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Conserved domains on  [gi|339906577|ref|YP_004733451|]
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ATP synthase F0 subunit 6 (mitochondrion) [Auchenoglanis occidentalis]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009577)

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 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 3.39e-123

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177190  Cd Length: 227  Bit Score: 348.40  E-value: 3.39e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577   1 MALNLFDQFMSPTHLGIPLIAIALTLPWALIPSPTNRYQNNRLISLQSWFIKTFTQQLLMPLNQGGHKWAMILASLMIFI 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  81 LALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339906577 161 LTANLTAGHLLIQLISTATITLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 3.39e-123

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 348.40  E-value: 3.39e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577   1 MALNLFDQFMSPTHLGIPLIAIALTLPWALIPSPTNRYQNNRLISLQSWFIKTFTQQLLMPLNQGGHKWAMILASLMIFI 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  81 LALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339906577 161 LTANLTAGHLLIQLISTATITLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-227 3.71e-45

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: 150.05  E-value: 3.71e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577    5 LFDQFMSP----THLGIPLIAIALTLPWALIPSPTNRY-QNNRLISLQSWFIKTFTQQLLMPLNQGGHKWAMILASLMIF 79
Cdd:TIGR01131   1 LFSQFDISpitlFSLTLLSLILLLSLLIFLISSSLSRWlIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577   80 ILALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETISLFIRPLALGV 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339906577  160 RLTANLTAGHLLIQLISTATITLMPMMttVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 227
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-224 4.09e-33

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: 116.73  E-value: 4.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  66 GHKWAMILASLMIFILALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIII 145
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339906577 146 ETISLFIRPLALGVRLTANLTAGHLLIQLISTATITlmpMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQ 224
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPS---LLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
65-224 4.51e-28

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 105.65  E-value: 4.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577   65 GGHKWAMILASLMIFIL---ALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVA-LGHLLPEGTPAPLIP 140
Cdd:pfam00119  53 KGRKFFPLLLTLFFFILvsnLLGLIPKSPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  141 VLIIIETISLFIRPLALGVRLTANLTAGHLLIQLISTATITLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLS 220
Cdd:pfam00119 133 LLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTA 212


                  ....
gi 339906577  221 LYLQ 224
Cdd:pfam00119 213 VYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 66-225 2.55e-17

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: 77.04  E-value: 2.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  66 GHKWAMILASLMIFILALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVA-LGHLLPEGTPaPLIPVLII 144
Cdd:COG0356   54 GRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLP 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577 145 IETISLFIRPLALGVRLTANLTAGHLLIqlistATITLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQ 224
Cdd:COG0356  133 IEIISELARPLSLSLRLFGNMFAGHIIL-----LLLAGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYIS 207


                 .
gi 339906577 225 E 225
Cdd:COG0356  208 L 208
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 3.39e-123

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 348.40  E-value: 3.39e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577   1 MALNLFDQFMSPTHLGIPLIAIALTLPWALIPSPTNRYQNNRLISLQSWFIKTFTQQLLMPLNQGGHKWAMILASLMIFI 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  81 LALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339906577 161 LTANLTAGHLLIQLISTATITLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-227 2.67e-109

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 313.06  E-value: 2.67e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577   1 MALNLFDQFMSPTHLGIPLIAIALTLPWALIPSPTNRYQNNRLISLQSWFIKTFTQQLLMPLNQGGHKWAMILASLMIFI 80
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  81 LALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339906577 161 LTANLTAGHLLIQLISTATITLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-227 8.44e-99

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 286.72  E-value: 8.44e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577   1 MALNLFDQFMSPTHLGIPLIAIALTLPWALIPSPTNRYQNNRLISLQSWFIKTFTQQLLMPLNQGGHKWAMILASLMIFI 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  81 LALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339906577 161 LTANLTAGHLLIQLISTATITLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-227 1.86e-86

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 255.26  E-value: 1.86e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577   1 MALNLFDQFMSPTHLGIPLIAIALTLPWALIPSPTNRYQNNRLISLQSWFIKTFTQQLLMPLNQGGHKWAMILASLMIFI 80
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  81 LALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 339906577 161 LTANLTAGHLLIQLISTATITLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 5.48e-72

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 218.67  E-value: 5.48e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577   1 MALNLFDQFMSPTHLGIPLIAIALTLPWALIPSPtNRYQNNRLISLQSWFIKTFTQQLLMPLNQGGHKWAMILASLMIFI 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTP-NRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  81 LALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00101  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339906577 161 LTANLTAGHLLIQLISTATITLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQEN 226
Cdd:MTH00101 160 LTANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-227 3.71e-45

