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Conserved domains on  [gi|699256683|ref|YP_009092591|]
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ATP synthase F0 subunit 6 (mitochondrion) [Rhabdosargus sarba]

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 2.19e-110

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177190  Cd Length: 227  Bit Score: 316.04  E-value: 2.19e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   1 MMTSFFDQFSSPLYMGIPLMAIAMLLPWVLFPTPTLRWLGNRLLTLQNWFLGMFTRQLLLPVNLPGHKWALILASLMIFL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  81 LSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIIIETISLMIRPIALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 699256683 161 LTANLTAGHLLIQLISTGFFVLLSLQPIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 2.19e-110

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 316.04  E-value: 2.19e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   1 MMTSFFDQFSSPLYMGIPLMAIAMLLPWVLFPTPTLRWLGNRLLTLQNWFLGMFTRQLLLPVNLPGHKWALILASLMIFL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  81 LSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIIIETISLMIRPIALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 699256683 161 LTANLTAGHLLIQLISTGFFVLLSLQPIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYLQENV 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 ...
 6-227 1.14e-37

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: 130.79  E-value: 1.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683    6 FDQFSSPLYM--GIPLMAIAMLLPWVLF---PTPTLRWLGNRLLTLQNWFLGMFTRQLLLPVNLPGHKWALILASLMIFL 80
Cdd:TIGR01131   2 FSQFDISPITlfSLTLLSLILLLSLLIFlisSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   81 LSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIIIETISLMIRPIALGVR 160
Cdd:TIGR01131  82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 699256683  161 LTANLTAGHLLIQLISTGFFVLLSLQPIAavFTGALLLMLSILELAVAIIQAYVFVLLLSLYLQENV 227
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLLFSLMSSAIFA--LLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-224 5.84e-28

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: 103.63  E-value: 5.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  66 GHKWALILASLMIFLLSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIII 145
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 699256683 146 ETISLMIRPIALGVRLTANLTAGHLLIQLISTGFFVLLSlqpIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYLQ 224
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLS---SVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
66-224 1.22e-21

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 88.70  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   66 GHKWALILASLMIFLL---SLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLS-LAHLLPEGTPLLLIPI 141
Cdd:pfam00119  54 GRKFFPLLLTLFFFILvsnLLGLIPKSPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  142 LIIIETISLMIRPIALGVRLTANLTAGHLLIQLISTGFFVLLSLQPIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSL 221
Cdd:pfam00119 134 LLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAV 213


                  ...
gi 699256683  222 YLQ 224
Cdd:pfam00119 214 YIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 66-225 7.65e-12

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: 62.40  E-value: 7.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  66 GHKWALILASLMIFLLSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLS-LAHLLPEGTPLLLIPILII 144
Cdd:COG0356   54 GRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFPWLAPLMLPI 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683 145 iETISLMIRPIALGVRLTANLTAGHLLIQLISTGFFVLLslqpiAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYLQ 224
Cdd:COG0356  134 -EIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLL-----LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYIS 207


                 .
gi 699256683 225 E 225
Cdd:COG0356  208 L 208
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 2.19e-110

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 316.04  E-value: 2.19e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   1 MMTSFFDQFSSPLYMGIPLMAIAMLLPWVLFPTPTLRWLGNRLLTLQNWFLGMFTRQLLLPVNLPGHKWALILASLMIFL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  81 LSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIIIETISLMIRPIALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 699256683 161 LTANLTAGHLLIQLISTGFFVLLSLQPIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-227 5.67e-98

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 284.55  E-value: 5.67e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   1 MMTSFFDQFSSPLYMGIPLMAIAMLLPWVLFPTPTLRWLGNRLLTLQNWFLGMFTRQLLLPVNLPGHKWALILASLMIFL 80
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  81 LSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIIIETISLMIRPIALGVR 160
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 699256683 161 LTANLTAGHLLIQLISTGFFVLLSLQPIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-227 3.88e-88

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 259.76  E-value: 3.88e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   1 MMTSFFDQFSSPLYMGIPLMAIAMLLPWVLFPTPTLRWLGNRLLTLQNWFLGMFTRQLLLPVNLPGHKWALILASLMIFL 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  81 LSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIIIETISLMIRPIALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 699256683 161 LTANLTAGHLLIQLISTGFFVLLSLQPIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-227 1.38e-75

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 227.91  E-value: 1.38e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   1 MMTSFFDQFSSPLYMGIPLMAIAMLLPWVLFPTPTLRWLGNRLLTLQNWFLGMFTRQLLLPVNLPGHKWALILASLMIFL 80
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  81 LSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIIIETISLMIRPIALGVR 160
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 699256683 161 LTANLTAGHLLIQLISTGFFVLLSLQPIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 1.37e-63

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 197.10  E-value: 1.37e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   1 MMTSFFDQFSSPLYMGIPLMAIAMLLPWVLFPTPTlRWLGNRLLTLQNWFLGMFTRQLLLPVNLPGHKWALILASLMIFL 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPN-RLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  81 LSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIIIETISLMIRPIALGVR 160
Cdd:MTH00101  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 699256683 161 LTANLTAGHLLIQLISTGFFVLLSLQPIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYLQEN 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 ...
 6-227 1.14e-37

