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Conserved domains on  [gi|1268891688|gb|ATN41233|]
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ATP synthase F0 subunit 6 (mitochondrion) [Endopterygota sp. 24 LC-2017]

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 2.01e-93

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 272.81  E-value: 2.01e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688   1 MTNLFSVFDPSSSiFNLSLNWMSTFIGILLIPSMYWFMPSRHHIMWNTILITLHKEFKTLLGPTgHNGSSFIFVSLFSMI 80
Cdd:MTH00157    2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  81 LFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1268891688 161 LAANMIAGHLLLTLLGNTGPSLSYLMIMLLLIAQIALLVLESAVAIIQSYVFAVLSTLYSSEVN 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-224 2.01e-93

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 272.81  E-value: 2.01e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688   1 MTNLFSVFDPSSSiFNLSLNWMSTFIGILLIPSMYWFMPSRHHIMWNTILITLHKEFKTLLGPTgHNGSSFIFVSLFSMI 80
Cdd:MTH00157    2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  81 LFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1268891688 161 LAANMIAGHLLLTLLGNTGPSLSYLMIMLLLIAQIALLVLESAVAIIQSYVFAVLSTLYSSEVN 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 2.76e-40

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: 137.34  E-value: 2.76e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688   4 LFSVFDPSS-SIFNLSLNWMSTFIGILLI----PSMYWFMPSRHHIMWNTILITLHKEFKTLLGPTGHNGSSFIFvSLFS 78
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  79 MILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLA 158
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1268891688 159 VRLAANMIAGHLLLTLLGNTGPSL-SYLMIMLLLIAQIALLVLESAVAIIQSYVFAVLSTLYSSEVN 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 ...
 72-221 2.55e-31

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: 112.11  E-value: 2.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  72 IFVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNI 151
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688 152 IRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSYLMIMLLLIAQIALLVLESAVAIIQSYVFAVLSTLYSS 221
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
39-221 1.11e-16

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 75.60  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  39 PSRHHIMWNTILITLHKEFKTLLGPTGHNGSSFIFVSLFSMILFNNFMGLF---PYIFTSTSHLTLTLTLALPLWLSFMV 115
Cdd:pfam00119  27 PGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHY 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688 116 YGWINH-TQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSYLMIMLLLIAQ 194
Cdd:pfam00119 107 YGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPP 186

                         170       180       190
                  ....*....|....*....|....*....|
gi 1268891688 195 IALLV---LESAVAIIQSYVFAVLSTLYSS 221
Cdd:pfam00119 187 LLGVAwtlFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 22-219 4.15e-12

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: 62.78  E-value: 4.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  22 MSTFIGILLIPSMYWFM------PSRHHIMWNTILITLHKEFKTLLGPTGHNGSSFIFvSLFSMILFNNFMGLFPYIFTS 95
Cdd:COG0356     5 MSWLAMLLLLLLFLLATrklklvPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLL-TLFLFILVSNLLGLIPGLFPP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  96 TSHLTLTLTLALPLWLSFMVYGWINH-TQHMFAHLVPQGTPAvLMPFMVCIETISNIIRPGTLAVRLAANMIAGHLLLTL 174
Cdd:COG0356    84 TADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPW-LAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLL 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1268891688 175 LGNTGPSLsyLMIMLLLIAQIALLVLESAVAIIQSYVFAVLSTLY 219
Cdd:COG0356   163 LAGLAPFL--LLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-224 2.01e-93

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 272.81  E-value: 2.01e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688   1 MTNLFSVFDPSSSiFNLSLNWMSTFIGILLIPSMYWFMPSRHHIMWNTILITLHKEFKTLLGPTgHNGSSFIFVSLFSMI 80
Cdd:MTH00157    2 MTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  81 LFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1268891688 161 LAANMIAGHLLLTLLGNTGPSLSYLMIMLLLIAQIALLVLESAVAIIQSYVFAVLSTLYSSEVN 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-223 1.05e-40

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 138.63  E-value: 1.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688   1 MTNLFSVFDPSSSIF--NLSLNWMSTFIGILLIPSMYWFMPSRHHIMWNTiLITLHKEFKTLLGPTGHNGSSFIFVSLFS 78
Cdd:MTH00176    2 LVDLFSSFDPPNKNIfsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLM-FSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  79 MILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLA 158
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1268891688 159 VRLAANMIAGHLLLTLLGNTGPSL---SYLMIMLLLIAQIALLVLESAVAIIQSYVFAVLSTLYSSEV 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 2.76e-40

