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Conserved domains on  [gi|470235833|ref|YP_007627009|]
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ATP synthase F0 subunit 6 (mitochondrion) [Tristira magellanica]

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 2.82e-98

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 285.14  E-value: 2.82e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833   1 MSNLFSTFDPSTNiFNLPLNWISAFIGLLMIPSLFWLTPSRINFLWNKLNLTLHNEFKTLLGPSsFNGTTFIFISLFIMM 80
Cdd:MTH00157   2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSFI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  81 MFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNIIRPGTLAVR 160
Cdd:MTH00157  80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 470235833 161 LTANMIAGHLLLTLLGNSGPSLTINMMSMLIFMQIMLLILESAVAMIQAYVFSILSTLYSSEV 223
Cdd:MTH00157 160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEV 222
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-223 2.82e-98

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 285.14  E-value: 2.82e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833   1 MSNLFSTFDPSTNiFNLPLNWISAFIGLLMIPSLFWLTPSRINFLWNKLNLTLHNEFKTLLGPSsFNGTTFIFISLFIMM 80
Cdd:MTH00157   2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSFI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  81 MFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNIIRPGTLAVR 160
Cdd:MTH00157  80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 470235833 161 LTANMIAGHLLLTLLGNSGPSLTINMMSMLIFMQIMLLILESAVAMIQAYVFSILSTLYSSEV 223
Cdd:MTH00157 160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEV 222
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 4-222 6.29e-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: 149.28  E-value: 6.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833    4 LFSTFDPST-NIFNLPLNWISAFIGLLMIPSLF----WLTPSRINFLWNKLNLTLHNEFKTLLGPSSFNGTTFIFiSLFI 78
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFLISSslsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833   79 MMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNIIRPGTLA 158
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 470235833  159 VRLTANMIAGHLLLTLLGNSGPSLTINMMSMLIFM-QIMLLILESAVAMIQAYVFSILSTLYSSE 222
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFSLMSSAIFALLLLiLVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 72-221 1.13e-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: 135.99  E-value: 1.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  72 IFISLFIMMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNI 151
Cdd:cd00310    7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833 152 IRPGTLAVRLTANMIAGHLLLTLLGNSGPSLTINMMSMLIFMQIMLLILESAVAMIQAYVFSILSTLYSS 221
Cdd:cd00310   87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
21-221 1.30e-26

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 101.80  E-value: 1.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833   21 WISAFIGLLMIPSLFWLT----PSRINFLWNKLNLTLHNEFKTLLGPSSFNGTTFIFISLFIMMMFNNFMGLF---PYIF 93
Cdd:pfam00119   5 LIVALILLLFLLLATRKTkklvPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833   94 TSTSHLTLTFTIALPMWMSFMLFGWINN-INHMFSHLVPQGTPTALMSFMVLIETISNIIRPGTLAVRLTANMIAGHLLL 172
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 470235833  173 TLLGNSGPSLTINMMSMLIF---MQIMLLILESAVAMIQAYVFSILSTLYSS 221
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVIpplLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 75-219 1.32e-21

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: 88.59  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  75 SLFIMMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFG-WINNINHMFSHLVPQGTPtALMSFMVLIETISNIIR 153
Cdd:COG0356   63 TLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISELAR 141

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 470235833 154 PGTLAVRLTANMIAGHLLLTLLGNSGPSLTINMMSmlIFMQIMLLILESAVAMIQAYVFSILSTLY 219
Cdd:COG0356  142 PLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLS--LLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-223 2.82e-98

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 285.14  E-value: 2.82e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833   1 MSNLFSTFDPSTNiFNLPLNWISAFIGLLMIPSLFWLTPSRINFLWNKLNLTLHNEFKTLLGPSsFNGTTFIFISLFIMM 80
Cdd:MTH00157   2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSFI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  81 MFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNIIRPGTLAVR 160
Cdd:MTH00157  80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 470235833 161 LTANMIAGHLLLTLLGNSGPSLTINMMSMLIFMQIMLLILESAVAMIQAYVFSILSTLYSSEV 223
Cdd:MTH00157 160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEV 222
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-223 1.14e-52

