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Conserved domains on  [gi|1910804883|gb|QOD98073|]
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ATP synthase F0 subunit 6 (mitochondrion) [Chionis minor]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009573)

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 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-227 7.30e-109

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177181  Cd Length: 227  Bit Score: 312.14  E-value: 7.30e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883   1 MNLSFFDQFTSPCMLGIPLILLSMLFPALLLPSPNNRWITNRLSTLQLWFLHLITKQLMMPLNKGGHKWALILTSLMAFL 80
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  81 LAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPLALGVR 160
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1910804883 161 LTANLTAGHLLIQLISTATTALLPIIPAVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
 
Name Accession Description Interval E-value
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-227 7.30e-109

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 312.14  E-value: 7.30e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883   1 MNLSFFDQFTSPCMLGIPLILLSMLFPALLLPSPNNRWITNRLSTLQLWFLHLITKQLMMPLNKGGHKWALILTSLMAFL 80
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  81 LAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPLALGVR 160
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1910804883 161 LTANLTAGHLLIQLISTATTALLPIIPAVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 6-227 1.33e-46

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: 153.90  E-value: 1.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883   6 FDQFTSPC--MLGIPLILLSMLFP---ALLLPSPNNRWITNRLSTLQLWFLHLITKQLMMPLNKGGHKWALILTSLMAFL 80
Cdd:TIGR01131   2 FSQFDISPitLFSLTLLSLILLLSlliFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  81 LAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPLALGVR 160
Cdd:TIGR01131  82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1910804883 161 LTANLTAGHLLIQLISTATTALLPiiPAVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLLFSLMS--SAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-224 6.16e-33

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: 116.34  E-value: 6.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  66 GHKWALILTSLMAFLLAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIII 145
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1910804883 146 ETTSLLIRPLALGVRLTANLTAGHLLIQLISTATTALLPIipaVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
63-224 1.78e-27

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 104.11  E-value: 1.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  63 NKGGHKWALILTSLMAFLL---AINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSAS-LGHLLPEGTPTPL 138
Cdd:pfam00119  51 KKKGRKFFPLLLTLFFFILvsnLLGLIPKSPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883 139 IPALIIIETTSLLIRPLALGVRLTANLTAGHLLIQLISTATTALLPIIPAVSILTALILLLLTILEVAVAMIQAYVFVLL 218
Cdd:pfam00119 131 VPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTML 210


                  ....*.
gi 1910804883 219 LSLYLQ 224
Cdd:pfam00119 211 TAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 61-225 1.00e-16

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: 75.49  E-value: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  61 PLNKGGHKWALILTSLMAFLLAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQ-PSASLGHLLPEGTPtPLI 139
Cdd:COG0356    49 TIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883 140 PALIIIETTSLLIRPLALGVRLTANLTAGHLLIQLIstattALLPIIPAVSILTALILLLLTILEVAVAMIQAYVFVLLL 219
Cdd:COG0356   128 PLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLL-----AGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLT 202


                  ....*.
gi 1910804883 220 SLYLQE 225
Cdd:COG0356   203 AVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-227 7.30e-109

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 312.14  E-value: 7.30e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883   1 MNLSFFDQFTSPCMLGIPLILLSMLFPALLLPSPNNRWITNRLSTLQLWFLHLITKQLMMPLNKGGHKWALILTSLMAFL 80
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  81 LAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPLALGVR 160
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1910804883 161 LTANLTAGHLLIQLISTATTALLPIIPAVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 2.15e-107

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 308.34  E-value: 2.15e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883   1 MNLSFFDQFTSPCMLGIPLILLSMLFPALLLPSPNNRWITNRLSTLQLWFLHLITKQLMMPLNKGGHKWALILTSLMAFL 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  81 LAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPLALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1910804883 161 LTANLTAGHLLIQLISTATTALLPIIPAVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-227 6.92e-106

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 304.58  E-value: 6.92e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883   1 MNLSFFDQFTSPCMLGIPLILLSMLFPALLLPSPNNRWITNRLSTLQLWFLHLITKQLMMPLNKGGHKWALILTSLMAFL 80
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  81 LAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPLALGVR 160
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1910804883 161 LTANLTAGHLLIQLISTATTALLPIIPAVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-226 6.06e-81

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 241.39  E-value: 6.06e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883   1 MNLSFFDQFTSPCMLGIPLILLSMLFPALLLPSPNNRWITNRLSTLQLWFLHLITKQLMMPLNKGGHKWALILTSLMAFL 80
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  81 LAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPLALGVR 160
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1910804883 161 LTANLTAGHLLIQLISTATTALLPIIPAVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00179  161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 5.14e-80

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 239.08  E-value: 5.14e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883   1 MNLSFFDQFTSPCMLGIPLILLSMLFPALLLPSPNnRWITNRLSTLQLWFLHLITKQLMMPLNKGGHKWALILTSLMAFL 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPN-RLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  81 LAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPLALGVR 160
Cdd:MTH00101   80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1910804883 161 LTANLTAGHLLIQLISTATTALLPIIPAVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00101  160 LTANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 6-227 1.33e-46

