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Conserved domains on  [gi|1150150877|ref|YP_009349874|]
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ATP synthase F0 subunit 6 (mitochondrion) [Pseudorhynchus crassiceps]

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
1-224 6.60e-104

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 299.39  E-value: 6.60e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877   1 MMTNLFSIFDPSTTiMNLPLNWMSTILGIFILPTTYWFLPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFTLL 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  81 LFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150150877 161 LAANMIAGHLLLTLLGNTGPALSSSMISLLIMAQLALLTLECAVAMIQSYVFAILITLYSSEVN 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-224 6.60e-104

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 299.39  E-value: 6.60e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877   1 MMTNLFSIFDPSTTiMNLPLNWMSTILGIFILPTTYWFLPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFTLL 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  81 LFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150150877 161 LAANMIAGHLLLTLLGNTGPALSSSMISLLIMAQLALLTLECAVAMIQSYVFAILITLYSSEVN 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
5-224 7.30e-51

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: 164.69  E-value: 7.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877   5 LFSIFDPST-TIMNLPLNWMSTILGIFIL----PTTYWFLPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFTL 79
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  80 LLFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLAV 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150150877 160 RLAANMIAGHLLLTLLGNTGPALSSSMI-SLLIMAQLALLTLECAVAMIQSYVFAILITLYSSEVN 224
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIfALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
66-221 3.17e-38

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 129.83  E-value: 3.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  66 NKGSTFLFISLFTLLLFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCI 145
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150150877 146 ETISNMIRPGTLAVRLAANMIAGHLLLTLLGNTGPALSSSMISLLIMAQLALLTLECAVAMIQSYVFAILITLYSS 221
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
22-221 2.56e-25

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 98.33  E-value: 2.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  22 WMSTILGIFILPTTYW----FLPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFI-SLFTLLLFNNFL---GLFPYIF 93
Cdd:pfam00119   5 LIVALILLLFLLLATRktkkLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLlTLFFFILVSNLLgliPKSPGGF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  94 TSTSHLVMTLALALPLWLSFMIYGWFNH-TQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLAVRLAANMIAGHLLL 172
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1150150877 173 TLLGNTGPALSSSMISLLI---MAQLALLTLECAVAMIQSYVFAILITLYSS 221
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVippLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
40-219 3.11e-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: 79.35  E-value: 3.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  40 PSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFTLLLFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWF 119
Cdd:COG0356    28 PGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIK 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877 120 NH-TQHMFAHLVPQGTPPtLMPFMVCIETISNMIRPGTLAVRLAANMIAGHLLLTLLGNTGPALSSSMISLLImaQLALL 198
Cdd:COG0356   108 KKgLGGYLKHLFFPPFPW-LAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWT 184
                         170       180
                  ....*....|....*....|.
gi 1150150877 199 TLECAVAMIQSYVFAILITLY 219
Cdd:COG0356   185 AFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-224 6.60e-104

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 299.39  E-value: 6.60e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877   1 MMTNLFSIFDPSTTiMNLPLNWMSTILGIFILPTTYWFLPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFTLL 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  81 LFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150150877 161 LAANMIAGHLLLTLLGNTGPALSSSMISLLIMAQLALLTLECAVAMIQSYVFAILITLYSSEVN 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
5-224 7.30e-51

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: 164.69  E-value: 7.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877   5 LFSIFDPST-TIMNLPLNWMSTILGIFIL----PTTYWFLPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFTL 79
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  80 LLFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLAV 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150150877 160 RLAANMIAGHLLLTLLGNTGPALSSSMI-SLLIMAQLALLTLECAVAMIQSYVFAILITLYSSEVN 224
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIfALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
1-223 9.22e-51

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 164.44  E-value: 9.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877   1 MMTNLFSIFDPSTTIM--NLPLNWMSTILGIFILPTTYWFLPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFT 78
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIfsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  79 LLLFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLA 158
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150150877 159 VRLAANMIAGHLLLTLLGNTGPALSSSMI---SLLIMAQLALLTLECAVAMIQSYVFAILITLYSSEV 223
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPligFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
1-222 5.71e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 136.79  E-value: 5.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877   1 MMTNLFSIFDPST-TIMNLPLN---WMSTILGIFILPTTYWFLPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISL 76
Cdd:MTH00005    1 MLTDIFSSFDPATnSLFNNLSStafWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  77 FTLLLFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGT 156
Cdd:MTH00005   81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150150877 157 LAVRLAANMIAGHLLLTLLGN-TGPALSSSMIS--LLIMAQLALLTLECAVAMIQSYVFAILITLYSSE 222
Cdd:MTH00005  161 LSFRLAANMSAGHIVLSLIGIyAASALFSSISStiLLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
66-221 3.17e-38

