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Conserved domains on  [gi|1276850349|gb|PIO76785|]
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HEAT repeat protein [Teladorsagia circumcincta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HEAT super family cl46509
HEAT repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see ...
 83-161 4.09e-39

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: 4.09e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276850349  83 KNAPPYTVHLIEPVLSCFNDPDLRVRYYACESLYNIVKICKIAVLSHFDQLFDVLWKLSADTDQNVRSGAELLDRLLMD 161
Cdd:pfam12755  19 KDIAPYLDDIIPPVLACFSDQDSRVRYYACESLYNIAKVARGEVLPYFNDIFDGLCKLFADSDPSVKNGAELLDRLLKD 97
Vac14_Fig4_bd super family cl13369
Vacuolar protein 14 C-terminal Fig4p binding; Vac14 is a scaffold for the Fab1 kinase complex, ...
 197-220 2.76e-04

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: 40.54  E-value: 2.76e-04
                          10        20
                  ....*....|....*....|....
gi 1276850349 197 VDMTLDVLVEIDKLVNMIESPVLA 220
Cdd:pfam11916 114 LEITVEFLVQIDKLVQLLESPVFT 137
 
Name Accession Description Interval E-value
Vac14_Fab1_bd pfam12755
Vacuolar 14 Fab1-binding region; Vac14 is a scaffold for the Fab1 kinase complex, a complex ...
 83-161 4.09e-39

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: 4.09e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276850349  83 KNAPPYTVHLIEPVLSCFNDPDLRVRYYACESLYNIVKICKIAVLSHFDQLFDVLWKLSADTDQNVRSGAELLDRLLMD 161
Cdd:pfam12755  19 KDIAPYLDDIIPPVLACFSDQDSRVRYYACESLYNIAKVARGEVLPYFNDIFDGLCKLFADSDPSVKNGAELLDRLLKD 97
Vac14_Fig4_bd pfam11916
Vacuolar protein 14 C-terminal Fig4p binding; Vac14 is a scaffold for the Fab1 kinase complex, ...
 197-220 2.76e-04

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: 40.54  E-value: 2.76e-04
                          10        20
                  ....*....|....*....|....
gi 1276850349 197 VDMTLDVLVEIDKLVNMIESPVLA 220
Cdd:pfam11916 114 LEITVEFLVQIDKLVQLLESPVFT 137
 
Name Accession Description Interval E-value
Vac14_Fab1_bd pfam12755
Vacuolar 14 Fab1-binding region; Vac14 is a scaffold for the Fab1 kinase complex, a complex ...
 83-161 4.09e-39

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: 4.09e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276850349  83 KNAPPYTVHLIEPVLSCFNDPDLRVRYYACESLYNIVKICKIAVLSHFDQLFDVLWKLSADTDQNVRSGAELLDRLLMD 161
Cdd:pfam12755  19 KDIAPYLDDIIPPVLACFSDQDSRVRYYACESLYNIAKVARGEVLPYFNDIFDGLCKLFADSDPSVKNGAELLDRLLKD 97
Vac14_Fig4_bd pfam11916
Vacuolar protein 14 C-terminal Fig4p binding; Vac14 is a scaffold for the Fab1 kinase complex, ...
 197-220 2.76e-04

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: 40.54  E-value: 2.76e-04
                          10        20
                  ....*....|....*....|....
gi 1276850349 197 VDMTLDVLVEIDKLVNMIESPVLA 220
Cdd:pfam11916 114 LEITVEFLVQIDKLVQLLESPVFT 137
HEAT pfam02985
HEAT repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see ...
 92-122 1.34e-03

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


Pssm-ID: 460773  Cd Length: 31  Bit Score: 35.20  E-value: 1.34e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1276850349  92 LIEPVLSCFNDPDLRVRYYACESLYNIVKIC 122
Cdd:pfam02985   1 LLPLLLKLLNDPSPEVREAAAEALGELAEVL 31
 
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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