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Conserved domains on  [gi|722489951|ref|YP_009107100|]
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ATP synthase F0 subunit 6 (mitochondrion) [Neomys fodiens]

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 1.68e-143

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 399.71  E-value: 1.68e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   1 MNENLFASFATPTMMGFPIVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIG 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 722489951 161 TANITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.68e-143

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 399.71  E-value: 1.68e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   1 MNENLFASFATPTMMGFPIVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIG 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 722489951 161 TANITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDNT 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 7.50e-55

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: 174.70  E-value: 7.50e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   15 MGFPIVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGSTNLLGLLPHSFTP 94
Cdd:TIGR01131  17 LLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   95 TTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLI 174
Cdd:TIGR01131  97 TSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 722489951  175 GEATLVLMSISPATafITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 177 SGLLFSLMSSAIFA--LLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 1.28e-42

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: 141.38  E-value: 1.28e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  65 GQTWTLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIII 144
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 722489951 145 ETISLFIQPMALAVRLTANITAGHLLIHLIGEATLVLMSISpatAFITFIILVMLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSV---GLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
14-223 1.20e-39

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 135.70  E-value: 1.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   14 MMGFPIVILIIMFPSIMFPTPnRLINNRLVAIQQWLIQLISKQMMA-IHNQKGQTWTLMLISLILFIGSTNLLGLL---P 89
Cdd:pfam00119   3 MSLIVALILLLFLLLATRKTK-KLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   90 HSFTPTTQLSMNLGMAIPLWAGTVISGFR-HKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLTANITAGH 168
Cdd:pfam00119  82 GGFTVTADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGH 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 722489951  169 LLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 162 LLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 19-224 1.83e-26

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: 101.30  E-value: 1.83e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  19 IVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGSTNLLGLLPHSFTPTTQL 98
Cdd:COG0356    8 LAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  99 SMNLGMAIPLWAGTVISGFRHK-TKASLAHFLPQGTPlPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLIgea 177
Cdd:COG0356   88 NVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLL--- 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 722489951 178 tlVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:COG0356  164 --AGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.68e-143

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 399.71  E-value: 1.68e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   1 MNENLFASFATPTMMGFPIVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIG 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00101  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 722489951 161 TANITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-226 2.68e-92

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 270.16  E-value: 2.68e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   1 MNENLFASFATPTMMGFPIVILIIMFPSIMFPTP-NRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFI 79
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPkNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 722489951 160 LTANITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-226 4.15e-89

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 262.21  E-value: 4.15e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   1 MNENLFASFATPTMMGFPIVILIIMFPSIMFPTP-NRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFI 79
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPtNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 722489951 160 LTANITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-225 7.91e-89

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 261.35  E-value: 7.91e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   1 MNENLFASFATPTMMGFPIVILIIMFPSIMFPTP-NRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFI 79
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPtSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 722489951 160 LTANITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-226 1.02e-76

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 230.61  E-value: 1.02e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   1 MNENLFASFATPTMMGFPIVILIIMFPSIMFPTP-NRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFI 79
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLtNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 722489951 160 LTANITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDNT 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 7.50e-55

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: 174.70  E-value: 7.50e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   15 MGFPIVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGSTNLLGLLPHSFTP 94
Cdd:TIGR01131  17 LLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   95 TTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLI 174
Cdd:TIGR01131  97 TSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 722489951  175 GEATLVLMSISPATafITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 177 SGLLFSLMSSAIFA--LLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-221 4.16e-50

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 162.64  E-value: 4.16e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   1 MNENLFASFATPTMMGFPIVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIG 80
Cdd:MTH00157   1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00157  81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 722489951 161 TANITAGHLLIHLIGEATLVLMSIspaTAFITFIILVMLTILEFAVALIQAYVFTLLVSLY 221
Cdd:MTH00157 161 AANMIAGHLLLTLLGNTGPSLSSM---ILSILILIQILLLILESAVAIIQSYVFSVLSTLY 218
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-225 7.38e-50