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 129.83  E-value: 3.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  66 NKGSTFLFISLFTLLLFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCI 145
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150150877 146 ETISNMIRPGTLAVRLAANMIAGHLLLTLLGNTGPALSSSMISLLIMAQLALLTLECAVAMIQSYVFAILITLYSS 221
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
1-222 2.82e-37

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 129.68  E-value: 2.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877   1 MMTNLFSIFDpSTTIMNLPLNWMSTILGIFILPT-TYWFLPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFTL 79
Cdd:MTH00179    1 MMLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSlTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  80 LLFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLAV 159
Cdd:MTH00179   80 LLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGV 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150150877 160 RLAANMIAGHLLLTLLGNTGPALSSSMISLLIMAQL---ALLTLECAVAMIQSYVFAILITLYSSE 222
Cdd:MTH00179  160 RLTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLvlfLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
1-222 1.44e-36

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 128.06  E-value: 1.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877   1 MMTNLFSIFDPSTTIMNLP--LNWMSTILGIFILPTTYWFLPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFT 78
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSSLsfLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  79 LLLFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLA 158
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150150877 159 VRLAANMIAGHLLLTLLGNTGPALSSSMIS----LLIMAQLALLTLECAVAMIQSYVFAILITLYSSE 222
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYLSSSLFSSSVvsllLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
3-222 2.91e-35

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 124.70  E-value: 2.91e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877   3 TNLFSIFDPsTTIMNLPLNWMSTILGI---FILPTTYWFlPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFTL 79
Cdd:MTH00035    5 NSIFGQFSP-DTILFIPLTLLSSVIALswlFFINPTNWL-PSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  80 LLFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLAV 159
Cdd:MTH00035   83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150150877 160 RLAANMIAGHLLLTLLGNTGPALSSSMI--SLLIMAQLALLTLECAVAMIQSYVFAILITLYSSE 222
Cdd:MTH00035  163 RLAANLTAGHLLIFLLSTAIWELSNSPLisIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
1-222 1.61e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 122.63  E-value: 1.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877   1 MMTNLFSIFDpSTTIMNLPLNWMSTILGIFILPTTywflPSRL--NYMWNSIVSTLHNEFKTLIGPSNKGS---TFLFIS 75
Cdd:MTH00120    1 MNLNFFDQFS-SPELLGIPLILLAMLIPALLIPSP----KNRLltNRLTTLQLWLIKLITKQLMLPLNKKGhkwALILTS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  76 LFTLLLFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPG 155
Cdd:MTH00120   76 LMLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPL 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877 156 TLAVRLAANMIAGHLLLTLLGNTGPALSSSM--ISLLIMAQLALLT-LECAVAMIQSYVFAILITLYSSE 222
Cdd:MTH00120  156 ALGVRLTANLTAGHLLIQLISTATLNLLPTMptLSLLTLIILLLLTiLELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-222 2.22e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 119.59  E-value: 2.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877   1 MMTNLFSIFdPSTTIMNLPLNWMSTILG--IFILPTTYWfLPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFT 78
Cdd:MTH00132    1 MTLSFFDQF-MSPTYLGIPLIALALTLPwiLFPTPTSRW-LNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLML 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  79 LLLFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLA 158
Cdd:MTH00132   79 FLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150150877 159 VRLAANMIAGHLLLTLLGNTGPALSSSM--ISLLIMAQLALLT-LECAVAMIQSYVFAILITLYSSE 222
Cdd:MTH00132  159 VRLTANLTAGHLLIQLIATAAFVLLPLMptVAILTATLLFLLTlLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
1-222 3.62e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 119.30  E-value: 3.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877   1 MMTNLFSIFdPSTTIMNLPLNWMSTILGIFILPT-TYWFLPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFTL 79
Cdd:MTH00073    1 MNLSFFDQF-LSPTLLGIPLIMLAMLLPWLLFPTpTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  80 LLFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLAV 159
Cdd:MTH00073   80 LITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGV 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150150877 160 RLAANMIAGHLLLTLLGNTGPALSSSM--ISLLIMAQLALLT-LECAVAMIQSYVFAILITLYSSE 222
Cdd:MTH00073  160 RLTANLTAGHLLIQLISTATLVLLPLMptVSILTMIVLFLLTlLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-219 6.77e-33

