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Conserved domains on  [gi|2458278144|gb|WEL32836|]
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ATP synthase F0 subunit 6 (mitochondrion) [Ptygomastax nihilsulcus]

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
 1-225 7.74e-86

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 253.55  E-value: 7.74e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144   1 MMTNLFSTFDPSTdIMNLSINWLSSIIGFFLLPAIYWLMPSRIVIMMNNTYNSLYMEFKMLMNNNKSfKMTLMFISVLMM 80
Cdd:MTH00157    1 MMTNLFSIFDPST-SFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNK-GSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  81 MVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIETISNMIRPGTLAV 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2458278144 161 RLSANMIAGHLLLTLMGNTGPSISYKLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILYSNEVH 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 7.74e-86

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 253.55  E-value: 7.74e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144   1 MMTNLFSTFDPSTdIMNLSINWLSSIIGFFLLPAIYWLMPSRIVIMMNNTYNSLYMEFKMLMNNNKSfKMTLMFISVLMM 80
Cdd:MTH00157    1 MMTNLFSIFDPST-SFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNK-GSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  81 MVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIETISNMIRPGTLAV 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2458278144 161 RLSANMIAGHLLLTLMGNTGPSISYKLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILYSNEVH 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-223 1.04e-45

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: 151.59  E-value: 1.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144   5 LFSTFDPSTDIMNLSINW-----LSSIIGFFLLPAIYWLMPSRIVIMMNNTYNSLYMEFKMLMNNnKSFKMTLMFISVLM 79
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLslillLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGG-KKGKFFPLIFTLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  80 MMVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIETISNMIRPGTLA 159
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2458278144 160 VRLSANMIAGHLLLTLMGNTGPS-ISYKLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILYSNE 223
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFSlMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 69-222 9.80e-40

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: 133.68  E-value: 9.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  69 KMTLMFISVLMMMVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIET 148
Cdd:cd00310     3 KYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIEL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2458278144 149 ISNMIRPGTLAVRLSANMIAGHLLLTLMGNTGPSISYKLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILYSN 222
Cdd:cd00310    83 ISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
22-220 5.22e-24

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 94.86  E-value: 5.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  22 WLSSIIGFFLLPAIYW----LMPSRIVIMMNNTYNSLYMEFKMLMNNNKSFKMTLMFISVLMMMVMNNFMGLF---PYIF 94
Cdd:pfam00119   5 LIVALILLLFLLLATRktkkLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  95 TSTSHLSMTLTIALPFWISFMLYGWIIN-TNHMFTHLVPQGTPNMLMSFMVIIETISNMIRPGTLAVRLSANMIAGHLLL 173
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2458278144 174 TLMGNTGPSISYKLMM---IMLIIQLMLMILESAVAIIQGYVFSVLSILY 220
Cdd:pfam00119 165 LLLAGLIFALLSAGFLlgvIPPLLGVAWTLFELLVAFIQAYVFTMLTAVY 214
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 69-220 2.48e-18

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: 79.73  E-value: 2.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  69 KMTLMFISVLMMMVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIIN-TNHMFTHLVPQGTPnMLMSFMVIIE 147
Cdd:COG0356    56 KFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIE 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2458278144 148 TISNMIRPGTLAVRLSANMIAGHLLLTLMGNTGPSISykLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILY 220
Cdd:COG0356   135 IISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLL--LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 7.74e-86

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 253.55  E-value: 7.74e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144   1 MMTNLFSTFDPSTdIMNLSINWLSSIIGFFLLPAIYWLMPSRIVIMMNNTYNSLYMEFKMLMNNNKSfKMTLMFISVLMM 80
Cdd:MTH00157    1 MMTNLFSIFDPST-SFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNK-GSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  81 MVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIETISNMIRPGTLAV 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2458278144 161 RLSANMIAGHLLLTLMGNTGPSISYKLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILYSNEVH 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-223 1.04e-45

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: 151.59  E-value: 1.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144   5 LFSTFDPSTDIMNLSINW-----LSSIIGFFLLPAIYWLMPSRIVIMMNNTYNSLYMEFKMLMNNnKSFKMTLMFISVLM 79
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLslillLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGG-KKGKFFPLIFTLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  80 MMVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIETISNMIRPGTLA 159
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2458278144 160 VRLSANMIAGHLLLTLMGNTGPS-ISYKLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILYSNE 223
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFSlMSSAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-224 6.68e-43

