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Conserved domains on  [gi|2052620755|gb|QWQ55655|]
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ATP synthase F0 subunit 6 (mitochondrion) [Zichya tenggerensis]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009593)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 4.82e-98

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 284.37  E-value: 4.82e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755   1 MMNNLFSIFDPTTSiMNFSFNWLSTFLGLLLLPTLYWLIPTRMTTVWNSIINTLHTEFKILIGPtSHNGSTLIFIALFSM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGP-KNKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  81 ILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIETISNLIRPGTLAV 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2052620755 161 RLAANMIAGHLLLTLLGNTGSSLVLSTLSLLVIAQMLLMLLESAVAIIQSYVFAILATLYSSEVN 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 4.82e-98

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 284.37  E-value: 4.82e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755   1 MMNNLFSIFDPTTSiMNFSFNWLSTFLGLLLLPTLYWLIPTRMTTVWNSIINTLHTEFKILIGPtSHNGSTLIFIALFSM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGP-KNKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  81 ILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIETISNLIRPGTLAV 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2052620755 161 RLAANMIAGHLLLTLLGNTGSSLVLSTLSLLVIAQMLLMLLESAVAIIQSYVFAILATLYSSEVN 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-225 1.26e-47

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: 156.21  E-value: 1.26e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755   5 LFSIFDPTTSIM-NFSFNWLSTFLGLLLLPTLYWL----IPTRMTTVWNSIINTLHTEFKILIGPTSHNgSTLIFIALFS 79
Cdd:TIGR01131   1 LFSQFDISPITLfSLTLLSLILLLSLLIFLISSSLsrwlIPSRWQNLMESIYEFVLSIVKSQIGGKKGK-FFPLIFTLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  80 MILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIETISNLIRPGTLA 159
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2052620755 160 VRLAANMIAGHLLLTLLGNTGSSLVLSTLSLLVIA-QMLLMLLESAVAIIQSYVFAILATLYSSEVN 225
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFSLMSSAIFALLLLiLVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 69-222 3.78e-42

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: 139.84  E-value: 3.78e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  69 GSTLIFIALFSMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIET 148
Cdd:cd00310     3 KYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIEL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2052620755 149 ISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGSSLVLSTLSLLVIAQMLLMLLESAVAIIQSYVFAILATLYSS 222
Cdd:cd00310    83 ISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
39-222 6.53e-28

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 105.26  E-value: 6.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  39 IPTRMTTVWNSIINTLHTEFKILIGPTSHNGSTLIFIALFSMILFNNFLGLF---PYIFTSSSHLTFTLTLALPLWLSFM 115
Cdd:pfam00119  26 VPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVH 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755 116 IYGWFNH-TTHMFAHMVPQGTPPILMPFMVCIETISNLIRPGTLAVRLAANMIAGH---LLLTLLGNTGSSLVLSTLSLL 191
Cdd:pfam00119 106 YYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHlllLLLAGLIFALLSAGFLLGVIP 185

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2052620755 192 VIAQMLLMLLESAVAIIQSYVFAILATLYSS 222
Cdd:pfam00119 186 PLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 39-220 1.29e-22

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: 91.29  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  39 IPTRMTTVWNSIINTLHTEFKILIGPTSHNGSTLIFiALFSMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYG 118
Cdd:COG0356    27 VPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLL-TLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755 119 WFNH-TTHMFAHMVPQGTPPiLMPFMVCIETISNLIRPGTLAVRLAANMIAGHLLLTLLgnTGSSLVLSTLSLLVIAQML 197
Cdd:COG0356   106 IKKKgLGGYLKHLFFPPFPW-LAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLL--AGLAPFLLLGVLSLLLPVA 182

                         170       180
                  ....*....|....*....|...
gi 2052620755 198 LMLLESAVAIIQSYVFAILATLY 220
Cdd:COG0356   183 WTAFELLVGFLQAYIFTMLTAVY 205
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 4.82e-98

