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Conserved domains on  [gi|2062575563|gb|QXG19442|]
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ATP synthase F0 subunit 6 (mitochondrion) [Drosophila nigrosparsa]

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 1.05e-99

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 288.60  E-value: 1.05e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563   1 MMTNLFSVFDPSAIFGLSLNWLSTFLGLLMIPSIYWLMPSRYNIFWNSILVTLHKEFKTLLGPSaHNGSTFIFISLFSLI 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  81 LFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2062575563 161 LTANMIAGHLLLTLLGNTGPSMSYMLVTFLLIGQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-224 1.05e-99

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 288.60  E-value: 1.05e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563   1 MMTNLFSVFDPSAIFGLSLNWLSTFLGLLMIPSIYWLMPSRYNIFWNSILVTLHKEFKTLLGPSaHNGSTFIFISLFSLI 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  81 LFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2062575563 161 LTANMIAGHLLLTLLGNTGPSMSYMLVTFLLIGQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 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 ...
 5-224 1.71e-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: 143.12  E-value: 1.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563   5 LFSVFDPS--AIFGLSLNWLSTFLGLLMI----PSIYWLMPSRYNIFWNSILVTLHKEFKTLLGPSAHNGSTFIFiSLFS 78
Cdd:TIGR01131   1 LFSQFDISpiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  79 LILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIRPGTLA 158
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2062575563 159 VRLTANMIAGHLLLTLLGNTGPS-MSYMLVTFLLIGQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 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 1.83e-32

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: 115.19  E-value: 1.83e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  72 IFISLFSLILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNV 151
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563 152 IRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSYMLVTFLLIGQIALLVLESAVAMIQSYVFAVLSTLYSS 221
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
21-221 8.68e-19

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 81.00  E-value: 8.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  21 WLSTFLGLLMIPSIYW----LMPSRYNIFWNSILVTLHKEFKTLLGPSAHNGSTFIFISLFSLILFNNFMGLF---PYIF 93
Cdd:pfam00119   5 LIVALILLLFLLLATRktkkLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  94 TSTSHLTLTLTLALPLWLSFMMYGWINH-TQHMFAHLVPQGTPAILMPFMVCIETISNVIRPGTLAVRLTANMIAGH--- 169
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHlll 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2062575563 170 LLLTLLGNTGPSMSYMLVTFLLIGQIALLVLESAVAMIQSYVFAVLSTLYSS 221
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 37-219 1.86e-13

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: 66.64  E-value: 1.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  37 LMPSRYNIFWNSILVTLHKEFKTLLGPSAHNGSTFIFiSLFSLILFNNFMGLFPYIF-----TSTSHLTLTLTLALPLWL 111
Cdd:COG0356    26 LVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLL-TLFLFILVSNLLGLIPGLFpptadINVTLALALIVFVLVHYY 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563 112 SFMMYGWINHTQHMFAHLVPqgtpaILMPFMVCIETISNVIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSYMLVTFLL 191
Cdd:COG0356   105 GIKKKGLGGYLKHLFFPPFP-----WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL 179

                         170       180
                  ....*....|....*....|....*...
gi 2062575563 192 igQIALLVLESAVAMIQSYVFAVLSTLY 219
Cdd:COG0356   180 --PVAWTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-224 1.05e-99

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 288.60  E-value: 1.05e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563   1 MMTNLFSVFDPSAIFGLSLNWLSTFLGLLMIPSIYWLMPSRYNIFWNSILVTLHKEFKTLLGPSaHNGSTFIFISLFSLI 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPK-NKGSTLIFISLFSFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  81 LFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIRPGTLAVR 160
Cdd:MTH00157   80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2062575563 161 LTANMIAGHLLLTLLGNTGPSMSYMLVTFLLIGQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 224
Cdd:MTH00157  160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-223 1.25e-44