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 144.41  E-value: 6.68e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144   1 MMTNLFSTFDP--STDIMNLSINWLSSIIGFFLLPAIYWLMPSRIVIMMNnTYNSLYMEFKMLMNNNKSFKMTLMFISVL 78
Cdd:MTH00176    1 MLVDLFSSFDPpnKNIFSMISLSWITLLLFLLLMPSSVWFCPSKLQVFML-MFSTFLPEMILRSNGSYILGSASIIISLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  79 MMMVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIETISNMIRPGTL 158
Cdd:MTH00176   80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2458278144 159 AVRLSANMIAGHLLLTLMGNTGPS---ISYKLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILYSNEV 224
Cdd:MTH00176  160 AVRLAANLSAGHLLLGLLGAAMWGllpVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 69-222 9.80e-40

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: 133.68  E-value: 9.80e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  69 KMTLMFISVLMMMVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIET 148
Cdd:cd00310     3 KYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIEL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2458278144 149 ISNMIRPGTLAVRLSANMIAGHLLLTLMGNTGPSISYKLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILYSN 222
Cdd:cd00310    83 ISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 3-220 5.38e-37

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 129.32  E-value: 5.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144   3 TNLFSTFDPSTdIMNLSINWLSSIIG---FFLLPAIYWLmPSRIVIMMNNTYNSLymeFKMLMNN--NKSFKMTLMFISV 77
Cdd:MTH00035    5 NSIFGQFSPDT-ILFIPLTLLSSVIAlswLFFINPTNWL-PSRSQSIWLTFRQEI---LKLIFQNtnPNTAPWAGLLTTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  78 LMMMVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIETISNMIRPGT 157
Cdd:MTH00035   80 FILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2458278144 158 LAVRLSANMIAGHLLLTLMGNTGPSI--SYKLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILY 220
Cdd:MTH00035  160 LGLRLAANLTAGHLLIFLLSTAIWELsnSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFY 224
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-220 6.89e-37

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 128.92  E-value: 6.89e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144   1 MMTNLFSTFDPSTdIMNLSINWLSSIIGFFLLPAIYWLMPSRIVIMMNNTYnSLYMEFKMLMNNNKSFKMTLMFISVLMM 80
Cdd:MTH00101    1 MNENLFASFITPT-ILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLI-QLTSKQMMTIHNTKGQTWSLMLMSLILF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  81 MVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIETISNMIRPGTLAV 160
Cdd:MTH00101   79 IGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2458278144 161 RLSANMIAGHLLLTLMGNTG---PSISYKLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILY 220
Cdd:MTH00101  159 RLTANITAGHLLIHLIGGATlalMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-223 5.00e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 124.21  E-value: 5.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144   1 MMTNLFSTFDPSTDIMNL--SINWLSSIIGFFLLPAIYWLMPSRIVIMMNNTYNSLYMEFKMLMNNNKSfKMTLMFISVL 78
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSSlsFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLG-GFSLLLSSLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  79 MMMVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIETISNMIRPGTL 158
Cdd:MTH00173   80 LFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2458278144 159 AVRLSANMIAGHLLLTLMGNTGPS----ISYKLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILYSNE 223
Cdd:MTH00173  160 TVRLLANISAGHIVLTLIGNYLSSslfsSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-223 1.08e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 123.30  E-value: 1.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144   1 MMTNLFSTFDPSTDIMNL----SINWLSSIIGFFLLPAIYWLMPSRIVIMMNNTYNSLYMEF-KMLMNNNKSFkmTLMFI 75
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFNnlssTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLsRTFGKHLKGF--SSLIS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  76 SVLMMMVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIETISNMIRP 155
Cdd:MTH00005   79 ALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2458278144 156 GTLAVRLSANMIAGHLLLTLMGNTGPSI---SYKLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILYSNE 223
Cdd:MTH00005  159 ITLSFRLAANMSAGHIVLSLIGIYAASAlfsSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-223 1.97e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 122.36  E-value: 1.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144   1 MMTNLFSTFDpSTDIMNLSINWLSSIIGFFLLPAIYWLMP-SRIVIMMNNTYNSLYMEFkMLMNNNKSFKMTLMFISVLM 79
Cdd:MTH00179    1 MMLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLTNRWLnNRLSTLQSWFFGSFTFQL-MQPINKKGHKWAVLFLSLML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  80 MMVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIETISNMIRPGTLA 159
Cdd:MTH00179   79 FLLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2458278144 160 VRLSANMIAGHLLLTLMGNT---GPSISYKLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILYSNE 223
Cdd:MTH00179  159 VRLTANITAGHLLMHLISSAvfvLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 60-223 1.00e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 120.70  E-value: 1.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  60 MLMNNNKSFKMTLMFISVLMMMVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNML 139
Cdd:MTH00120   59 MLPLNKKGHKWALILTSLMLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144 140 MSFMVIIETISNMIRPGTLAVRLSANMIAGHLLLTLMGNTG---PSISYKLMMIMLIIQLMLMILESAVAIIQGYVFSVL 216
Cdd:MTH00120  139 IPALILIETISLLIRPLALGVRLTANLTAGHLLIQLISTATlnlLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLL 218


