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Conserved domains on  [gi|296940285|ref|YP_003667965|]
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ATP synthase F0 subunit 6 (mitochondrion) [Leiolepis guttata]

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 4.52e-91

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177181  Cd Length: 227  Bit Score: 267.08  E-value: 4.52e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   1 MMTNLFDQFMVPQMLGIQLLPMNLLVAPALTFTKSNRLKNNRFITIGHWMMKTITKHTMTPINKPGHKWAPILISLILLL 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  81 LTMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIETVSLFIRPLALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940285 161 LTANLTAGHLLLHLISTTTMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQENT 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
 
Name Accession Description Interval E-value
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
1-227 4.52e-91

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 267.08  E-value: 4.52e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   1 MMTNLFDQFMVPQMLGIQLLPMNLLVAPALTFTKSNRLKNNRFITIGHWMMKTITKHTMTPINKPGHKWAPILISLILLL 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  81 LTMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIETVSLFIRPLALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940285 161 LTANLTAGHLLLHLISTTTMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQENT 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 ...
5-226 5.79e-47

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: 154.67  E-value: 5.79e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285    5 LFDQFMVPQMlGIQLLPMNLLVAPALT------FTKSNRLKNNRFITIGHWMMKTITKHTMTPINKPGHKWAPILISLIL 78
Cdd:TIGR01131   1 LFSQFDISPI-TLFSLTLLSLILLLSLliflisSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   79 LLLTMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIETVSLFIRPLALG 158
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296940285  159 VRLTANLTAGHLLLHLIstTTMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQEN 226
Cdd:TIGR01131 160 VRLFANISAGHLLLTLL--SGLLFSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
66-224 1.02e-38

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: 131.37  E-value: 1.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  66 GHKWAPILISLILLLLTMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILI 145
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296940285 146 ETVSLFIRPLALGVRLTANLTAGHLLLHLISTTTMSLTTlmpIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQ 224
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLS---SVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
24-224 2.90e-31

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 114.12  E-value: 2.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   24 LLVAPALTFTKSNRLKNNRFITIGHWMMKTITKHTMTPI-NKPGHKWAPILISLILLLLTMNVIGLL---PYTFTPTTQL 99
Cdd:pfam00119  11 LLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIgKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  100 SMNTALALPMWLATVMLGLRTQTTAT-LAHLLPTGTPTPLIPALILIETVSLFIRPLALGVRLTANLTAGHLLLHLISTT 178
Cdd:pfam00119  91 NVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGL 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 296940285  179 TMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQ 224
Cdd:pfam00119 171 IFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
24-225 1.23e-23

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: 93.98  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  24 LLVAPALTFTKSNRLKNNRFITIGHWMMKTITKHTMTPINKPGHKWAPILISLILLLLTMNVIGLLPYTFTPTTQLSMNT 103
Cdd:COG0356   12 LLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285 104 ALALPMWLATVMLGLRTQTTAT-LAHLLPTGTPtPLIPALILIETVSLFIRPLALGVRLTANLTAGHLLLHLIST-TTMS 181
Cdd:COG0356   92 ALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGlAPFL 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 296940285 182 LTTLMPIIAPLPMtillllTILEIAVALIQAYVFTLLLSLYLQE 225
Cdd:COG0356  171 LLGVLSLLLPVAW------TAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
1-227 4.52e-91

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 267.08  E-value: 4.52e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   1 MMTNLFDQFMVPQMLGIQLLPMNLLVAPALTFTKSNRLKNNRFITIGHWMMKTITKHTMTPINKPGHKWAPILISLILLL 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  81 LTMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIETVSLFIRPLALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940285 161 LTANLTAGHLLLHLISTTTMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQENT 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-226 1.60e-84

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 250.56  E-value: 1.60e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   1 MMTNLFDQFMVPQMLGIQLLPMNLLVAPALTFTKSNRLKNNRFITIGHWMMKTITKHTMTPINKPGHKWAPILISLILLL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  81 LTMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIETVSLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296940285 161 LTANLTAGHLLLHLISTTTMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQEN 226
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
1-227 1.61e-83

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 247.96  E-value: 1.61e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   1 MMTNLFDQFMVPQMLGIQLLPMNLLVAPALTFTKSNRLKNNRFITIGHWMMKTITKHTMTPINKPGHKWAPILISLILLL 80
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  81 LTMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIETVSLFIRPLALGVR 160
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940285 161 LTANLTAGHLLLHLISTTTMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQENT 227
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
1-227 8.38e-71