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 148.64  E-value: 1.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563   1 MMTNLFSVFDPSAIF---GLSLNWLSTFLGLLMIPSIYWLMPSRYNIFWNsILVTLHKEFKTLLGPSAHNGSTFIFISLF 77
Cdd:MTH00176    1 MLVDLFSSFDPPNKNifsMISLSWITLLLFLLLMPSSVWFCPSKLQVFML-MFSTFLPEMILRSNGSYILGSASIIISLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  78 SLILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIRPGTL 157
Cdd:MTH00176   80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2062575563 158 AVRLTANMIAGHLLLTLLGNTGPS---MSYMLVTFLLIGQIALLVLESAVAMIQSYVFAVLSTLYSSEV 223
Cdd:MTH00176  160 AVRLAANLSAGHLLLGLLGAAMWGllpVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-224 1.71e-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: 143.12  E-value: 1.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563   5 LFSVFDPS--AIFGLSLNWLSTFLGLLMI----PSIYWLMPSRYNIFWNSILVTLHKEFKTLLGPSAHNGSTFIFiSLFS 78
Cdd:TIGR01131   1 LFSQFDISpiTLFSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  79 LILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIRPGTLA 158
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2062575563 159 VRLTANMIAGHLLLTLLGNTGPS-MSYMLVTFLLIGQIALLVLESAVAMIQSYVFAVLSTLYSSEVN 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 1.83e-32

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: 115.19  E-value: 1.83e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  72 IFISLFSLILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNV 151
Cdd:cd00310     7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563 152 IRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSYMLVTFLLIGQIALLVLESAVAMIQSYVFAVLSTLYSS 221
Cdd:cd00310    87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-222 1.42e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 109.65  E-value: 1.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563   1 MMTNLFSVFDPSAIFGLSLNWLSTFLGLLMIPSIYWLMP-SRYNIFWNSILVTLHKEFKTLLGPSAHNGStFIFISLFSL 79
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLnNRLSTLQSWFFGSFTFQLMQPINKKGHKWA-VLFLSLMLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  80 ILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIRPGTLAV 159
Cdd:MTH00179   80 LLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2062575563 160 RLTANMIAGHLLLTLLGNT---GPSMSYMLVTFLLIGQIALLVLESAVAMIQSYVFAVLSTLYSSE 222
Cdd:MTH00179  160 RLTANITAGHLLMHLISSAvfvLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-222 3.84e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 108.80  E-value: 3.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563   1 MMTNLFSVFDPSAIFGLSLN---WLSTFLGLLMIPSIYWLMPSRYNIFWNSILVTLHKEFKTLLGPSAHNGSTFIFiSLF 77
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFSSLSflmWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLS-SLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  78 SLILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIRPGTL 157
Cdd:MTH00173   80 LFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2062575563 158 AVRLTANMIAGHLLLTLLGNTGPS----MSYMLVTFLLIGQIALLVLESAVAMIQSYVFAVLSTLYSSE 222
Cdd:MTH00173  160 TVRLLANISAGHIVLTLIGNYLSSslfsSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-222 1.71e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 106.83  E-value: 1.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563   1 MMTNLFSVFDPSAIFGLSLNWLSTFLGLLMIPSI-YWLMPSRYNIFWNSILVTLHKEFKTLLGPSAHNGSTfIFISLFSL 79
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPkNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWAL-ILTSLMLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  80 ILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIRPGTLAV 159
Cdd:MTH00120   80 LLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563 160 RLTANMIAGH-------LLLTLLGNTGPSMSYMLVTFLLIgqiaLLVLESAVAMIQSYVFAVLSTLYSSE 222
Cdd:MTH00120  160 RLTANLTAGHlliqlisTATLNLLPTMPTLSLLTLIILLL----LTILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-222 1.56e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 104.43  E-value: 1.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563   1 MMTNLFSVFDPSAI-----FGLSLNWLSTFLGLLMIPSIYWLMPSRYNIFWNSILVTLHKEFKTLLGpSAHNGSTFIFIS 75
Cdd:MTH00005    1 MLTDIFSSFDPATNslfnnLSSTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFG-KHLKGFSSLISA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  76 LFSLILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIRPG 155
Cdd:MTH00005   80 LFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563 156 TLAVRLTANMIAGHLLLTLLGNTGPSM---SYMLVTFLLIGQIALLVLESAVAMIQSYVFAVLSTLYSSE 222
Cdd:MTH00005  160 TLSFRLAANMSAGHIVLSLIGIYAASAlfsSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 3-222 4.53e-26

