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Conserved domains on  [gi|1241822517|gb|ATA58322|]
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ATP synthase F0 subunit 6 [Bolivaritettix sikkinensis]

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 1.07e-93

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 273.20  E-value: 1.07e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517   1 MMTNLFSSFDPSTNWQIQFNWLSTMTFIMIIPPMFWLIKSRSNTIFNLITHLLNKELTIILNNSNKSSTLMFIGIFMMIL 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  81 INNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCIESISNIIRPATLAIRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1241822517 161 AANMIAGHLLLTLLGNSGNQVTEIMMLMLLTTQILLFMLESAVSMIQAYVFSVLSTLYSSEIN 223
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-223 1.07e-93

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 273.20  E-value: 1.07e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517   1 MMTNLFSSFDPSTNWQIQFNWLSTMTFIMIIPPMFWLIKSRSNTIFNLITHLLNKELTIILNNSNKSSTLMFIGIFMMIL 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  81 INNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCIESISNIIRPATLAIRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1241822517 161 AANMIAGHLLLTLLGNSGNQVTEIMMLMLLTTQILLFMLESAVSMIQAYVFSVLSTLYSSEIN 223
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-223 2.14e-46

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: 153.13  E-value: 2.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517   5 LFSSFDPSTNWQIQFNWLSTMTFIMIIPPMF------WLIKSRSNTIFNLITHLLNKELTIILNNSNKSSTLMFIGIFMM 78
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLSLILLLSLLIFLIssslsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  79 ILINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCIESISNIIRPATLAI 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1241822517 159 RLAANMIAGHLLLTLLGNSGNQVTEIMMLML-LTTQILLFMLESAVSMIQAYVFSVLSTLYSSEIN 223
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIFALlLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-220 7.97e-44

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: 144.08  E-value: 7.97e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  65 NKSSTLMFIGIFMMILINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCI 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1241822517 145 ESISNIIRPATLAIRLAANMIAGHLLLTLLGNSGNQVTEIMMLMLLTTQILLFMLESAVSMIQAYVFSVLSTLYSS 220
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
71-220 5.94e-27

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 102.57  E-value: 5.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  71 MFIGIFMMILINNMMGLF---PYIFTSTSHLIMTLSIALPMWVSLNLFG-WLNKPNHMLEHMVPQGTPSILMPFMVCIES 146
Cdd:pfam00119  60 LLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEI 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1241822517 147 ISNIIRPATLAIRLAANMIAGHLLLTLLGNSGNQVTEIMMLMLLTT---QILLFMLESAVSMIQAYVFSVLSTLYSS 220
Cdd:pfam00119 140 ISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPpllGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 75-218 2.97e-23

FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 92.83  E-value: 2.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  75 IFMMILINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFG-WLNKPNHMLEHMVPQGTPsILMPFMVCIESISNIIRP 153
Cdd:COG0356    64 LFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISELARP 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1241822517 154 ATLAIRLAANMIAGHLLLTLLGNSGNQVTEIMMLMLLTtqILLFMLESAVSMIQAYVFSVLSTLY 218
Cdd:COG0356   143 LSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLLP--VAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-223 1.07e-93

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 273.20  E-value: 1.07e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517   1 MMTNLFSSFDPSTNWQIQFNWLSTMTFIMIIPPMFWLIKSRSNTIFNLITHLLNKELTIILNNSNKSSTLMFIGIFMMIL 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  81 INNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCIESISNIIRPATLAIRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1241822517 161 AANMIAGHLLLTLLGNSGNQVTEIMMLMLLTTQILLFMLESAVSMIQAYVFSVLSTLYSSEIN 223
Cdd:MTH00157  161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-221 4.81e-48

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 157.50  E-value: 4.81e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517   1 MMTNLFSSFDP--STNWQ-IQFNWLSTMTFIMIIPPMFWLIKSRSNTIFNLITHLLNKELTIILNNSNKSSTLMFIGIFM 77
Cdd:MTH00176    1 MLVDLFSSFDPpnKNIFSmISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  78 MILINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCIESISNIIRPATLA 157
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1241822517 158 IRLAANMIAGHLLLTLLGNSGNQVTEIMML---MLLTTQILLFMLESAVSMIQAYVFSVLSTLYSSE 221
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLigfLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDE 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-223 2.14e-46

