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Conserved domains on  [gi|1811917338|gb|QID03607|]
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ATP synthase F0 subunit 6 (mitochondrion) [Heteropternis respondens]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009593)

ATP synthase F0 subunit 6 is part of the mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V), which produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 1.89e-97

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 282.83  E-value: 1.89e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338   1 MMTNLFSTFDPSTNiFNLSLNWTSTFLGLMMIPMMFWLTPSRINIMWNKLNLNLHNEFKTLLGKNsFQGSTFIFISIFIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  81 MMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLIETISNIIRPGTLAV 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811917338 161 RLAANMIAGHLLLTLLGNTGPSLTMSIMIIMISSQMLLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 1.89e-97

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 282.83  E-value: 1.89e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338   1 MMTNLFSTFDPSTNiFNLSLNWTSTFLGLMMIPMMFWLTPSRINIMWNKLNLNLHNEFKTLLGKNsFQGSTFIFISIFIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  81 MMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLIETISNIIRPGTLAV 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811917338 161 RLAANMIAGHLLLTLLGNTGPSLTMSIMIIMISSQMLLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-225 1.07e-43

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: 146.20  E-value: 1.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338   5 LFSTFDPST-NIFNLSLNWTSTFLGLMMIPMMF----WLTPSRINIMWNKLNLNLHNEFKTLLGKNSFQGSTFIFiSIFI 79
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFLISSslsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  80 MMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLIETISNIIRPGTLA 159
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811917338 160 VRLAANMIAGHLLLTLLGNTGPSLTMSIMIIMISS-QMLLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFSLMSSAIFALLLLiLVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 67-222 2.07e-39

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: 132.91  E-value: 2.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  67 FQGSTFIFISIFIMMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLI 146
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1811917338 147 ETISNIIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLTMSIMIIMISSQMLLLILESAVAMIQAYVFSILSTLYSS 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
38-222 1.42e-22

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 91.01  E-value: 1.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  38 LTPSRINIMWNKLNLNLHNEFKTLLGKNSFQGSTFIFISIFIMMMFNNFMGLF---PYIFTSTSHMTLTFTIALPMWMSF 114
Cdd:pfam00119  25 LVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338 115 MLFGWINN-TNHMFMHLVPQGTPTALMSFMVLIETISNIIRPGTLAVRLAANMIAGH---LLLTLLGNTGPSLTMSIMII 190
Cdd:pfam00119 105 HYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHlllLLLAGLIFALLSAGFLLGVI 184

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1811917338 191 MISSQMLLLILESAVAMIQAYVFSILSTLYSS 222
Cdd:pfam00119 185 PPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 76-220 3.60e-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: 3.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  76 SIFIMMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFG-WINNTNHMFMHLVPQGTPtALMSFMVLIETISNIIR 154
Cdd:COG0356    63 TLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISELAR 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1811917338 155 PGTLAVRLAANMIAGHLLLTLLGNTGPSLTmsIMIIMISSQMLLLILESAVAMIQAYVFSILSTLY 220
Cdd:COG0356   142 PLSLSLRLFGNMFAGHIILLLLAGLAPFLL--LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 1.89e-97

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 282.83  E-value: 1.89e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338   1 MMTNLFSTFDPSTNiFNLSLNWTSTFLGLMMIPMMFWLTPSRINIMWNKLNLNLHNEFKTLLGKNsFQGSTFIFISIFIM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  81 MMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLIETISNIIRPGTLAV 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811917338 161 RLAANMIAGHLLLTLLGNTGPSLTMSIMIIMISSQMLLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-225 1.18e-50

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 164.05  E-value: 1.18e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338   1 MMTNLFSTFDP-STNIFN-LSLNWTSTFLGLMMIPMMFWLTPSRINIMWNKLNlNLHNEFKTLLGKNSFQGSTFIFISIF 78
Cdd:MTH00176    1 MLVDLFSSFDPpNKNIFSmISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFS-TFLPEMILRSNGSYILGSASIIISLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  79 IMMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLIETISNIIRPGTL 158
Cdd:MTH00176   80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338 159 AVRLAANMIAGHLLLTLLGNTGPSLTMS---IMIIMISSQMLLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:MTH00176  160 AVRLAANLSAGHLLLGLLGAAMWGLLPVsplIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-225 1.07e-43

