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Conserved domains on  [gi|754348059|ref|XP_011270415|]
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hypothetical protein CAOG_08785 [Capsaspora owczarzaki ATCC 30864]

Protein Classification

alternative oxidase( domain architecture ID 10484894)

alternative oxidase from plant mitochondria, some fungi, and protists, is a terminal oxidase that is not sensitive to cyanide inhibition and does not generate a proton motive force; may function to reoxidize reducing equivalents produced by glycolysis such as ubiquinol

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AOX pfam01786
Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the ...
 150-364 3.40e-136

Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the mitochondria, electrons are transfered directly from reduced ubiquinol to oxygen forming water. This is not coupled to ATP synthesis and is not inhibited by cyanide, this pathway is a single step process. In rice the transcript levels of the alternative oxidase are increased by low temperature.


:

Pssm-ID: 460328  Cd Length: 218  Bit Score: 387.29  E-value: 3.40e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348059  150 WTKEELSQVELTHHKPDNLVDWTAFAAIKCIRLGFDVLSGFAF---GERTPDKWLTRIIFLETVAAVPGMVGAMIRHLQS 226
Cdd:pfam01786   1 YTEEELESVKLTHREPKTFSDKVAYGLVKFLRWLFDLLTGYKHpppPEMTERKWLHRAIFLETVAGVPGMVAGMLRHLRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348059  227 LRLMRRDHGWIHTLLEEAENERMHLLTALQLKQPSQLFRLAVLAVQGVMTNTFFFLYILAPRFVHRFVGYLEEEAVYTYT 306
Cdd:pfam01786  81 LRLMKRDNGWIHTLLEEAENERMHLLTFLKLAKPGWFERLLVLGAQGVFFNAFFLLYLISPRTCHRFVGYLEEEAVITYT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 754348059  307 KCLDDIKTGKLPEWKTGKAPEIAINYWKLDKAATMEDVIYAIRSDEAHHRLVNHTFAN 364
Cdd:pfam01786 161 HAIEDIDAGKLPNWENMPAPEIAIDYWGLPEDATLRDLILAIRADEAKHRDVNHTLAN 218
 
Name Accession Description Interval E-value
AOX pfam01786
Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the ...
 150-364 3.40e-136

Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the mitochondria, electrons are transfered directly from reduced ubiquinol to oxygen forming water. This is not coupled to ATP synthesis and is not inhibited by cyanide, this pathway is a single step process. In rice the transcript levels of the alternative oxidase are increased by low temperature.


Pssm-ID: 460328  Cd Length: 218  Bit Score: 387.29  E-value: 3.40e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348059  150 WTKEELSQVELTHHKPDNLVDWTAFAAIKCIRLGFDVLSGFAF---GERTPDKWLTRIIFLETVAAVPGMVGAMIRHLQS 226
Cdd:pfam01786   1 YTEEELESVKLTHREPKTFSDKVAYGLVKFLRWLFDLLTGYKHpppPEMTERKWLHRAIFLETVAGVPGMVAGMLRHLRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348059  227 LRLMRRDHGWIHTLLEEAENERMHLLTALQLKQPSQLFRLAVLAVQGVMTNTFFFLYILAPRFVHRFVGYLEEEAVYTYT 306
Cdd:pfam01786  81 LRLMKRDNGWIHTLLEEAENERMHLLTFLKLAKPGWFERLLVLGAQGVFFNAFFLLYLISPRTCHRFVGYLEEEAVITYT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 754348059  307 KCLDDIKTGKLPEWKTGKAPEIAINYWKLDKAATMEDVIYAIRSDEAHHRLVNHTFAN 364
Cdd:pfam01786 161 HAIEDIDAGKLPNWENMPAPEIAIDYWGLPEDATLRDLILAIRADEAKHRDVNHTLAN 218
AOX cd01053
Alternative oxidase, ferritin-like diiron-binding domain; Alternative oxidase (AOX) is a ...
 196-366 6.77e-91