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: 153.13  E-value: 2.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517   5 LFSSFDPSTNWQIQFNWLSTMTFIMIIPPMF------WLIKSRSNTIFNLITHLLNKELTIILNNSNKSSTLMFIGIFMM 78
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLSLILLLSLLIFLIssslsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  79 ILINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCIESISNIIRPATLAI 158
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1241822517 159 RLAANMIAGHLLLTLLGNSGNQVTEIMMLML-LTTQILLFMLESAVSMIQAYVFSVLSTLYSSEIN 223
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIFALlLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 65-220 7.97e-44

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: 144.08  E-value: 7.97e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  65 NKSSTLMFIGIFMMILINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCI 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1241822517 145 ESISNIIRPATLAIRLAANMIAGHLLLTLLGNSGNQVTEIMMLMLLTTQILLFMLESAVSMIQAYVFSVLSTLYSS 220
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-221 9.20e-43

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 144.11  E-value: 9.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517   1 MMTNLFSSFDPSTNWQIQFN-----WLSTMTFIMIIPPMFWLIKSRSNTIFNLITHLLNKELTIILNNSNKSSTLMFIGI 75
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFNNLsstafWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  76 FMMILINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCIESISNIIRPAT 155
Cdd:MTH00005   81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1241822517 156 LAIRLAANMIAGHLLLTLLGNSGNQV---TEIMMLMLLTTQILLFMLESAVSMIQAYVFSVLSTLYSSE 221
Cdd:MTH00005  161 LSFRLAANMSAGHIVLSLIGIYAASAlfsSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-221 5.22e-41

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 139.19  E-value: 5.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517   1 MMTNLFSSFDPStnwqiQFNWLSTMTFIMIIPPMFW------LIKSRSNTIFNLITHLLNKELTIILNNSNKSSTLMFIG 74
Cdd:MTH00120    1 MNLNFFDQFSSP-----ELLGIPLILLAMLIPALLIpspknrLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  75 IFMMILINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCIESISNIIRPA 154
Cdd:MTH00120   76 LMLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517 155 TLAIRLAANMIAGHLLLTLLGNSGNQVTEIMMLMLLTTQILLF---MLESAVSMIQAYVFSVLSTLYSSE 221
Cdd:MTH00120  156 ALGVRLTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLlltILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-222 1.06e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 136.15  E-value: 1.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517   1 MMTNLFSSFDPSTN---WQIQFNWLSTMTFIMIIPPMFWLIKSRSNTIFNLITHLLNKELTIILNNSNKSSTLMFIGIFM 77
Cdd:MTH00173    1 MMVDLFSSFDDHNSsfsSLSFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  78 MILINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCIESISNIIRPATLA 157
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1241822517 158 IRLAANMIAGHLLLTLLGNSGNQVTEIM----MLMLLTTQILLFMLESAVSMIQAYVFSVLSTLYSSEI 222
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYLSSSLFSSsvvsLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDEH 229
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 3-221 1.15e-39

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 135.87  E-value: 1.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517   3 TNLFSSFDPSTNWQIQFNWLSTM---TFIMIIPPMFWLIkSRSNTIFNLIthlLNKELTIILNNSNKSS---TLMFIGIF 76
Cdd:MTH00035    5 NSIFGQFSPDTILFIPLTLLSSVialSWLFFINPTNWLP-SRSQSIWLTF---RQEILKLIFQNTNPNTapwAGLLTTVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  77 MMILINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCIESISNIIRPATL 156
Cdd:MTH00035   81 ILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIAL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517 157 AIRLAANMIAGHLLLTLLGN-----SGNQVTEIMMLMLLttqILLFMLESAVSMIQAYVFSVLSTLYSSE 221
Cdd:MTH00035  161 GLRLAANLTAGHLLIFLLSTaiwelSNSPLISIITLIIF---FLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-221 1.73e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 132.76  E-value: 1.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517   1 MMTNLFSSFDPSTNWQIQFNWLSTMT-FIMIIPPMFWLIKSRSNTIFNLITHLLNKELTIILNNSNKSSTLMFIGIFMMI 79
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLpWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  80 LINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCIESISNIIRPATLAIR 159
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1241822517 160 LAANMIAGHLLLTLLGNSGNQVTEIMMLMLLTTQILLFM---LESAVSMIQAYVFSVLSTLYSSE 221
Cdd:MTH00179  161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLltlLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-218 6.72e-38

