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Conserved domains on  [gi|2267399882|gb|UTE83116|]
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ATP synthase F0 subunit 6 (mitochondrion) [Propithecus deckenii coronatus]

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 3.81e-130

ATP synthase F0 subunit 6; Validated


:

Pssm-ID: 177163  Cd Length: 226  Bit Score: 365.81  E-value: 3.81e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882   1 MNENLFASFITPTIVGIPIVILIIAIPSILFPSPTRLITSRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2267399882 161 TANITAGHLLMHLIGGATLVLTSISPTTASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 3.81e-130

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 365.81  E-value: 3.81e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882   1 MNENLFASFITPTIVGIPIVILIIAIPSILFPSPTRLITSRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2267399882 161 TANITAGHLLMHLIGGATLVLTSISPTTASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 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 1.34e-52

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: 169.31  E-value: 1.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  29 ILFPSPTRLITSRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL 108
Cdd:TIGR01131  31 ISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882 109 WAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPtt 188
Cdd:TIGR01131 111 WLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSLMSSAI-- 188

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2267399882 189 ASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDN 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 9.29e-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: 139.07  E-value: 9.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  65 GRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2267399882 145 ETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISpttASITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSV---GLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
35-223 9.87e-39

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 133.38  E-value: 9.87e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  35 TRLITSRLTSLQQWLIQLVLKQLM-MMHSIKGRTWSLMLISLILFIGSTNLLGLL---PHSFTPTTQLSMNLGMAIPLWA 110
Cdd:pfam00119  23 KKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882 111 AAVITGFR-HKTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPTTA 189
Cdd:pfam00119 103 LVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLG 182

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2267399882 190 SITFIILTLLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 183 VIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 64-224 2.97e-26

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: 100.92  E-value: 2.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  64 KGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHK-TKMSLAHLLPQGTPvLLIPMLV 142
Cdd:COG0356    53 KGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLML 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882 143 IIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSispttASITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:COG0356   132 PIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206


                  ..
gi 2267399882 223 HD 224
Cdd:COG0356   207 SL 208
 
Name Accession Description Interval E-value
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 3.81e-130

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 365.81  E-value: 3.81e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882   1 MNENLFASFITPTIVGIPIVILIIAIPSILFPSPTRLITSRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIG 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00101   81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2267399882 161 TANITAGHLLMHLIGGATLVLTSISPTTASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101  161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-226 1.60e-83

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 247.82  E-value: 1.60e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882   1 MNENLFASFITPTIVGIPIVILIIAIPSILFPSPT-RLITSRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFI 79
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKnRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2267399882 160 LTANITAGHLLMHLIGGATLVLTSISPTTASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-226 1.06e-81

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 243.34  E-value: 1.06e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882   1 MNENLFASFITPTIVGIPIVILIIAIPSILFPSPT-RLITSRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFI 79
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTnKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2267399882 160 LTANITAGHLLMHLIGGATLVLTSISPTTASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-225 9.31e-81

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 240.93  E-value: 9.31e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882   1 MNENLFASFITPTIVGIPIVILIIAIPSILFPSPT-RLITSRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFI 79
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTsRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2267399882 160 LTANITAGHLLMHLIGGATLVLTSISPTTASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-226 1.63e-68

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 209.80  E-value: 1.63e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882   1 MNENLFASFITPTIVGIPIVILIIAIPSILFPSPT-RLITSRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFI 79
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTnRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALAVR 159
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2267399882 160 LTANITAGHLLMHLIGGATLVLTSISPTTASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 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 1.34e-52

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: 169.31  E-value: 1.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  29 ILFPSPTRLITSRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL 108
Cdd:TIGR01131  31 ISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882 109 WAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPtt 188
Cdd:TIGR01131 111 WLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSLMSSAI-- 188

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2267399882 189 ASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 189 FALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-221 3.02e-49

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 160.33  E-value: 3.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882   1 MNENLFASFITPTIVGIPIVILIIAIPSILFPSPTRLITSRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIG 80
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALAVRL 160
Cdd:MTH00157   81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2267399882 161 TANITAGHLLMHLIGGatlVLTSISPTTASITFIILTLLTILEFAVALIQAYVFTLLVSLY 221
Cdd:MTH00157  161 AANMIAGHLLLTLLGN---TGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLY 218
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 29-225 7.65e-49

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 159.75  E-value: 7.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  29 ILFPSPTRLITSRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL 108
Cdd:MTH00035   33 LFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILILSINVLGLFPYAFTSTSHISLTYSLGIPL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882 109 WAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSiSPTT 188
Cdd:MTH00035  113 WMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRLAANLTAGHLLIFLLSTAIWELSN-SPLI 191

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2267399882 189 ASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDN 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 9.29e-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: 139.07  E-value: 9.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  65 GRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVII 144
Cdd:cd00310     1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2267399882 145 ETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISpttASITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310    81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSV---GLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 29-224 5.47e-41

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 139.62  E-value: 5.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  29 ILFPSPTRLITSRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL 108
Cdd:MTH00173   32 FFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSLALPL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882 109 WAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGA-TLVLTSISPT 187
Cdd:MTH00173  112 WLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYlSSSLFSSSVV 191