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 284.37  E-value: 4.82e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755   1 MMNNLFSIFDPTTSiMNFSFNWLSTFLGLLLLPTLYWLIPTRMTTVWNSIINTLHTEFKILIGPtSHNGSTLIFIALFSM 80
Cdd:MTH00157    1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGP-KNKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  81 ILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIETISNLIRPGTLAV 160
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2052620755 161 RLAANMIAGHLLLTLLGNTGSSLVLSTLSLLVIAQMLLMLLESAVAIIQSYVFAILATLYSSEVN 225
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-225 1.26e-47

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: 156.21  E-value: 1.26e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755   5 LFSIFDPTTSIM-NFSFNWLSTFLGLLLLPTLYWL----IPTRMTTVWNSIINTLHTEFKILIGPTSHNgSTLIFIALFS 79
Cdd:TIGR01131   1 LFSQFDISPITLfSLTLLSLILLLSLLIFLISSSLsrwlIPSRWQNLMESIYEFVLSIVKSQIGGKKGK-FFPLIFTLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  80 MILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIETISNLIRPGTLA 159
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2052620755 160 VRLAANMIAGHLLLTLLGNTGSSLVLSTLSLLVIA-QMLLMLLESAVAIIQSYVFAILATLYSSEVN 225
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFSLMSSAIFALLLLiLVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-224 7.52e-47

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 154.42  E-value: 7.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755   1 MMNNLFSIFDP--TTSIMNFSFNWLSTFLGLLLLPTLYWLIPTRMTTVWNsIINTLHTEFKILIGPTSHNGSTLIFIALF 78
Cdd:MTH00176    1 MLVDLFSSFDPpnKNIFSMISLSWITLLLFLLLMPSSVWFCPSKLQVFML-MFSTFLPEMILRSNGSYILGSASIIISLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  79 SMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIETISNLIRPGTL 158
Cdd:MTH00176   80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2052620755 159 AVRLAANMIAGHLLLTLLGNTGSSLVLS---TLSLLVIAQMLLMLLESAVAIIQSYVFAILATLYSSEV 224
Cdd:MTH00176  160 AVRLAANLSAGHLLLGLLGAAMWGLLPVsplIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 69-222 3.78e-42

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: 139.84  E-value: 3.78e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  69 GSTLIFIALFSMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIET 148
Cdd:cd00310     3 KYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIEL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2052620755 149 ISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGSSLVLSTLSLLVIAQMLLMLLESAVAIIQSYVFAILATLYSS 222
Cdd:cd00310    83 ISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-223 2.78e-37

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 129.85  E-value: 2.78e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755   1 MMNNLFSIFDPTTSIMNFSFN----WLSTFLGLLLLPTLYWLIPTRMTTVWNSIINTLHTEFKILIGpTSHNGSTLIFIA 76
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFNNLSstafWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFG-KHLKGFSSLISA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  77 LFSMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIETISNLIRPG 156
Cdd:MTH00005   80 LFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755 157 TLAVRLAANMIAGHLLLTLLG---NTGSSLVLSTLSLLVIAQMLLMLLESAVAIIQSYVFAILATLYSSE 223
Cdd:MTH00005  160 TLSFRLAANMSAGHIVLSLIGiyaASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-223 4.26e-36

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 126.60  E-value: 4.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755   1 MMNNLFSIFDpTTSIMNFSFNWLSTFLG-LLLLPTLYWLIPTRMTTVWNSIINTLHTEFKILIGPTSHNGStLIFIALFS 79
Cdd:MTH00179    1 MMLSMFDQFE-SPSLLGIPLLALALLLPwLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWA-VLFLSLML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  80 MILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIETISNLIRPGTLA 159
Cdd:MTH00179   79 FLLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2052620755 160 VRLAANMIAGHLLLTLLGNTGSSLVLSTLSLLVIAQ---MLLMLLESAVAIIQSYVFAILATLYSSE 223
Cdd:MTH00179  159 VRLTANITAGHLLMHLISSAVFVLMNFMGMVALLTLlvlFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 42-223 4.45e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 124.17  E-value: 4.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  42 RMTTVWNSIINTLHTEFKILIGPTSHNGStLIFIALFSMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFN 121
Cdd:MTH00120   42 RLTTLQLWLIKLITKQLMLPLNKKGHKWA-LILTSLMLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRN 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755 122 HTTHMFAHMVPQGTPPILMPFMVCIETISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGSSLVLSTLSLLVIAQ---MLL 198
Cdd:MTH00120  121 QPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVRLTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLiilLLL 200