                  ....*..
gi 2458278144 217 SILYSNE 223
Cdd:MTH00120  219 LSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 69-223 4.18e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 113.81  E-value: 4.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  69 KMTLMFISVLMMMVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIET 148
Cdd:MTH00132   68 KWALLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIET 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2458278144 149 ISNMIRPGTLAVRLSANMIAGHLLLTLMGnTGPSISYKLM----MIMLIIQLMLMILESAVAIIQGYVFSVLSILYSNE 223
Cdd:MTH00132  148 ISLFIRPLALGVRLTANLTAGHLLIQLIA-TAAFVLLPLMptvaILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 60-223 1.59e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 109.67  E-value: 1.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  60 MLMNNNKSFKMTLMFISVLMMMVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNML 139
Cdd:MTH00073   59 MLPLNTPGHKWALILTSLMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144 140 MSFMVIIETISNMIRPGTLAVRLSANMIAGHLLLTLMgNTGPSISYKLMMIM----LIIQLMLMILESAVAIIQGYVFSV 215
Cdd:MTH00073  139 IPILIIIETISLFIRPLALGVRLTANLTAGHLLIQLI-STATLVLLPLMPTVsiltMIVLFLLTLLEIAVAMIQAYVFVL 217


                  ....*...
gi 2458278144 216 LSILYSNE 223
Cdd:MTH00073  218 LLSLYLQE 225
ATP-synt_A pfam00119
ATP synthase A chain;
22-220 5.22e-24

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 94.86  E-value: 5.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  22 WLSSIIGFFLLPAIYW----LMPSRIVIMMNNTYNSLYMEFKMLMNNNKSFKMTLMFISVLMMMVMNNFMGLF---PYIF 94
Cdd:pfam00119   5 LIVALILLLFLLLATRktkkLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  95 TSTSHLSMTLTIALPFWISFMLYGWIIN-TNHMFTHLVPQGTPNMLMSFMVIIETISNMIRPGTLAVRLSANMIAGHLLL 173
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2458278144 174 TLMGNTGPSISYKLMM---IMLIIQLMLMILESAVAIIQGYVFSVLSILY 220
Cdd:pfam00119 165 LLLAGLIFALLSAGFLlgvIPPLLGVAWTLFELLVAFIQAYVFTMLTAVY 214
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 17-220 1.11e-22

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 91.99  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  17 NLSINWLSSIIGFFLLPAIYWLMPSRIVIMMNNTYNSLYMEFKMlmNNNKSFKMTLMFI-SVLMMMVMNNFMGLFPYIFT 95
Cdd:MTH00175   30 NSSMMMVLAVIIFWLLLKGDKLIPNRWQSIMELIYLNIRSVVHD--NLGKSGQKYFPFIlSLFLFIAILNILGLFPYVFT 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  96 STSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIETISNMIRPGTLAVRLSANMIAGHLLLT- 174
Cdd:MTH00175  108 PTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAi 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2458278144 175 -------LMGNTGPSISYKLMMIMLIIqlmlMILESAVAIIQGYVFSVLSILY 220
Cdd:MTH00175  188 lsgfafnMLSNGLIILSLFPMLIMIFI----TLLEMAVAVIQAYVFCLLTTIY 236
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 15-220 5.27e-22

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 90.10  E-value: 5.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  15 IMNLSINWLSSIIGFFLLPAIYWLMPSRIVIMMNNTYNSLYMEFKMLMNNNkSFKMTLMFISVLMMMVMNNFMGLFPYIF 94
Cdd:MTH00172   17 LTNSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNE-GLKYFPFIISLFFFIVFLNLLGLFPYVF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  95 TSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIETISNMIRPGTLAVRLSANMIAGHLLLT 174
Cdd:MTH00172   96 TPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFA 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2458278144 175 LMGNTGPSI---SYKLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILY 220
Cdd:MTH00172  176 ILAGFGFNMlcaSGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIY 224
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 69-220 2.48e-18

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: 79.73  E-value: 2.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  69 KMTLMFISVLMMMVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLYGWIIN-TNHMFTHLVPQGTPnMLMSFMVIIE 147
Cdd:COG0356    56 KFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIE 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2458278144 148 TISNMIRPGTLAVRLSANMIAGHLLLTLMGNTGPSISykLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILY 220
Cdd:COG0356   135 IISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLL--LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 65-220 3.69e-16