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 215.58  E-value: 8.38e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   1 MMTNLFDQFMVPQMLGIQLLPMNLLVAPALTFTKSNRLKNNRFITIGHWMMKTITKHTMTPINKPGHKWAPILISLILLL 80
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  81 LTMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIETVSLFIRPLALGVR 160
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940285 161 LTANLTAGHLLLHLISTTTMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQENT 227
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-227 4.61e-69

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 210.96  E-value: 4.61e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   1 MMTNLFDQFMVPQMLGIQLLPMNLLVaPALTFTKSNRLKNNRFITIGHWMMKTITKHTMTPINKPGHKWAPILISLILLL 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMF-PSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  81 LTMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIETVSLFIRPLALGVR 160
Cdd:MTH00101  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940285 161 LTANLTAGHLLLHLISTTTMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQENT 227
Cdd:MTH00101 160 LTANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
5-226 5.79e-47

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: 154.67  E-value: 5.79e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285    5 LFDQFMVPQMlGIQLLPMNLLVAPALT------FTKSNRLKNNRFITIGHWMMKTITKHTMTPINKPGHKWAPILISLIL 78
Cdd:TIGR01131   1 LFSQFDISPI-TLFSLTLLSLILLLSLliflisSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   79 LLLTMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIETVSLFIRPLALG 158
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296940285  159 VRLTANLTAGHLLLHLIstTTMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQEN 226
Cdd:TIGR01131 160 VRLFANISAGHLLLTLL--SGLLFSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-225 5.03e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 136.84  E-value: 5.03e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   1 MMTNLFDQF-----------MVPQMLGIQLLPMNLLVAPaltftksnrlknNRFITIGHWMMKTITKHTMTPINKPGHKW 69
Cdd:MTH00157   1 MMTNLFSIFdpstsfnlslnWLSTFLGLLFIPSSFWLIP------------SRYNILWNKILKTLHKEFKTLLGPKNKGS 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  70 APILISLILLLLTMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIETVS 149
Cdd:MTH00157  69 TLIFISLFSFILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETIS 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296940285 150 LFIRPLALGVRLTANLTAGHLLLHLISTTTMSLTTlmpIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQE 225
Cdd:MTH00157 149 NLIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSS---MILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
3-226 8.51e-40

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 136.26  E-value: 8.51e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   3 TNLFDQFmVPQMLGIqlLPMNLLVAPA----LTFTKSNRLKNNRFITIGHWMMKTITKHTMTPINKPGHKWAPILISLIL 78
Cdd:MTH00035   5 NSIFGQF-SPDTILF--IPLTLLSSVIalswLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  79 LLLTMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIETVSLFIRPLALG 158
Cdd:MTH00035  82 LILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALG 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296940285 159 VRLTANLTAGHLLLHLIsTTTMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQEN 226
Cdd:MTH00035 162 LRLAANLTAGHLLIFLL-STAIWELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
66-224 1.02e-38

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: 131.37  E-value: 1.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  66 GHKWAPILISLILLLLTMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILI 145
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296940285 146 ETVSLFIRPLALGVRLTANLTAGHLLLHLISTTTMSLTTlmpIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQ 224
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLS---SVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
1-227 1.50e-37

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 130.54  E-value: 1.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   1 MMTNLFDQFMVPQML---GIQLLPMNLLVAPALTFTKSNRLKNNRFITIGhwMMKTITKHTMTPINKPGHK-WAPILISL 76
Cdd:MTH00176   1 MLVDLFSSFDPPNKNifsMISLSWITLLLFLLLMPSSVWFCPSKLQVFML--MFSTFLPEMILRSNGSYILgSASIIISL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  77 ILLLLTMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIETVSLFIRPLA 156
Cdd:MTH00176  79 FILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLT 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296940285 157 LGVRLTANLTAGHLLLHLISTTTMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQENT 227
Cdd:MTH00176 159 LAVRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
82-225 1.68e-37