                         170       180
                  ....*....|....*....|....*
gi 2052620755 199 MLLESAVAIIQSYVFAILATLYSSE 223
Cdd:MTH00120  201 TILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-223 6.97e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 123.82  E-value: 6.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755   1 MMNNLFSIFDPTTSIM--NFSFNWLSTFLGLLLLPTLYWLIPTRMTTVWNSIINTLHTEFKILIGpTSHNGSTLIFIALF 78
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFssLSFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSG-LNLGGFSLLLSSLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  79 SMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIETISNLIRPGTL 158
Cdd:MTH00173   80 LFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2052620755 159 AVRLAANMIAGHLLLTLLGNTGSSLV----LSTLSLLVIAQMLLMLLESAVAIIQSYVFAILATLYSSE 223
Cdd:MTH00173  160 TVRLLANISAGHIVLTLIGNYLSSSLfsssVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 3-223 1.52e-32

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 117.77  E-value: 1.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755   3 NNLFSIFDPTTsIMNFSFNWLSTFLGLLLLPTLYWL--IPTRMTTVWNSIINTLhteFKILIGPTSHNGS--TLIFIALF 78
Cdd:MTH00035    5 NSIFGQFSPDT-ILFIPLTLLSSVIALSWLFFINPTnwLPSRSQSIWLTFRQEI---LKLIFQNTNPNTApwAGLLTTVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  79 SMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIETISNLIRPGTL 158
Cdd:MTH00035   81 ILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2052620755 159 AVRLAANMIAGHLLLTLLGNT--GSSLVLSTLSLLVIAQMLLMLLESAVAIIQSYVFAILATLYSSE 223
Cdd:MTH00035  161 GLRLAANLTAGHLLIFLLSTAiwELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 72-223 3.64e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 113.81  E-value: 3.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  72 LIFIALFSMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIETISN 151
Cdd:MTH00132   71 LLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISL 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2052620755 152 LIRPGTLAVRLAANMIAGHLLLTLLGNTGSSLVLSTLSLLVIAQMLLML---LESAVAIIQSYVFAILATLYSSE 223
Cdd:MTH00132  151 FIRPLALGVRLTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLltlLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 54-223 1.10e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 110.06  E-value: 1.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  54 LHTEFKILIGPTSHNGS--TLIFIALFSMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMV 131
Cdd:MTH00073   51 LQNFTKQLMLPLNTPGHkwALILTSLMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755 132 PQGTPPILMPFMVCIETISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGSSLVLSTLSLLVIAQM---LLMLLESAVAII 208
Cdd:MTH00073  131 PEGTPTLLIPILIIIETISLFIRPLALGVRLTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIvlfLLTLLEIAVAMI 210

                         170
                  ....*....|....*
gi 2052620755 209 QSYVFAILATLYSSE 223
Cdd:MTH00073  211 QAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 71-220 5.99e-29

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 108.12  E-value: 5.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  71 TLIFIALFSMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIETIS 150
Cdd:MTH00101   69 SLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETIS 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2052620755 151 NLIRPGTLAVRLAANMIAGHLLLTLLGNTGSSLVLSTLSLLVIAQMLLML---LESAVAIIQSYVFAILATLY 220
Cdd:MTH00101  149 LFIQPMALAVRLTANITAGHLLIHLIGGATLALMSISTTTALITFIILILltiLEFAVALIQAYVFTLLVSLY 221
ATP-synt_A pfam00119
ATP synthase A chain;
39-222 6.53e-28