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 162.06  E-value: 7.38e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   1 MNENLFASFATPTMMGFPIVIL--IIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILF 78
Cdd:MTH00035   3 INNSIFGQFSPDTILFIPLTLLssVIALSWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  79 IGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAV 158
Cdd:MTH00035  83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 722489951 159 RLTANITAGHLLIHLIGEATLVLMSiSPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00035 163 RLAANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-222 1.28e-42

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: 141.38  E-value: 1.28e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  65 GQTWTLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIII 144
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 722489951 145 ETISLFIQPMALAVRLTANITAGHLLIHLIGEATLVLMSISpatAFITFIILVMLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSV---GLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 5-224 3.19e-41

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 140.00  E-value: 3.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   5 LFASFATPTMMGFPIVILIIMFPS---IMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGS 81
Cdd:MTH00173   5 LFSSFDDHNSSFSSLSFLMWLLSLmslFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLIS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  82 TNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLT 161
Cdd:MTH00173  85 LNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 722489951 162 ANITAGHLLIHLIGEA-TLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00173 165 ANISAGHIVLTLIGNYlSSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 1.24e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 138.63  E-value: 1.24e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   1 MNENLFASFATPTMMGFPIVILI---IMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLIL 77
Cdd:MTH00176   1 MLVDLFSSFDPPNKNIFSMISLSwitLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  78 FIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALA 157
Cdd:MTH00176  81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 722489951 158 VRLTANITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP-synt_A pfam00119
ATP synthase A chain;
14-223 1.20e-39

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 135.70  E-value: 1.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   14 MMGFPIVILIIMFPSIMFPTPnRLINNRLVAIQQWLIQLISKQMMA-IHNQKGQTWTLMLISLILFIGSTNLLGLL---P 89
Cdd:pfam00119   3 MSLIVALILLLFLLLATRKTK-KLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   90 HSFTPTTQLSMNLGMAIPLWAGTVISGFR-HKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLTANITAGH 168
Cdd:pfam00119  82 GGFTVTADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGH 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 722489951  169 LLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 162 LLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 5-224 4.80e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 118.99  E-value: 4.80e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   5 LFASFATPTMMGFPIVILIIMFPSimfptpNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGSTNL 84
Cdd:MTH00172  14 LIGLTNSSIMMILVIIVVLLLFKG------IKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  85 LGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLTANI 164
Cdd:MTH00172  88 LGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANL 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 165 TAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00172 168 SAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 4-226 5.92e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 118.68  E-value: 5.92e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951   4 NLFASFATPTMMGFPIVILIIMFPSIMFPTPNRLInnrlvAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGSTN 83
Cdd:MTH00005  14 NSLFNNLSSTAFWAFNFSIILLLSSSFWITPNRLS-----SIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  84 LLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLTAN 163
Cdd:MTH00005  89 LSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAAN 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 722489951 164 ITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00005 169 MSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 14-224 8.26e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 113.56  E-value: 8.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  14 MMGFPIVILIIMFPSimfptpNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGSTNLLGLLPHSFT 93
Cdd:MTH00175  34 MMVLAVIIFWLLLKG------DKLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVFT 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  94 PTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHL 173
Cdd:MTH00175 108 PTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAI 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 722489951 174 I-GEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00175 188 LsGFAFNMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 19-224 1.83e-26

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: 101.30  E-value: 1.83e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  19 IVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGSTNLLGLLPHSFTPTTQL 98
Cdd:COG0356    8 LAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  99 SMNLGMAIPLWAGTVISGFRHK-TKASLAHFLPQGTPlPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLIgea 177
Cdd:COG0356   88 NVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLL--- 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 722489951 178 tlVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:COG0356  164 --AGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 19-224 2.07e-23

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 93.71  E-value: 2.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  19 IVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGSTNLLGLLP-HSFTPTTQ 97
Cdd:PRK05815  23 LGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTAD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  98 LSMNLGMAIPLWAGTVISGFRHKtkaSLAHFLPQGTPLPlIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLIGea 177
Cdd:PRK05815 103 INVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGELILALIA-- 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 722489951 178 tlVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:PRK05815 177 --LLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 64-224 2.25e-22

