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Conserved domains on  [gi|697890999|ref|XP_009690741|]
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HEAT repeat containing protein [Theileria orientalis strain Shintoku]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Vac14_Fig4_bd super family cl13369
Vacuolar protein 14 C-terminal Fig4p binding; Vac14 is a scaffold for the Fab1 kinase complex, ...
 476-662 3.08e-41

Vacuolar protein 14 C-terminal Fig4p binding; Vac14 is a scaffold for the Fab1 kinase complex, a complex that allows for the dynamic interconversion of PI3P and PI(3,5)P2p (phosphoinositide phosphate (PIP) lipids, that are generated transiently on the cytoplasmic face of selected intracellular membranes). This interconversion is regulated by at least five proteins in yeast: the lipid kinase Fab1p, lipid phosphatase Fig4p, the Fab1p activator Vac7p, the Fab1p inhibitor Atg18p, and Vac14p, a protein required for the activity of both Fab1p and Fig4p. The C-terminal region of Vac14 binds to Fig4p. The full length Vac14 in yeasts is likely to be a protein carrying a succession of HEAT repeats, most of which have now degenerated. This regulatory system is crucial for the proper functioning of the mammalian nervous system.


The actual alignment was detected with superfamily member pfam11916:

Pssm-ID: 463395  Cd Length: 179  Bit Score: 148.02  E-value: 3.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697890999  476 NLLEESGRVIVLNLCKQVGFERFYTIITNSMKLSNDKHFLNIMVHNLNWTLLTSVEAQEFRNAL---LTQEKRSLADQLQ 552
Cdd:pfam11916   2 RLLERRGSLIIRQLCLLLNAERIYRTLAEILEKEEDLEFASTMVQTLNTILLTSPELAELRNKLrnlDSEEDRELFSTLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697890999  553 EIWSFNSASALSFALWTEKYDLAQEIVNDISTSTLSIDFLVNLDQIVQLMDTHIFIRLRLHLLKPDVYPSLLKSllgkqk 632
Cdd:pfam11916  82 KSWCHNPVATLSLCLLAQAYEHAYNLLQSFGELEITVEFLVQIDKLVQLLESPVFTYLRLQLLEPEKYPYLYKC------ 155

                         170       180       190
                  ....*....|....*....|....*....|
gi 697890999  633 hiLYckyvvGLSMILPQNETNRNLMRRLNM 662
Cdd:pfam11916 156 --LY-----GLLMLLPQSSAFNTLRNRLQS 178
HEAT super family cl46509
HEAT repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see ...
 95-197 2.70e-36

HEAT repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514).


The actual alignment was detected with superfamily member pfam12755:

Pssm-ID: 480849  Cd Length: 97  Bit Score: 131.18  E-value: 2.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697890999   95 NYRIGGLMAVACAALALDKNLTRYSGSFIKQVLLSFYDQDIKVRYYACESLYNIIKKCKFESISCVDEIFDGICKnvrne 174
Cdd:pfam12755   1 NARKGGLIGLAATAIALGKDIAPYLDDIIPPVLACFSDQDSRVRYYACESLYNIAKVARGEVLPYFNDIFDGLCK----- 75

                          90       100
                  ....*....|....*....|...
gi 697890999  175 iqLTCDVDEDVKYASQMLNRLLC 197
Cdd:pfam12755  76 --LFADSDPSVKNGAELLDRLLK 96
 
Name Accession Description Interval E-value
Vac14_Fig4_bd pfam11916
Vacuolar protein 14 C-terminal Fig4p binding; Vac14 is a scaffold for the Fab1 kinase complex, ...
 476-662 3.08e-41

Vacuolar protein 14 C-terminal Fig4p binding; Vac14 is a scaffold for the Fab1 kinase complex, a complex that allows for the dynamic interconversion of PI3P and PI(3,5)P2p (phosphoinositide phosphate (PIP) lipids, that are generated transiently on the cytoplasmic face of selected intracellular membranes). This interconversion is regulated by at least five proteins in yeast: the lipid kinase Fab1p, lipid phosphatase Fig4p, the Fab1p activator Vac7p, the Fab1p inhibitor Atg18p, and Vac14p, a protein required for the activity of both Fab1p and Fig4p. The C-terminal region of Vac14 binds to Fig4p. The full length Vac14 in yeasts is likely to be a protein carrying a succession of HEAT repeats, most of which have now degenerated. This regulatory system is crucial for the proper functioning of the mammalian nervous system.


Pssm-ID: 463395  Cd Length: 179  Bit Score: 148.02  E-value: 3.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697890999  476 NLLEESGRVIVLNLCKQVGFERFYTIITNSMKLSNDKHFLNIMVHNLNWTLLTSVEAQEFRNAL---LTQEKRSLADQLQ 552
Cdd:pfam11916   2 RLLERRGSLIIRQLCLLLNAERIYRTLAEILEKEEDLEFASTMVQTLNTILLTSPELAELRNKLrnlDSEEDRELFSTLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697890999  553 EIWSFNSASALSFALWTEKYDLAQEIVNDISTSTLSIDFLVNLDQIVQLMDTHIFIRLRLHLLKPDVYPSLLKSllgkqk 632
Cdd:pfam11916  82 KSWCHNPVATLSLCLLAQAYEHAYNLLQSFGELEITVEFLVQIDKLVQLLESPVFTYLRLQLLEPEKYPYLYKC------ 155

                         170       180       190
                  ....*....|....*....|....*....|
gi 697890999  633 hiLYckyvvGLSMILPQNETNRNLMRRLNM 662
Cdd:pfam11916 156 --LY-----GLLMLLPQSSAFNTLRNRLQS 178
Vac14_Fab1_bd pfam12755
Vacuolar 14 Fab1-binding region; Vac14 is a scaffold for the Fab1 kinase complex, a complex ...
 95-197 2.70e-36

