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Conserved domains on  [gi|16357071|ref|NP_443403|]
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ATP synthase F0 subunit 6 (mitochondrion) [Zenopsis nebulosus]

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 3.01e-119

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177190  Cd Length: 227  Bit Score: 338.39  E-value: 3.01e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    1 MMLSFFDQFAAPVYLGIPLIVLALALPWILLPTPSARWKNNRFVNLEGWFIRNFAKELLLPIKQGGHKWALLFTSLVVFL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   81 ITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIIIETVSLLVRPLALGLR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16357071  161 LTANLTAGHLLIELIASAATTLLPLMPVVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 3.01e-119

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 338.39  E-value: 3.01e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    1 MMLSFFDQFAAPVYLGIPLIVLALALPWILLPTPSARWKNNRFVNLEGWFIRNFAKELLLPIKQGGHKWALLFTSLVVFL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   81 ITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIIIETVSLLVRPLALGLR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16357071  161 LTANLTAGHLLIELIASAATTLLPLMPVVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 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 ...
 4-227 1.80e-46

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: 153.52  E-value: 1.80e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071     4 SFFDQFAAPVYLGIPLIVLALALPWILLPTPSAR-WKNNRFVNLEGWFIRNFAKELLLPIKQGGHKWALLFTSLVVFLIT 82
Cdd:TIGR01131   4 QFDISPITLFSLTLLSLILLLSLLIFLISSSLSRwLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    83 MNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIIIETVSLLVRPLALGLRLT 162
Cdd:TIGR01131  84 SNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLF 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16357071   163 ANLTAGHLLIELIASAATTLLPLMpvVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
Cdd:TIGR01131 164 ANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-224 1.56e-36

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: 125.59  E-value: 1.56e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071  66 GHKWALLFTSLVVFLITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIII 145
Cdd:cd00310   1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16357071 146 ETVSLLVRPLALGLRLTANLTAGHLLIELIASAATTLLPLMPVVAFLtavILFLLTLLEIAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310  81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLL---LPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
19-224 8.36e-30

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 110.27  E-value: 8.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    19 LIVLALALPWILLPTPSARWKNNRFVNLEGW---FIRNFAKELLLpiKQGGHKWALLFTSLVVFLITMNVLGLL---PYI 92
Cdd:pfam00119   6 IVALILLLFLLLATRKTKKLVPGRLQNFVEMlveFVDNIVKDNIG--KKKGRKFFPLLLTLFFFILVSNLLGLIpksPGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    93 FTPTTQLSLSLGFAVPLWLATVITGMRNQ-PKIAFAHLLPEGTPTLLIPILIIIETVSLLVRPLALGLRLTANLTAGHLL 171
Cdd:pfam00119  84 FTVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLL 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 16357071   172 IELIASAATTLLPLMPVVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 164 LLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 50-225 1.51e-23

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: 93.60  E-value: 1.51e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071  50 FIRNFAKElllPIKQGGHKWALLFTSLVVFLITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHL 129
Cdd:COG0356  41 FVRNQVKD---TIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKH 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071 130 LPEGTPTLLIPILIIIETVSLLVRPLALGLRLTANLTAGHLLIELIASAATTLLplmpvVAFLTAVILFLLTLLEIAVAM 209
Cdd:COG0356 118 LFFPPFPWLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLL-----LGVLSLLLPVAWTAFELLVGF 192

                       170
                ....*....|....*.
gi 16357071 210 IQAYVFVLLLSLYLQE 225
Cdd:COG0356 193 LQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 3.01e-119

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 338.39  E-value: 3.01e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    1 MMLSFFDQFAAPVYLGIPLIVLALALPWILLPTPSARWKNNRFVNLEGWFIRNFAKELLLPIKQGGHKWALLFTSLVVFL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   81 ITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIIIETVSLLVRPLALGLR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16357071  161 LTANLTAGHLLIELIASAATTLLPLMPVVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-227 1.18e-105

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 303.81  E-value: 1.18e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    1 MMLSFFDQFAAPVYLGIPLIVLALALPWILLPTPSARWKNNRFVNLEGWFIRNFAKELLLPIKQGGHKWALLFTSLVVFL 80
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   81 ITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIIIETVSLLVRPLALGLR 160
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16357071  161 LTANLTAGHLLIELIASAATTLLPLMPVVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-227 6.98e-96

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 279.40  E-value: 6.98e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    1 MMLSFFDQFAAPVYLGIPLIVLALALPWILLPTPSARWKNNRFVNLEGWFIRNFAKELLLPIKQGGHKWALLFTSLVVFL 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   81 ITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIIIETVSLLVRPLALGLR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16357071  161 LTANLTAGHLLIELIASAATTLLPLMPVVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-227 6.32e-82

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 243.70  E-value: 6.32e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    1 MMLSFFDQFAAPVYLGIPLIVLALALPWILLPTPSARWKNNRFVNLEGWFIRNFAKELLLPIKQGGHKWALLFTSLVVFL 80
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   81 ITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIIIETVSLLVRPLALGLR 160
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16357071  161 LTANLTAGHLLIELIASAATTLLPLMPVVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.30e-72