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: 153.90  E-value: 1.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883   6 FDQFTSPC--MLGIPLILLSMLFP---ALLLPSPNNRWITNRLSTLQLWFLHLITKQLMMPLNKGGHKWALILTSLMAFL 80
Cdd:TIGR01131   2 FSQFDISPitLFSLTLLSLILLLSlliFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  81 LAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPLALGVR 160
Cdd:TIGR01131  82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1910804883 161 LTANLTAGHLLIQLISTATTALLPiiPAVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLLFSLMS--SAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-227 2.09e-44

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 148.20  E-value: 2.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883   1 MNLSFFDQFTSPCMLGIPLILLSMLFPAL-LLPSPNNRWITNRLSTLQLWFLHLITKQLMMPLNKGGHKWALILTSLMAF 79
Cdd:MTH00035    3 INNSIFGQFSPDTILFIPLTLLSSVIALSwLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  80 LLAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPLALGV 159
Cdd:MTH00035   83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1910804883 160 RLTANLTAGHLLIQLISTAtTALLPIIPAVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00035  163 RLAANLTAGHLLIFLLSTA-IWELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 3.38e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 137.22  E-value: 3.38e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883   1 MNL-SFFDQFTSpcmLGIPLILLSMLFPALLLPSpnNRW-ITNRLSTLQLWFLHLITKQLMMPLNKGGHKWALILTSLMA 78
Cdd:MTH00157    3 TNLfSIFDPSTS---FNLSLNWLSTFLGLLFIPS--SFWlIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  79 FLLAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPLALG 158
Cdd:MTH00157   78 FILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1910804883 159 VRLTANLTAGHLLIQLISTATTALLPIIpavSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00157  158 VRLAANMIAGHLLLTLLGNTGPSLSSMI---LSILILIQILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 1.80e-37

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 130.54  E-value: 1.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883   1 MNLSFFDQFTSPCMLGIPLILLS---MLFPALLLPSpNNRWITNRLSTLQLWFLHLITKQLMMPLNKGGHKWALILTSLM 77
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFSMISLSwitLLLFLLLMPS-SVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  78 AFLLAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPLAL 157
Cdd:MTH00176   80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1910804883 158 GVRLTANLTAGHLLIQLISTATTALLPIIPAVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00176  160 AVRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 4-225 3.00e-37

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 129.99  E-value: 3.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883   4 SFFDQFTSPCMLGIPLILLSMLFPALLLPSPNnRWITNRLSTLQLWFLHLITKQLMMPLNKGGHKWALILTSLMAFLLAI 83
Cdd:MTH00173    7 SSFDDHNSSFSSLSFLMWLLSLMSLFFFSSSV-WVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  84 NLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPLALGVRLTA 163
Cdd:MTH00173   86 NLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLA 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1910804883 164 NLTAGHLLIQLISTATTALLPIIPAVSILTALILLLL-TILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00173  166 NISAGHIVLTLIGNYLSSSLFSSSVVSLLLVLLIQVGyFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-224 6.16e-33

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: 116.34  E-value: 6.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  66 GHKWALILTSLMAFLLAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIII 145
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1910804883 146 ETTSLLIRPLALGVRLTANLTAGHLLIQLISTATTALLPIipaVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 18-222 1.05e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 112.90  E-value: 1.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  18 PLILLSMLFPALLLPSpNNRWIT-NRLSTLQLWFLHLITKQLMMPLNKGGHKWALILTSLMAFLLAINLLGLLPYTFTPT 96
Cdd:MTH00005   22 STAFWAFNFSIILLLS-SSFWITpNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTS 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  97 TQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPLALGVRLTANLTAGHLLIQLIS 176
Cdd:MTH00005  101 SHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIG 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1910804883 177 TATTALLPIIPAVSILTALILLLLTILEVAVAMIQAYVFVLLLSLY 222
Cdd:MTH00005  181 IYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP-synt_A pfam00119
ATP synthase A chain;
63-224 1.78e-27

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 104.11  E-value: 1.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  63 NKGGHKWALILTSLMAFLL---AINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSAS-LGHLLPEGTPTPL 138
Cdd:pfam00119  51 KKKGRKFFPLLLTLFFFILvsnLLGLIPKSPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883 139 IPALIIIETTSLLIRPLALGVRLTANLTAGHLLIQLISTATTALLPIIPAVSILTALILLLLTILEVAVAMIQAYVFVLL 218
Cdd:pfam00119 131 VPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTML 210