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: 137.34  E-value: 2.76e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688   4 LFSVFDPSS-SIFNLSLNWMSTFIGILLI----PSMYWFMPSRHHIMWNTILITLHKEFKTLLGPTGHNGSSFIFvSLFS 78
Cdd:TIGR01131   1 LFSQFDISPiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  79 MILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLA 158
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1268891688 159 VRLAANMIAGHLLLTLLGNTGPSL-SYLMIMLLLIAQIALLVLESAVAIIQSYVFAVLSTLYSSEVN 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 ...
 72-221 2.55e-31

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: 112.11  E-value: 2.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  72 IFVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNI 151
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688 152 IRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSYLMIMLLLIAQIALLVLESAVAIIQSYVFAVLSTLYSS 221
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-222 5.57e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 105.72  E-value: 5.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688   1 MTNLFSVFDPSSSIFNL--SLNWMSTFIGILLIPSMYWFMPSRHHIMWNTILITLHKEFKTLLGpTGHNGSSFIFVSLFS 78
Cdd:MTH00173    2 MVDLFSSFDDHNSSFSSlsFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSG-LNLGGFSLLLSSLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  79 MILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLA 158
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1268891688 159 VRLAANMIAGHLLLTLLGNTGPSLSYLMIMLLLIAQIALLV----LESAVAIIQSYVFAVLSTLYSSE 222
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYLSSSLFSSSVVSLLLVLLIQVgyfiFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-222 6.99e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 105.59  E-value: 6.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688   1 MTNLFSVFDPSSSIFNLSLN----WMSTFIGILLIPSMYWFMPSRHHIMWNTILITLHKEFKTLLGpTGHNGSSFIFVSL 76
Cdd:MTH00005    2 LTDIFSSFDPATNSLFNNLSstafWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFG-KHLKGFSSLISAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  77 FSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGT 156
Cdd:MTH00005   81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1268891688 157 LAVRLAANMIAGHLLLTLLGNTGPSL---SYLMIMLLLIAQIALLVLESAVAIIQSYVFAVLSTLYSSE 222
Cdd:MTH00005  161 LSFRLAANMSAGHIVLSLIGIYAASAlfsSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-222 9.35e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 105.03  E-value: 9.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688   1 MTNLFSVFDpSSSIFNLSLNWMSTFIGILLIPSMY-WFMPSRHHIMWNTILITLHKEFKTLLGPTGHNGSsFIFVSLFSM 79
Cdd:MTH00179    2 MLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLTnRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWA-VLFLSLMLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  80 ILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAV 159
Cdd:MTH00179   80 LLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1268891688 160 RLAANMIAGHLLLTLLGNTGPSLSYLMIMLLLIAQIAL---LVLESAVAIIQSYVFAVLSTLYSSE 222
Cdd:MTH00179  160 RLTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLfllTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-222 5.35e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 95.28  E-value: 5.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688   1 MTNLFSVFDpSSSIFNLSLNWMSTFIGILLIPSM-YWFMPSRHHIMWNTILITLHKEFKTLLGPTGHNGSSfIFVSLFSM 79
Cdd:MTH00120    2 NLNFFDQFS-SPELLGIPLILLAMLIPALLIPSPkNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWAL-ILTSLMLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  80 ILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAV 159
Cdd:MTH00120   80 LLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688 160 RLAANMIAGH-------LLLTLLGNTGPSLSYLMIMllliAQIALLVLESAVAIIQSYVFAVLSTLYSSE 222
Cdd:MTH00120  160 RLTANLTAGHlliqlisTATLNLLPTMPTLSLLTLI----ILLLLTILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 2-222 3.44e-23