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 131.23  E-value: 6.72e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517   1 MMTNLFSSFDPSTNWQIQFNWLSTMTFIMIIPPMFWLIKSRSNTIFNLITHLLNKELTIILNNSNKSSTLMFIGIFMMIL 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  81 INNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCIESISNIIRPATLAIRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1241822517 161 AANMIAGHLLLTLLGNSGNQVTEIMMLMLLTTQILLF---MLESAVSMIQAYVFSVLSTLY 218
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILIlltILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 70-221 1.25e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 123.06  E-value: 1.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  70 LMFIGIFMMILINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCIESISN 149
Cdd:MTH00132   71 LLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISL 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1241822517 150 IIRPATLAIRLAANMIAGHLLLTLLGNSGNQVTEIMMLMLLTTQILLFM---LESAVSMIQAYVFSVLSTLYSSE 221
Cdd:MTH00132  151 FIRPLALGVRLTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLltlLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-221 6.26e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 118.53  E-value: 6.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517   1 MMTNLFSSFDPSTNWQIQFNWLSTMTFIMIIP-PMFWLIKSRSNTIFNLITHLLNKELTIILNNSNKSSTLMFIGIFMMI 79
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPtPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  80 LINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCIESISNIIRPATLAIR 159
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1241822517 160 LAANMIAGHLLLTLLGNSGNQVTEIMMLMLLTTQILLF---MLESAVSMIQAYVFSVLSTLYSSE 221
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFlltLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP-synt_A pfam00119
ATP synthase A chain;
71-220 5.94e-27

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 102.57  E-value: 5.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  71 MFIGIFMMILINNMMGLF---PYIFTSTSHLIMTLSIALPMWVSLNLFG-WLNKPNHMLEHMVPQGTPSILMPFMVCIES 146
Cdd:pfam00119  60 LLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEI 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1241822517 147 ISNIIRPATLAIRLAANMIAGHLLLTLLGNSGNQVTEIMMLMLLTT---QILLFMLESAVSMIQAYVFSVLSTLYSS 220
Cdd:pfam00119 140 ISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPpllGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 14-218 1.33e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 99.70  E-value: 1.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  14 NWQIQFNWLSTMTFIMIIppMFWLIKSRSNTIFN---LITHLLNKEL-TIILNNSNKSSTLMF---IGIFMMILINNMMG 86
Cdd:MTH00175   23 DWLVTFTNSSMMMVLAVI--IFWLLLKGDKLIPNrwqSIMELIYLNIrSVVHDNLGKSGQKYFpfiLSLFLFIAILNILG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  87 LFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCIESISNIIRPATLAIRLAANMIA 166
Cdd:MTH00175  101 LFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISA 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1241822517 167 GHLLLTLL-GNSGNQVT-EIMMLMLLTTQILLF--MLESAVSMIQAYVFSVLSTLY 218
Cdd:MTH00175  181 GHLLFAILsGFAFNMLSnGLIILSLFPMLIMIFitLLEMAVAVIQAYVFCLLTTIY 236
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 37-218 4.48e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 98.19  E-value: 4.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  37 LIKSRSNTIFNLITHLLNKELTIILNNSNKSSTLMFIGIFMMILINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFG 116
Cdd:MTH00172   40 LIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAG 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517 117 WLNKPNHMLEHMVPQGTPSILMPFMVCIESISNIIRPATLAIRLAANMIAGHLLLTLLGNSG-NQVTEIMMLMLLTTQIL 195
Cdd:MTH00172  120 FWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGfNMLCASGFLSLFPLLIM 199

                         170       180
                  ....*....|....*....|....*
gi 1241822517 196 LFM--LESAVSMIQAYVFSVLSTLY 218
Cdd:MTH00172  200 VFItlLEIAVAVIQAYVFCLLTTIY 224
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 75-218 2.97e-23

FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 92.83  E-value: 2.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  75 IFMMILINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFG-WLNKPNHMLEHMVPQGTPsILMPFMVCIESISNIIRP 153
Cdd:COG0356    64 LFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISELARP 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1241822517 154 ATLAIRLAANMIAGHLLLTLLGNSGNQVTEIMMLMLLTtqILLFMLESAVSMIQAYVFSVLSTLY 218
Cdd:COG0356   143 LSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLLP--VAWTAFELLVGFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 75-218 1.25e-19

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 83.69  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  75 IFMMILINNMMGLFP-YIFTSTSHLIMTLSIALPMWVSLNLFG-WLNKPNHMLEHMVPQgtpsiLMPFMVCIESISNIIR 152
Cdd:PRK05815   79 LFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQ-----PHPLLLPIEIISEFSR 153

