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Conserved domains on  [gi|2473932267|ref|YP_010735798|]
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ATP synthase F0 subunit 6 (mitochondrion) [China mantispoides]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009593)

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 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-223 2.15e-90

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 265.11  E-value: 2.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267   1 MMTNLFSSFDPSTNSMMSINWMSTVIGMMIMPYMYWMLPSRMMLMWTNTSNKLHNELNNIINQKDKSMTLMFISMFIMLL 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  81 VNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIRPGTLAVRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2473932267 161 SANMIAGHLLMTLMGNTGTNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLYFSEIY 223
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-223 2.15e-90

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 265.11  E-value: 2.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267   1 MMTNLFSSFDPSTNSMMSINWMSTVIGMMIMPYMYWMLPSRMMLMWTNTSNKLHNELNNIINQKDKSMTLMFISMFIMLL 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  81 VNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIRPGTLAVRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2473932267 161 SANMIAGHLLMTLMGNTGTNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLYFSEIY 223
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-223 1.07e-48

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: 159.29  E-value: 1.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267   5 LFSSFDPSTNSMMSINWMSTVIGMMIMPYM------YWMLPSRMMLMWTNTSNKLHNELNNIINQKDKSMTLMFISMFIM 78
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLSLILLLSLLIFLissslsRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  79 LLVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIRPGTLAV 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2473932267 159 RLSANMIAGHLLMTLMGNTG-TNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLYFSEIY 223
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLfSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-220 2.74e-43

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: 142.92  E-value: 2.74e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  66 KSMTLMFISMFIMLLVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIE 145
Cdd:cd00310     2 KKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIE 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2473932267 146 TISNMIRPGTLAVRLSANMIAGHLLMTLMGNTGTNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLYFS 220
Cdd:cd00310    82 LISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
21-220 1.00e-28

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 107.19  E-value: 1.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  21 WMSTVIGMMIMPYMYWML----PSRMMLMWTNTSNKLHNELNNIINQKDKSM-TLMFISMFIMLLVNNFMGLF---PYIF 92
Cdd:pfam00119   5 LIVALILLLFLLLATRKTkklvPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKfFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  93 TSTSHMVMTFSLAMPLWLTYMFFG-WIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIRPGTLAVRLSANMIAGHLLM 171
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2473932267 172 TL---MGNTGTNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLYFS 220
Cdd:pfam00119 165 LLlagLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 53-221 1.74e-22

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: 90.90  E-value: 1.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  53 LHNELNNIINQKDKSMTLMFISMFIMLLVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFG-WIKKTKNMFAHLVPM 131
Cdd:COG0356    42 VRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFP 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267 132 STPPiLMPFMVMIETISNMIRPGTLAVRLSANMIAGHLLMTLMGNTGtnLSMMMLYIMLMMQMLLIILESAVAVIQAYVY 211
Cdd:COG0356   122 PFPW-LAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLA--PFLLLGVLSLLLPVAWTAFELLVGFLQAYIF 198

                         170
                  ....*....|
gi 2473932267 212 TVLSTLYFSE 221
Cdd:COG0356   199 TMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-223 2.15e-90

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 265.11  E-value: 2.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267   1 MMTNLFSSFDPSTNSMMSINWMSTVIGMMIMPYMYWMLPSRMMLMWTNTSNKLHNELNNIINQKDKSMTLMFISMFIMLL 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  81 VNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIRPGTLAVRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2473932267 161 SANMIAGHLLMTLMGNTGTNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLYFSEIY 223
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-223 1.07e-48

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: 159.29  E-value: 1.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267   5 LFSSFDPSTNSMMSINWMSTVIGMMIMPYM------YWMLPSRMMLMWTNTSNKLHNELNNIINQKDKSMTLMFISMFIM 78
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLSLILLLSLLIFLissslsRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  79 LLVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIRPGTLAV 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2473932267 159 RLSANMIAGHLLMTLMGNTG-TNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLYFSEIY 223
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLfSLMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-223 2.65e-44

