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Conserved domains on  [gi|1789851285|gb|QHB76536|]
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ATP synthase F0 subunit 6 (mitochondrion) [Hylomyscus alleni]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009564)

ATP synthase F0 subunit 6 is part of the mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V), which produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 3.95e-135

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 378.53  E-value: 3.95e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285   1 MNENLFSSFITPTVMGLPIVITIIMFPSILFPSSERLINNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  81 STNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1789851285 161 TANITAGHLLMHLIGGATLVLMNISPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 3.95e-135

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 378.53  E-value: 3.95e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285   1 MNENLFSSFITPTVMGLPIVITIIMFPSILFPSSERLINNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  81 STNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1789851285 161 TANITAGHLLMHLIGGATLVLMNISPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 15-225 2.54e-52

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: 168.54  E-value: 2.54e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  15 MGLPIVITIIMFPSILFPSSERLINNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIGSTNLLGLLPHTFTP 94
Cdd:TIGR01131  17 LLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  95 TTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLI 174
Cdd:TIGR01131  97 TSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1789851285 175 GGATLVLMniSPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 177 SGLLFSLM--SSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 4.19e-41

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: 137.53  E-value: 4.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  65 GRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1789851285 145 ETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLMNISPPtatITFIILLMLTVLEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGL---LPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
13-223 6.41e-39

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 133.77  E-value: 6.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  13 TVMGLPIVITIIMFPSILFPSSERLINNRLHSFQHWLIKLIIKQMM-LIHTPKGRTWALMIVSLIMFIGSTNLLGLL--- 88
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpks 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  89 PHTFTPTTQLSMNLSMAIPLWAGAVILGFR-HKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAG 167
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1789851285 168 HLLMHLIGGATLVLMNISPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 63-224 1.90e-25

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: 98.61  E-value: 1.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  63 PKGRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHK-LKNSLAHFLPQGTPIsLIPML 141
Cdd:COG0356    52 KKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPW-LAPLM 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285 142 IIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLMnisppTATITFIILLMLTVLEFAVALIQAYVFTLLVSLY 221
Cdd:COG0356   131 LPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLL-----LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVY 205


                  ...
gi 1789851285 222 LHD 224
Cdd:COG0356   206 ISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 3.95e-135

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 378.53  E-value: 3.95e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285   1 MNENLFSSFITPTVMGLPIVITIIMFPSILFPSSERLINNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  81 STNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1789851285 161 TANITAGHLLMHLIGGATLVLMNISPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-226 8.96e-88

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 258.60  E-value: 8.96e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285   1 MNENLFSSFITPTVMGLPIVITIIMFPSILFPSSE-RLINNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFI 79
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKnRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  80 GSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1789851285 160 LTANITAGHLLMHLIGGATLVLMNISPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-225 1.14e-83

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 248.25  E-value: 1.14e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285   1 MNENLFSSFITPTVMGLPIVITIIMFPSILFPS-SERLINNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFI 79
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTpTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  80 GSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1789851285 160 LTANITAGHLLMHLIGGATLVLMNISPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-226 2.06e-83

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 247.57  E-value: 2.06e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285   1 MNENLFSSFITPTVMGLPIVITIIMFPSILFPS-SERLINNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFI 79
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTpTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  80 GSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1789851285 160 LTANITAGHLLMHLIGGATLVLMNISPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-226 1.74e-72

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 219.82  E-value: 1.74e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285   1 MNENLFSSFITPTVMGLPIVITIIMFPSILFPSS-ERLINNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFI 79
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLtNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  80 GSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1789851285 160 LTANITAGHLLMHLIGGATLVLMNISPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00179  161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 15-225 2.54e-52

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: 168.54  E-value: 2.54e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  15 MGLPIVITIIMFPSILFPSSERLINNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIGSTNLLGLLPHTFTP 94
Cdd:TIGR01131  17 LLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  95 TTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLI 174
Cdd:TIGR01131  97 TSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1789851285 175 GGATLVLMniSPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 177 SGLLFSLM--SSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-225 3.52e-51