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: 150.05  E-value: 3.71e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577    5 LFDQFMSP----THLGIPLIAIALTLPWALIPSPTNRY-QNNRLISLQSWFIKTFTQQLLMPLNQGGHKWAMILASLMIF 79
Cdd:TIGR01131   1 LFSQFDISpitlFSLTLLSLILLLSLLIFLISSSLSRWlIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577   80 ILALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETISLFIRPLALGV 159
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339906577  160 RLTANLTAGHLLIQLISTATITLMPMMttVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 227
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 4-227 2.43e-42

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 142.80  E-value: 2.43e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577   4 NLFDQFMSPTHLGIPL--IAIALTLPWALIPSPTNrYQNNRLISLQSWFIKTFTQQLLMPLNQGGHKWAMILASLMIFIL 81
Cdd:MTH00035   6 SIFGQFSPDTILFIPLtlLSSVIALSWLFFINPTN-WLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  82 ALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETISLFIRPLALGVRL 161
Cdd:MTH00035  85 SINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339906577 162 TANLTAGHLLIQLISTATITLMPmMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00035 165 AANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 8.94e-37

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 128.36  E-value: 8.94e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577   1 MALNLFDQFMSPTHLGIPLIAIALTLPWALIPSPTNrYQNNRLISLQSWFIKTFTQQLLMPLNQGGHKWAMILASLMIFI 80
Cdd:MTH00157   1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFW-LIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  81 LALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETISLFIRPLALGVR 160
Cdd:MTH00157  80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339906577 161 LTANLTAGHLLIQLISTATITLMPMMTTVatlTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQE 225
Cdd:MTH00157 160 LAANMIAGHLLLTLLGNTGPSLSSMILSI---LILIQILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 4.95e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 123.99  E-value: 4.95e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577   1 MALNLFDQFMSPTHLGIPLIAIALTLPW-ALIPSPTNRYQNNRLISLQSWFIKTFTQQLLMPLNQGGHK-WAMILASLMI 78
Cdd:MTH00176   1 MLVDLFSSFDPPNKNIFSMISLSWITLLlFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILgSASIIISLFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  79 FILALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETISLFIRPLALG 158
Cdd:MTH00176  81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 339906577 159 VRLTANLTAGHLLIQLISTATITLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQEN 226
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-224 4.09e-33

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: 116.73  E-value: 4.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  66 GHKWAMILASLMIFILALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIII 145
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 339906577 146 ETISLFIRPLALGVRLTANLTAGHLLIQLISTATITlmpMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQ 224
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPS---LLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 6-225 2.05e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 114.96  E-value: 2.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577   6 FDQFMSPTHLGIPLIAIALTLPWALIPSPTnRYQNNRLISLQSWFIKTFTQQLLMPLNQGGHKWAMILASLMIFILALNL 85
Cdd:MTH00173   9 FDDHNSSFSSLSFLMWLLSLMSLFFFSSSV-WVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  86 LGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETISLFIRPLALGVRLTANL 165
Cdd:MTH00173  88 SGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANI 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 339906577 166 TAGHLLIQLI-STATITLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQE 225
Cdd:MTH00173 168 SAGHIVLTLIgNYLSSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_A pfam00119
ATP synthase A chain;
65-224 4.51e-28

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 105.65  E-value: 4.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577   65 GGHKWAMILASLMIFIL---ALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVA-LGHLLPEGTPAPLIP 140
Cdd:pfam00119  53 KGRKFFPLLLTLFFFILvsnLLGLIPKSPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  141 VLIIIETISLFIRPLALGVRLTANLTAGHLLIQLISTATITLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLS 220
Cdd:pfam00119 133 LLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTA 212