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 148.26  E-value: 2.65e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267   1 MMTNLFSSFDPSTN---SMMSINWMSTVIGMMIMPYMYWMLPSRMMLMWTNTSNKLHNELNNIINQKDKSMTLMFISMFI 77
Cdd:MTH00176    1 MLVDLFSSFDPPNKnifSMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  78 MLLVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIRPGTLA 157
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2473932267 158 VRLSANMIAGHLLMTLMGNTG---TNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLYFSEIY 223
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMwglLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-220 2.74e-43

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: 142.92  E-value: 2.74e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  66 KSMTLMFISMFIMLLVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIE 145
Cdd:cd00310     2 KKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIE 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2473932267 146 TISNMIRPGTLAVRLSANMIAGHLLMTLMGNTGTNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLYFS 220
Cdd:cd00310    82 LISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 3-221 2.03e-39

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 135.49  E-value: 2.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267   3 TNLFSSFDPSTNSMMSINWMSTVIGMMIMPYMY---WmLPSRMMLMWTNTSNKLHNELNNIINQKDKSMTLMFISMFIML 79
Cdd:MTH00035    5 NSIFGQFSPDTILFIPLTLLSSVIALSWLFFINptnW-LPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  80 LVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIRPGTLAVR 159
Cdd:MTH00035   84 LSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLR 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2473932267 160 LSANMIAGHLLMTLMGNT--GTNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLYFSE 221
Cdd:MTH00035  164 LAANLTAGHLLIFLLSTAiwELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-218 2.09e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 135.63  E-value: 2.09e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267   1 MMTNLFSSFDPSTNSMM-----SINWMSTVIGMMIMPYMYWMLPSRMMLMWTNTSNKLHNELNNIINQKDKSMTLMFISM 75
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFnnlssTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  76 FIMLLVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIRPGT 155
Cdd:MTH00005   81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2473932267 156 LAVRLSANMIAGHLLMTLMGNTGTNLS---MMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLY 218
Cdd:MTH00005  161 LSFRLAANMSAGHIVLSLIGIYAASALfssISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-222 2.66e-37

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 129.99  E-value: 2.66e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267   1 MMTNLFSSFDPSTNSMMSINWMSTVIGMMIM---PYMYWMLPSRMMLMWTNTSNKLHNELNNIINQKDKSMTLMFISMFI 77
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSSLSFLMWLLSLMSLfffSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  78 MLLVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIRPGTLA 157
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2473932267 158 VRLSANMIAGHLLMTLMGNTGTNLSMMMLYIMLMMQMLLIIL----ESAVAVIQAYVYTVLSTLYFSEI 222
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYLSSSLFSSSVVSLLLVLLIQVGyfifEVAVMLIQAYIFTLLIKLYSDEH 229
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-221 3.28e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 124.68  E-value: 3.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267   1 MMTNLFSSFDPSTNSMMSINWMSTVIGMMIMPYMYWM-LPSRMMLMWTNTSNKLHNELNNIINQKDKSMTLMFISMFIML 79
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRwLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  80 LVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIRPGTLAVR 159
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2473932267 160 LSANMIAGHLLMTLMGNT---GTNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLYFSE 221
Cdd:MTH00179  161 LTANITAGHLLMHLISSAvfvLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-221 1.32e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 123.01  E-value: 1.32e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267   1 MMTNLFSSFDPSTNSMMSINWMSTVIGMMIMPYM-YWMLPSRMMLMWTNTSNKLHNELNNIINQKDKSMTLMFISMFIML 79
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPkNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  80 LVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIRPGTLAVR 159
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2473932267 160 LSANMIAGHLLMTLMGNTGTNLSMMMLYIMLMMQMLLI---ILESAVAVIQAYVYTVLSTLYFSE 221
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLlltILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-218 8.16e-34