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 165.53  E-value: 3.52e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285   1 MNENLFSSFITPTVMGLPIVIT--IIMFPSILFPSSERLINNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMF 78
Cdd:MTH00035    3 INNSIFGQFSPDTILFIPLTLLssVIALSWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  79 IGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAV 158
Cdd:MTH00035   83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1789851285 159 RLTANITAGHLLMHLIGGATLVLMNiSPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00035  163 RLAANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-221 2.62e-49

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 160.72  E-value: 2.62e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285   1 MNENLFSSFITPTVMGLPIVITIIMFPSILFPSSERLINNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIG 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  81 STNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1789851285 161 TANITAGHLLMHLIGGATLVLMNISPPtatITFIILLMLTVLEFAVALIQAYVFTLLVSLY 221
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMILS---ILILIQILLLILESAVAIIQSYVFSVLSTLY 218
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 1.20e-41

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 141.32  E-value: 1.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285   1 MNENLFSSFITPTVMGLPIVI---TIIMFPSILFPSSERLINNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIM 77
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFSMISlswITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  78 FIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALA 157
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1789851285 158 VRLTANITAGHLLMHLIGGATLVLMNISPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 4.19e-41

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: 137.53  E-value: 4.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  65 GRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1789851285 145 ETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLMNISPPtatITFIILLMLTVLEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGL---LPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
13-223 6.41e-39

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 133.77  E-value: 6.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  13 TVMGLPIVITIIMFPSILFPSSERLINNRLHSFQHWLIKLIIKQMM-LIHTPKGRTWALMIVSLIMFIGSTNLLGLL--- 88
Cdd:pfam00119   1 LLMSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpks 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  89 PHTFTPTTQLSMNLSMAIPLWAGAVILGFR-HKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAG 167
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1789851285 168 HLLMHLIGGATLVLMNISPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 25-224 5.39e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 131.91  E-value: 5.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  25 MFPSILFPSSERLINNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSM 104
Cdd:MTH00173   28 LMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285 105 AIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLIGGA-TLVLMN 183
Cdd:MTH00173  108 ALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYlSSSLFS 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1789851285 184 ISPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00173  188 SSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-226 3.48e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 116.76  E-value: 3.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285   1 MNENLFSSF-----ITPTVMGLPIVITIIMFPSILFPSSERLINNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSL 75
Cdd:MTH00005    1 MLTDIFSSFdpatnSLFNNLSSTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  76 IMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMA 155
Cdd:MTH00005   81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1789851285 156 LAVRLTANITAGHLLMHLIGGATLVLMnISPPTATITFIILLMLTVL-EFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00005  161 LSFRLAANMSAGHIVLSLIGIYAASAL-FSSISSTILLILTQMGYILfEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 19-224 1.50e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 115.14  E-value: 1.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  19 IVITIIMFPSILFPSSERLINNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQL 98
Cdd:MTH00172   22 IMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHI 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  99 SMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLIGGAT 178
Cdd:MTH00172  102 VVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFG 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1789851285 179 LVLMNISPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00172  182 FNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 10-224 7.28e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 111.25  E-value: 7.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  10 ITPTVMGLPIVITIIMFpsILFPSSERLINNRLHSFQHwLIKLIIKQMMLIHTPK-GRTWALMIVSLIMFIGSTNLLGLL 88
Cdd:MTH00175   26 VTFTNSSMMMVLAVIIF--WLLLKGDKLIPNRWQSIME-LIYLNIRSVVHDNLGKsGQKYFPFILSLFLFIAILNILGLF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  89 PHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAGH 168
Cdd:MTH00175  103 PYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGH 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1789851285 169 LLMHLIGGATL-VLMNISPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00175  183 LLFAILSGFAFnMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 63-224 1.90e-25