Alternative oxidase, ferritin-like diiron-binding domain; Alternative oxidase (AOX) is a mitochondrial ubiquinol oxidase found in plants and some fungi and protists. AOX is a member of the ferritin-like diiron-carboxylate superfamily. The plant mitochondrial protein alternative oxidase catalyses dioxygen dependent ubiquinol oxidation to yield ubiquinone and water. AOX is a cyanide-resistant, salicylhydroxamic acid-sensitive oxidase that transfers electrons from ubiquinol to oxygen, bypassing the cytochrome chain. AOX has been proposed to contain a hydroxo-bridged diiron center within a four-helix bundle and a proximal redox-active tyrosine residue. AOX is proposed to be peripherally associated with the matrix side of the inner mitochondrial membrane. Fungal and protozoan AOXs generally exist as monomers. In plants, AOX is dimeric. Pyruvate is an allosteric activator of plant AOX involved in the reversible inactivation of the enzyme though the formation of an intermolecular disulfide bridge between monomeric subunits. The enzyme is non-proton-motive and does not contribute to the conservation of energy. The heat that dissipates from AOX activity is used in thermogenic plants to volatilize primary amines to attract pollinating insects. Other functions have been proposed: i) that the alternative oxidase allows Krebs-cycle turnover when the energy charge of the cell is high, and ii) that the enzyme protects against oxidative stress. The expression of AOX is induced when plants are exposed to a variety of stresses including chilling, pathogen attack, senescence and fruit ripening.


Pssm-ID: 153112  Cd Length: 168  Bit Score: 270.23  E-value: 6.77e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348059 196 TPDKWLTRIIFLETVAAVPGMVGAMIRHLQSLRLMRRDHGWIHTLLEEAENERMHLLTALQLKQPSQLFRLAVLAVQGVM 275
Cdd:cd01053    1 YEDRWLARFIFLETVARVPGMVAGMLLHLYSLRGMWRDGGWIKTLLEEAENERMHLLIFEELGGPGWWFRRFVAQHQAVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348059 276 TNTFFFLYILAPRFVHRFVGYLEEEAVYTYTKCLDDIKTGKLPewkTGKAPEIAINYWKLDKAATMEDVIYAIRSDEAHH 355
Cdd:cd01053   81 YNAYFLLYLISPRLAHRFVGYLEEEAVDTYTEFLKDIEEGLKP---DLPAPEIAIEYYRLGEDATLYDVFVAIRADEAEH 157

                        170
                 ....*....|.
gi 754348059 356 RLVNHTFANLH 366
Cdd:cd01053  158 RKVNHACADLG 168
PLN02478 PLN02478
alternative oxidase
 162-370 3.26e-74

alternative oxidase


Pssm-ID: 215265  Cd Length: 328  Bit Score: 233.64  E-value: 3.26e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348059 162 HHKPDNLVDWTAFAAIKCIRLGFDVlsgfaFGERtpdKWLTRIIFLETVAAVPGMVGAMIRHLQSLRLMRRDHGWIHTLL 241
Cdd:PLN02478 119 HHVPKTLLDKIAYWTVKSLRVPTDL-----FFQR---RYGCRAMMLETVAAVPGMVGGMLLHLKSLRRFEHSGGWIKALL 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348059 242 EEAENERMHLLTALQLKQPSQLFRLAVLAVQGVMTNTFFFLYILAPRFVHRFVGYLEEEAVYTYTKCLDDIKTGKLpewK 321
Cdd:PLN02478 191 EEAENERMHLMTFMEVAKPKWYERALVIAVQGVFFNAYFLGYLISPKFAHRIVGYLEEEAIHSYTEFLKDLDAGKI---E 267

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 754348059 322 TGKAPEIAINYWKLDKAATMEDVIYAIRSDEAHHRLVNHTFANLHQLGQ 370
Cdd:PLN02478 268 NVPAPAIAIDYWRLPADATLRDVVTVVRADEAHHRDVNHFASDIHYQGK 316
 
Name Accession Description Interval E-value
AOX pfam01786
Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the ...
 150-364 3.40e-136

Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the mitochondria, electrons are transfered directly from reduced ubiquinol to oxygen forming water. This is not coupled to ATP synthesis and is not inhibited by cyanide, this pathway is a single step process. In rice the transcript levels of the alternative oxidase are increased by low temperature.


Pssm-ID: 460328  Cd Length: 218  Bit Score: 387.29  E-value: 3.40e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348059  150 WTKEELSQVELTHHKPDNLVDWTAFAAIKCIRLGFDVLSGFAF---GERTPDKWLTRIIFLETVAAVPGMVGAMIRHLQS 226
Cdd:pfam01786   1 YTEEELESVKLTHREPKTFSDKVAYGLVKFLRWLFDLLTGYKHpppPEMTERKWLHRAIFLETVAGVPGMVAGMLRHLRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348059  227 LRLMRRDHGWIHTLLEEAENERMHLLTALQLKQPSQLFRLAVLAVQGVMTNTFFFLYILAPRFVHRFVGYLEEEAVYTYT 306
Cdd:pfam01786  81 LRLMKRDNGWIHTLLEEAENERMHLLTFLKLAKPGWFERLLVLGAQGVFFNAFFLLYLISPRTCHRFVGYLEEEAVITYT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 754348059  307 KCLDDIKTGKLPEWKTGKAPEIAINYWKLDKAATMEDVIYAIRSDEAHHRLVNHTFAN 364
Cdd:pfam01786 161 HAIEDIDAGKLPNWENMPAPEIAIDYWGLPEDATLRDLILAIRADEAKHRDVNHTLAN 218
AOX cd01053
Alternative oxidase, ferritin-like diiron-binding domain; Alternative oxidase (AOX) is a ...
 196-366 6.77e-91

