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Conserved domains on  [gi|733386791|ref|YP_009112308|]
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ATP synthase F0 subunit 6 (mitochondrion) [Sarcophaga africa]

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 1.57e-97

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 283.21  E-value: 1.57e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   1 MMTNLFSVFDPSSSiFNLSLNWLSTFLGILMIPSAYWLMPSRYHIFWNNILLTLHKEFKTLLGPMGaNGSTFLFVSLFSM 80
Cdd:MTH00157   1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKN-KGSTLIFISLFSF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  81 ILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAV 160
Cdd:MTH00157  79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 733386791 161 RLTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 225
Cdd:MTH00157 159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-225 1.57e-97

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 283.21  E-value: 1.57e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   1 MMTNLFSVFDPSSSiFNLSLNWLSTFLGILMIPSAYWLMPSRYHIFWNNILLTLHKEFKTLLGPMGaNGSTFLFVSLFSM 80
Cdd:MTH00157   1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKN-KGSTLIFISLFSF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  81 ILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAV 160
Cdd:MTH00157  79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 733386791 161 RLTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 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 2.44e-42

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: 142.73  E-value: 2.44e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791    5 LFSVFDPSS-SIFNLSLNWLSTFLGILMI----PSAYWLMPSRYHIFWNNILLTLHKEFKTLLGPMGANgSTFLFVSLFS 79
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGK-FFPLIFTLFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   80 MILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLA 159
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 733386791  160 VRLTANMIAGHLLLTLLGNTGPSMSSI-LLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 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 6.91e-33

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: 116.34  E-value: 6.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  67 ANGSTFLFVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCI 146
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 733386791 147 ETISNIIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSS 222
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
22-222 1.04e-19

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 83.69  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   22 WLSTFLGILMIPSAYW----LMPSRYHIFWNNILLTLHKEFKTLLGPMGANGSTFLFVSLFSMILFNNFMGLF---PYIF 94
Cdd:pfam00119   5 LIVALILLLFLLLATRktkkLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   95 TSTSHLTLTLTLALPLWLCFMLFGWINN-TQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAVRLTANMIAGHLLL 173
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 733386791  174 TLLGNTGPSMSSILLSVLIIT---QIALLVLESAVAMIQSYVFAVLSTLYSS 222
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVIPpllGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
63-220 3.33e-14

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: 68.56  E-value: 3.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  63 GPMGANGSTF--LFVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFG-WINNTQHMFAHLVPQGTPAvL 139
Cdd:COG0356   48 DTIGKKGRKFapLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFPW-L 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791 140 MPFMVCIETISNIIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSSILLSVLIitQIALLVLESAVAMIQSYVFAVLSTL 219
Cdd:COG0356  127 APLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAV 204

                 .
gi 733386791 220 Y 220
Cdd:COG0356  205 Y 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-225 1.57e-97

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 283.21  E-value: 1.57e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   1 MMTNLFSVFDPSSSiFNLSLNWLSTFLGILMIPSAYWLMPSRYHIFWNNILLTLHKEFKTLLGPMGaNGSTFLFVSLFSM 80
Cdd:MTH00157   1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKN-KGSTLIFISLFSF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  81 ILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAV 160
Cdd:MTH00157  79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 733386791 161 RLTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 225
Cdd:MTH00157 159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
1-224 3.77e-43

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 145.18  E-value: 3.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   1 MMTNLFSVFDPSSSIF--NLSLNWLSTFLGILMIPSAYWLMPSRYHIFWNnILLTLHKEFKTLLGPMGANGSTFLFVSLF 78
Cdd:MTH00176   1 MLVDLFSSFDPPNKNIfsMISLSWITLLLFLLLMPSSVWFCPSKLQVFML-MFSTFLPEMILRSNGSYILGSASIIISLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  79 SMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTL 158
Cdd:MTH00176  80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 733386791 159 AVRLTANMIAGHLLLTLLGNTGPS---MSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSEV 224
Cdd:MTH00176 160 AVRLAANLSAGHLLLGLLGAAMWGllpVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
5-225 2.44e-42

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: 142.73  E-value: 2.44e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791    5 LFSVFDPSS-SIFNLSLNWLSTFLGILMI----PSAYWLMPSRYHIFWNNILLTLHKEFKTLLGPMGANgSTFLFVSLFS 79
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGK-FFPLIFTLFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   80 MILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLA 159
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 733386791  160 VRLTANMIAGHLLLTLLGNTGPSMSSI-LLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 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 6.91e-33

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: 116.34  E-value: 6.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  67 ANGSTFLFVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCI 146
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 733386791 147 ETISNIIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSS 222
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
1-223 8.26e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 118.30  E-value: 8.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   1 MMTNLFSVFDPSSSIFNLSLN----WLSTFLGILMIPSAYWLMPSRYHIFWNNILLTLHKEFKTLLGPMgANGSTFLFVS 76
Cdd:MTH00005   1 MLTDIFSSFDPATNSLFNNLSstafWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKH-LKGFSSLISA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  77 LFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPG 156
Cdd:MTH00005  80 LFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPI 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791 157 TLAVRLTANMIAGHLLLTLLGNTGPSM---SSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSE 223
Cdd:MTH00005 160 TLSFRLAANMSAGHIVLSLIGIYAASAlfsSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
1-223 9.05e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 113.04  E-value: 9.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   1 MMTNLFSVFDPSSSIFNL--SLNWLSTFLGILMIPSAYWLMPSRYHIFWNNILLTLHKEFKTLLGpMGANGSTFLFVSLF 78
Cdd:MTH00173   1 MMVDLFSSFDDHNSSFSSlsFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSG-LNLGGFSLLLSSLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  79 SMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTL 158
Cdd:MTH00173  80 LFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791 159 AVRLTANMIAGHLLLTLLGNT-----GPSMSSILLSVLIItQIALLVLESAVAMIQSYVFAVLSTLYSSE 223
Cdd:MTH00173 160 TVRLLANISAGHIVLTLIGNYlssslFSSSVVSLLLVLLI-QVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
1-223 1.65e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 109.65  E-value: 1.65e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   1 MMTNLFSVFDpSSSIFNLSLNWLSTFLGILMIPSAYWLMP-SRYHIFWNNILLTLHKEFKTLLGPMGANGStFLFVSLFS 79
Cdd:MTH00179   1 MMLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLTNRWLnNRLSTLQSWFFGSFTFQLMQPINKKGHKWA-VLFLSLML 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  80 MILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLA 159
Cdd:MTH00179  79 FLLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALG 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 733386791 160 VRLTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQ---IALLVLESAVAMIQSYVFAVLSTLYSSE 223
Cdd:MTH00179 159 VRLTANITAGHLLMHLISSAVFVLMNFMGMVALLTLlvlFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-220 3.05e-26

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 101.18  E-value: 3.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   1 MMTNLFSVFDpSSSIFNLSLNWLSTFLGILMIPSAYWLMPSRYHIFWNNILLTLHKEFKTLLGPMGANGSTFLfVSLFSM 80
Cdd:MTH00101   1 MNENLFASFI-TPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLML-MSLILF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  81 ILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAV 160
Cdd:MTH00101  79 IGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAV 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 733386791 161 RLTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIALL---VLESAVAMIQSYVFAVLSTLY 220
Cdd:MTH00101 159 RLTANITAGHLLIHLIGGATLALMSISTTTALITFIILIlltILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
1-223 6.29e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 100.28  E-value: 6.29e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   1 MMTNLFSVFDpSSSIFNLSLNWLSTFLGILMIPSA-YWLMPSRYHIFwnnILLTLHKEFKTLLGPMGANGS--TFLFVSL 77
Cdd:MTH00120   1 MNLNFFDQFS-SPELLGIPLILLAMLIPALLIPSPkNRLLTNRLTTL---QLWLIKLITKQLMLPLNKKGHkwALILTSL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  78 FSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGT 157
Cdd:MTH00120  77 MLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 733386791 158 LAVRLTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIALL---VLESAVAMIQSYVFAVLSTLYSSE 223
Cdd:MTH00120 157 LGVRLTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLlltILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
1-223 2.72e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 98.50  E-value: 2.72e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   1 MMTNLFSVFdPSSSIFNLSLNWLSTFLGILMIPSA--YWLmpsryhifwNNILLTLHKEF-----KTLLGPMGANGS--T 71
Cdd:MTH00073   1 MNLSFFDQF-LSPTLLGIPLIMLAMLLPWLLFPTPtnKWL---------NNRLSTLQIWFlqnftKQLMLPLNTPGHkwA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  72 FLFVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISN 151
Cdd:MTH00073  71 LILTSLMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISL 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 733386791 152 IIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIALL---VLESAVAMIQSYVFAVLSTLYSSE 223
Cdd:MTH00073 151 FIRPLALGVRLTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFlltLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
25-223 3.62e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 98.41  E-value: 3.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  25 TFLGILMIPSAY---WLM-PSRYHIFWNNILLTLHKEF-----KTLLGPMGANGSTF--LFVSLFSMILFNNFMGLFPYI 93
Cdd:MTH00132  13 TYLGIPLIALALtlpWILfPTPTSRWLNNRLLTLQGWFinrftQQLLLPLNVGGHKWalLLTSLMLFLITLNMLGLLPYT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  94 FTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAVRLTANMIAGHLLL 173
Cdd:MTH00132  93 FTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLI 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 733386791 174 TLLGNTGPSMSSILLSVLIITQIALL---VLESAVAMIQSYVFAVLSTLYSSE 223
Cdd:MTH00132 173 QLIATAAFVLLPLMPTVAILTATLLFlltLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
3-223 3.68e-25

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 98.51  E-value: 3.68e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   3 TNLFSVFDPSSsIFNLSLNWLSTFLGI---LMIPSAYWLmPSRYHIFWNNILLTLhkeFKTLLGPMGANGSTF--LFVSL 77
Cdd:MTH00035   5 NSIFGQFSPDT-ILFIPLTLLSSVIALswlFFINPTNWL-PSRSQSIWLTFRQEI---LKLIFQNTNPNTAPWagLLTTV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  78 FSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGT 157
Cdd:MTH00035  80 FILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIA 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 733386791 158 LAVRLTANMIAGHLLLTLLGNT--GPSMSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSE 223
Cdd:MTH00035 160 LGLRLAANLTAGHLLIFLLSTAiwELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP-synt_A pfam00119
ATP synthase A chain;
22-222 1.04e-19

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 83.69  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   22 WLSTFLGILMIPSAYW----LMPSRYHIFWNNILLTLHKEFKTLLGPMGANGSTFLFVSLFSMILFNNFMGLF---PYIF 94
Cdd:pfam00119   5 LIVALILLLFLLLATRktkkLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791   95 TSTSHLTLTLTLALPLWLCFMLFGWINN-TQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAVRLTANMIAGHLLL 173
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 733386791  174 TLLGNTGPSMSSILLSVLIIT---QIALLVLESAVAMIQSYVFAVLSTLYSS 222
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVIPpllGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
15-220 6.79e-19

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 81.63  E-value: 6.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  15 IFNLSLNWLSTFLGILMIPSAYWLMPSRYHIFWNNILLTLHKEFKTLLGPMGANGSTFLFvSLFSMILFNNFMGLFPYIF 94
Cdd:MTH00172  17 LTNSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFII-SLFFFIVFLNLLGLFPYVF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  95 TSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAVRLTANMIAGHLLLT 174
Cdd:MTH00172  96 TPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFA 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 733386791 175 LLGNTGPSM--SSILLSVL-IITQIALLVLESAVAMIQSYVFAVLSTLY 220
Cdd:MTH00172 176 ILAGFGFNMlcASGFLSLFpLLIMVFITLLEIAVAVIQAYVFCLLTTIY 224
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
37-220 2.09e-16

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 75.43  E-value: 2.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  37 WLMPSRYHIFWNNILLTLHKEFKTLLGPMGANGSTFLFvSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFML 116
Cdd:MTH00175  50 KLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFIL-SLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTL 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791 117 FGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSS----ILLSVLI 192
Cdd:MTH00175 129 LGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSngliILSLFPM 208
                        170       180
                 ....*....|....*....|....*...
gi 733386791 193 ITQIALLVLESAVAMIQSYVFAVLSTLY 220
Cdd:MTH00175 209 LIMIFITLLEMAVAVIQAYVFCLLTTIY 236
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
63-220 3.33e-14

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: 68.56  E-value: 3.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  63 GPMGANGSTF--LFVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFG-WINNTQHMFAHLVPQGTPAvL 139
Cdd:COG0356   48 DTIGKKGRKFapLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFPW-L 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791 140 MPFMVCIETISNIIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSSILLSVLIitQIALLVLESAVAMIQSYVFAVLSTL 219
Cdd:COG0356  127 APLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAV 204

                 .
gi 733386791 220 Y 220
Cdd:COG0356  205 Y 205
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
38-220 1.57e-13

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 67.66  E-value: 1.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  38 LMPSRYHIFWNNILLTLHKEFKTLLGPMGANGSTFLfVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLF 117
Cdd:MTH00174  59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFV-LSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLA 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791 118 GWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIA 197
Cdd:MTH00174 138 GLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSFVPFA 217
                        170       180
                 ....*....|....*....|....*..
gi 733386791 198 LL----VLESAVAMIQSYVFAVLSTLY 220
Cdd:MTH00174 218 ILifvtILEMAVAIIQAYVFTLLTIVY 244
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
73-220 2.89e-09

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 55.19  E-value: 2.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  73 LFVSLFSMILFNNFMGLFP-YIFTSTSHLTLTLTLALPLWLCFMLFG-WINNTQHMFAHLVPQgtpavLMPFMVCIETIS 150
Cdd:PRK05815  75 LAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQ-----PHPLLLPIEIIS 149
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791 151 NIIRPGTLAVRLTANMIAGHLLLTLLGnTGPSMSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLY 220
Cdd:PRK05815 150 EFSRPISLSLRLFGNMLAGELILALIA-LLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVY 218
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
128-220 8.07e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 48.73  E-value: 8.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791 128 AHLVPQGTPAVLMPFMVCIETI-SNIIRPGTLAVRLTANMIAGHLLLT-LLGNTGPSMSSILLSVLIITQIALLVLESAV 205
Cdd:PRK13417 250 WHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVIILaLMGFIFQFQSWGIVPVSVIGSGLIYVLEIFV 329
                         90
                 ....*....|....*
gi 733386791 206 AMIQSYVFAVLSTLY 220
Cdd:PRK13417 330 AFLQAYIFVLLTSLF 344
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
127-220 1.27e-05

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 45.12  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791 127 FAHLVpQGTPAVLMPFMVCIETISNIIRPGTLAVRLTANMIAGHLLLtllgntgpsMSSILLSVLIITQIALLV------ 200
Cdd:PRK13419 228 LAHLT-GGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAGHIVI---------LSLIFISFILKSYIVAVAvsvpfa 297
                         90       100
                 ....*....|....*....|....*
gi 733386791 201 -----LESAVAMIQSYVFAVLSTLY 220
Cdd:PRK13419 298 ifiylLELFVAFLQAYIFTMLSALF 322
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
70-223 1.23e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 38.42  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 733386791  70 STFLFVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQhmFAHLVPQGTPAVLMPF-MVCIET 148
Cdd:MTH00087  51 SSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEK--FSVYLSKGSDSFLKTFsMLFVEI 128
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 733386791 149 ISNIIRPGTLAVRLTANMIAGHLLLtllgntgpSMSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSE 223
Cdd:MTH00087 129 VSELSRPLALTLRLTVNLMVGHLIS--------SLLNFLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
 
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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