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: 98.61  E-value: 1.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  63 PKGRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHK-LKNSLAHFLPQGTPIsLIPML 141
Cdd:COG0356    52 KKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPW-LAPLM 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285 142 IIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLMnisppTATITFIILLMLTVLEFAVALIQAYVFTLLVSLY 221
Cdd:COG0356   131 LPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLL-----LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVY 205


                  ...
gi 1789851285 222 LHD 224
Cdd:COG0356   206 ISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 10-224 9.59e-23

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 91.78  E-value: 9.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  10 ITPTVMGLPIVITIIMFPSILFPSSERLINNRLHSFQHWLIKLIIKQMMLIHTPKGRTWALMIVSLIMFIGSTNLLGLLP 89
Cdd:PRK05815   14 FDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  90 -HTFTPTTQLSMNLSMAIPLWAGAVILGFR-HKLKNSLAHFLPQGTPIslipmLIIIETISLFIQPMALAVRLTANITAG 167
Cdd:PRK05815   94 yLLFPPTADINVTLALALIVFVLVIYYGIKkKGLGGYLKEFYLQPHPL-----LLPIEIISEFSRPISLSLRLFGNMLAG 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1789851285 168 HLLMHLIGGatlvLMNISPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYLHD 224
Cdd:PRK05815  169 ELILALIAL----LGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 64-224 2.27e-20

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 86.15  E-value: 2.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  64 KGRTWALMIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLII 143
Cdd:MTH00174   86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285 144 IETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLMNISPPTAT-ITFIILLMLTVLEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00174  166 IETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSfVPFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245


                  ..
gi 1789851285 223 HD 224
Cdd:MTH00174  246 RD 247
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 72-222 9.76e-18

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 80.17  E-value: 9.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  72 IVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFR-HKLKNSLAHfLPQGTPISLIPMLIIIETISLF 150
Cdd:PRK13419  174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAH-LTGGTHWSLWIIMIPIEFIGLF 252

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1789851285 151 IQPMALAVRLTANITAGHL-LMHLIGGATLVLMNISPPTATITFIILLMLtvLEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13419  253 TKPFALTVRLFANMTAGHIvILSLIFISFILKSYIVAVAVSVPFAIFIYL--LELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 71-222 3.28e-10

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 57.30  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  71 MIVSLIMFigstNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHKLKnsLAHFLPQGTPISLIPM-LIIIETISL 149
Cdd:MTH00087   58 TFIVLLLF----CFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEK--FSVYLSKGSDSFLKTFsMLFVEIVSE 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1789851285 150 FIQPMALAVRLTANITAGHLLMHLIGGATLvlmnispptatITFIILLMLTVLEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00087  132 LSRPLALTLRLTVNLMVGHLISSLLNFLGE-----------KYVWLSILAIMMECFVAFIQSYIFSRLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 93-222 8.69e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 54.51  E-value: 8.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  93 TPTTQLSMNLSMAIPLWAGAVILGFRHKLKNSLAHFLPQGTPISLIPMLIIIETI-SLFIQPMALAVRLTANITAGHLLM 171
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1789851285 172 HLIGGatLVLMNISPPTATITFIILLMLTVLEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13417  297 LALMG--FIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 71-222 4.32e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 45.89  E-value: 4.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789851285  71 MIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVILGFRHK-LKNSLAHFLpqgtpiSLIPMLIIIETISL 149
Cdd:PRK13420   77 FVGTLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEgLREYLKHYL------SPSPFLLPFHLISE 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1789851285 150 FIQPMALAVRLTANITAghllMHLIGGATLVLMNISPPtatitfIILLMLTVLEfavALIQAYVFTLLVSLYL 222
Cdd:PRK13420  151 ITRTLALAVRLFGNIMS----LELAALLVLLVAGFLVP------VPILMLHIIE---ALVQAYIFGMLALIYI 210
 
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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