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 100.82  E-value: 4.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563   3 TNLFSVFDPSAIFGLSLNWLSTFLGL---LMIPSIYWLmPSRYNIFWNSILVTLhkeFKTLLGPSAHNGSTFI--FISLF 77
Cdd:MTH00035    5 NSIFGQFSPDTILFIPLTLLSSVIALswlFFINPTNWL-PSRSQSIWLTFRQEI---LKLIFQNTNPNTAPWAglLTTVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  78 SLILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIRPGTL 157
Cdd:MTH00035   81 ILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2062575563 158 AVRLTANMIAGHLLLTLLGNT--GPSMSYMLVTFLLIGQIALLVLESAVAMIQSYVFAVLSTLYSSE 222
Cdd:MTH00035  161 GLRLAANLTAGHLLIFLLSTAiwELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-222 6.22e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 97.73  E-value: 6.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563   1 MMTNLFSVFDPSAIFGLSLNWLSTFLGLLMI--PSIYWLmPSRYNIFWNSILVTLHKEFKTLLGPSAHNGStFIFISLFS 78
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFptPTNKWL-NNRLSTLQIWFLQNFTKQLMLPLNTPGHKWA-LILTSLMV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  79 LILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIRPGTLA 158
Cdd:MTH00073   79 FLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2062575563 159 VRLTANMIAGHLLLTLLGNTGPSMSYMLVTFLLIGQIALL---VLESAVAMIQSYVFAVLSTLYSSE 222
Cdd:MTH00073  159 VRLTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFlltLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-219 1.17e-24

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 96.95  E-value: 1.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563   1 MMTNLFSVFDPSAIFGLSLNWLSTFLGLLMIPSIYWLMPSRYNIF--WNSILVTlhkefKTLLGPSAHNGSTFIFIsLFS 78
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIqqWLIQLTS-----KQMMTIHNTKGQTWSLM-LMS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  79 LILF---NNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIRPG 155
Cdd:MTH00101   75 LILFigsTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPM 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2062575563 156 TLAVRLTANMIAGHLLLTLLGN-----TGPSMSYMLVTFLLIgqIALLVLESAVAMIQSYVFAVLSTLY 219
Cdd:MTH00101  155 ALAVRLTANITAGHLLIHLIGGatlalMSISTTTALITFIIL--ILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-222 3.16e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 88.01  E-value: 3.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563   1 MMTNLFSVFDPSAIFGLSLNWLStflglLMIPSIywLMPSRYNIFWNSILVTLHKEF-----KTLLGPSAHNGSTF--IF 73
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALA-----LTLPWI--LFPTPTSRWLNNRLLTLQGWFinrftQQLLLPLNVGGHKWalLL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  74 ISLFSLILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIR 153
Cdd:MTH00132   74 TSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2062575563 154 PGTLAVRLTANMIAGHLLLTLLGNTGPSMSYMLVTFLLIGQIALL---VLESAVAMIQSYVFAVLSTLYSSE 222
Cdd:MTH00132  154 PLALGVRLTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFlltLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 1-219 3.84e-19

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 82.40  E-value: 3.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563   1 MMTNLFSVFDPSAIFGL---SLNWLSTFLGLLMIPSIYWLMPSRYNIFWNSILVTLHKEFKTLLGPSAHNGSTFIfISLF 77
Cdd:MTH00172    1 MSSSYFDQFNIVWLIGLtnsSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFI-ISLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  78 SLILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIRPGTL 157
Cdd:MTH00172   80 FFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2062575563 158 AVRLTANMIAGHLLLTLLGNTGPSM---SYMLVTFLLIGQIALLVLESAVAMIQSYVFAVLSTLY 219
Cdd:MTH00172  160 GVRLAANLSAGHLLFAILAGFGFNMlcaSGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIY 224
ATP-synt_A pfam00119
ATP synthase A chain;
21-221 8.68e-19

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 81.00  E-value: 8.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  21 WLSTFLGLLMIPSIYW----LMPSRYNIFWNSILVTLHKEFKTLLGPSAHNGSTFIFISLFSLILFNNFMGLF---PYIF 93
Cdd:pfam00119   5 LIVALILLLFLLLATRktkkLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  94 TSTSHLTLTLTLALPLWLSFMMYGWINH-TQHMFAHLVPQGTPAILMPFMVCIETISNVIRPGTLAVRLTANMIAGH--- 169
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHlll 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2062575563 170 LLLTLLGNTGPSMSYMLVTFLLIGQIALLVLESAVAMIQSYVFAVLSTLYSS 221
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 36-219 4.18e-16

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 74.27  E-value: 4.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  36 WLMPSRYNIFWNSILVTLHKEFKTLLGPSAHNGSTFIFiSLFSLILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMM 115
Cdd:MTH00175   50 KLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFIL-SLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563 116 YGWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSYMLVTFLLIGQI 195
Cdd:MTH00175  129 LGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNGLIILSLFPM 208

                         170       180
                  ....*....|....*....|....*...
gi 2062575563 196 ALLV----LESAVAMIQSYVFAVLSTLY 219
Cdd:MTH00175  209 LIMIfitlLEMAVAVIQAYVFCLLTTIY 236
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 37-219 1.86e-13