Alternative oxidase, ferritin-like diiron-binding domain; Alternative oxidase (AOX) is a mitochondrial ubiquinol oxidase found in plants and some fungi and protists. AOX is a member of the ferritin-like diiron-carboxylate superfamily. The plant mitochondrial protein alternative oxidase catalyses dioxygen dependent ubiquinol oxidation to yield ubiquinone and water. AOX is a cyanide-resistant, salicylhydroxamic acid-sensitive oxidase that transfers electrons from ubiquinol to oxygen, bypassing the cytochrome chain. AOX has been proposed to contain a hydroxo-bridged diiron center within a four-helix bundle and a proximal redox-active tyrosine residue. AOX is proposed to be peripherally associated with the matrix side of the inner mitochondrial membrane. Fungal and protozoan AOXs generally exist as monomers. In plants, AOX is dimeric. Pyruvate is an allosteric activator of plant AOX involved in the reversible inactivation of the enzyme though the formation of an intermolecular disulfide bridge between monomeric subunits. The enzyme is non-proton-motive and does not contribute to the conservation of energy. The heat that dissipates from AOX activity is used in thermogenic plants to volatilize primary amines to attract pollinating insects. Other functions have been proposed: i) that the alternative oxidase allows Krebs-cycle turnover when the energy charge of the cell is high, and ii) that the enzyme protects against oxidative stress. The expression of AOX is induced when plants are exposed to a variety of stresses including chilling, pathogen attack, senescence and fruit ripening.


Pssm-ID: 153112  Cd Length: 168  Bit Score: 270.23  E-value: 6.77e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348059 196 TPDKWLTRIIFLETVAAVPGMVGAMIRHLQSLRLMRRDHGWIHTLLEEAENERMHLLTALQLKQPSQLFRLAVLAVQGVM 275
Cdd:cd01053    1 YEDRWLARFIFLETVARVPGMVAGMLLHLYSLRGMWRDGGWIKTLLEEAENERMHLLIFEELGGPGWWFRRFVAQHQAVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348059 276 TNTFFFLYILAPRFVHRFVGYLEEEAVYTYTKCLDDIKTGKLPewkTGKAPEIAINYWKLDKAATMEDVIYAIRSDEAHH 355
Cdd:cd01053   81 YNAYFLLYLISPRLAHRFVGYLEEEAVDTYTEFLKDIEEGLKP---DLPAPEIAIEYYRLGEDATLYDVFVAIRADEAEH 157

                        170
                 ....*....|.
gi 754348059 356 RLVNHTFANLH 366
Cdd:cd01053  158 RKVNHACADLG 168
PLN02478 PLN02478
alternative oxidase
 162-370 3.26e-74

alternative oxidase


Pssm-ID: 215265  Cd Length: 328  Bit Score: 233.64  E-value: 3.26e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348059 162 HHKPDNLVDWTAFAAIKCIRLGFDVlsgfaFGERtpdKWLTRIIFLETVAAVPGMVGAMIRHLQSLRLMRRDHGWIHTLL 241
Cdd:PLN02478 119 HHVPKTLLDKIAYWTVKSLRVPTDL-----FFQR---RYGCRAMMLETVAAVPGMVGGMLLHLKSLRRFEHSGGWIKALL 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754348059 242 EEAENERMHLLTALQLKQPSQLFRLAVLAVQGVMTNTFFFLYILAPRFVHRFVGYLEEEAVYTYTKCLDDIKTGKLpewK 321
Cdd:PLN02478 191 EEAENERMHLMTFMEVAKPKWYERALVIAVQGVFFNAYFLGYLISPKFAHRIVGYLEEEAIHSYTEFLKDLDAGKI---E 267

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 754348059 322 TGKAPEIAINYWKLDKAATMEDVIYAIRSDEAHHRLVNHTFANLHQLGQ 370
Cdd:PLN02478 268 NVPAPAIAIDYWRLPADATLRDVVTVVRADEAHHRDVNHFASDIHYQGK 316
 
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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