFANMTAGH--IVILSLIFISFILKSYIVAVAVSVPFAIFiyllELFVAFLQAYIFTMLSALFIGL 325

                        250
                 ....*....|.
gi 15600753  284 A-----HEDNH 289
Cdd:PRK13419 326 AtahegHDEEH 336
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 48-282 7.12e-12

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 63.61  E-value: 7.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753   48 TLGWSVLLGVVFLFIFRLAAKKAT---SGQPGGLQNFVEVMVEFVDTSVKDTFHGRNPLIAPLALTVFVWIFLLNLIDLV 124
Cdd:PRK13420  15 PITESVLTTWGIMIVLVLASWLTTrrlSLDPGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFVGTLWIFILVANLIGLI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  125 PVDYLPmlaakitgdehlffravaTTDPNATLGLSISVFALIVFYSIKVKGIGGFLGEltlhpfssknivvqiLLIPVNF 204
Cdd:PRK13420  95 PGFHSP------------------TADLSVTAALALLVFFSVHWFGIRAEGLREYLKH---------------YLSPSPF 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  205 LLEF--VTLIAKPVSLALRLFGNMYAGELIFILIAVMFGsgmfLLSALGVALnwawavFHILIITLQAFIFMMLTIVYLS 282
Cdd:PRK13420 142 LLPFhlISEITRTLALAVRLFGNIMSLELAALLVLLVAG----FLVPVPILM------LHIIEALVQAYIFGMLALIYIA 211
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
 75-289 3.25e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 58.94  E-value: 3.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753   75 PGGLQNFVEVMVEFVDTSVKDTFHGRNPLIAPLALTVFVWIFLLNLIDLVPvdylpmlaakitgdehlffravATTDPNA 154
Cdd:PRK13421  48 PGRLQSVLELVVTTIDAQIRDTMQTDPAPYRALIGTLFLFVLVANWSSLVP----------------------GVEPPTA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  155 TL----GLSISVFALIVFYSIKVKGIGGFLGEltlhpFSSKNIVvqilLIPVNFLLEfvtlIAKPVSLALRLFGNMYAGE 230
Cdd:PRK13421 106 HLetdaALALIVFLATIYYGVRARGVRGYLAT-----FAEPTWV----MIPLNLVEQ----LTRTFSLIVRLFGNVMSGV 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600753  231 liFILIAVMFGSGMFLLSALgVALNwawavfhILIITLQAFIFMMLTIVYLSMAHEDNH 289
Cdd:PRK13421 173 --FVIGIVLSLAGLLVPIPL-MALD-------LLTGAVQAYIFAVLAMVFIGAAVSDDE 221
atpI CHL00046
ATP synthase CF0 A subunit
 38-245 2.09e-07

ATP synthase CF0 A subunit


Pssm-ID: 176987  Cd Length: 228  Bit Score: 50.70  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753   38 EMGFWAFHVDTLGWSVLLGVVFLFIFRLAAKKATSgQPGGLQNFVEVMVEFVDTSVKDTFHGRN-----PLIAPLALTVF 112
Cdd:CHL00046  15 QIGGFQVHGQVLITSWVVIAILLGSALLATRNLQT-IPTGGQNFFEYVLEFIRDLAKTQIGEEEyrpwvPFIGTMFLFIF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  113 VW-----IFLLNLIDLVPVDylpmLAAkitgdehlffravATTDPNATLGLsisvfALIV----FYS-IKVKGIGGFLGE 182
Cdd:CHL00046  94 VSnwsgaLLPWKLIELPHGE----LAA-------------PTNDINTTVAL-----ALLTsvayFYAgLSKKGLGYFGKY 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600753  183 LTLHPFssknivvqilLIPVNFLLEFvtliAKPVSLALRLFGNMYAGEL----------IFILIAVMFgSGMF 245
Cdd:CHL00046 152 IQPTPI----------LLPINILEDF----TKPLSLSFRLFGNILADELvvavlvslvpLVVPIPVMF-LGLF 209
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 59-284 1.05e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 49.50  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753   59 FLFIFRLAAKKATSGQPGGLQ----NFVEVMVEFVDTSVKD-TFHGRNPLIAPLALTVFVWIFLLNLIDLVPV------- 126
Cdd:PRK13417 107 FLFLIFIPAANIIAKNPLKVQsrfaNTVEVFVNFLRKDIVDeSMHGHGHSYYHYIFTLFFFILFCNLMGLVPSvgeltvv 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  127 --DYLPMLAAKITGDEHLFFRAVATTDPNATLGLSISVFALIVFYSIKVKGIGGFLGELTLHPFSSKNIVVQILLIPVNF 204
Cdd:PRK13417 187 asDYGGLVALGVMDHTPHALPTFAKVWSGITVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMW 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  205 LLEF-VTLIAKPVSLALRLFGNMYAGE-LIFILIAVMFGSGMFLLSALGVALNWAWAVFHILIITLQAFIFMMLTIVYLS 282
Cdd:PRK13417 267 PLEFiVSPMAKTFALTVRLLANMTAGHvIILALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFVG 346


