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Conserved domains on  [gi|2267398510|gb|UTE81842|]
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ATP synthase F0 subunit 6 (mitochondrion) [Propithecus edwardsi]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009564)

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 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 4.08e-133

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 373.52  E-value: 4.08e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510   1 MNENLFASFITPTIVGIPIVILIIAIPSILFPSPTRLISNRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2267398510 161 TANITAGHLLMHLIGGATLVLTSISPTTASITFTILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 4.08e-133

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 373.52  E-value: 4.08e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510   1 MNENLFASFITPTIVGIPIVILIIAIPSILFPSPTRLISNRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2267398510 161 TANITAGHLLMHLIGGATLVLTSISPTTASITFTILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
29-225 2.27e-54

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: 173.55  E-value: 2.27e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  29 ILFPSPTRLISNRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL 108
Cdd:TIGR01131  31 ISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510 109 WAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPtt 188
Cdd:TIGR01131 111 WLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSLMSSAI-- 188
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2267398510 189 ASITFTILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 189 FALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
65-222 1.01e-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: 141.38  E-value: 1.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  65 GRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2267398510 145 ETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISpttASITFTILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSV---GLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
35-223 1.45e-39

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 135.31  E-value: 1.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  35 TRLISNRLTSLQQWLIQLVLKQLM-MMHSIKGRTWSLMLISLILFIGSTNLLGLL---PHSFTPTTQLSMNLGMAIPLWA 110
Cdd:pfam00119  23 KKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510 111 AAVITGFR-HKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPTTA 189
Cdd:pfam00119 103 LVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLG 182
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2267398510 190 SITFTILILLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 183 VIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
64-224 9.56e-27

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: 102.07  E-value: 9.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  64 KGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHK-TKMSLAHLLPQGTPvPLIPMLV 142
Cdd:COG0356    53 KGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLML 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510 143 IIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSispttASITFTILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:COG0356   132 PIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206

                  ..
gi 2267398510 223 HD 224
Cdd:COG0356   207 SL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 4.08e-133

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 373.52  E-value: 4.08e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510   1 MNENLFASFITPTIVGIPIVILIIAIPSILFPSPTRLISNRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2267398510 161 TANITAGHLLMHLIGGATLVLTSISPTTASITFTILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
1-226 3.64e-86

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 254.36  E-value: 3.64e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510   1 MNENLFASFITPTIVGIPIVILIIAIPSILFPSPT-RLISNRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFI 79
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKnRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2267398510 160 LTANITAGHLLMHLIGGATLVLTSISPTTASITFTILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
1-226 1.40e-83

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 247.96  E-value: 1.40e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510   1 MNENLFASFITPTIVGIPIVILIIAIPSILFPSPT-RLISNRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFI 79
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTnKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2267398510 160 LTANITAGHLLMHLIGGATLVLTSISPTTASITFTILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-225 3.51e-83

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 247.09  E-value: 3.51e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510   1 MNENLFASFITPTIVGIPIVILIIAIPSILFPSPT-RLISNRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFI 79
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTsRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2267398510 160 LTANITAGHLLMHLIGGATLVLTSISPTTASITFTILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
1-226 3.37e-70

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 214.04  E-value: 3.37e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510   1 MNENLFASFITPTIVGIPIVILIIAIPSILFPSPT-RLISNRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFI 79
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTnRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2267398510 160 LTANITAGHLLMHLIGGATLVLTSISPTTASITFTILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00179  161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
29-225 2.27e-54

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: 173.55  E-value: 2.27e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  29 ILFPSPTRLISNRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL 108
Cdd:TIGR01131  31 ISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510 109 WAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPtt 188
Cdd:TIGR01131 111 WLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSLMSSAI-- 188
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2267398510 189 ASITFTILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 189 FALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
1-221 1.96e-49

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 160.72  E-value: 1.96e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510   1 MNENLFASFITPTIVGIPIVILIIAIPSILFPSPTRLISNRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIG 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2267398510 161 TANITAGHLLMHLIGGatlVLTSISPTTASITFTILILLTILEFAVALIQAYVFTLLVSLY 221
Cdd:MTH00157  161 AANMIAGHLLLTLLGN---TGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLY 218
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
29-225 2.13e-49

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 160.91  E-value: 2.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  29 ILFPSPTRLISNRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL 108
Cdd:MTH00035   33 LFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILILSINVLGLFPYAFTSTSHISLTYSLGIPL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510 109 WAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSiSPTT 188
Cdd:MTH00035  113 WMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRLAANLTAGHLLIFLLSTAIWELSN-SPLI 191
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2267398510 189 ASITFTILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00035  192 SIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
65-222 1.01e-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: 141.38  E-value: 1.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  65 GRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2267398510 145 ETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISpttASITFTILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSV---GLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
29-224 8.58e-42

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 141.54  E-value: 8.58e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  29 ILFPSPTRLISNRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL 108
Cdd:MTH00173   32 FFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSLALPL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510 109 WAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGA-TLVLTSISPT 187
Cdd:MTH00173  112 WLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYlSSSLFSSSVV 191
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2267398510 188 TASITFTILILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00173  192 SLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_A pfam00119
ATP synthase A chain;
35-223 1.45e-39