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1241822517 153 PATLAIRLAANMIAGHLLLTLLGNSGNQVTEIMMLMLLTTqILLFMLESAVSMIQAYVFSVLSTLY 218
Cdd:PRK05815  154 PISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILP-VAWTIFEIFVGTLQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 37-218 1.92e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 78.44  E-value: 1.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  37 LIKSRSNTIFNLITHLLNKELTIILNNSNKSSTLMFIGIFMMILINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFG 116
Cdd:MTH00174   59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAG 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517 117 WLNKPNHMLEHMVPQGTPSILMPFMVCIESISNIIRPATLAIRLAANMIAGHLLLTLLGNSGNQV--TEIMMLMLLTTQI 194
Cdd:MTH00174  139 LITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMinTGILIGSFVPFAI 218

                         170       180
                  ....*....|....*....|....*.
gi 1241822517 195 LLF--MLESAVSMIQAYVFSVLSTLY 218
Cdd:MTH00174  219 LIFvtILEMAVAIIQAYVFTLLTIVY 244
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 75-218 2.03e-13

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 68.23  E-value: 2.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  75 IFMMILINNMMGLFPYIFTSTSHLIMTLSIALPMWV--------SLNLFGWLnkpnhmlEHMVpQGTPSILMPFMVCIES 146
Cdd:PRK13419  177 VFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFitqyaaikAHGIKGYL-------AHLT-GGTHWSLWIIMIPIEF 248

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1241822517 147 ISNIIRPATLAIRLAANMIAGHL-LLTLLGNSGNQVTEIM-MLMLLTTQILLFMLESAVSMIQAYVFSVLSTLY 218
Cdd:PRK13419  249 IGLFTKPFALTVRLFANMTAGHIvILSLIFISFILKSYIVaVAVSVPFAIFIYLLELFVAFLQAYIFTMLSALF 322
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 93-218 1.28e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 54.13  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  93 TSTSHLIMTLSIALPMWVSLNLFGWLNKPNHMLEHMVPQGTPSILMPFMVCIESI-SNIIRPATLAIRLAANMIAGH-LL 170
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHvII 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1241822517 171 LTLLGNSGNQVTEIMMLMLLTTQILLFMLESAVSMIQAYVFSVLSTLY 218
Cdd:PRK13417  297 LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 62-221 4.97e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 51.13  E-value: 4.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  62 NNSNKSSTLMFIGIFMMILINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKpnHMLEHMVPQGTPSILMPF- 140
Cdd:MTH00087   45 SNKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKS--EKFSVYLSKGSDSFLKTFs 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517 141 MVCIESISNIIRPATLAIRLAANMIAGHLLLTLLGNSGNQVTEIMMLMLlttqillfMLESAVSMIQAYVFSVLSTLYSS 220
Cdd:MTH00087  123 MLFVEIVSELSRPLALTLRLTVNLMVGHLISSLLNFLGEKYVWLSILAI--------MMECFVAFIQSYIFSRLIYLYLN 194


                  .
gi 1241822517 221 E 221
Cdd:MTH00087  195 E 195
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 45-176 1.18e-07

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 49.88  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  45 IFNLITHLLNKELTIILNNSNKSSTLMFIGIFMMILinnMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFGWLNKPNHM 124
Cdd:MTH00050    2 FVNDFSSLFSLIYKLILGGSVSYYYSVVLFIVLFLF---LLYRLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEF 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1241822517 125 LEHMVPQGTPSILMPFMVCIESISNIIRPATLAIRLAANMIAGHLLLTLLGN 176
Cdd:MTH00050   79 FSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGCFGGVALGN 130
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 70-218 5.58e-05

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 42.81  E-value: 5.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241822517  70 LMFIGIF-MMILINNMMGLFPYIFTSTSHLIMTLSIALPMWVSLNLFG-----WLNKPNHMLehmvpqgTPS-ILMPFMV 142
Cdd:PRK13420   75 LPFVGTLwIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGiraegLREYLKHYL-------SPSpFLLPFHL 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1241822517 143 ciesISNIIRPATLAIRLAANMIAGHLLLTLlgnsgnqvteIMMLMLLTTQILLFMLESAVSMIQAYVFSVLSTLY 218
Cdd:PRK13420  148 ----ISEITRTLALAVRLFGNIMSLELAALL----------VLLVAGFLVPVPILMLHIIEALVQAYIFGMLALIY 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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