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Conserved domains on  [gi|767990256|ref|XP_011521527|]
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protein VAC14 homolog isoform X2 [Homo sapiens]

Protein Classification

HEAT repeat domain-containing protein( domain architecture ID 10579298)

HEAT repeat domain-containing protein may function as a scaffold, anchoring and/or adaptor protein

Gene Ontology:  GO:0005515
PubMed:  35552740|10378263
SCOP:  4001283

Graphical summary

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List of domain hits

 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 ...
 67-163 8.79e-57

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: 185.88  E-value: 8.79e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990256   67 HSRKGGLIGLAACSIALGKDSGLYLKELIEPVLTCFNDADSRLRYYACEALYNIVKVARGAVLPHFNVLFDGLSKLAADP 146
Cdd:pfam12755   1 NARKGGLIGLAATAIALGKDIAPYLDDIIPPVLACFSDQDSRVRYYACESLYNIAKVARGEVLPYFNDIFDGLCKLFADS 80

                          90
                  ....*....|....*..
gi 767990256  147 DPNVKSGSELLDRLLKD 163
Cdd:pfam12755  81 DPSVKNGAELLDRLLKD 97
 
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 ...
 67-163 8.79e-57

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: 185.88  E-value: 8.79e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990256   67 HSRKGGLIGLAACSIALGKDSGLYLKELIEPVLTCFNDADSRLRYYACEALYNIVKVARGAVLPHFNVLFDGLSKLAADP 146
Cdd:pfam12755   1 NARKGGLIGLAATAIALGKDIAPYLDDIIPPVLACFSDQDSRVRYYACESLYNIAKVARGEVLPYFNDIFDGLCKLFADS 80

                          90
                  ....*....|....*..
gi 767990256  147 DPNVKSGSELLDRLLKD 163
Cdd:pfam12755  81 DPSVKNGAELLDRLLKD 97
 
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 ...
 67-163 8.79e-57

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: 185.88  E-value: 8.79e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767990256   67 HSRKGGLIGLAACSIALGKDSGLYLKELIEPVLTCFNDADSRLRYYACEALYNIVKVARGAVLPHFNVLFDGLSKLAADP 146
Cdd:pfam12755   1 NARKGGLIGLAATAIALGKDIAPYLDDIIPPVLACFSDQDSRVRYYACESLYNIAKVARGEVLPYFNDIFDGLCKLFADS 80

                          90
                  ....*....|....*..
gi 767990256  147 DPNVKSGSELLDRLLKD 163
Cdd:pfam12755  81 DPSVKNGAELLDRLLKD 97
 
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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