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 135.31  E-value: 1.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  35 TRLISNRLTSLQQWLIQLVLKQLM-MMHSIKGRTWSLMLISLILFIGSTNLLGLL---PHSFTPTTQLSMNLGMAIPLWA 110
Cdd:pfam00119  23 KKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510 111 AAVITGFR-HKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPTTA 189
Cdd:pfam00119 103 LVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLG 182
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2267398510 190 SITFTILILLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 183 VIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
1-226 1.34e-38

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 133.23  E-value: 1.34e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510   1 MNENLFASFITPTIV---GIPIVILIIAIPSILFPSPTRLISNRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLIL 77
Cdd:MTH00176    1 MLVDLFSSFDPPNKNifsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  78 FIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALA 157
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2267398510 158 VRLTANITAGHLLMHLIGGATLVLTSISPTTASITFTILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
40-226 5.00e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 113.67  E-value: 5.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  40 NRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRH 119
Cdd:MTH00005   45 NRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTF 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510 120 KTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPTTASITFTILILL 199
Cdd:MTH00005  125 SPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGIYAASALFSSISSTILLILTQMGY 204
                         170       180
                  ....*....|....*....|....*..
gi 2267398510 200 TILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00005  205 ILFEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
29-224 1.74e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 112.44  E-value: 1.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  29 ILFPSPTRLISNRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL 108
Cdd:MTH00172   32 LLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510 109 WAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPTT 188
Cdd:MTH00172  112 IIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNMLCASGFL 191
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2267398510 189 ASITFTILILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00172  192 SLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
36-224 2.56e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 107.01  E-value: 2.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  36 RLISNRLTSLQQwLIQLVLKQLMMMH-SIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVI 114
Cdd:MTH00175   50 KLIPNRWQSIME-LIYLNIRSVVHDNlGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510 115 TGFRHKTKMSLAHLLPQGTPVPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATL-VLTSISPTTASITF 193
Cdd:MTH00175  129 LGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFnMLSNGLIILSLFPM 208
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2267398510 194 TILILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00175  209 LIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
64-224 9.56e-27

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: 102.07  E-value: 9.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  64 KGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHK-TKMSLAHLLPQGTPvPLIPMLV 142
Cdd:COG0356    53 KGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLML 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510 143 IIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSispttASITFTILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:COG0356   132 PIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206

                  ..
gi 2267398510 223 HD 224
Cdd:COG0356   207 SL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
35-224 1.85e-21

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 88.31  E-value: 1.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  35 TRLISNRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIGSTNLLGLLP-HSFTPTTQLSMNLGMAIPLWAAAV 113
Cdd:PRK05815   39 LSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510 114 ITGFRHKtkmSLAHLLPQGTPVPlIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGatlvLTSISPTTASITF 193
Cdd:PRK05815  119 YYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGELILALIAL----LGGAGLLLALAPL 190
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2267398510 194 TILILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:PRK05815  191 ILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
64-224 4.33e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 88.07  E-value: 4.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  64 KGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVI 143
Cdd:MTH00174   86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510 144 IETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPTTAS-ITFTILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00174  166 IETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSfVPFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245

                  ..
gi 2267398510 223 HD 224
Cdd:MTH00174  246 RD 247
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
72-222 2.84e-19

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 84.79  E-value: 2.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  72 LISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFR-HKTKMSLAHLlPQGTPVPLIPMLVIIETISLF 150
Cdd:PRK13419  174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAHL-TGGTHWSLWIIMIPIEFIGLF 252
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2267398510 151 IQPMALAVRLTANITAGHL-LMHLIGGATLVLTSISPTTASITFTILILLtiLEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13419  253 TKPFALTVRLFANMTAGHIvILSLIFISFILKSYIVAVAVSVPFAIFIYL--LELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
71-222 1.81e-11

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 60.76  E-value: 1.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  71 MLISLILFigstNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSlaHLLPQGTPVPLIPM-LVIIETISL 149
Cdd:MTH00087   58 TFIVLLLF----CFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTFsMLFVEIVSE 131
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2267398510 150 FIQPMALAVRLTANITAGHLLMHLIggatlvltsispTTASITFTILILLTIL-EFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00087  132 LSRPLALTLRLTVNLMVGHLISSLL------------NFLGEKYVWLSILAIMmECFVAFIQSYIFSRLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
93-222 5.19e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 58.36  E-value: 5.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  93 TPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVPLIPMLVIIETI-SLFIQPMALAVRLTANITAGHLLM 171
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2267398510 172 HLIGGATLVLTSISPTTASITFTILILltILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13417  297 LALMGFIFQFQSWGIVPVSVIGSGLIY--VLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
74-222 2.97e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 37.80  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510  74 SLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRhkTKMSLAHLLPQGTPVP-LIPMLVIIEtislFIQ 152
Cdd:PRK13420   80 TLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIR--AEGLREYLKHYLSPSPfLLPFHLISE----ITR 153
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267398510 153 PMALAVRLTANITAghllMHLIGGATLVLTSispttasitFTILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13420  154 TLALAVRLFGNIMS----LELAALLVLLVAG---------FLVPVPILMLHIIEALVQAYIFGMLALIYI 210
 
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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