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 91.54  E-value: 2.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  64 KGQTWTLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLII 143
Cdd:MTH00174  86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 144 IETISLFIQPMALAVRLTANITAGHLLIHLIGEATLVLMSISPAT-AFITFIILVMLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00174 166 IETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245


                 ..
gi 722489951 223 HD 224
Cdd:MTH00174 246 RD 247
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 72-222 8.03e-19

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 83.25  E-value: 8.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  72 LISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFR-HKTKASLAHfLPQGTPLPLIPMLIIIETISLF 150
Cdd:PRK13419 174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAH-LTGGTHWSLWIIMIPIEFIGLF 252

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 722489951 151 IQPMALAVRLTANITAGHLLI-HLIGEATLVLMSISPATAFITFIILVMLtiLEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13419 253 TKPFALTVRLFANMTAGHIVIlSLIFISFILKSYIVAVAVSVPFAIFIYL--LELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 71-222 3.11e-11

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 60.38  E-value: 3.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  71 MLISLILFigstNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASlaHFLPQGTPLPLIPM-LIIIETISL 149
Cdd:MTH00087  58 TFIVLLLF----CFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTFsMLFVEIVSE 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 722489951 150 FIQPMALAVRLTANITAGHLLIHLIGEATlvlmsispataFITFIILVMLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00087 132 LSRPLALTLRLTVNLMVGHLISSLLNFLG-----------EKYVWLSILAIMMECFVAFIQSYIFSRLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 65-222 1.15e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 57.21  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  65 GQTWTLMLISLILFIGSTNLLGLLP----------------------------HSF-------TPTTQLSMNLGMAIPLW 109
Cdd:PRK13417 154 GHSYYHYIFTLFFFILFCNLMGLVPsvgeltvvasdygglvalgvmdhtphalPTFakvwsgiTVTGDISVTMTLALLTM 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 110 AGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETI-SLFIQPMALAVRLTANITAGHLLIhlIGEATLVLMSISPAT 188
Cdd:PRK13417 234 FLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII--LALMGFIFQFQSWGI 311

                        170       180       190
                 ....*....|....*....|....*....|....
gi 722489951 189 AFITFIILVMLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13417 312 VPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 74-222 2.15e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 40.88  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951  74 SLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL-----WAGTVISGFRhktkASLAHFLPQGtplpliPMLIIIETIS 148
Cdd:PRK13420  80 TLWIFILVANLIGLIPGFHSPTADLSVTAALALLVffsvhWFGIRAEGLR----EYLKHYLSPS------PFLLPFHLIS 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 722489951 149 LFIQPMALAVRLTANITAGHLLihligeATLVLMsispATAFITFIILVMLTILEfavALIQAYVFTLLVSLYL 222
Cdd:PRK13420 150 EITRTLALAVRLFGNIMSLELA------ALLVLL----VAGFLVPVPILMLHIIE---ALVQAYIFGMLALIYI 210
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 6-64 5.78e-03

cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; Cytochrome P450 5A1 (CYP5A1), also called thromboxane-A synthase (EC 5.3.99.5) or thromboxane synthetase, converts prostaglandin H2 into thromboxane A2, a biologically active metabolite of arachidonic acid that has been implicated in stroke, asthma, and various cardiovascular diseases, due to its acute and chronic effects in promoting platelet aggregation, vasoconstriction, bronchoconstriction, and proliferation. CYP5A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410742 [Multi-domain]  Cd Length: 457  Bit Score: 37.13  E-value: 5.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 722489951   6 FASFATPtmmgFPIVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLIsKQMMAIHNQK 64
Cdd:cd20649  144 FFEFSFF----RPILILFLAFPFIMIPLARILPNKSRDELNSFFTQCI-RNMIAFRDQQ 197
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 126-215 8.31e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 36.02  E-value: 8.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 126 AHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLIGeaTLVLMSispataFITFIILVMLTILEFA 205
Cdd:MTH00050  80 SSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGCFGGVALG--NLCFIS------YWWFLVLFFLFFYEVF 151

                         90
                 ....*....|
gi 722489951 206 VALIQAYVFT 215
Cdd:MTH00050 152 VALVHWFIVS 161
 
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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