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 93.11  E-value: 3.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688   2 TNLFSVFDPSSsIFNLSLNWMSTFIGI---LLIPSMYWFmPSRHHIMWNTILITLhkeFKTLLGPTGHNGSSFI--FVSL 76
Cdd:MTH00035    5 NSIFGQFSPDT-ILFIPLTLLSSVIALswlFFINPTNWL-PSRSQSIWLTFRQEI---LKLIFQNTNPNTAPWAglLTTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  77 FSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGT 156
Cdd:MTH00035   80 FILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1268891688 157 LAVRLAANMIAGHLLLTLLGNTGPSL--SYLMIMLLLIAQIALLVLESAVAIIQSYVFAVLSTLYSSE 222
Cdd:MTH00035  160 LGLRLAANLTAGHLLIFLLSTAIWELsnSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-222 2.30e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 88.10  E-value: 2.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688   1 MTNLFSVFdPSSSIFNLSLNWMStfigiLLIPSMYWFMPSRHHImwNTILITLHKEF-----KTLLGPTGHNGS--SFIF 73
Cdd:MTH00073    2 NLSFFDQF-LSPTLLGIPLIMLA-----MLLPWLLFPTPTNKWL--NNRLSTLQIWFlqnftKQLMLPLNTPGHkwALIL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  74 VSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNIIR 153
Cdd:MTH00073   74 TSLMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1268891688 154 PGTLAVRLAANMIAGHLLLTLLGNTGPSLSYLMIMLLLIAQIALL---VLESAVAIIQSYVFAVLSTLYSSE 222
Cdd:MTH00073  154 PLALGVRLTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFlltLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 76-219 3.80e-20

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 85.00  E-value: 3.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  76 LFSMILF---NNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNII 152
Cdd:MTH00101   72 LMSLILFigsTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFI 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688 153 RPGTLAVRLAANMIAGHLLLTLLGNTG---PSLSYLMIMLLLIAQIALLVLESAVAIIQSYVFAVLSTLY 219
Cdd:MTH00101  152 QPMALAVRLTANITAGHLLIHLIGGATlalMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 24-222 6.08e-19

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 81.84  E-value: 6.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  24 TFIGI------LLIPSMYWFMPSRHHImwNTILITLHKEF-----KTLLGPTGHNGS--SFIFVSLFSMILFNNFMGLFP 90
Cdd:MTH00132   13 TYLGIplialaLTLPWILFPTPTSRWL--NNRLLTLQGWFinrftQQLLLPLNVGGHkwALLLTSLMLFLITLNMLGLLP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  91 YIFTSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAVRLAANMIAGHL 170
Cdd:MTH00132   91 YTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTAGHL 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1268891688 171 LLTLLGNTGPSLSYLM---IMLLLIAQIALLVLESAVAIIQSYVFAVLSTLYSSE 222
Cdd:MTH00132  171 LIQLIATAAFVLLPLMptvAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 14-219 4.57e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 79.70  E-value: 4.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  14 IFNLSLNWMSTFIGILLIPSMYWFMPSRHHIMWNTILITLHKEFKTLLGPTGHNGSSFIFvSLFSMILFNNFMGLFPYIF 93
Cdd:MTH00172   17 LTNSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFII-SLFFFIVFLNLLGLFPYVF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  94 TSTSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAVRLAANMIAGHLLLT 173
Cdd:MTH00172   96 TPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFA 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1268891688 174 LLGNTGPSL---SYLMIMLLLIAQIALLVLESAVAIIQSYVFAVLSTLY 219
Cdd:MTH00172  176 ILAGFGFNMlcaSGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIY 224
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 16-219 3.54e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 77.35  E-value: 3.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  16 NLSLNWMSTFIGILLIPSMYWFMPSRHHIMWNTILITLHKEFKTLLGPTGHNGSSFIFvSLFSMILFNNFMGLFPYIFTS 95
Cdd:MTH00175   30 NSSMMMVLAVIIFWLLLKGDKLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFIL-SLFLFIAILNILGLFPYVFTP 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  96 TSHLTLTLTLALPLWLSFMVYGWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAVRLAANMIAGHLLLTLL 175
Cdd:MTH00175  109 TAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAIL 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1268891688 176 G--------NTGPSLSYLMIMllliAQIALLVLESAVAIIQSYVFAVLSTLY 219
Cdd:MTH00175  189 SgfafnmlsNGLIILSLFPML----IMIFITLLEMAVAVIQAYVFCLLTTIY 236
ATP-synt_A pfam00119
ATP synthase A chain;
39-221 1.11e-16

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 75.60  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  39 PSRHHIMWNTILITLHKEFKTLLGPTGHNGSSFIFVSLFSMILFNNFMGLF---PYIFTSTSHLTLTLTLALPLWLSFMV 115
Cdd:pfam00119  27 PGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHY 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688 116 YGWINH-TQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSYLMIMLLLIAQ 194
Cdd:pfam00119 107 YGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPP 186

                         170       180       190
                  ....*....|....*....|....*....|
gi 1268891688 195 IALLV---LESAVAIIQSYVFAVLSTLYSS 221
Cdd:pfam00119 187 LLGVAwtlFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 37-219 2.91e-13