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 169.44  E-value: 1.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833   1 MSNLFSTFDP--STNIFNLPLNWISAFIGLLMIPSLFWLTPSRINFLWNKLNlTLHNEFKTLLGPSSFNGTTFIFISLFI 78
Cdd:MTH00176   2 LVDLFSSFDPpnKNIFSMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFS-TFLPEMILRSNGSYILGSASIIISLFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  79 MMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNIIRPGTLA 158
Cdd:MTH00176  81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 470235833 159 VRLTANMIAGHLLLTLLGNSGPSLTINM---MSMLIFMQIMLLILESAVAMIQAYVFSILSTLYSSEV 223
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSpliGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 4-222 6.29e-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: 149.28  E-value: 6.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833    4 LFSTFDPST-NIFNLPLNWISAFIGLLMIPSLF----WLTPSRINFLWNKLNLTLHNEFKTLLGPSSFNGTTFIFiSLFI 78
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFLISSslsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833   79 MMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNIIRPGTLA 158
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 470235833  159 VRLTANMIAGHLLLTLLGNSGPSLTINMMSMLIFM-QIMLLILESAVAMIQAYVFSILSTLYSSE 222
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFSLMSSAIFALLLLiLVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 72-221 1.13e-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: 135.99  E-value: 1.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  72 IFISLFIMMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNI 151
Cdd:cd00310    7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833 152 IRPGTLAVRLTANMIAGHLLLTLLGNSGPSLTINMMSMLIFMQIMLLILESAVAMIQAYVFSILSTLYSS 221
Cdd:cd00310   87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 2-222 1.83e-40

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 138.18  E-value: 1.83e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833   2 SNLFSTFDPSTnIFNLPLNWISAFIGL---LMIPSLFWLtPSRINFLWNKLNLTLhneFKTLLGPSSFNGTTFI--FISL 76
Cdd:MTH00035   5 NSIFGQFSPDT-ILFIPLTLLSSVIALswlFFINPTNWL-PSRSQSIWLTFRQEI---LKLIFQNTNPNTAPWAglLTTV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  77 FIMMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNIIRPGT 156
Cdd:MTH00035  80 FILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833 157 LAVRLTANMIAGHLLLTLLGNS----GPSLTINMMSMLIFmqIMLLILESAVAMIQAYVFSILSTLYSSE 222
Cdd:MTH00035 160 LGLRLAANLTAGHLLIFLLSTAiwelSNSPLISIITLIIF--FLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-222 6.02e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 134.09  E-value: 6.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833   1 MSNLFSTFDPSTNIFNL----PLNWISAFIGLLMIPSLFWLTPSRINFLWNKLNLTLHNEFKTLLGpSSFNGTTFIFISL 76
Cdd:MTH00005   2 LTDIFSSFDPATNSLFNnlssTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFG-KHLKGFSSLISAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  77 FIMMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNIIRPGT 156
Cdd:MTH00005  81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 470235833 157 LAVRLTANMIAGHLLLTLLGNSGPSL---TINMMSMLIFMQIMLLILESAVAMIQAYVFSILSTLYSSE 222
Cdd:MTH00005 161 LSFRLAANMSAGHIVLSLIGIYAASAlfsSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-222 8.31e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 131.14  E-value: 8.31e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833   1 MSNLFSTFDPSTNIFNLP--LNWISAFIGLLMIPSLFWLTPSRINFLWNKLNLTLHNEFKTLLGpSSFNGTTFIFISLFI 78
Cdd:MTH00173   2 MVDLFSSFDDHNSSFSSLsfLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSG-LNLGGFSLLLSSLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  79 MMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNIIRPGTLA 158
Cdd:MTH00173  81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 470235833 159 VRLTANMIAGHLLLTLLGNSGPSLTINMMSM----LIFMQIMLLILESAVAMIQAYVFSILSTLYSSE 222
Cdd:MTH00173 161 VRLLANISAGHIVLTLIGNYLSSSLFSSSVVslllVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-222 2.66e-36