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 105.26  E-value: 6.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  39 IPTRMTTVWNSIINTLHTEFKILIGPTSHNGSTLIFIALFSMILFNNFLGLF---PYIFTSSSHLTFTLTLALPLWLSFM 115
Cdd:pfam00119  26 VPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVH 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755 116 IYGWFNH-TTHMFAHMVPQGTPPILMPFMVCIETISNLIRPGTLAVRLAANMIAGH---LLLTLLGNTGSSLVLSTLSLL 191
Cdd:pfam00119 106 YYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHlllLLLAGLIFALLSAGFLLGVIP 185

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2052620755 192 VIAQMLLMLLESAVAIIQSYVFAILATLYSS 222
Cdd:pfam00119 186 PLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 39-220 8.52e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 97.42  E-value: 8.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  39 IPTRMTTVWNSIINTLHTEFKILIGPTSHNGSTLIfIALFSMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYG 118
Cdd:MTH00172   41 IPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFI-ISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAG 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755 119 WFNHTTHMFAHMVPQGTPPILMPFMVCIETISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGSSLVLSTLSLLVIAQMLL 198
Cdd:MTH00172  120 FWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIM 199

                         170       180
                  ....*....|....*....|....*
gi 2052620755 199 M---LLESAVAIIQSYVFAILATLY 220
Cdd:MTH00172  200 VfitLLEIAVAVIQAYVFCLLTTIY 224
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 39-220 1.29e-22

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: 91.29  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  39 IPTRMTTVWNSIINTLHTEFKILIGPTSHNGSTLIFiALFSMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYG 118
Cdd:COG0356    27 VPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLL-TLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755 119 WFNH-TTHMFAHMVPQGTPPiLMPFMVCIETISNLIRPGTLAVRLAANMIAGHLLLTLLgnTGSSLVLSTLSLLVIAQML 197
Cdd:COG0356   106 IKKKgLGGYLKHLFFPPFPW-LAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLL--AGLAPFLLLGVLSLLLPVA 182

                         170       180
                  ....*....|....*....|...
gi 2052620755 198 LMLLESAVAIIQSYVFAILATLY 220
Cdd:COG0356   183 WTAFELLVGFLQAYIFTMLTAVY 205
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 75-220 3.83e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 88.14  E-value: 3.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  75 IALFSMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIETISNLIR 154
Cdd:MTH00175   87 LSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIR 166

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755 155 PGTLAVRLAANMIAGHLLLTLLGNTGSSLVLSTLSLLVIAQMLLM----LLESAVAIIQSYVFAILATLY 220
Cdd:MTH00175  167 AISLGVRLAANISAGHLLFAILSGFAFNMLSNGLIILSLFPMLIMifitLLEMAVAVIQAYVFCLLTTIY 236
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 39-220 5.21e-17

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 76.76  E-value: 5.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  39 IPTRMTTVWNSIINTLHTEFKILIGPTSHNGSTLIFiALFSMILFNNFLGLFP-YIFTSSSHLTFTLTLALPLWLSFMIY 117
Cdd:PRK05815   42 VPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAF-TLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYY 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755 118 G-WFNHTTHMFAHMVPQgtppiLMPFMVCIETISNLIRPGTLAVRLAANMIAGHLLLTLLGnTGSSLVLSTLSLLVIAQM 196
Cdd:PRK05815  121 GiKKKGLGGYLKEFYLQ-----PHPLLLPIEIISEFSRPISLSLRLFGNMLAGELILALIA-LLGGAGLLLALAPLILPV 194

                         170       180
                  ....*....|....*....|....
gi 2052620755 197 LLMLLESAVAIIQSYVFAILATLY 220
Cdd:PRK05815  195 AWTIFEIFVGTLQAYIFMMLTIVY 218
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 39-220 3.76e-15