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 66.89  E-value: 2.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  37 FMPSRHHIMWNTILITLHKEFKTLLGPTGHNGSSFIfVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVY 116
Cdd:MTH00174   59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFV-LSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688 117 GWINHTQHMFAHLVPQGTPAVLMPFMVCIETISNIIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSYLMIMLLL----I 192
Cdd:MTH00174  138 GLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSfvpfA 217

                         170       180
                  ....*....|....*....|....*..
gi 1268891688 193 AQIALLVLESAVAIIQSYVFAVLSTLY 219
Cdd:MTH00174  218 ILIFVTILEMAVAIIQAYVFTLLTIVY 244
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 22-219 4.15e-12

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: 62.78  E-value: 4.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  22 MSTFIGILLIPSMYWFM------PSRHHIMWNTILITLHKEFKTLLGPTGHNGSSFIFvSLFSMILFNNFMGLFPYIFTS 95
Cdd:COG0356     5 MSWLAMLLLLLLFLLATrklklvPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLL-TLFLFILVSNLLGLIPGLFPP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  96 TSHLTLTLTLALPLWLSFMVYGWINH-TQHMFAHLVPQGTPAvLMPFMVCIETISNIIRPGTLAVRLAANMIAGHLLLTL 174
Cdd:COG0356    84 TADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPW-LAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLL 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1268891688 175 LGNTGPSLsyLMIMLLLIAQIALLVLESAVAIIQSYVFAVLSTLY 219
Cdd:COG0356   163 LAGLAPFL--LLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 8-219 6.33e-08

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 51.33  E-value: 6.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688   8 FDPSSSIFNLSLNWMSTFIGILLIPSMYWFM-------PSRHHIMWNTILITLHKEFKTLLGPTGHNGSSFIFvSLFSMI 80
Cdd:PRK05815    5 LIIGFGGFNFDSLLLSVLLGVLILLLFALVAtrklsgvPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAF-TLFLFI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  81 LFNNFMGLFP-YIFTSTSHLTLTLTLALPLWLSFMVYG-WINHTQHMFAHLVPQgtpavLMPFMVCIETISNIIRPGTLA 158
Cdd:PRK05815   84 LLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQ-----PHPLLLPIEIISEFSRPISLS 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1268891688 159 VRLAANMIAGHLLLTLLGNTGPSLSYLMImLLLIAQIALLVLESAVAIIQSYVFAVLSTLY 219
Cdd:PRK05815  159 LRLFGNMLAGELILALIALLGGAGLLLAL-APLILPVAWTIFEIFVGTLQAYIFMMLTIVY 218
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 127-219 8.75e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 45.65  E-value: 8.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688 127 AHLVPQGTPAVLMPFMVCIETI-SNIIRPGTLAVRLAANMIAGHLLLT-LLGNTGPSLSYLMIMLLLIAQIALLVLESAV 204
Cdd:PRK13417  250 WHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVIILaLMGFIFQFQSWGIVPVSVIGSGLIYVLEIFV 329

                          90
                  ....*....|....*
gi 1268891688 205 AIIQSYVFAVLSTLY 219
Cdd:PRK13417  330 AFLQAYIFVLLTSLF 344
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 126-219 3.14e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 40.88  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688 126 FAHLVpQGTPAVLMPFMVCIETISNIIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSYLMIMLLLIAQIALLV--LESA 203
Cdd:PRK13419  228 LAHLT-GGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAGHIVILSLIFISFILKSYIVAVAVSVPFAIFIylLELF 306

                          90
                  ....*....|....*.
gi 1268891688 204 VAIIQSYVFAVLSTLY 219
Cdd:PRK13419  307 VAFLQAYIFTMLSALF 322
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 69-222 1.57e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 38.04  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268891688  69 SSFIFVSLFSMILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMVYGWINhtQHMFAHLVPQGTPAVLMPF-MVCIET 147
Cdd:MTH00087   51 SSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSK--SEKFSVYLSKGSDSFLKTFsMLFVEI 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1268891688 148 ISNIIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSYLMIMllliaqiaLLVLESAVAIIQSYVFAVLSTLYSSE 222
Cdd:MTH00087  129 VSELSRPLALTLRLTVNLMVGHLISSLLNFLGEKYVWLSIL--------AIMMECFVAFIQSYIFSRLIYLYLNE 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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