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: 130.79  E-value: 1.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683    6 FDQFSSPLYM--GIPLMAIAMLLPWVLF---PTPTLRWLGNRLLTLQNWFLGMFTRQLLLPVNLPGHKWALILASLMIFL 80
Cdd:TIGR01131   2 FSQFDISPITlfSLTLLSLILLLSLLIFlisSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   81 LSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIIIETISLMIRPIALGVR 160
Cdd:TIGR01131  82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 699256683  161 LTANLTAGHLLIQLISTGFFVLLSLQPIAavFTGALLLMLSILELAVAIIQAYVFVLLLSLYLQENV 227
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLLFSLMSSAIFA--LLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 3-227 1.03e-35

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 125.86  E-value: 1.03e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   3 TSFFDQFSSPLYMGIPLMAIAML--LPWVLFPTPTlRWLGNRLLTLQNWFLGMFTRQLLLPVNLPGHKWALILASLMIFL 80
Cdd:MTH00035   5 NSIFGQFSPDTILFIPLTLLSSViaLSWLFFINPT-NWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  81 LSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIIIETISLMIRPIALGVR 160
Cdd:MTH00035  84 LSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLR 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 699256683 161 LTANLTAGHLLIQLISTGFFVLLSLqPIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00035 164 LAANLTAGHLLIFLLSTAIWELSNS-PLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 2.52e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 122.20  E-value: 2.52e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   1 MMTSFFDQFSSPLYMGIPLMAIAMLLPWVLFPTptLRWL-GNRLLTLQNWFLGMFTRQLLLPVNLPGHKWALILASLMIF 79
Cdd:MTH00157   1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPS--SFWLiPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  80 LLSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIIIETISLMIRPIALGV 159
Cdd:MTH00157  79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 699256683 160 RLTANLTAGHLLIQLISTgffVLLSLQPIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYLQE 225
Cdd:MTH00157 159 RLAANMIAGHLLLTLLGN---TGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 1.95e-31

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 114.74  E-value: 1.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   1 MMTSFFDQFSSPLYMGIPLMAIAMLLPWV-LFPTPTLRWL-GNRLLTLQNWFLGMFTRQLLLPVNLPGHKWALILASLMI 78
Cdd:MTH00176   1 MLVDLFSSFDPPNKNIFSMISLSWITLLLfLLLMPSSVWFcPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  79 FLLSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIIIETISLMIRPIALG 158
Cdd:MTH00176  81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 699256683 159 VRLTANLTAGHLLIQLISTGFFVLLSLQPIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYLQEN 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 5.84e-28

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: 103.63  E-value: 5.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  66 GHKWALILASLMIFLLSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIII 145
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 699256683 146 ETISLMIRPIALGVRLTANLTAGHLLIQLISTGFFVLLSlqpIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYLQ 224
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLS---SVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-225 1.23e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 99.55  E-value: 1.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   1 MMTSFFDQFSSPLYMGIPLMAIAMLLP-WVLFPTPTLRWL-GNRLLTLQNWFLGMFTRQLLLPVNLPGHKWALILASLMI 78
Cdd:MTH00173   1 MMVDLFSSFDDHNSSFSSLSFLMWLLSlMSLFFFSSSVWVsSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  79 FLLSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIIIETISLMIRPIALG 158
Cdd:MTH00173  81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 699256683 159 VRLTANLTAGHLLIQLISTGFFVLLSLQPIAAVFTGALLLMLSILE-LAVAIIQAYVFVLLLSLYLQE 225
Cdd:MTH00173 161 VRLLANISAGHIVLTLIGNYLSSSLFSSSVVSLLLVLLIQVGYFIFeVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_A pfam00119
ATP synthase A chain;
66-224 1.22e-21

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 88.70  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   66 GHKWALILASLMIFLL---SLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLS-LAHLLPEGTPLLLIPI 141
Cdd:pfam00119  54 GRKFFPLLLTLFFFILvsnLLGLIPKSPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  142 LIIIETISLMIRPIALGVRLTANLTAGHLLIQLISTGFFVLLSLQPIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSL 221
Cdd:pfam00119 134 LLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAV 213


                  ...
gi 699256683  222 YLQ 224
Cdd:pfam00119 214 YIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 1-223 9.83e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 86.63  E-value: 9.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   1 MMTSFFDQFSSPLYMGIPLMAIAMLLPW--VLFPTPTLRWLGNRLLTLQNWFLGMFTRQLLLPVNLPGHKWALILASLMI 78
Cdd:MTH00172   1 MSSSYFDQFNIVWLIGLTNSSIMMILVIivVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  79 FLLSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIIIETISLMIRPIALG 158
Cdd:MTH00172  81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 699256683 159 VRLTANLTAGHLLIQLISTGFFVLLSLQPIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYL 223
Cdd:MTH00172 161 VRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYL 225
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 2-222 4.08e-20