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 74.45  E-value: 3.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  65 NKSFKMTLMFISVLMMMVMNNFMGLFP-YIFTSTSHLSMTLTIALPFWISFMLYGWIIN-TNHMFTHLVPQGTPnmlmsF 142
Cdd:PRK05815   67 GKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKKgLGGYLKEFYLQPHP-----L 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2458278144 143 MVIIETISNMIRPGTLAVRLSANMIAGHLLLTLMGnTGPSISYKLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILY 220
Cdd:PRK05815  142 LLPIEIISEFSRPISLSLRLFGNMLAGELILALIA-LLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 38-220 8.79e-16

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 73.82  E-value: 8.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  38 LMPSRIVIMMNNTYNSLYMEFKMLMNNnKSFKMTLMFISVLMMMVMNNFMGLFPYIFTSTSHLSMTLTIALPFWISFMLY 117
Cdd:MTH00174   59 LVPNRILVGLELIYSHFYTVLKDNLGN-KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144 118 GWIINTNHMFTHLVPQGTPNMLMSFMVIIETISNMIRPGTLAVRLSANMIAGHLLLTLMGNTGPSISYKLMMI----MLI 193
Cdd:MTH00174  138 GLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgsfvPFA 217

                         170       180
                  ....*....|....*....|....*..
gi 2458278144 194 IQLMLMILESAVAIIQGYVFSVLSILY 220
Cdd:MTH00174  218 ILIFVTILEMAVAIIQAYVFTLLTIVY 244
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 75-220 3.50e-11

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 61.68  E-value: 3.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  75 ISVLMMMVMNNFMGLFPYIFTSTSHLSMTLTIAL-PFWISFMLYGWIINTNHMFTHLVpQGTPNMLMSFMVIIETISNMI 153
Cdd:PRK13419  175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLAVfTFFITQYAAIKAHGIKGYLAHLT-GGTHWSLWIIMIPIEFIGLFT 253

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2458278144 154 RPGTLAVRLSANMIAGHL-LLTLMGNTGPSISYKLMMIMLI-IQLMLMILESAVAIIQGYVFSVLSILY 220
Cdd:PRK13419  254 KPFALTVRLFANMTAGHIvILSLIFISFILKSYIVAVAVSVpFAIFIYLLELFVAFLQAYIFTMLSALF 322
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 95-220 2.33e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 53.36  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  95 TSTSHLSMTLTIALPFWISFMLYGWIINTNHMFTHLVPQGTPNMLMSFMVIIETI-SNMIRPGTLAVRLSANMIAGH-LL 172
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHvII 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2458278144 173 LTLMGNTGPSISYKLMMIMLIIQLMLMILESAVAIIQGYVFSVLSILY 220
Cdd:PRK13417  297 LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 29-223 1.04e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 50.36  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  29 FFLLPAIYWLMPSRIVIMMNNTYNSLYMEFKMLMNNNKSFKMtlmFISVLMMMVMNNFMGLFPYIFTSTSHLSMTLTIAL 108
Cdd:MTH00087   13 VFLLQYLLYFKESMLNVLVKKFFGLLIIVFSYSNKLPLSSVI---SFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYAL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144 109 PFWISFMLYgwIINTNHMFTHLVPQGTPNMLMSF-MVIIETISNMIRPGTLAVRLSANMIAGHLLLTLMGntgpSISYKL 187
Cdd:MTH00087   90 VAWLSTFLS--FLSKSEKFSVYLSKGSDSFLKTFsMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLLN----FLGEKY 163

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2458278144 188 MMIMLIIQLMlmilESAVAIIQGYVFSVLSILYSNE 223
Cdd:MTH00087  164 VWLSILAIMM----ECFVAFIQSYIFSRLIYLYLNE 195
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 46-219 8.78e-07

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 47.19  E-value: 8.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144  46 MMNNTYNSLYMEFKMLMNNNKSfkmtLMFISVLMMMVMNNFMGL-FPYIFTSTSHLSMTLTIALPFWISFMLYGWIINTN 124
Cdd:MTH00050    1 MFVNDFSSLFSLIYKLILGGSV----SYYYSVVLFIVLFLFLLYrLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2458278144 125 HMFTHLVPQGTPNMLMSFMVIIETISNMIRPGTLAVRLSANMIAGHLLLTLMGNTGpSISYKLMMIMLIiqlmLMILESA 204
Cdd:MTH00050   77 EFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGCFGGVALGNLC-FISYWWFLVLFF----LFFYEVF 151

                         170
                  ....*....|....*
gi 2458278144 205 VAIIQGYVfsVLSIL 219
Cdd:MTH00050  152 VALVHWFI--VSSIL 164
 
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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