                 ..
gi 15600753  283 MA 284
Cdd:PRK13417 347 LS 348
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 197-282 9.98e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 45.79  E-value: 9.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  197 ILLIPVNFLLEFVTLIAKPVSLALRLFGNMYAGELIFILIAVMFGSG-------MFLLSALGVALnwawAVFHILIITLQ 269
Cdd:MTH00176 138 PLLNPFLVLIELVSLLIRPLTLAVRLAANLSAGHLLLGLLGAAMWGLlpvspliGFLLLIVQILY----FMFEIAVCMIQ 213

                         90
                 ....*....|...
gi 15600753  270 AFIFMMLTIVYLS 282
Cdd:MTH00176 214 AYVFTLLLSLYLD 226
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 198-280 2.52e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 44.47  E-value: 2.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  198 LLIPVNFLLEFVTLIAKPVSLALRLFGNMYAGELIFILIA----VMFGSGMFLLSALGVALNWAWAVFHILIITLQAFIF 273
Cdd:MTH00173 139 GLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGnylsSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIF 218


                 ....*..
gi 15600753  274 MMLTIVY 280
Cdd:MTH00173 219 TLLIKLY 225
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 58-281 2.25e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 41.57  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753   58 VFLFIFRLAAKKATSGQPGGLQNFVEVMVEFVDTSVKDTFHGRNPLIAPLALTVFVWIFLLNLIDLVPVDYLPmlaakit 137
Cdd:MTH00172  25 ILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTP------- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  138 gdehlffravaTTDPNATLGLSISVFAlivfySIKVKGIGGFLGEL--TLHPFSSKnivvqILLIPVNFLLEFVTLIAKP 215
Cdd:MTH00172  98 -----------TTHIVVTLGLSFSIII-----GVTLAGFWRFKWDFfsILMPSGAP-----LGLAPLLVLIETVSYISRA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  216 VSLALRLFGNMYAGELIFILIAvMFGSGMFLLSALGVALNWAWAVFHIL----IITLQAFIFMMLTIVYL 281
Cdd:MTH00172 157 ISLGVRLAANLSAGHLLFAILA-GFGFNMLCASGFLSLFPLLIMVFITLleiaVAVIQAYVFCLLTTIYL 225
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 54-282 5.10e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 40.76  E-value: 5.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753   54 LLGVVFLFIFRLAAKKATsgqPGGLQNFVEVMVEFVDTSVKDTFHGRNPLIAPLALTVFVWIFLLNLIDLVPVDYLPmla 133
Cdd:MTH00175  35 MVLAVIIFWLLLKGDKLI---PNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVFTP--- 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  134 akitgdehlffravaTTDPNATLGLSISVF-ALIVFYSIKVKGigGFLGELTLHPfssknivVQILLIPVNFLLEFVTLI 212
Cdd:MTH00175 109 ---------------TAHIIITFGLSLSIIiAVTLLGFLTFKW--NFLSILMPGG-------APLVLAPFLVLIETLSYL 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600753  213 AKPVSLALRLFGNMYAGELIFILIA----VMFGSGMFLLSALGVALNWAWAVFHILIITLQAFIFMMLTIVYLS 282
Cdd:MTH00175 165 IRAISLGVRLAANISAGHLLFAILSgfafNMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLG 238
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 199-281 2.45e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 38.77  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  199 LIPVNFLLEFVTLIAKPVSLALRLFGNMYAGELIFILIAV----MFGSGMFLLSALGVALNWAWAVFHILIITLQAFIFM 274
Cdd:MTH00174 159 LAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASfawkMINTGILIGSFVPFAILIFVTILEMAVAIIQAYVFT 238


                 ....*..
gi 15600753  275 MLTIVYL 281
Cdd:MTH00174 239 LLTIVYL 245
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 197-282 3.05e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 38.23  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  197 ILLIPVNFLLEFVTLIAKPVSLALRLFGNMYAGELIFILIAVMFGSGMFLLSALGVALNWAWAVFHILIITLQAFIFMML 276
Cdd:MTH00157 135 PILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVL 214


                 ....*.
gi 15600753  277 TIVYLS 282
Cdd:MTH00157 215 STLYSS 220
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 197-281 6.35e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 37.25  E-value: 6.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600753  197 ILLIPVNFLLEFVTLIAKPVSLALRLFGNMYAGELIFILIA---VMFGSGMFLLSALGVALNWAWAVFHILIITLQAFIF 273
Cdd:MTH00073 136 TLLIPILIIIETISLFIRPLALGVRLTANLTAGHLLIQLIStatLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVF 215


                 ....*...
gi 15600753  274 MMLTIVYL 281
Cdd:MTH00073 216 VLLLSLYL 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH