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Conserved domains on  [gi|1593548938|ref|YP_009560400|]
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ATP synthase F0 subunit 6 (mitochondrion) [Peckia australis]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009593)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-224 1.42e-97

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 283.21  E-value: 1.42e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938   1 MTNLFSVFDPSSSiFNLSLNWLSTFLGILMIPSAYWLMPSRYHIFWNNILLTLHKEFKTLLGPMGaNGSTFLFVSLFSMI 80
Cdd:MTH00157    2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKN-KGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  81 LFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1593548938 161 LTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-224 1.42e-97

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 283.21  E-value: 1.42e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938   1 MTNLFSVFDPSSSiFNLSLNWLSTFLGILMIPSAYWLMPSRYHIFWNNILLTLHKEFKTLLGPMGaNGSTFLFVSLFSMI 80
Cdd:MTH00157    2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKN-KGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  81 LFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1593548938 161 LTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 4-224 1.18e-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: 143.50  E-value: 1.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938   4 LFSVFDPSS-SIFNLSLNWLSTFLGILMI----PSAYWLMPSRYHIFWNNILLTLHKEFKTLLGPMGANgSTFLFVSLFS 78
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGK-FFPLIFTLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  79 MILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGTLA 158
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1593548938 159 VRLTANMIAGHLLLTLLGNTGPSMSSI-LLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 224
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFSLMSSaIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-221 6.49e-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: 6.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  66 ANGSTFLFVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCI 145
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1593548938 146 ETISNVIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSS 221
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
21-221 9.68e-20

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 83.69  E-value: 9.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  21 WLSTFLGILMIPSAYW----LMPSRYHIFWNNILLTLHKEFKTLLGPMGANGSTFLFVSLFSMILFNNFMGLF---PYIF 93
Cdd:pfam00119   5 LIVALILLLFLLLATRktkkLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  94 TSTSHLTLTLTLALPLWLCFMLFG-WINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGTLAVRLTANMIAGHLLL 172
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1593548938 173 TLLGNTGPSMSSILLSVLIIT---QIALLVLESAVAMIQSYVFAVLSTLYSS 221
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVIPpllGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 62-219 4.05e-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: 4.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  62 GPMGANGSTF--LFVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFG-WINNTQHMFAHLVPQGTPAvL 138
Cdd:COG0356    48 DTIGKKGRKFapLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFPW-L 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938 139 MPFMVCIETISNVIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSSILLSVLIitQIALLVLESAVAMIQSYVFAVLSTL 218
Cdd:COG0356   127 APLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAV 204


                  .
gi 1593548938 219 Y 219
Cdd:COG0356   205 Y 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-224 1.42e-97

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 283.21  E-value: 1.42e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938   1 MTNLFSVFDPSSSiFNLSLNWLSTFLGILMIPSAYWLMPSRYHIFWNNILLTLHKEFKTLLGPMGaNGSTFLFVSLFSMI 80
Cdd:MTH00157    2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKN-KGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  81 LFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1593548938 161 LTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-223 8.94e-43

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 144.02  E-value: 8.94e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938   1 MTNLFSVFDPSSSIF--NLSLNWLSTFLGILMIPSAYWLMPSRYHIFWNnILLTLHKEFKTLLGPMGANGSTFLFVSLFS 78
Cdd:MTH00176    2 LVDLFSSFDPPNKNIfsMISLSWITLLLFLLLMPSSVWFCPSKLQVFML-MFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  79 MILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGTLA 158
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1593548938 159 VRLTANMIAGHLLLTLLGNTGPS---MSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSEV 223
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGllpVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 4-224 1.18e-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: 143.50  E-value: 1.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938   4 LFSVFDPSS-SIFNLSLNWLSTFLGILMI----PSAYWLMPSRYHIFWNNILLTLHKEFKTLLGPMGANgSTFLFVSLFS 78
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGK-FFPLIFTLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  79 MILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGTLA 158
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1593548938 159 VRLTANMIAGHLLLTLLGNTGPSMSSI-LLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 224
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFSLMSSaIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-221 6.49e-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: 6.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  66 ANGSTFLFVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCI 145
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1593548938 146 ETISNVIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSS 221
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-222 6.36e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 115.99  E-value: 6.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938   1 MTNLFSVFDPSSSIFNLSLN----WLSTFLGILMIPSAYWLMPSRYHIFWNNILLTLHKEFKTLLGPMgANGSTFLFVSL 76
Cdd:MTH00005    2 LTDIFSSFDPATNSLFNNLSstafWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKH-LKGFSSLISAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  77 FSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGT 156
Cdd:MTH00005   81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1593548938 157 LAVRLTANMIAGHLLLTLLGNTGPSM---SSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSE 222
Cdd:MTH00005  161 LSFRLAANMSAGHIVLSLIGIYAASAlfsSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-222 4.63e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 111.11  E-value: 4.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938   1 MTNLFSVFDPSSSIFNL--SLNWLSTFLGILMIPSAYWLMPSRYHIFWNNILLTLHKEFKTLLGpMGANGSTFLFVSLFS 78
Cdd:MTH00173    2 MVDLFSSFDDHNSSFSSlsFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSG-LNLGGFSLLLSSLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  79 MILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGTLA 158
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1593548938 159 VRLTANMIAGHLLLTLLGNT-----GPSMSSILLSVLIItQIALLVLESAVAMIQSYVFAVLSTLYSSE 222
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYlssslFSSSVVSLLLVLLI-QVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-222 7.32e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 108.11  E-value: 7.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938   1 MTNLFSVFDpSSSIFNLSLNWLSTFLGILMIPSAYWLMP-SRYHIFWNNILLTLHKEFKTLLGPMGANGStFLFVSLFSM 79
Cdd:MTH00179    2 MLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLTNRWLnNRLSTLQSWFFGSFTFQLMQPINKKGHKWA-VLFLSLMLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  80 ILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGTLAV 159
Cdd:MTH00179   80 LLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1593548938 160 RLTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQ---IALLVLESAVAMIQSYVFAVLSTLYSSE 222
Cdd:MTH00179  160 RLTANITAGHLLMHLISSAVFVLMNFMGMVALLTLlvlFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 3-219 5.31e-26

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 100.41  E-value: 5.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938   3 NLFSVFDpSSSIFNLSLNWLSTFLGILMIPSAYWLMPSRYHIFWNNILLTLHKEFKTLLGPMGANGSTFLfVSLFSMILF 82
Cdd:MTH00101    4 NLFASFI-TPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLML-MSLILFIGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  83 NNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGTLAVRLT 162
Cdd:MTH00101   82 TNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLT 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938 163 ANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIALL---VLESAVAMIQSYVFAVLSTLY 219
Cdd:MTH00101  162 ANITAGHLLIHLIGGATLALMSISTTTALITFIILIlltILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 24-222 3.31e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 98.41  E-value: 3.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  24 TFLGILMIPSAY---WLM-PSRYHIFWNNILLTLHKEF-----KTLLGPMGANGSTF--LFVSLFSMILFNNFMGLFPYI 92
Cdd:MTH00132   13 TYLGIPLIALALtlpWILfPTPTSRWLNNRLLTLQGWFinrftQQLLLPLNVGGHKWalLLTSLMLFLITLNMLGLLPYT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  93 FTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGTLAVRLTANMIAGHLLL 172
Cdd:MTH00132   93 FTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLI 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1593548938 173 TLLGNTGPSMSSILLSVLIITQIALL---VLESAVAMIQSYVFAVLSTLYSSE 222
Cdd:MTH00132  173 QLIATAAFVLLPLMPTVAILTATLLFlltLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-222 5.50e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 97.59  E-value: 5.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938   1 MTNLFSVFDpSSSIFNLSLNWLSTFLGILMIPSA-YWLMPSRYHIFwnnILLTLHKEFKTLLGPMGANGS--TFLFVSLF 77
Cdd:MTH00120    2 NLNFFDQFS-SPELLGIPLILLAMLIPALLIPSPkNRLLTNRLTTL---QLWLIKLITKQLMLPLNKKGHkwALILTSLM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  78 SMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGTL 157
Cdd:MTH00120   78 LLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLAL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1593548938 158 AVRLTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIALL---VLESAVAMIQSYVFAVLSTLYSSE 222
Cdd:MTH00120  158 GVRLTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLlltILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 2-222 5.76e-25

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 97.74  E-value: 5.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938   2 TNLFSVFDPSSsIFNLSLNWLSTFLGI---LMIPSAYWLmPSRYHIFWNNILLTLhkeFKTLLGPMGANGSTF--LFVSL 76
Cdd:MTH00035    5 NSIFGQFSPDT-ILFIPLTLLSSVIALswlFFINPTNWL-PSRSQSIWLTFRQEI---LKLIFQNTNPNTAPWagLLTTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  77 FSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGT 156
Cdd:MTH00035   80 FILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1593548938 157 LAVRLTANMIAGHLLLTLLGNT--GPSMSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSE 222
Cdd:MTH00035  160 LGLRLAANLTAGHLLIFLLSTAiwELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-222 2.37e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 96.19  E-value: 2.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938   1 MTNLFSVFdPSSSIFNLSLNWLSTFLGILMIPSA--YWLmpsryhifwNNILLTLHKEF-----KTLLGPMGANGS--TF 71
Cdd:MTH00073    2 NLSFFDQF-LSPTLLGIPLIMLAMLLPWLLFPTPtnKWL---------NNRLSTLQIWFlqnftKQLMLPLNTPGHkwAL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  72 LFVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNV 151
Cdd:MTH00073   72 ILTSLMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLF 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1593548938 152 IRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIALL---VLESAVAMIQSYVFAVLSTLYSSE 222
Cdd:MTH00073  152 IRPLALGVRLTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFlltLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP-synt_A pfam00119
ATP synthase A chain;
21-221 9.68e-20

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 83.69  E-value: 9.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  21 WLSTFLGILMIPSAYW----LMPSRYHIFWNNILLTLHKEFKTLLGPMGANGSTFLFVSLFSMILFNNFMGLF---PYIF 93
Cdd:pfam00119   5 LIVALILLLFLLLATRktkkLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  94 TSTSHLTLTLTLALPLWLCFMLFG-WINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGTLAVRLTANMIAGHLLL 172
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1593548938 173 TLLGNTGPSMSSILLSVLIIT---QIALLVLESAVAMIQSYVFAVLSTLYSS 221
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVIPpllGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 14-219 7.67e-19

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 81.63  E-value: 7.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  14 IFNLSLNWLSTFLGILMIPSAYWLMPSRYHIFWNNILLTLHKEFKTLLGPMGANGSTFLFvSLFSMILFNNFMGLFPYIF 93
Cdd:MTH00172   17 LTNSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFII-SLFFFIVFLNLLGLFPYVF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  94 TSTSHLTLTLTLALPLWLCFMLFGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGTLAVRLTANMIAGHLLLT 173
Cdd:MTH00172   96 TPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFA 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1593548938 174 LLGNTGPSM--SSILLSVL-IITQIALLVLESAVAMIQSYVFAVLSTLY 219
Cdd:MTH00172  176 ILAGFGFNMlcASGFLSLFpLLIMVFITLLEIAVAVIQAYVFCLLTTIY 224
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 36-219 1.38e-16

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 75.81  E-value: 1.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  36 WLMPSRYHIFWNNILLTLHKEFKTLLGPMGANGSTFLFvSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFML 115
Cdd:MTH00175   50 KLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFIL-SLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938 116 FGWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSS----ILLSVLI 191
Cdd:MTH00175  129 LGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSngliILSLFPM 208

                         170       180
                  ....*....|....*....|....*...
gi 1593548938 192 ITQIALLVLESAVAMIQSYVFAVLSTLY 219
Cdd:MTH00175  209 LIMIFITLLEMAVAVIQAYVFCLLTTIY 236
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 62-219 4.05e-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: 4.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  62 GPMGANGSTF--LFVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFG-WINNTQHMFAHLVPQGTPAvL 138
Cdd:COG0356    48 DTIGKKGRKFapLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFPW-L 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938 139 MPFMVCIETISNVIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSSILLSVLIitQIALLVLESAVAMIQSYVFAVLSTL 218
Cdd:COG0356   127 APLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL--PVAWTAFELLVGFLQAYIFTMLTAV 204


                  .
gi 1593548938 219 Y 219
Cdd:COG0356   205 Y 205
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 37-219 2.25e-13

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 67.27  E-value: 2.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  37 LMPSRYHIFWNNILLTLHKEFKTLLGPMGANGSTFLfVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLF 116
Cdd:MTH00174   59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFV-LSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938 117 GWINNTQHMFAHLVPQGTPAVLMPFMVCIETISNVIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSSILLSVLIITQIA 196
Cdd:MTH00174  138 GLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSFVPFA 217

                         170       180
                  ....*....|....*....|....*..
gi 1593548938 197 LL----VLESAVAMIQSYVFAVLSTLY 219
Cdd:MTH00174  218 ILifvtILEMAVAIIQAYVFTLLTIVY 244
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 72-219 3.36e-09

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 54.80  E-value: 3.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  72 LFVSLFSMILFNNFMGLFP-YIFTSTSHLTLTLTLALPLWLCFMLFG-WINNTQHMFAHLVPQgtpavLMPFMVCIETIS 149
Cdd:PRK05815   75 LAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQ-----PHPLLLPIEIIS 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938 150 NVIRPGTLAVRLTANMIAGHLLLTLLGnTGPSMSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLY 219
Cdd:PRK05815  150 EFSRPISLSLRLFGNMLAGELILALIA-LLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVY 218
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 127-219 1.30e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 47.96  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938 127 AHLVPQGTPAVLMPFMVCIETI-SNVIRPGTLAVRLTANMIAGHLLLT-LLGNTGPSMSSILLSVLIITQIALLVLESAV 204
Cdd:PRK13417  250 WHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVIILaLMGFIFQFQSWGIVPVSVIGSGLIYVLEIFV 329

                          90
                  ....*....|....*
gi 1593548938 205 AMIQSYVFAVLSTLY 219
Cdd:PRK13417  330 AFLQAYIFVLLTSLF 344
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 126-219 1.48e-05

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 45.12  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938 126 FAHLVpQGTPAVLMPFMVCIETISNVIRPGTLAVRLTANMIAGHLLLtllgntgpsMSSILLSVLIITQIALLV------ 199
Cdd:PRK13419  228 LAHLT-GGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAGHIVI---------LSLIFISFILKSYIVAVAvsvpfa 297

                          90       100
                  ....*....|....*....|....*
gi 1593548938 200 -----LESAVAMIQSYVFAVLSTLY 219
Cdd:PRK13419  298 ifiylLELFVAFLQAYIFTMLSALF 322
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 69-222 9.66e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 38.81  E-value: 9.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593548938  69 STFLFVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLCFMLFGWINNTQhmFAHLVPQGTPAVLMPF-MVCIET 147
Cdd:MTH00087   51 SSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEK--FSVYLSKGSDSFLKTFsMLFVEI 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1593548938 148 ISNVIRPGTLAVRLTANMIAGHLLLtllgntgpSMSSILLSVLIITQIALLVLESAVAMIQSYVFAVLSTLYSSE 222
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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