                  ....
gi 339906577  221 LYLQ 224
Cdd:pfam00119 213 VYIS 216
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 18-222 5.76e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 97.88  E-value: 5.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  18 PLIAIALTLPWALIPSPTNRYQNNRLISLQSWFIKTFTQQLLMPLNQGGHKWAMILASLMIFILALNLLGLLPYTFTPTT 97
Cdd:MTH00005  22 STAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  98 QLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIST 177
Cdd:MTH00005 102 HLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGI 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 339906577 178 ATITLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLY 222
Cdd:MTH00005 182 YAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 1-223 1.43e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 88.94  E-value: 1.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577   1 MALNLFDQFMSPTHLGIPLIAIALTLPWA--LIPSPTNRYQNNRLISLQSWFIKTFTQQLLMPLNQGGHKWAMILASLMI 78
Cdd:MTH00172   1 MSSSYFDQFNIVWLIGLTNSSIMMILVIIvvLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  79 FILALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETISLFIRPLALG 158
Cdd:MTH00172  81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 339906577 159 VRLTANLTAGHLLIQLISTATITLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYL 223
Cdd:MTH00172 161 VRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYL 225
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 62-227 1.72e-20

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 86.21  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  62 LNQGGHKWAMILASLMIFILALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPV 141
Cdd:MTH00175  75 LGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPF 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577 142 LIIIETISLFIRPLALGVRLTANLTAGHLLIQLISTATITLMPM-MTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLS 220
Cdd:MTH00175 155 LVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNgLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTT 234


                 ....*..
gi 339906577 221 LYLQENV 227
Cdd:MTH00175 235 IYLGDTI 241
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 66-225 2.55e-17

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: 77.04  E-value: 2.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  66 GHKWAMILASLMIFILALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVA-LGHLLPEGTPaPLIPVLII 144
Cdd:COG0356   54 GRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLP 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577 145 IETISLFIRPLALGVRLTANLTAGHLLIqlistATITLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQ 224
Cdd:COG0356  133 IEIISELARPLSLSLRLFGNMFAGHIIL-----LLLAGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYIS 207


                 .
gi 339906577 225 E 225
Cdd:COG0356  208 L 208
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 63-227 2.14e-15

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 72.66  E-value: 2.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  63 NQGGHKWAMILaSLMIFILALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVL 142
Cdd:MTH00174  85 NKGGNYLAFVL-SLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLL 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577 143 IIIETISLFIRPLALGVRLTANLTAGHLLIQLISTATITLMPMMTTV-ATLTAILLVLLTLLEVAVAIIQAYVFVLLLSL 221
Cdd:MTH00174 164 TIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPFAILIFVTILEMAVAIIQAYVFTLLTIV 243


                 ....*.
gi 339906577 222 YLQENV 227
Cdd:MTH00174 244 YLRDTV 249
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 66-225 5.44e-15

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 70.98  E-value: 5.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  66 GHKWAMILASLMIFILALNLLGLLP-YTFTPTTQLSLNMGLAVPLWLATVIIGLRNQptvALGHLLPEGTPAPlIPVLII 144
Cdd:PRK05815  69 GKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLP 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577 145 IETISLFIRPLALGVRLTANLTAGHLLIQLIStatiTLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYLQ 224
Cdd:PRK05815 145 IEIISEFSRPISLSLRLFGNMLAGELILALIA----LLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYIS 220


                 .
gi 339906577 225 E 225
Cdd:PRK05815 221 M 221
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 73-223 1.43e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 53.98  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  73 LASLMIFILALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETISLFI 152
Cdd:PRK13419 174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGTHWSLWIIMIPIEFIGLFT 253

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 339906577 153 RPLALGVRLTANLTAGHLLI-QLISTATITLMPMMTtvATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYL 223
Cdd:PRK13419 254 KPFALTVRLFANMTAGHIVIlSLIFISFILKSYIVA--VAVSVPFAIFIYLLELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 71-225 1.54e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 52.67  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  71 MILASLMIFILALNLLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGLRNQptVALGHLLPEGTPAPLIP-VLIIIETIS 149
Cdd:MTH00087  53 VISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKS--EKFSVYLSKGSDSFLKTfSMLFVEIVS 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 339906577 150 LFIRPLALGVRLTANLTAGHLLIQLISTATITLMPMMttvatltaillVLLTLLEVAVAIIQAYVFVLLLSLYLQE 225
Cdd:MTH00087 131 ELSRPLALTLRLTVNLMVGHLISSLLNFLGEKYVWLS-----------ILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 94-223 2.48e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 50.27  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 339906577  94 TPTTQLSLNMGLAVPLWLATVIIGLRNQPTVALGHLLPEGTPAPLIPVLIIIETI-SLFIRPLALGVRLTANLTAGHLLI 172
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 339906577 173 qlISTATITLMPMMTTVATLTAILLVLLTLLEVAVAIIQAYVFVLLLSLYL 223
Cdd:PRK13417 297 --LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
 
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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