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 127.25  E-value: 2.66e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833   1 MSNLFSTFDpSTNIFNLPLNWISafiglLMIPSLFWLTPS---RINFLWNKLNLTLHNEFKTLLGPSSFNGT--TFIFIS 75
Cdd:MTH00120   2 NLNFFDQFS-SPELLGIPLILLA-----MLIPALLIPSPKnrlLTNRLTTLQLWLIKLITKQLMLPLNKKGHkwALILTS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  76 LFIMMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNIIRPG 155
Cdd:MTH00120  76 LMLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833 156 TLAVRLTANMIAGHLLLTLLGNSGPSLTINMMSMLIFMQIMLL---ILESAVAMIQAYVFSILSTLYSSE 222
Cdd:MTH00120 156 ALGVRLTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLlltILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-222 4.28e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 123.90  E-value: 4.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833   1 MSNLFSTFDpSTNIFNLPLNWISAFIGLLMIPSL-FWLTPSRINFLWNKLNLTLHNEFKTLLGPSSFNGTtFIFISLFIM 79
Cdd:MTH00179   2 MLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLtNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWA-VLFLSLMLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  80 MMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNIIRPGTLAV 159
Cdd:MTH00179  80 LLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 470235833 160 RLTANMIAGHLLLTLLGnSGPSLTINMMSMLIFMQ----IMLLILESAVAMIQAYVFSILSTLYSSE 222
Cdd:MTH00179 160 RLTANITAGHLLMHLIS-SAVFVLMNFMGMVALLTllvlFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 72-222 4.46e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 121.52  E-value: 4.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  72 IFISLFIMMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNI 151
Cdd:MTH00132  72 LLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLF 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 470235833 152 IRPGTLAVRLTANMIAGHLLLTLLGNSGPSLTINMMSMLIFMQIMLL---ILESAVAMIQAYVFSILSTLYSSE 222
Cdd:MTH00132 152 IRPLALGVRLTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFlltLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-222 1.10e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 117.76  E-value: 1.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833   1 MSNLFSTFDPSTnIFNLPLNWISAFIGLLMI--PSLFWLTpsriNFLWNKLNLTLHNEFKTLLGPSSFNGT--TFIFISL 76
Cdd:MTH00073   2 NLSFFDQFLSPT-LLGIPLIMLAMLLPWLLFptPTNKWLN----NRLSTLQIWFLQNFTKQLMLPLNTPGHkwALILTSL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  77 FIMMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNIIRPGT 156
Cdd:MTH00073  77 MVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 470235833 157 LAVRLTANMIAGHLLLTLLGNSGPSL--TINMMSMLIFMQIMLL-ILESAVAMIQAYVFSILSTLYSSE 222
Cdd:MTH00073 157 LGVRLTANLTAGHLLIQLISTATLVLlpLMPTVSILTMIVLFLLtLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 70-219 1.24e-31

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 115.05  E-value: 1.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  70 TFIFISLFIMMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETIS 149
Cdd:MTH00101  69 SLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETIS 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 470235833 150 NIIRPGTLAVRLTANMIAGHLLLTLLGNSGPSL-TINMMSMLIFMQIMLL--ILESAVAMIQAYVFSILSTLY 219
Cdd:MTH00101 149 LFIQPMALAVRLTANITAGHLLIHLIGGATLALmSISTTTALITFIILILltILEFAVALIQAYVFTLLVSLY 221
ATP-synt_A pfam00119
ATP synthase A chain;
21-221 1.30e-26

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 101.80  E-value: 1.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833   21 WISAFIGLLMIPSLFWLT----PSRINFLWNKLNLTLHNEFKTLLGPSSFNGTTFIFISLFIMMMFNNFMGLF---PYIF 93
Cdd:pfam00119   5 LIVALILLLFLLLATRKTkklvPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833   94 TSTSHLTLTFTIALPMWMSFMLFGWINN-INHMFSHLVPQGTPTALMSFMVLIETISNIIRPGTLAVRLTANMIAGHLLL 172
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 470235833  173 TLLGNSGPSLTINMMSMLIF---MQIMLLILESAVAMIQAYVFSILSTLYSS 221
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVIpplLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 22-219 3.79e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 100.89  E-value: 3.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  22 ISAFIGLLMIPSLFwLTPSRINFLWNKLNLTLHNEFKTLLGPSSFNGTTFIfISLFIMMMFNNFMGLFPYIFTSTSHLTL 101
Cdd:MTH00172  26 LVIIVVLLLFKGIK-LIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFI-ISLFFFIVFLNLLGLFPYVFTPTTHIVV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833 102 TFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNIIRPGTLAVRLTANMIAGHLLLTLLGNSGPS 181
Cdd:MTH00172 104 TLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFN 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 470235833 182 LTINMMSMLIF---MQIMLLILESAVAMIQAYVFSILSTLY 219
Cdd:MTH00172 184 MLCASGFLSLFpllIMVFITLLEIAVAVIQAYVFCLLTTIY 224
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 74-219 2.79e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 96.23  E-value: 2.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  74 ISLFIMMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNIIR 153
Cdd:MTH00175  87 LSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIR 166

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 470235833 154 PGTLAVRLTANMIAGHLLLTLLgnSGPSLTINMMSMLIF----MQIMLLI--LESAVAMIQAYVFSILSTLY 219
Cdd:MTH00175 167 AISLGVRLAANISAGHLLFAIL--SGFAFNMLSNGLIILslfpMLIMIFItlLEMAVAVIQAYVFCLLTTIY 236
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 75-219 1.32e-21

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: 88.59  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  75 SLFIMMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFG-WINNINHMFSHLVPQGTPtALMSFMVLIETISNIIR 153
Cdd:COG0356   63 TLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISELAR 141

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 470235833 154 PGTLAVRLTANMIAGHLLLTLLGNSGPSLTINMMSmlIFMQIMLLILESAVAMIQAYVFSILSTLY 219
Cdd:COG0356  142 PLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLS--LLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 72-219 3.64e-18