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: 146.20  E-value: 1.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338   5 LFSTFDPST-NIFNLSLNWTSTFLGLMMIPMMF----WLTPSRINIMWNKLNLNLHNEFKTLLGKNSFQGSTFIFiSIFI 79
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFLISSslsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  80 MMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLIETISNIIRPGTLA 159
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811917338 160 VRLAANMIAGHLLLTLLGNTGPSLTMSIMIIMISS-QMLLLILESAVAMIQAYVFSILSTLYSSEVY 225
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFSLMSSAIFALLLLiLVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-223 1.11e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 136.02  E-value: 1.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338   1 MMTNLFSTFDPSTNIFNLSLN----WTSTFLGLMMIPMMFWLTPSRINIMWNKLNLNLHNEFKTLLGKNsFQGSTFIFIS 76
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFNNLSstafWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKH-LKGFSSLISA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  77 IFIMMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLIETISNIIRPG 156
Cdd:MTH00005   80 LFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338 157 TLAVRLAANMIAGHLLLTLLGNTGPSL---TMSIMIIMISSQMLLLILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00005  160 TLSFRLAANMSAGHIVLSLIGIYAASAlfsSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 67-222 2.07e-39

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: 132.91  E-value: 2.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  67 FQGSTFIFISIFIMMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLI 146
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1811917338 147 ETISNIIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLTMSIMIIMISSQMLLLILESAVAMIQAYVFSILSTLYSS 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 3-223 1.30e-36

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 128.17  E-value: 1.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338   3 TNLFSTFDPSTnIFNLSLNWTSTFLGLMMIPMMF---WLtPSRINIMWNKLNLNLhneFKTLLGKNSFQGSTFI--FISI 77
Cdd:MTH00035    5 NSIFGQFSPDT-ILFIPLTLLSSVIALSWLFFINptnWL-PSRSQSIWLTFRQEI---LKLIFQNTNPNTAPWAglLTTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  78 FIMMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLIETISNIIRPGT 157
Cdd:MTH00035   80 FILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811917338 158 LAVRLAANMIAGHLLLTLLGNTGPSL--TMSIMIIMISSQMLLLILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00035  160 LGLRLAANLTAGHLLIFLLSTAIWELsnSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-223 2.60e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 124.98  E-value: 2.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338   1 MMTNLFSTFDPSTNIFNL--SLNWTSTFLGLMMIPMMFWLTPSRINIMWNKLNLNLHNEFKTLLGKNsFQGSTFIFISIF 78
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSSlsFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLN-LGGFSLLLSSLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  79 IMMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLIETISNIIRPGTL 158
Cdd:MTH00173   80 LFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811917338 159 AVRLAANMIAGHLLLTLLGNTGPSL----TMSIMIIMISSQMLLLILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00173  160 TVRLLANISAGHIVLTLIGNYLSSSlfssSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-223 1.35e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 112.61  E-value: 1.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338   1 MMTNLFSTFDPSTNIFnlslnwTSTFLGLMMIPMMFWLTPS---RINIMWNKLNLNLHNEFKTLLGKNSFQGS--TFIFI 75
Cdd:MTH00120    1 MNLNFFDQFSSPELLG------IPLILLAMLIPALLIPSPKnrlLTNRLTTLQLWLIKLITKQLMLPLNKKGHkwALILT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  76 SIFIMMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLIETISNIIRP 155
Cdd:MTH00120   75 SLMLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRP 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1811917338 156 GTLAVRLAANMIAGHLLLTLLGNTGPSLTMSIMIIMISSQMLLL---ILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00120  155 LALGVRLTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLlltILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-223 3.10e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 111.58  E-value: 3.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338   1 MMTNLFSTFDpSTNIFNLSLNWTSTFLGLMMIPMMF--WLTPSRINIMWNKLNLNLHNEFKTLlgKNSFQGSTFIFISIF 78
Cdd:MTH00179    1 MMLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLTnrWLNNRLSTLQSWFFGSFTFQLMQPI--NKKGHKWAVLFLSLM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  79 IMMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLIETISNIIRPGTL 158
Cdd:MTH00179   78 LFLLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLAL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811917338 159 AVRLAANMIAGHLLLTLLGNTGPSLTMSIMIIMISSQ---MLLLILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00179  158 GVRLTANITAGHLLMHLISSAVFVLMNFMGMVALLTLlvlFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 73-223 3.25e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 108.81  E-value: 3.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  73 IFISIFIMMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLIETISNI 152
Cdd:MTH00132   72 LLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLF 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1811917338 153 IRPGTLAVRLAANMIAGHLLLTLLGNTGPSLTMSIMIIMISSQMLLL---ILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00132  152 IRPLALGVRLTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFlltLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-220 6.00e-28