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 220.21  E-value: 1.30e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    1 MMLSFFDQFAAPVYLGIPLIVLALALPWILLPTPSaRWKNNRFVNLEGWFIRNFAKELLLPIKQGGHKWALLFTSLVVFL 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPN-RLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   81 ITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIIIETVSLLVRPLALGLR 160
Cdd:MTH00101  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16357071  161 LTANLTAGHLLIELIASAATTLLPLMPVVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQEN 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 ...
 4-227 1.80e-46

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: 153.52  E-value: 1.80e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071     4 SFFDQFAAPVYLGIPLIVLALALPWILLPTPSAR-WKNNRFVNLEGWFIRNFAKELLLPIKQGGHKWALLFTSLVVFLIT 82
Cdd:TIGR01131   4 QFDISPITLFSLTLLSLILLLSLLIFLISSSLSRwLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    83 MNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIIIETVSLLVRPLALGLRLT 162
Cdd:TIGR01131  84 SNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLF 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16357071   163 ANLTAGHLLIELIASAATTLLPLMpvVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
Cdd:TIGR01131 164 ANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 4-227 1.64e-43

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 145.89  E-value: 1.64e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    4 SFFDQFAAPVYLGIPLIVLA--LALPWILLPTPSaRWKNNRFVNLEGWFIRNFAKELLLPIKQGGHKWALLFTSLVVFLI 81
Cdd:MTH00035   6 SIFGQFSPDTILFIPLTLLSsvIALSWLFFINPT-NWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   82 TMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIIIETVSLLVRPLALGLRL 161
Cdd:MTH00035  85 SINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16357071  162 TANLTAGHLLIELIaSAATTLLPLMPVVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
Cdd:MTH00035 165 AANLTAGHLLIFLL-STAIWELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 9.27e-42

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 141.32  E-value: 9.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    1 MMLSFFDQFAAPVYLGIPLIVLALALPWI-LLPTPSARWKNNRFVNLEGWFIRNFAKELLLPIKQGGHK-WALLFTSLVV 78
Cdd:MTH00176   1 MLVDLFSSFDPPNKNIFSMISLSWITLLLfLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILgSASIIISLFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   79 FLITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIIIETVSLLVRPLALG 158
Cdd:MTH00176  81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16357071  159 LRLTANLTAGHLLIELIASAATTLLPLMPVVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 5.90e-41

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 139.15  E-value: 5.90e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    1 MMLSFFDQFAAPVYLGIPLIVLALALPWILLP-----TPSarwKNNRFVNLEGWFIRNFAKELLLPIKQGGHkwaLLFTS 75
Cdd:MTH00157   1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPssfwlIPS---RYNILWNKILKTLHKEFKTLLGPKNKGST---LIFIS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   76 LVVFLITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIIIETVSLLVRPL 155
Cdd:MTH00157  75 LFSFILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPG 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071  156 ALGLRLTANLTAGHLLIELIASAATTLLPLMPVVAFLtavILFLLTLLEIAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00157 155 TLAVRLAANMIAGHLLLTLLGNTGPSLSSMILSILIL---IQILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-224 1.56e-36

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: 125.59  E-value: 1.56e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071  66 GHKWALLFTSLVVFLITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIII 145
Cdd:cd00310   1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16357071 146 ETVSLLVRPLALGLRLTANLTAGHLLIELIASAATTLLPLMPVVAFLtavILFLLTLLEIAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310  81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLL---LPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-225 4.29e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 124.21  E-value: 4.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    1 MMLSFFDQFAAPVYLGIPLIVLALALP-WILLPTPSARW-KNNRFVNLEGWFIRNFAKELLLPIKQGGHKWALLFTSLVV 78
Cdd:MTH00173   1 MMVDLFSSFDDHNSSFSSLSFLMWLLSlMSLFFFSSSVWvSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   79 FLITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIIIETVSLLVRPLALG 158
Cdd:MTH00173  81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16357071  159 LRLTANLTAGHLLIELIASAATTLLPLMPVV-AFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00173 161 VRLLANISAGHIVLTLIGNYLSSSLFSSSVVsLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 72-222 4.37e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 111.36  E-value: 4.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   72 LFTSLVVFLITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIIIETVSLL 151
Cdd:MTH00005  76 LISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISIL 155

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16357071  152 VRPLALGLRLTANLTAGHLLIELIASAATTLLPLMPVVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLY 222
Cdd:MTH00005 156 VRPITLSFRLAANMSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP-synt_A pfam00119
ATP synthase A chain;
19-224 8.36e-30