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2267399882 188 TASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00173  192 SLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 3.45e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 134.78  E-value: 3.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882   1 MNENLFASFITPTIV---GIPIVILIIAIPSILFPSPTRLITSRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLIL 77
Cdd:MTH00176    1 MLVDLFSSFDPPNKNifsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  78 FIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALA 157
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2267399882 158 VRLTANITAGHLLMHLIGGATLVLTSISPTTASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP-synt_A pfam00119
ATP synthase A chain;
35-223 9.87e-39

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 133.38  E-value: 9.87e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  35 TRLITSRLTSLQQWLIQLVLKQLM-MMHSIKGRTWSLMLISLILFIGSTNLLGLL---PHSFTPTTQLSMNLGMAIPLWA 110
Cdd:pfam00119  23 KKLVPGRLQNFVEMLVEFVDNIVKdNIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882 111 AAVITGFR-HKTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPTTA 189
Cdd:pfam00119 103 LVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLG 182

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2267399882 190 SITFIILTLLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 183 VIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 40-226 6.06e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 113.67  E-value: 6.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  40 SRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRH 119
Cdd:MTH00005   45 NRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTF 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882 120 KTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPTTASITFIILTLL 199
Cdd:MTH00005  125 SPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGIYAASALFSSISSTILLILTQMGY 204

                         170       180
                  ....*....|....*....|....*..
gi 2267399882 200 TILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00005  205 ILFEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 29-224 2.81e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 111.67  E-value: 2.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  29 ILFPSPTRLITSRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL 108
Cdd:MTH00172   32 LLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSI 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882 109 WAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPTT 188
Cdd:MTH00172  112 IIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNMLCASGFL 191

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2267399882 189 ASITFIILTLLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00172  192 SLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 63-224 1.20e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 105.09  E-value: 1.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  63 IKGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLV 142
Cdd:MTH00175   77 KSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLV 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882 143 IIETISLFIQPMALAVRLTANITAGHLLMHLIGGATL-VLTSISPTTASITFIILTLLTILEFAVALIQAYVFTLLVSLY 221
Cdd:MTH00175  157 LIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFnMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIY 236


                  ...
gi 2267399882 222 LHD 224
Cdd:MTH00175  237 LGD 239
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 64-224 2.97e-26

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: 100.92  E-value: 2.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  64 KGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHK-TKMSLAHLLPQGTPvLLIPMLV 142
Cdd:COG0356    53 KGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLML 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882 143 IIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSispttASITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:COG0356   132 PIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206


                  ..
gi 2267399882 223 HD 224
Cdd:COG0356   207 SL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 35-224 5.42e-21

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 87.16  E-value: 5.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  35 TRLITSRLTSLQQWLIQLVLKQLMMMHSIKGRTWSLMLISLILFIGSTNLLGLLP-HSFTPTTQLSMNLGMAIPLWAAAV 113
Cdd:PRK05815   39 LSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVI 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882 114 ITGFR-HKTKMSLAHLLPQGTPVLLIpmlviIETISLFIQPMALAVRLTANITAGHLLMHLIGGatlvLTSISPTTASIT 192
Cdd:PRK05815  119 YYGIKkKGLGGYLKEFYLQPHPLLLP-----IEIISEFSRPISLSLRLFGNMLAGELILALIAL----LGGAGLLLALAP 189

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2267399882 193 FIILTLLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:PRK05815  190 LILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 64-224 5.68e-20

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 84.99  E-value: 5.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  64 KGRTWSLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVI 143
Cdd:MTH00174   86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882 144 IETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLTSISPTTAS-ITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00174  166 IETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSfVPFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245


                  ..
gi 2267399882 223 HD 224
Cdd:MTH00174  246 RD 247
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 72-222 5.60e-18

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 80.94  E-value: 5.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  72 LISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFR-HKTKMSLAHLlPQGTPVLLIPMLVIIETISLF 150
Cdd:PRK13419  174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAHL-TGGTHWSLWIIMIPIEFIGLF 252

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2267399882 151 IQPMALAVRLTANITAGHL-LMHLIGGATLVLTSISPTTASITFIILTLLtiLEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13419  253 TKPFALTVRLFANMTAGHIvILSLIFISFILKSYIVAVAVSVPFAIFIYL--LELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 71-222 1.07e-11

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 61.53  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  71 MLISLILFigstNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSlaHLLPQGTPVLLIPM-LVIIETISL 149
Cdd:MTH00087   58 TFIVLLLF----CFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTFsMLFVEIVSE 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2267399882 150 FIQPMALAVRLTANITAGHLLMHLIggatlvltsispTTASITFIILTLLTIL-EFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00087  132 LSRPLALTLRLTVNLMVGHLISSLL------------NFLGEKYVWLSILAIMmECFVAFIQSYIFSRLIYLYL 193
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 93-222 5.71e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 57.98  E-value: 5.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  93 TPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVLLIPMLVIIETI-SLFIQPMALAVRLTANITAGHLLM 171
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2267399882 172 HLIGGatLVLTSISPTTASITFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13417  297 LALMG--FIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 74-222 4.07e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 37.41  E-value: 4.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2267399882  74 SLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKTKMSLAHLLPQGTPVLLiPMLVIIEtislFIQP 153
Cdd:PRK13420   80 TLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEGLREYLKHYLSPSPFLL-PFHLISE----ITRT 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2267399882 154 MALAVRLTANITAghllMHLIGGATLVLTSispttasitFIILTLLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13420  155 LALAVRLFGNIMS----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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