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 130.37  E-value: 1.68e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  82 TMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIETVSLFIRPLALGVRL 161
Cdd:MTH00173  84 SLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRL 163
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296940285 162 TANLTAGHLLLHLISTTTMSLTTLMPIIAPLP-MTILLLLTILEIAVALIQAYVFTLLLSLYLQE 225
Cdd:MTH00173 164 LANISAGHIVLTLIGNYLSSSLFSSSVVSLLLvLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
1-223 1.80e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 115.14  E-value: 1.80e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   1 MMTNLFDQFMVPQMLGI--QLLPMNLLVAPALTFTKSNRLKNNRFITIGHWMMKTITKHTMTPINKPGHKWAPILISLIL 78
Cdd:MTH00172   1 MSSSYFDQFNIVWLIGLtnSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  79 LLLTMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIETVSLFIRPLALG 158
Cdd:MTH00172  81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296940285 159 VRLTANLTAGHLLLHLISTTTMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYL 223
Cdd:MTH00172 161 VRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYL 225
ATP-synt_A pfam00119
ATP synthase A chain;
24-224 2.90e-31

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 114.12  E-value: 2.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   24 LLVAPALTFTKSNRLKNNRFITIGHWMMKTITKHTMTPI-NKPGHKWAPILISLILLLLTMNVIGLL---PYTFTPTTQL 99
Cdd:pfam00119  11 LLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIgKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  100 SMNTALALPMWLATVMLGLRTQTTAT-LAHLLPTGTPTPLIPALILIETVSLFIRPLALGVRLTANLTAGHLLLHLISTT 178
Cdd:pfam00119  91 NVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGL 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 296940285  179 TMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQ 224
Cdd:pfam00119 171 IFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
1-223 1.51e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 112.79  E-value: 1.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   1 MMTNLFDQFMVPQMLGIQL-------------LPMNLLVAPALTFTKSNRLKNNRFITIGHWMMKTITKHTMTPINKPGH 67
Cdd:MTH00175   1 MLAAYFDQFNIIRLITIQAflgdwlvtftnssMMMVLAVIIFWLLLKGDKLIPNRWQSIMELIYLNIRSVVHDNLGKSGQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  68 KWAPILISLILLLLTMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIET 147
Cdd:MTH00175  81 KYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIET 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940285 148 VSLFIRPLALGVRLTANLTAGHLLLHLIS-TTTMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYL 223
Cdd:MTH00175 161 LSYLIRAISLGVRLAANISAGHLLFAILSgFAFNMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYL 237
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
9-227 9.70e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 110.59  E-value: 9.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   9 FMVPQMLGIQLLPMNLLVAPALTFTKSNRLKNnrfiTIGHWMMKTITKHTmtpinkpgHKWAPILISLILLLLTMNVIGL 88
Cdd:MTH00005  25 FWAFNFSIILLLSSSFWITPNRLSSIMSPPKS----TMHTQLSRTFGKHL--------KGFSSLISALFTMIILMNLSGL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  89 LPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIETVSLFIRPLALGVRLTANLTAG 168
Cdd:MTH00005  93 LPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAG 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 296940285 169 HLLLHLISTTTMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYLQENT 227
Cdd:MTH00005 173 HIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDDHP 231
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
24-225 1.23e-23

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: 93.98  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  24 LLVAPALTFTKSNRLKNNRFITIGHWMMKTITKHTMTPINKPGHKWAPILISLILLLLTMNVIGLLPYTFTPTTQLSMNT 103
Cdd:COG0356   12 LLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285 104 ALALPMWLATVMLGLRTQTTAT-LAHLLPTGTPtPLIPALILIETVSLFIRPLALGVRLTANLTAGHLLLHLIST-TTMS 181
Cdd:COG0356   92 ALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGlAPFL 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 296940285 182 LTTLMPIIAPLPMtillllTILEIAVALIQAYVFTLLLSLYLQE 225
Cdd:COG0356  171 LLGVLSLLLPVAW------TAFELLVGFLQAYIFTMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
6-225 3.03e-20