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 85.17  E-value: 4.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683   2 MTSFFDQFSSPLYMGIPLMAIaMLLPWVLFPTPtlrwlgNRLLTLQNWFLGMFTRQLLLPVNLPGHKWALILASLMIFLL 81
Cdd:MTH00005  13 TNSLFNNLSSTAFWAFNFSII-LLLSSSFWITP------NRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMII 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  82 SLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIIIETISLMIRPIALGVRL 161
Cdd:MTH00005  86 LMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRL 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 699256683 162 TANLTAGHLLIQLISTGFFVLLSLQPIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLY 222
Cdd:MTH00005 166 AANMSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 65-227 5.93e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 79.67  E-value: 5.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  65 PGHKWALILASLMIFLLSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILII 144
Cdd:MTH00175  78 SGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683 145 IETISLMIRPIALGVRLTANLTAGHLLIQLIST-GFFVLLSLQPIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYL 223
Cdd:MTH00175 158 IETLSYLIRAISLGVRLAANISAGHLLFAILSGfAFNMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYL 237


                 ....
gi 699256683 224 QENV 227
Cdd:MTH00175 238 GDTI 241
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 41-227 7.75e-13

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 65.73  E-value: 7.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  41 NRLLTLQNWFLGMFTRQLLLPVNLPGHKWALILASLMIFLLSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRN 120
Cdd:MTH00174  62 NRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLIT 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683 121 QPNLSLAHLLPEGTPLLLIPILIIIETISLMIRPIALGVRLTANLTAGHLLIQLISTGFFVLLSLQPIAAVFTG-ALLLM 199
Cdd:MTH00174 142 FRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSFVPfAILIF 221

                        170       180
                 ....*....|....*....|....*...
gi 699256683 200 LSILELAVAIIQAYVFVLLLSLYLQENV 227
Cdd:MTH00174 222 VTILEMAVAIIQAYVFTLLTIVYLRDTV 249
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 66-225 7.65e-12

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: 62.40  E-value: 7.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  66 GHKWALILASLMIFLLSLNLLGLLPYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQPNLS-LAHLLPEGTPLLLIPILII 144
Cdd:COG0356   54 GRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFPWLAPLMLPI 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683 145 iETISLMIRPIALGVRLTANLTAGHLLIQLISTGFFVLLslqpiAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYLQ 224
Cdd:COG0356  134 -EIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLL-----LGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYIS 207


                 .
gi 699256683 225 E 225
Cdd:COG0356  208 L 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 66-225 2.11e-10

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 58.27  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  66 GHKWALILASLMIFLLSLNLLGLLP-YTFTPTTQLSVNLGLAVPLWLATVLIGMRNQpnlSLAHLLPEGTPLLLIPILII 144
Cdd:PRK05815  69 GKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQPHPLLLPI 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683 145 iETISLMIRPIALGVRLTANLTAGHLLIQLISTGFFVLLSLQPIAAVFTGALLLMLSIlelaVAIIQAYVFVLLLSLYLQ 224
Cdd:PRK05815 146 -EIISEFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILPVAWTIFEIF----VGTLQAYIFMMLTIVYIS 220


                 .
gi 699256683 225 E 225
Cdd:PRK05815 221 M 221
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 90-223 1.66e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 50.90  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  90 PYTFTPTTQLSVNLGLAVPLWLATVLIGMRNQP-NLSLAHLlPEGTPLLLIPILIIIETISLMIRPIALGVRLTANLTAG 168
Cdd:PRK13419 191 PYGATATGNINVTLTLAVFTFFITQYAAIKAHGiKGYLAHL-TGGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAG 269

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 699256683 169 HLLI-QLISTGFfvLLSLQPIAAVFTGALLLMLSILELAVAIIQAYVFVLLLSLYL 223
Cdd:PRK13419 270 HIVIlSLIFISF--ILKSYIVAVAVSVPFAIFIYLLELFVAFLQAYIFTMLSALFI 323
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 94-223 7.41e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 46.04  E-value: 7.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  94 TPTTQLSVNLGLAVPLWLATVLIGMRNQPNLSLAHLLPEGTPLLLIPILIIIETI-SLMIRPIALGVRLTANLTAGHLLI 172
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 699256683 173 qLISTGFFVLLSLQPIAAVFTGALLLMLSILELaVAIIQAYVFVLLLSLYL 223
Cdd:PRK13417 297 -LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIF-VAFLQAYIFVLLTSLFV 345
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 90-225 1.37e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 44.20  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699256683  90 PYTFTPTTQLSVNLGLAVPLWLATVLIGMRNqpNLSLAHLLP-EGTPLLLIPILIIIETISLMIRPIALGVRLTANLTAG 168
Cdd:MTH00087  72 PYSFSPCGMVEFTFLYALVAWLSTFLSFLSK--SEKFSVYLSkGSDSFLKTFSMLFVEIVSELSRPLALTLRLTVNLMVG 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 699256683 169 HLLIQLISTGFFVLLSLQPIAAVFTgalllmlsileLAVAIIQAYVFVLLLSLYLQE 225
Cdd:MTH00087 150 HLISSLLNFLGEKYVWLSILAIMME-----------CFVAFIQSYIFSRLIYLYLNE 195
 
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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