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 105.42  E-value: 6.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338   1 MMTNLFSTFDpstnifnlslnwTSTFLGL------MMIPMMFWLTPSR-INIMWNKLNLNL-HNEFKTLLGKNSFQGSTF 72
Cdd:MTH00101    1 MNENLFASFI------------TPTILGLpivtliIMFPSLLFPTPNRlINNRLISIQQWLiQLTSKQMMTIHNTKGQTW 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  73 --IFISIFIMMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLIETIS 150
Cdd:MTH00101   69 slMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETIS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1811917338 151 NIIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLT---MSIMIIMISSQMLLLILESAVAMIQAYVFSILSTLY 220
Cdd:MTH00101  149 LFIQPMALAVRLTANITAGHLLIHLIGGATLALMsisTTTALITFIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 72-223 3.11e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 103.89  E-value: 3.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  72 FIFISIFIMMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLIETISN 151
Cdd:MTH00073   71 LILTSLMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISL 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811917338 152 IIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLTMSIMIIMISSQMLLL---ILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00073  151 FIRPLALGVRLTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFlltLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 17-220 5.69e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 95.46  E-value: 5.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  17 NLSLNWTSTFLGLMMIPMMFWL-------TPSRINIMWNKLNLNLHNEFKTLLGKNSFQGSTFIFiSIFIMMMFNNFMGL 89
Cdd:MTH00175   23 DWLVTFTNSSMMMVLAVIIFWLllkgdklIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFIL-SLFLFIAILNILGL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  90 FPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLIETISNIIRPGTLAVRLAANMIAG 169
Cdd:MTH00175  102 FPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAG 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1811917338 170 HLLLTLLGNTGPSLTMSIMIIMISSQMLLLI----LESAVAMIQAYVFSILSTLY 220
Cdd:MTH00175  182 HLLFAILSGFAFNMLSNGLIILSLFPMLIMIfitlLEMAVAVIQAYVFCLLTTIY 236
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 38-220 8.88e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 94.72  E-value: 8.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  38 LTPSRINIMWNKLNLNLHNEFKTLLGKNSFQGSTFIfISIFIMMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLF 117
Cdd:MTH00172   40 LIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFI-ISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLA 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338 118 GWINNTNHMFMHLVPQGTPTALMSFMVLIETISNIIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLTMSIMIIMISSQML 197
Cdd:MTH00172  119 GFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLI 198

                         170       180
                  ....*....|....*....|....*.
gi 1811917338 198 LL---ILESAVAMIQAYVFSILSTLY 220
Cdd:MTH00172  199 MVfitLLEIAVAVIQAYVFCLLTTIY 224
ATP-synt_A pfam00119
ATP synthase A chain;
38-222 1.42e-22

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 91.01  E-value: 1.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  38 LTPSRINIMWNKLNLNLHNEFKTLLGKNSFQGSTFIFISIFIMMMFNNFMGLF---PYIFTSTSHMTLTFTIALPMWMSF 114
Cdd:pfam00119  25 LVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338 115 MLFGWINN-TNHMFMHLVPQGTPTALMSFMVLIETISNIIRPGTLAVRLAANMIAGH---LLLTLLGNTGPSLTMSIMII 190
Cdd:pfam00119 105 HYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHlllLLLAGLIFALLSAGFLLGVI 184

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1811917338 191 MISSQMLLLILESAVAMIQAYVFSILSTLYSS 222
Cdd:pfam00119 185 PPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 76-220 3.60e-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: 3.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  76 SIFIMMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLFG-WINNTNHMFMHLVPQGTPtALMSFMVLIETISNIIR 154
Cdd:COG0356    63 TLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISELAR 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1811917338 155 PGTLAVRLAANMIAGHLLLTLLGNTGPSLTmsIMIIMISSQMLLLILESAVAMIQAYVFSILSTLY 220
Cdd:COG0356   142 PLSLSLRLFGNMFAGHIILLLLAGLAPFLL--LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 38-220 2.15e-16