Vacuolar 14 Fab1-binding region; Vac14 is a scaffold for the Fab1 kinase complex, a complex that allows for the dynamic interconversion of PI3P and PI(3,5)P2p (phosphoinositide phosphate (PIP) lipids, that are generated transiently on the cytoplasmic face of selected intracellular membranes). This interconversion is regulated by at least five proteins in yeast: the lipid kinase Fab1p, lipid phosphatase Fig4p, the Fab1p activator Vac7p, the Fab1p inhibitor Atg18p, and Vac14p, a protein required for the activity of both Fab1p and Fig4p. This domain appears to be the one responsible for binding to Fab1. The full length Vac14 in yeasts is likely to be a protein carrying a succession of HEAT repeats, most of which have now degenerated. This regulatory system is crucial for the proper functioning of the mammalian nervous system.


Pssm-ID: 403838  Cd Length: 97  Bit Score: 131.18  E-value: 2.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697890999   95 NYRIGGLMAVACAALALDKNLTRYSGSFIKQVLLSFYDQDIKVRYYACESLYNIIKKCKFESISCVDEIFDGICKnvrne 174
Cdd:pfam12755   1 NARKGGLIGLAATAIALGKDIAPYLDDIIPPVLACFSDQDSRVRYYACESLYNIAKVARGEVLPYFNDIFDGLCK----- 75

                          90       100
                  ....*....|....*....|...
gi 697890999  175 iqLTCDVDEDVKYASQMLNRLLC 197
Cdd:pfam12755  76 --LFADSDPSVKNGAELLDRLLK 96
 
Name Accession Description Interval E-value
Vac14_Fig4_bd pfam11916
Vacuolar protein 14 C-terminal Fig4p binding; Vac14 is a scaffold for the Fab1 kinase complex, ...
 476-662 3.08e-41

Vacuolar protein 14 C-terminal Fig4p binding; Vac14 is a scaffold for the Fab1 kinase complex, a complex that allows for the dynamic interconversion of PI3P and PI(3,5)P2p (phosphoinositide phosphate (PIP) lipids, that are generated transiently on the cytoplasmic face of selected intracellular membranes). This interconversion is regulated by at least five proteins in yeast: the lipid kinase Fab1p, lipid phosphatase Fig4p, the Fab1p activator Vac7p, the Fab1p inhibitor Atg18p, and Vac14p, a protein required for the activity of both Fab1p and Fig4p. The C-terminal region of Vac14 binds to Fig4p. The full length Vac14 in yeasts is likely to be a protein carrying a succession of HEAT repeats, most of which have now degenerated. This regulatory system is crucial for the proper functioning of the mammalian nervous system.


Pssm-ID: 463395  Cd Length: 179  Bit Score: 148.02  E-value: 3.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697890999  476 NLLEESGRVIVLNLCKQVGFERFYTIITNSMKLSNDKHFLNIMVHNLNWTLLTSVEAQEFRNAL---LTQEKRSLADQLQ 552
Cdd:pfam11916   2 RLLERRGSLIIRQLCLLLNAERIYRTLAEILEKEEDLEFASTMVQTLNTILLTSPELAELRNKLrnlDSEEDRELFSTLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697890999  553 EIWSFNSASALSFALWTEKYDLAQEIVNDISTSTLSIDFLVNLDQIVQLMDTHIFIRLRLHLLKPDVYPSLLKSllgkqk 632
Cdd:pfam11916  82 KSWCHNPVATLSLCLLAQAYEHAYNLLQSFGELEITVEFLVQIDKLVQLLESPVFTYLRLQLLEPEKYPYLYKC------ 155

                         170       180       190
                  ....*....|....*....|....*....|
gi 697890999  633 hiLYckyvvGLSMILPQNETNRNLMRRLNM 662
Cdd:pfam11916 156 --LY-----GLLMLLPQSSAFNTLRNRLQS 178
Vac14_Fab1_bd pfam12755
Vacuolar 14 Fab1-binding region; Vac14 is a scaffold for the Fab1 kinase complex, a complex ...
 95-197 2.70e-36

Vacuolar 14 Fab1-binding region; Vac14 is a scaffold for the Fab1 kinase complex, a complex that allows for the dynamic interconversion of PI3P and PI(3,5)P2p (phosphoinositide phosphate (PIP) lipids, that are generated transiently on the cytoplasmic face of selected intracellular membranes). This interconversion is regulated by at least five proteins in yeast: the lipid kinase Fab1p, lipid phosphatase Fig4p, the Fab1p activator Vac7p, the Fab1p inhibitor Atg18p, and Vac14p, a protein required for the activity of both Fab1p and Fig4p. This domain appears to be the one responsible for binding to Fab1. The full length Vac14 in yeasts is likely to be a protein carrying a succession of HEAT repeats, most of which have now degenerated. This regulatory system is crucial for the proper functioning of the mammalian nervous system.


Pssm-ID: 403838  Cd Length: 97  Bit Score: 131.18  E-value: 2.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697890999   95 NYRIGGLMAVACAALALDKNLTRYSGSFIKQVLLSFYDQDIKVRYYACESLYNIIKKCKFESISCVDEIFDGICKnvrne 174
Cdd:pfam12755   1 NARKGGLIGLAATAIALGKDIAPYLDDIIPPVLACFSDQDSRVRYYACESLYNIAKVARGEVLPYFNDIFDGLCK----- 75

                          90       100
                  ....*....|....*....|...
gi 697890999  175 iqLTCDVDEDVKYASQMLNRLLC 197
Cdd:pfam12755  76 --LFADSDPSVKNGAELLDRLLK 96
 
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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