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 118.52  E-value: 6.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877   1 MMTNLFSIFDpSTTIMNLPLNWMSTILGIFILPTTYWFLPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFTLL 80
Cdd:MTH00101    1 MNENLFASFI-TPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  81 LFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLAVR 160
Cdd:MTH00101   80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150150877 161 LAANMIAGHLLLTLLGNTGPALS--SSMISLLIMAQLALLT-LECAVAMIQSYVFAILITLY 219
Cdd:MTH00101  160 LTANITAGHLLIHLIGGATLALMsiSTTTALITFIILILLTiLEFAVALIQAYVFTLLVSLY 221
ATP-synt_A pfam00119
ATP synthase A chain;
22-221 2.56e-25

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 98.33  E-value: 2.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  22 WMSTILGIFILPTTYW----FLPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFI-SLFTLLLFNNFL---GLFPYIF 93
Cdd:pfam00119   5 LIVALILLLFLLLATRktkkLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLlTLFFFILVSNLLgliPKSPGGF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  94 TSTSHLVMTLALALPLWLSFMIYGWFNH-TQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLAVRLAANMIAGHLLL 172
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1150150877 173 TLLGNTGPALSSSMISLLI---MAQLALLTLECAVAMIQSYVFAILITLYSS 221
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVippLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
25-219 5.71e-22

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 90.10  E-value: 5.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  25 TILGIFILPTTYWFLPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFTLLLFNNFLGLFPYIFTSTSHLVMTLA 104
Cdd:MTH00172   27 VIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHIVVTLG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877 105 LALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLAVRLAANMIAGHLLLTLLGNTGPALSS 184
Cdd:MTH00172  107 LSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNMLC 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1150150877 185 -----SMISLLIMAQLALltLECAVAMIQSYVFAILITLY 219
Cdd:MTH00172  187 asgflSLFPLLIMVFITL--LEIAVAVIQAYVFCLLTTIY 224
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
10-219 4.14e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 87.75  E-value: 4.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  10 DPSTTIMNLPLNWMSTILGIFILPTTYWFLPSRlnymWNSIVSTLHNEFKTLI----GPSNKGSTFLFISLFTLLLFNNF 85
Cdd:MTH00175   23 DWLVTFTNSSMMMVLAVIIFWLLLKGDKLIPNR----WQSIMELIYLNIRSVVhdnlGKSGQKYFPFILSLFLFIAILNI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  86 LGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLAVRLAANM 165
Cdd:MTH00175   99 LGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANI 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877 166 IAGHLLLTLLGN------TGPALSSSMISLLIMAQLALltLECAVAMIQSYVFAILITLY 219
Cdd:MTH00175  179 SAGHLLFAILSGfafnmlSNGLIILSLFPMLIMIFITL--LEMAVAVIQAYVFCLLTTIY 236
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
40-219 3.11e-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: 79.35  E-value: 3.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  40 PSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFTLLLFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYGWF 119
Cdd:COG0356    28 PGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIK 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877 120 NH-TQHMFAHLVPQGTPPtLMPFMVCIETISNMIRPGTLAVRLAANMIAGHLLLTLLGNTGPALSSSMISLLImaQLALL 198
Cdd:COG0356   108 KKgLGGYLKHLFFPPFPW-LAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWT 184
                         170       180
                  ....*....|....*....|.
gi 1150150877 199 TLECAVAMIQSYVFAILITLY 219
Cdd:COG0356   185 AFELLVGFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
23-219 7.09e-15

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 70.59  E-value: 7.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  23 MSTILGIFILPTTYWFL-------PSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFTLLLFNNFLGLFP-YIFT 94
Cdd:PRK05815   19 LSVLLGVLILLLFALVAtrklsgvPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  95 STSHLVMTLALALPLWLSFMIYG-WFNHTQHMFAHLVPQgtpptLMPFMVCIETISNMIRPGTLAVRLAANMIAGHLLLT 173
Cdd:PRK05815   99 PTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQ-----PHPLLLPIEIISEFSRPISLSLRLFGNMLAGELILA 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1150150877 174 LLGNTGPALSSSMISLLIMAqLALLTLECAVAMIQSYVFAILITLY 219
Cdd:PRK05815  174 LIALLGGAGLLLALAPLILP-VAWTIFEIFVGTLQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
38-219 1.95e-13