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 75.36  E-value: 2.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  38 LTPSRINIMWNKLNLNLHNEFKTLLGKNSFQGSTFIfISIFIMMMFNNFMGLFPYIFTSTSHMTLTFTIALPMWMSFMLF 117
Cdd:MTH00174   59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFV-LSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338 118 GWINNTNHMFMHLVPQGTPTALMSFMVLIETISNIIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLTMSIMIIMISSQML 197
Cdd:MTH00174  138 GLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSFVPFA 217

                         170       180
                  ....*....|....*....|....*..
gi 1811917338 198 LL----ILESAVAMIQAYVFSILSTLY 220
Cdd:MTH00174  218 ILifvtILEMAVAIIQAYVFTLLTIVY 244
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 73-220 1.47e-14

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 69.82  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  73 IFISIFIMMMFNNFMGLFP-YIFTSTSHMTLTFTIALPMWMSFMLFG-WINNTNHMFMHLVPQGTPtalmsFMVLIETIS 150
Cdd:PRK05815   75 LAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQPHP-----LLLPIEIIS 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338 151 NIIRPGTLAVRLAANMIAGHLLLTLLGnTGPSLTMSIMIIMISSQMLLLILESAVAMIQAYVFSILSTLY 220
Cdd:PRK05815  150 EFSRPISLSLRLFGNMLAGELILALIA-LLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVY 218
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 75-220 7.04e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 57.83  E-value: 7.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  75 ISIFIMMMFNNFMGLFPYIFTSTSHMTLTFTIALpmwMSFMLFGWINNTNH----MFMHLVpQGTPTALMSFMVLIETIS 150
Cdd:PRK13419  175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLAV---FTFFITQYAAIKAHgikgYLAHLT-GGTHWSLWIIMIPIEFIG 250

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1811917338 151 NIIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLTMSIMIIMISSQMLLLI--LESAVAMIQAYVFSILSTLY 220
Cdd:PRK13419  251 LFTKPFALTVRLFANMTAGHIVILSLIFISFILKSYIVAVAVSVPFAIFIylLELFVAFLQAYIFTMLSALF 322
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 26-223 1.21e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 50.36  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  26 FLGLMMIPMMFWLTPSRINIMWNKLNLNLHNEFKTLlgkNSFQGSTFIFISIFIMMMFNNFMGLFPYIFTSTSHMTLTFT 105
Cdd:MTH00087   10 FMFVFLLQYLLYFKESMLNVLVKKFFGLLIIVFSYS---NKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338 106 IALPMWMSFMLFGWINNTnhMFMHLVPQGTPTALMSF-MVLIETISNIIRPGTLAVRLAANMIAGHLLLtllgntgpSLT 184
Cdd:MTH00087   87 YALVAWLSTFLSFLSKSE--KFSVYLSKGSDSFLKTFsMLFVEIVSELSRPLALTLRLTVNLMVGHLIS--------SLL 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1811917338 185 MSIMIIMISSQMLLLILESAVAMIQAYVFSILSTLYSSE 223
Cdd:MTH00087  157 NFLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 50-169 4.01e-06

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 45.65  E-value: 4.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  50 LNLNLHNEFKTLLGKNSFQGSTFIFISIFIMMMFNNFMGL-FPYIFTSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFM 128
Cdd:MTH00050    1 MFVNDFSSLFSLIYKLILGGSVSYYYSVVLFIVLFLFLLYrLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1811917338 129 HLVPQGTPTALMSFMVLIETISNIIRPGTLAVRLAANMIAG 169
Cdd:MTH00050   81 SFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLG 121
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 95-220 1.57e-05

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 44.88  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917338  95 TSTSHMTLTFTIALPMWMSFMLFGWINNTNHMFMHLVPQGTPTALMSFMVLIETI-SNIIRPGTLAVRLAANMIAGHLLL 173
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1811917338 174 T-LLGNTGPSLTMSIMIIMISSQMLLLILESAVAMIQAYVFSILSTLY 220
Cdd:PRK13417  297 LaLMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
 
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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