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 120.83  E-value: 8.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267   1 MMTNLFSSFdpSTNSMMSInwmSTVIGMMIMPYMYW-----MLPSRMMLMWTNTSNKLHNELNNIINQKDKSMTLMFISM 75
Cdd:MTH00101    1 MNENLFASF--ITPTILGL---PIVTLIIMFPSLLFptpnrLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  76 FIMLLVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIRPGT 155
Cdd:MTH00101   76 ILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMA 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2473932267 156 LAVRLSANMIAGHLLMTLMGNTG---TNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLY 218
Cdd:MTH00101  156 LAVRLTANITAGHLLIHLIGGATlalMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 70-221 1.51e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 109.96  E-value: 1.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  70 LMFISMFIMLLVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETISN 149
Cdd:MTH00132   71 LLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISL 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2473932267 150 MIRPGTLAVRLSANMIAGHLLMTLMGNTG---TNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLYFSE 221
Cdd:MTH00132  151 FIRPLALGVRLTANLTAGHLLIQLIATAAfvlLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP-synt_A pfam00119
ATP synthase A chain;
21-220 1.00e-28

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 107.19  E-value: 1.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  21 WMSTVIGMMIMPYMYWML----PSRMMLMWTNTSNKLHNELNNIINQKDKSM-TLMFISMFIMLLVNNFMGLF---PYIF 92
Cdd:pfam00119   5 LIVALILLLFLLLATRKTkklvPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKfFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  93 TSTSHMVMTFSLAMPLWLTYMFFG-WIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIRPGTLAVRLSANMIAGHLLM 171
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2473932267 172 TL---MGNTGTNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLYFS 220
Cdd:pfam00119 165 LLlagLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-221 1.11e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 105.05  E-value: 1.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267   1 MMTNLFSSFDPSTnsMMSInwmSTVIGMMIMPYMYWMLPS------RMMLMWTNTSNKLHNELNNIINQKDKSMTLMFIS 74
Cdd:MTH00073    1 MNLSFFDQFLSPT--LLGI---PLIMLAMLLPWLLFPTPTnkwlnnRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  75 MFIMLLVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIRPG 154
Cdd:MTH00073   76 LMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267 155 TLAVRLSANMIAGHLLMTLMGNTG---TNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLYFSE 221
Cdd:MTH00073  156 ALGVRLTANLTAGHLLIQLISTATlvlLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 73-221 4.81e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 101.24  E-value: 4.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  73 ISMFIMLLVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIR 152
Cdd:MTH00175   87 LSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIR 166

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2473932267 153 PGTLAVRLSANMIAGHLLMTLMG----NTGTNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLYFSE 221
Cdd:MTH00175  167 AISLGVRLAANISAGHLLFAILSgfafNMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 73-218 5.11e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 95.49  E-value: 5.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  73 ISMFIMLLVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIR 152
Cdd:MTH00172   76 ISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISR 155

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2473932267 153 PGTLAVRLSANMIAGHLLMTLMGNTGTNLSMMMLYIML---MMQMLLIILESAVAVIQAYVYTVLSTLY 218
Cdd:MTH00172  156 AISLGVRLAANLSAGHLLFAILAGFGFNMLCASGFLSLfplLIMVFITLLEIAVAVIQAYVFCLLTTIY 224
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 53-221 1.74e-22

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: 90.90  E-value: 1.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  53 LHNELNNIINQKDKSMTLMFISMFIMLLVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFG-WIKKTKNMFAHLVPM 131
Cdd:COG0356    42 VRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFP 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267 132 STPPiLMPFMVMIETISNMIRPGTLAVRLSANMIAGHLLMTLMGNTGtnLSMMMLYIMLMMQMLLIILESAVAVIQAYVY 211
Cdd:COG0356   122 PFPW-LAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLA--PFLLLGVLSLLLPVAWTAFELLVGFLQAYIF 198

                         170
                  ....*....|
gi 2473932267 212 TVLSTLYFSE 221
Cdd:COG0356   199 TMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 59-221 2.56e-18

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 80.22  E-value: 2.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  59 NIINQKDKSMTLMFISMFIMLLVNNFMGLFP-YIFTSTSHMVMTFSLAMPLWLTYMFFG-WIKKTKNMFAHLVPmstppI 136
Cdd:PRK05815   63 DNIGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYL-----Q 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267 137 LMPFMVMIETISNMIRPGTLAVRLSANMIAGHLLMTLMGNTGtNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLST 216
Cdd:PRK05815  138 PHPLLLPIEIISEFSRPISLSLRLFGNMLAGELILALIALLG-GAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTI 216