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 79.45  E-value: 3.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  72 IFISLFIMMMFNNFMGLFP-YIFTSTSHLTLTFTIALPMWMSFMLFG-WINNINHMFSHLVPQGTPtalmsFMVLIETIS 149
Cdd:PRK05815  75 LAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQPHP-----LLLPIEIIS 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833 150 NIIRPGTLAVRLTANMIAGHLLLTLLGNSGPSLTINMMSMLIFMqIMLLILESAVAMIQAYVFSILSTLY 219
Cdd:PRK05815 150 EFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILP-VAWTIFEIFVGTLQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 37-219 3.77e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 77.29  E-value: 3.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  37 LTPSRINFLWNKLNLTLHNEFKTLLGPSSFNGTTFIfISLFIMMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLF 116
Cdd:MTH00174  59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFV-LSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLA 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833 117 GWINNINHMFSHLVPQGTPTALMSFMVLIETISNIIRPGTLAVRLTANMIAGHLLLTLLGNSGPSLTINMMSMLIFMQIM 196
Cdd:MTH00174 138 GLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSFVPFA 217

                        170       180
                 ....*....|....*....|....*..
gi 470235833 197 LL----ILESAVAMIQAYVFSILSTLY 219
Cdd:MTH00174 218 ILifvtILEMAVAIIQAYVFTLLTIVY 244
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 74-219 6.79e-13

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 66.69  E-value: 6.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  74 ISLFIMMMFNNFMGLFPYIFTSTSHLTLTFTIALpmwMSFMLFGW----INNINHMFSHLVpQGTPTALMSFMVLIETIS 149
Cdd:PRK13419 175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLAV---FTFFITQYaaikAHGIKGYLAHLT-GGTHWSLWIIMIPIEFIG 250

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 470235833 150 NIIRPGTLAVRLTANMIAGHL-LLTLLGNSGPSLT-INMMSMLIFMQIMLLILESAVAMIQAYVFSILSTLY 219
Cdd:PRK13419 251 LFTKPFALTVRLFANMTAGHIvILSLIFISFILKSyIVAVAVSVPFAIFIYLLELFVAFLQAYIFTMLSALF 322
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 71-222 1.05e-09

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 56.14  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  71 FIFISLFIMMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNInhMFSHLVPQGTPTALMSF-MVLIETIS 149
Cdd:MTH00087  53 VISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSE--KFSVYLSKGSDSFLKTFsMLFVEIVS 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 470235833 150 NIIRPGTLAVRLTANMIAGHLLLTLLgnsgpsltINMMSMLIFMQIMLLILESAVAMIQAYVFSILSTLYSSE 222
Cdd:MTH00087 131 ELSRPLALTLRLTVNLMVGHLISSLL--------NFLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 94-219 5.37e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 49.12  E-value: 5.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  94 TSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETI-SNIIRPGTLAVRLTANMIAGH-LL 171
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHvII 296

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 470235833 172 LTLLGNSGPSLTINMMSMLIFMQIMLLILESAVAMIQAYVFSILSTLY 219
Cdd:PRK13417 297 LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 73-216 1.12e-06

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 47.19  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  73 FISLFIMMMFnnFMGL-FPYIFTSTSHLTLTFTIALPMWMSFMLFGWINNINHMFSHLVPQGTPTALMSFMVLIETISNI 151
Cdd:MTH00050  27 SVVLFIVLFL--FLLYrLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYI 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 470235833 152 IRPGTLAVRLTANMIAGHLLLTLLGNsgpsLTINMMSMLIFMqIMLLILESAVAMIQAY-VFSILS 216
Cdd:MTH00050 105 IRPVVLILRPFINISLGCFGGVALGN----LCFISYWWFLVL-FFLFFYEVFVALVHWFiVSSILS 165
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 37-219 4.56e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 37.03  E-value: 4.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833  37 LTPSRINFLWNKLNLTLHNEFKTLLgpSSFNGTTFIFI-SLFIMMMFNNFMGLFPYIFTSTSHLTLTFTIALPMWMSFML 115
Cdd:PRK13420  43 LDPGRFQVALEGVVSTIEDAIKEVL--PRHARLVLPFVgTLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHW 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470235833 116 FG-----WINNINHMFShlvpqgtPTAlmsFMVLIETISNIIRPGTLAVRLTANM----IAGHLLLTLLGnsgpsltinm 186
Cdd:PRK13420 121 FGiraegLREYLKHYLS-------PSP---FLLPFHLISEITRTLALAVRLFGNImsleLAALLVLLVAG---------- 180

                        170       180       190
                 ....*....|....*....|....*....|...
gi 470235833 187 msmlIFMQIMLLILESAVAMIQAYVFSILSTLY 219
Cdd:PRK13420 181 ----FLVPVPILMLHIIEALVQAYIFGMLALIY 209
 
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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