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: 66.64  E-value: 1.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  37 LMPSRYNIFWNSILVTLHKEFKTLLGPSAHNGSTFIFiSLFSLILFNNFMGLFPYIF-----TSTSHLTLTLTLALPLWL 111
Cdd:COG0356    26 LVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLL-TLFLFILVSNLLGLIPGLFpptadINVTLALALIVFVLVHYY 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563 112 SFMMYGWINHTQHMFAHLVPqgtpaILMPFMVCIETISNVIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSYMLVTFLL 191
Cdd:COG0356   105 GIKKKGLGGYLKHLFFPPFP-----WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL 179

                         170       180
                  ....*....|....*....|....*...
gi 2062575563 192 igQIALLVLESAVAMIQSYVFAVLSTLY 219
Cdd:COG0356   180 --PVAWTAFELLVGFLQAYIFTMLTAVY 205
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 37-219 1.51e-12

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 64.96  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  37 LMPSRYNIFWNSILVTLHKEFKTLLGPSAHNGSTFIfISLFSLILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMY 116
Cdd:MTH00174   59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFV-LSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563 117 GWINHTQHMFAHLVPQGTPAILMPFMVCIETISNVIRPGTLAVRLTANMIAGHLLLTLLGNTGPSmsyMLVTFLLIGQ-- 194
Cdd:MTH00174  138 GLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWK---MINTGILIGSfv 214

                         170       180       190
                  ....*....|....*....|....*....|
gi 2062575563 195 -----IALLVLESAVAMIQSYVFAVLSTLY 219
Cdd:MTH00174  215 pfailIFVTILEMAVAIIQAYVFTLLTIVY 244
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 72-219 3.14e-09

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 55.19  E-value: 3.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  72 IFISLFSLILFNNFMGLFPYIFT------STSHLTLTLTLALPLWLSFMMYGWINHTQHMFAHLvpqgtpailMPFMVCI 145
Cdd:PRK05815   75 LAFTLFLFILLMNLLGLIPYLLFpptadiNVTLALALIVFVLVIYYGIKKKGLGGYLKEFYLQP---------HPLLLPI 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2062575563 146 ETISNVIRPGTLAVRLTANMIAGHLLLTLLGNTGPSMSYMLVTFLLIGqIALLVLESAVAMIQSYVFAVLSTLY 219
Cdd:PRK05815  146 EIISEFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILP-VAWTIFEIFVGTLQAYIFMMLTIVY 218
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 127-219 4.65e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 49.50  E-value: 4.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563 127 AHLVPQGTPAILMPFMVCIETI-SNVIRPGTLAVRLTANMIAGHLLLT-LLGNTGPSMSYMLVTFLLIGQIALLVLESAV 204
Cdd:PRK13417  250 WHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVIILaLMGFIFQFQSWGIVPVSVIGSGLIYVLEIFV 329

                          90
                  ....*....|....*
gi 2062575563 205 AMIQSYVFAVLSTLY 219
Cdd:PRK13417  330 AFLQAYIFVLLTSLF 344
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 126-219 3.70e-05

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 43.58  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563 126 FAHLVpQGTPAILMPFMVCIETISNVIRPGTLAVRLTANMIAGHLLLtllgntgpsMSYMLVTFLLIGQIALLV------ 199
Cdd:PRK13419  228 LAHLT-GGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAGHIVI---------LSLIFISFILKSYIVAVAvsvpfa 297

                          90       100
                  ....*....|....*....|....*
gi 2062575563 200 -----LESAVAMIQSYVFAVLSTLY 219
Cdd:PRK13419  298 ifiylLELFVAFLQAYIFTMLSALF 322
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 69-222 9.22e-04

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 38.81  E-value: 9.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062575563  69 STFIFISLFSLILFNNFMGLFPYIFTSTSHLTLTLTLALPLWLSFMMYGWINhtQHMFAHLVPQGTPAILMPF-MVCIET 147
Cdd:MTH00087   51 SSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSK--SEKFSVYLSKGSDSFLKTFsMLFVEI 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2062575563 148 ISNVIRPGTLAVRLTANMIAGHLLLTLLGntgpSMSYMLVTFLLIgqiaLLVLESAVAMIQSYVFAVLSTLYSSE 222
Cdd:MTH00087  129 VSELSRPLALTLRLTVNLMVGHLISSLLN----FLGEKYVWLSIL----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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