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 71.89  E-value: 3.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  39 IPTRMTTVWNSIINTLHTEFKILIGPTSHNGSTLIfIALFSMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYG 118
Cdd:MTH00174   60 VPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFV-LSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAG 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755 119 WFNHTTHMFAHMVPQGTPPILMPFMVCIETISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGSSLVLSTLSLLVIAQMLL 198
Cdd:MTH00174  139 LITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSFVPFAI 218

                         170       180
                  ....*....|....*....|....*.
gi 2052620755 199 M----LLESAVAIIQSYVFAILATLY 220
Cdd:MTH00174  219 LifvtILEMAVAIIQAYVFTLLTIVY 244
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 75-220 9.35e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 57.45  E-value: 9.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  75 IALFSMILFNNFLGLFPYIFTSSSHLTFTLTLALplwLSFMIYGWFNHTTH----MFAHMVpQGTPPILMPFMVCIETIS 150
Cdd:PRK13419  175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLAV---FTFFITQYAAIKAHgikgYLAHLT-GGTHWSLWIIMIPIEFIG 250

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2052620755 151 NLIRPGTLAVRLAANMIAGHLLLTLLGNTGSSLVLSTLSLLVIAQMLLM--LLESAVAIIQSYVFAILATLY 220
Cdd:PRK13419  251 LFTKPFALTVRLFANMTAGHIVILSLIFISFILKSYIVAVAVSVPFAIFiyLLELFVAFLQAYIFTMLSALF 322
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 70-223 5.25e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 51.13  E-value: 5.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  70 STLIFIALFSMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNhtTHMFAHMVPQGTPPILMPF-MVCIET 148
Cdd:MTH00087   51 SSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSK--SEKFSVYLSKGSDSFLKTFsMLFVEI 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2052620755 149 ISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGSSLVLSTlsllviaqMLLMLLESAVAIIQSYVFAILATLYSSE 223
Cdd:MTH00087  129 VSELSRPLALTLRLTVNLMVGHLISSLLNFLGEKYVWLS--------ILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 95-220 2.08e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 47.58  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  95 TSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIETI-SNLIRPGTLAVRLAANMIAGHLLL 173
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2052620755 174 T-LLGNTGSSLVLSTLSLLVIAQMLLMLLESAVAIIQSYVFAILATLY 220
Cdd:PRK13417  297 LaLMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 80-169 8.13e-06

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 44.49  E-value: 8.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  80 MILFNNFLGL-FPYIFTSSSHLTFTLTLALPLWLSFMIYGWFNHTTHMFAHMVPQGTPPILMPFMVCIETISNLIRPGTL 158
Cdd:MTH00050   31 FIVLFLFLLYrLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVL 110

                          90
                  ....*....|.
gi 2052620755 159 AVRLAANMIAG 169
Cdd:MTH00050  111 ILRPFINISLG 121
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 40-220 2.81e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 40.88  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755  40 PTRMTTVWNSIINTLHTEFKILIgpTSHNGSTLIFIA-LFSMILFNNFLGLFPYIFTSSSHLTFTLTLALPLWLSFMIYG 118
Cdd:PRK13420   45 PGRFQVALEGVVSTIEDAIKEVL--PRHARLVLPFVGtLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052620755 119 -----WFNHTTHmfaHMVPQgtpPILMPFMVcietISNLIRPGTLAVRLAANMIAGHLlltllgnTGSSLVLSTLSLLVI 193
Cdd:PRK13420  123 iraegLREYLKH---YLSPS---PFLLPFHL----ISEITRTLALAVRLFGNIMSLEL-------AALLVLLVAGFLVPV 185

                         170       180
                  ....*....|....*....|....*..
gi 2052620755 194 AQMLLMLLEsavAIIQSYVFAILATLY 220
Cdd:PRK13420  186 PILMLHIIE---ALVQAYIFGMLALIY 209
 
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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