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 110.27  E-value: 8.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    19 LIVLALALPWILLPTPSARWKNNRFVNLEGW---FIRNFAKELLLpiKQGGHKWALLFTSLVVFLITMNVLGLL---PYI 92
Cdd:pfam00119   6 IVALILLLFLLLATRKTKKLVPGRLQNFVEMlveFVDNIVKDNIG--KKKGRKFFPLLLTLFFFILVSNLLGLIpksPGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071    93 FTPTTQLSLSLGFAVPLWLATVITGMRNQ-PKIAFAHLLPEGTPTLLIPILIIIETVSLLVRPLALGLRLTANLTAGHLL 171
Cdd:pfam00119  84 FTVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLL 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 16357071   172 IELIASAATTLLPLMPVVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 164 LLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 66-223 1.67e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 107.43  E-value: 1.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   66 GHKWALLFTSLVVFLITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIII 145
Cdd:MTH00172  68 GLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLI 147

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16357071  146 ETVSLLVRPLALGLRLTANLTAGHLLIELIASAATTLLPLMPVVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYL 223
Cdd:MTH00172 148 ETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYL 225
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 66-227 7.84e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 97.77  E-value: 7.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   66 GHKWALLFTSLVVFLITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIII 145
Cdd:MTH00175  79 GQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLI 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071  146 ETVSLLVRPLALGLRLTANLTAGHLLIELIASAATTLLPL-MPVVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQ 224
Cdd:MTH00175 159 ETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNgLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLG 238


                 ...
gi 16357071  225 ENV 227
Cdd:MTH00175 239 DTI 241
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 50-225 1.51e-23

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: 93.60  E-value: 1.51e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071  50 FIRNFAKElllPIKQGGHKWALLFTSLVVFLITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHL 129
Cdd:COG0356  41 FVRNQVKD---TIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKH 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071 130 LPEGTPTLLIPILIIIETVSLLVRPLALGLRLTANLTAGHLLIELIASAATTLLplmpvVAFLTAVILFLLTLLEIAVAM 209
Cdd:COG0356 118 LFFPPFPWLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLL-----LGVLSLLLPVAWTAFELLVGF 192

                       170
                ....*....|....*.
gi 16357071 210 IQAYVFVLLLSLYLQE 225
Cdd:COG0356 193 LQAYIFTMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 50-225 2.98e-22

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 90.62  E-value: 2.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   50 FIRNFAKELllpIKQGGHKWALLFTSLVVFLITMNVLGLLP-YIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAH 128
Cdd:PRK05815  56 FVRGQVKDN---IGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLK 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071  129 LLpegtPTLLIPILIIIETVSLLVRPLALGLRLTANLTAGHLLIELIASAATTLLPLMPVVAFLTAVilflLTLLEIAVA 208
Cdd:PRK05815 133 EF----YLQPHPLLLPIEIISEFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILPVA----WTIFEIFVG 204

                        170
                 ....*....|....*..
gi 16357071  209 MIQAYVFVLLLSLYLQE 225
Cdd:PRK05815 205 TLQAYIFMMLTIVYISM 221
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 66-227 1.07e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 81.91  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   66 GHKWALLFTSLVVFLITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIII 145
Cdd:MTH00174  87 GGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTII 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071  146 ETVSLLVRPLALGLRLTANLTAGHLLIELIASAATTLLPLMPVV-AFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQ 224
Cdd:MTH00174 167 ETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYLR 246


                 ...
gi 16357071  225 ENV 227
Cdd:MTH00174 247 DTV 249
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 72-225 7.82e-12

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 61.92  E-value: 7.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   72 LFTSLVVFLITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNqpKIAFAHLLP-EGTPTLLIPILIIIETVSL 150
Cdd:MTH00087  54 ISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSK--SEKFSVYLSkGSDSFLKTFSMLFVEIVSE 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16357071  151 LVRPLALGLRLTANLTAGHLLIELIASaattllplmpvVAFLTAVILFLLTLLEIAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00087 132 LSRPLALTLRLTVNLMVGHLISSLLNF-----------LGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 78-223 8.59e-11

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 60.53  E-value: 8.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   78 VFLITMNVLGLLPYIFTPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIIIETVSLLVRPLAL 157
Cdd:PRK13419 179 FFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGTHWSLWIIMIPIEFIGLFTKPFAL 258

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16357071  158 GLRLTANLTAGHLLIelIASAATTLLPLMPVVAFLTAVILFL-LTLLEIAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13419 259 TVRLFANMTAGHIVI--LSLIFISFILKSYIVAVAVSVPFAIfIYLLELFVAFLQAYIFTMLSALFI 323
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 94-223 8.45e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 48.73  E-value: 8.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16357071   94 TPTTQLSLSLGFAVPLWLATVITGMRNQPKIAFAHLLPEGTPTLLIPILIIIE-TVSLLVRPLALGLRLTANLTAGHLLI 172
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEfIVSPMAKTFALTVRLLANMTAGHVII 296

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 16357071  173 -ELIASAATTLLPLMPVVAFLTAVILFLLtllEIAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13417 297 lALMGFIFQFQSWGIVPVSVIGSGLIYVL---EIFVAFLQAYIFVLLTSLFV 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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