                  ....*
gi 2473932267 217 LYFSE 221
Cdd:PRK05815  217 VYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 37-221 3.49e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 77.67  E-value: 3.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  37 MLPSRMMLMWTNTSNKLHNELNNIINQKDKSMTLMFISMFIMLLVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFG 116
Cdd:MTH00174   59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAG 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267 117 WIKKTKNMFAHLVPMSTPPILMPFMVMIETISNMIRPGTLAVRLSANMIAGHLLMTLMGNTG----TNLSMMMLYIMLMM 192
Cdd:MTH00174  139 LITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAwkmiNTGILIGSFVPFAI 218

                         170       180
                  ....*....|....*....|....*....
gi 2473932267 193 QMLLIILESAVAVIQAYVYTVLSTLYFSE 221
Cdd:MTH00174  219 LIFVTILEMAVAIIQAYVFTLLTIVYLRD 247
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 73-218 9.90e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 57.45  E-value: 9.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  73 ISMFIMLLVNNFMGLFPYIFTSTSHMVMTFSLAmplwlTYMFF----GWIKK--TKNMFAHLVPmSTPPILMPFMVMIET 146
Cdd:PRK13419  175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLA-----VFTFFitqyAAIKAhgIKGYLAHLTG-GTHWSLWIIMIPIEF 248

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2473932267 147 ISNMIRPGTLAVRLSANMIAGHL-LMTLMG-NTGTNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLY 218
Cdd:PRK13419  249 IGLFTKPFALTVRLFANMTAGHIvILSLIFiSFILKSYIVAVAVSVPFAIFIYLLELFVAFLQAYIFTMLSALF 322
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 72-221 2.65e-09

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 54.98  E-value: 2.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  72 FISMFIMLLVNNFMGLFPYIFTSTSHMVMTFSLAMPLWLTYMFFGWIKKTKnmFAHLVPMSTPPILMPF-MVMIETISNM 150
Cdd:MTH00087   55 SFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEK--FSVYLSKGSDSFLKTFsMLFVEIVSEL 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2473932267 151 IRPGTLAVRLSANMIAGHLLMTLMGNTGtnlsmmmlYIMLMMQMLLIILESAVAVIQAYVYTVLSTLYFSE 221
Cdd:MTH00087  133 SRPLALTLRLTVNLMVGHLISSLLNFLG--------EKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 93-218 5.14e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 46.42  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  93 TSTSHMVMTFSLAMPLWLTYMFFGWIKKTKNMFAHLVPMSTPPILMPFMVMIETI-SNMIRPGTLAVRLSANMIAGH-LL 170
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHvII 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2473932267 171 MTLMGNTGTNLSMMMLYIMLMMQMLLIILESAVAVIQAYVYTVLSTLY 218
Cdd:PRK13417  297 LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 43-176 2.42e-05

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 43.33  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  43 MLMWTNTSnkLHNELNNIINQKDKSMTLMFISMFIMLLvnnFMGL-FPYIFTSTSHMVMTFSLAMP----LWLTYMFFGW 117
Cdd:MTH00050    1 MFVNDFSS--LFSLIYKLILGGSVSYYYSVVLFIVLFL---FLLYrLPYIYSPFLFVVFLFVVVFPlfisLFLSRVFDSL 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2473932267 118 ikktKNMFAHLVPMSTPPILMPFMVMIETISNMIRPGTLAVRLSANMIAGHLLMTLMGN 176
Cdd:MTH00050   76 ----NEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGCFGGVALGN 130
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 25-166 6.32e-05

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 42.81  E-value: 6.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473932267  25 VIGMMIMPYMYWMLPSRMMLMWTNTSNKLHNELNNIINQKDKSMTLMFISMFIMLLVNNFMGLFPYIFTSTSHMVMTFSL 104
Cdd:PRK13420   31 VLASWLTTRRLSLDPGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFVGTLWIFILVANLIGLIPGFHSPTADLSVTAAL 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2473932267 105 AMPLWLTYMFFGWikKTKNMFAHLVPMSTP-PILMPFMVmietISNMIRPGTLAVRLSANMIA 166
Cdd:PRK13420  111 ALLVFFSVHWFGI--RAEGLREYLKHYLSPsPFLLPFHL----ISEITRTLALAVRLFGNIMS 167
 
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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