                  ....*.
gi 1910804883 219 LSLYLQ 224
Cdd:pfam00119 211 TAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 1-227 1.37e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 102.43  E-value: 1.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883   1 MNLSFFDQFTSPCMLGI--PLILLSMLFPALLLPSPNNRWITNRLSTLQ---LWFLHLITKQlmmPLNKGGHKWALILTS 75
Cdd:MTH00172    1 MSSSYFDQFNIVWLIGLtnSSIMMILVIIVVLLLFKGIKLIPKRWQSIIeiiYNHFHGVVKD---NLGNEGLKYFPFIIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  76 LMAFLLAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPL 155
Cdd:MTH00172   78 LFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAI 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1910804883 156 ALGVRLTANLTAGHLLIQLISTATTALLPIIPAVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00172  158 SLGVRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTI 229
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 1-227 8.92e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 95.07  E-value: 8.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883   1 MNLSFFDQFTSPCMLGIPLILLSMLFP-------------ALLLPSPNNRWITNRLSTLqLWFLHLITKQLMMP-LNKGG 66
Cdd:MTH00175    1 MLAAYFDQFNIIRLITIQAFLGDWLVTftnssmmmvlaviIFWLLLKGDKLIPNRWQSI-MELIYLNIRSVVHDnLGKSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  67 HKWALILTSLMAFLLAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIE 146
Cdd:MTH00175   80 QKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883 147 TTSLLIRPLALGVRLTANLTAGHLLIQLIST-ATTALLPIIPAVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00175  160 TLSYLIRAISLGVRLAANISAGHLLFAILSGfAFNMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239


                  ..
gi 1910804883 226 NI 227
Cdd:MTH00175  240 TI 241
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 25-227 3.54e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 80.37  E-value: 3.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  25 LFPALLLPSPNNRWITNR-LSTLQLWFLHLITKQLMMPLNKGGHKWALILtSLMAFLLAINLLGLLPYTFTPTTQLSMNL 103
Cdd:MTH00174   46 LFYTIGAKGNNNTLVPNRiLVGLELIYSHFYTVLKDNLGNKGGNYLAFVL-SLFILILFGNGLGLFPYVFTPTVHMVITL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883 104 ALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPLALGVRLTANLTAGHLLIQLISTATTALL 183
Cdd:MTH00174  125 GLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMI 204

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1910804883 184 PI-IPAVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00174  205 NTgILIGSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYLRDTV 249
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 61-225 1.00e-16

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: 75.49  E-value: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  61 PLNKGGHKWALILTSLMAFLLAINLLGLLPYTFTPTTQLSMNLALAFPLWLATLLTGLRNQ-PSASLGHLLPEGTPtPLI 139
Cdd:COG0356    49 TIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883 140 PALIIIETTSLLIRPLALGVRLTANLTAGHLLIQLIstattALLPIIPAVSILTALILLLLTILEVAVAMIQAYVFVLLL 219
Cdd:COG0356   128 PLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLL-----AGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLT 202


                  ....*.
gi 1910804883 220 SLYLQE 225
Cdd:COG0356   203 AVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 64-225 5.55e-15

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 70.98  E-value: 5.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  64 KGGHKWALILTSLMAFLLAINLLGLLP-YTFTPTTQLSMNLALAFPLWLATLLTGLRNQpsaSLGHLLPEGTPTPlIPAL 142
Cdd:PRK05815   67 GKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLL 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883 143 IIIETTSLLIRPLALGVRLTANLTAGHLLIQLISTATTALLPIIPAvsilTALILLLLTILEVAVAMIQAYVFVLLLSLY 222
Cdd:PRK05815  143 LPIEIISEFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALA----PLILPVAWTIFEIFVGTLQAYIFMMLTIVY 218


                  ...
gi 1910804883 223 LQE 225
Cdd:PRK05815  219 ISM 221
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 90-225 5.70e-11

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 59.61  E-value: 5.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  90 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNqpSASLGHLLPEGTPTPLIP-ALIIIETTSLLIRPLALGVRLTANLTAG 168
Cdd:MTH00087   72 PYSFSPCGMVEFTFLYALVAWLSTFLSFLSK--SEKFSVYLSKGSDSFLKTfSMLFVEIVSELSRPLALTLRLTVNLMVG 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1910804883 169 HLLIQLISTattallpiipaVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00087  150 HLISSLLNF-----------LGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 90-223 5.81e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 52.05  E-value: 5.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  90 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQP-SASLGHLlPEGTPTPLIPALIIIETTSLLIRPLALGVRLTANLTAG 168
Cdd:PRK13419  191 PYGATATGNINVTLTLAVFTFFITQYAAIKAHGiKGYLAHL-TGGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAG 269

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1910804883 169 HLLI-QLISTATTALLPII-PAVSiltALILLLLTILEVAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13419  270 HIVIlSLIFISFILKSYIVaVAVS---VPFAIFIYLLELFVAFLQAYIFTMLSALFI 323
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 94-223 6.82e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 52.20  E-value: 6.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910804883  94 TPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIE-TTSLLIRPLALGVRLTANLTAGHLLI 172
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEfIVSPMAKTFALTVRLLANMTAGHVII 296

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1910804883 173 qlistatTALLPIIP-----AVSILTALILLLLTILEVAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13417  297 -------LALMGFIFqfqswGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 90-168 6.93e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 36.02  E-value: 6.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1910804883  90 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIIIETTSLLIRPLALGVRLTANLTAG 168
Cdd:MTH00050   43 PYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLG 121
 
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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