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 67.27  E-value: 1.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  38 FLPSRLNYMWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFTLLLFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYG 117
Cdd:MTH00174   59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAG 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877 118 WFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLAVRLAANMIAGHLLLTLLGNTGPALSSSMISLLIMAQLAL 197
Cdd:MTH00174  139 LITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSFVPFAI 218
                         170       180
                  ....*....|....*....|....*.
gi 1150150877 198 L----TLECAVAMIQSYVFAILITLY 219
Cdd:MTH00174  219 LifvtILEMAVAIIQAYVFTLLTIVY 244
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
90-219 2.58e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 53.21  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  90 PYIFTSTSHLVMTLALALplwLSFMIYGWFNHTQH----MFAHLVpQGTPPTLMPFMVCIETISNMIRPGTLAVRLAANM 165
Cdd:PRK13419  191 PYGATATGNINVTLTLAV---FTFFITQYAAIKAHgikgYLAHLT-GGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANM 266
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1150150877 166 IAGHLLLTLLGNTGPALSSSMISLLIMAQLALLT--LECAVAMIQSYVFAILITLY 219
Cdd:PRK13419  267 TAGHIVILSLIFISFILKSYIVAVAVSVPFAIFIylLELFVAFLQAYIFTMLSALF 322
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
94-219 1.58e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 47.96  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  94 TSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETI-SNMIRPGTLAVRLAANMIAGHLLL 172
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1150150877 173 T-LLGNTGPALSSSMISLLIMAQLALLTLECAVAMIQSYVFAILITLY 219
Cdd:PRK13417  297 LaLMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
46-222 7.69e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 44.97  E-value: 7.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  46 MWNSIVSTLHNEFKTLIGPSNKGSTFLFISLFTLLLFNNFLGL--FPYIFTSTSHLVMTLALALPLWLSFMIYGWFNhtQ 123
Cdd:MTH00087   26 MLNVLVKKFFGLLIIVFSYSNKLPLSSVISFFTFIVLLLFCFGglFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSK--S 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877 124 HMFAHLVPQGTPPTLMPF-MVCIETISNMIRPGTLAVRLAANMIAGHLLLTllgntgpaLSSSMISLLIMAQLALLTLEC 202
Cdd:MTH00087  104 EKFSVYLSKGSDSFLKTFsMLFVEIVSELSRPLALTLRLTVNLMVGHLISS--------LLNFLGEKYVWLSILAIMMEC 175
                         170       180
                  ....*....|....*....|
gi 1150150877 203 AVAMIQSYVFAILITLYSSE 222
Cdd:MTH00087  176 FVAFIQSYIFSRLIYLYLNE 195
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
39-219 7.68e-05

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 42.42  E-value: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877  39 LPSRLNYMWNSIVSTLHNEFKTLIgPSNKGSTFLFI-SLFTLLLFNNFLGLFPYIFTSTSHLVMTLALALPLWLSFMIYG 117
Cdd:PRK13420   44 DPGRFQVALEGVVSTIEDAIKEVL-PRHARLVLPFVgTLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFG 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150877 118 -----WFNHTQHmfaHLVPQgtpPTLMPFMVcietISNMIRPGTLAVRLAANMiaghllltllgntgpaLSSSMISLLIM 192
Cdd:PRK13420  123 iraegLREYLKH---YLSPS---PFLLPFHL----ISEITRTLALAVRLFGNI----------------MSLELAALLVL 176
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1150150877 193 ------AQLALLTLECAVAMIQSYVFAILITLY 219
Cdd:PRK13420  177 lvagflVPVPILMLHIIEALVQAYIFGMLALIY 209
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
90-168 1.25e-04

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 41.02  E-value: 1.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150150877  90 PYIFTSTSHLVMTLALALPLWLSFMIYGWFNHTQHMFAHLVPQGTPPTLMPFMVCIETISNMIRPGTLAVRLAANMIAG 168
Cdd:MTH00050   43 PYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLG 121
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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