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 85.23  E-value: 3.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285   6 FDQFMVPQMLGIQLLPMNLLVAPALTFTKSNRLKNNRFITIGHWMMKTITKHTMTPINKPGHKWAPILISLILLLLTMNV 85
Cdd:PRK05815   9 FGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  86 IGLLP-YTFTPTTQLSMNTALALPMWLATVMLGLRTQTtatLAHLLPTGTPTPlIPALILIETVSLFIRPLALGVRLTAN 164
Cdd:PRK05815  89 LGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKKG---LGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGN 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296940285 165 LTAGHLLLHLISTTTMSLTTLMPIIAPLPMtillLLTILEIAVALIQAYVFTLLLSLYLQE 225
Cdd:PRK05815 165 MLAGELILALIALLGGAGLLLALAPLILPV----AWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
84-225 1.14e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 78.83  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  84 NVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIETVSLFIRPLALGVRLTA 163
Cdd:MTH00174 105 NGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAA 184
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296940285 164 NLTAGHLLLHLISTTTMSLTTLMPIIAP-LPMTILLLLTILEIAVALIQAYVFTLLLSLYLQE 225
Cdd:MTH00174 185 NISSGHLLFSIIASFAWKMINTGILIGSfVPFAILIFVTILEMAVAIIQAYVFTLLTIVYLRD 247
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
84-223 8.88e-15

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 72.08  E-value: 8.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  84 NVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQ-TTATLAHLlPTGTPTPLIPALILIETVSLFIRPLALGVRLT 162
Cdd:PRK13419 185 NLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKAHgIKGYLAHL-TGGTHWSLWIIMIPIEFIGLFTKPFALTVRLF 263
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296940285 163 ANLTAGHL-LLHLISTTTMSLTTLMPIIAPLPMtiLLLLTILEIAVALIQAYVFTLLLSLYL 223
Cdd:PRK13419 264 ANMTAGHIvILSLIFISFILKSYIVAVAVSVPF--AIFIYLLELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
82-225 2.04e-12

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 63.46  E-value: 2.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  82 TMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLrtQTTATLAHLLPTGTPTPLIP-ALILIETVSLFIRPLALGVR 160
Cdd:MTH00087  64 LFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFL--SKSEKFSVYLSKGSDSFLKTfSMLFVEIVSELSRPLALTLR 141
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296940285 161 LTANLTAGHLLLHLISTTTMSLttlmpiiaplpMTILLLLTILEIAVALIQAYVFTLLLSLYLQE 225
Cdd:MTH00087 142 LTVNLMVGHLISSLLNFLGEKY-----------VWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
94-223 8.95e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 57.59  E-value: 8.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  94 TPTTQLSMNTALALPMWLATVMLGLRTQTTATLAHLLPTGTPTPLIPALILIE-TVSLFIRPLALGVRLTANLTAGHLLL 172
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEfIVSPMAKTFALTVRLLANMTAGHVII 296
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 296940285 173 hlISTTTMSLTTLMPIIAPLPMTILLLLTILEIAVALIQAYVFTLLLSLYL 223
Cdd:PRK13417 297 --LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
22-223 8.69e-05

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 42.42  E-value: 8.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  22 MNLLVAPALTFTKSNRLKNNRFITIGHWMMKTITKHTMTPINKPGHKWAPILISLILLLLTMNVIGLLPYTFTPTTQLSM 101
Cdd:PRK13420  27 MIVLVLASWLTTRRLSLDPGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFVGTLWIFILVANLIGLIPGFHSPTADLSV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285 102 NTALALPMWLATVMLGLRTQ-TTATLAHLLptgTPTPLipaLILIETVSLFIRPLALGVRLTANLTAGHLLLHLISTTTM 180
Cdd:PRK13420 107 TAALALLVFFSVHWFGIRAEgLREYLKHYL---SPSPF---LLPFHLISEITRTLALAVRLFGNIMSLELAALLVLLVAG 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 296940285 181 slttlmpIIAPLPMtillllTILEIAVALIQAYVFTLLLSLYL 223
Cdd:PRK13420 181 -------FLVPVPI------LMLHIIEALVQAYIFGMLALIYI 210
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
82-218 4.82e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 40.06  E-value: 4.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940285  82 TMNVIGLLPYTFTPTTQLSMNTALALPMWLATVMLGLRTQTTAtlAHLLPTGTPTPLIPALILIETVSlfiRPLALGVRL 161
Cdd:PRK13421  90 VANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVRARGVR--GYLATFAEPTWVMIPLNLVEQLT---RTFSLIVRL 164
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 296940285 162 TANLTAGHLLLHLISTTTMslttlmpIIAPLPMtillllTILEIAVALIQAYVFTLL 218
Cdd:PRK13421 165 FGNVMSGVFVIGIVLSLAG-------LLVPIPL------MALDLLTGAVQAYIFAVL 208
 
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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