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Conserved domains on  [gi|398366065|ref|NP_013490|]
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Vac14p [Saccharomyces cerevisiae S288C]

Protein Classification

VAC14 family protein( domain architecture ID 10579327)

VAC14 family protein similar to Saccharomyces cerevisiae vacuole morphology and inheritance protein 14 (VAC14) that is a component of the PI(3,5)P2 regulatory complex that regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate

Gene Ontology:  GO:0070772|GO:0006661|GO:0005515
PubMed:  23389034|19037259|35552740|10378263
SCOP:  4001283

Graphical summary

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List of domain hits

 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, ...
 573-746 2.00e-88

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: 278.21  E-value: 2.00e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366065  573 KLVKTRANFIMRQISSRLSPERVYKVISSILDNYNDTTFVKMMIQILSTNLITSPEMSSLRNKLR---TCEDGMFFNSLF 649
Cdd:pfam11916   2 RLLERRGSLIIRQLCLLLNAERIYRTLAEILEKEEDLEFASTMVQTLNTILLTSPELAELRNKLRnldSEEDRELFSTLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366065  650 KSWCPNPVSVISLCFVAENYELAYTVLQTYANYELKLNDLVQLDILIQLFESPVFTRMRLQLLEQQKHPFLHKCLFGILM 729
Cdd:pfam11916  82 KSWCHNPVATLSLCLLAQAYEHAYNLLQSFGELEITVEFLVQIDKLVQLLESPVFTYLRLQLLEPEKYPYLYKCLYGLLM 161

                         170
                  ....*....|....*..
gi 398366065  730 IIPQSKAFETLNRRLNS 746
Cdd:pfam11916 162 LLPQSSAFNTLRNRLQS 178
Vac14_Fab1_bd pfam12755
Vacuolar 14 Fab1-binding region; Vac14 is a scaffold for the Fab1 kinase complex, a complex ...
 59-156 5.61e-48

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: 165.08  E-value: 5.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366065   59 MARNAGLMGLAATAIALGiNDVGRYLRNILPPVLACFGDQNDQVRFYACESLYNIAKIAKGEILVYFNEIFDVLCKISAD 138
Cdd:pfam12755   1 NARKGGLIGLAATAIALG-KDIAPYLDDIIPPVLACFSDQDSRVRYYACESLYNIAKVARGEVLPYFNDIFDGLCKLFAD 79

                          90
                  ....*....|....*...
gi 398366065  139 TENSVRGAAELLDRLIKD 156
Cdd:pfam12755  80 SDPSVKNGAELLDRLLKD 97
 
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, ...
 573-746 2.00e-88

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: 278.21  E-value: 2.00e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366065  573 KLVKTRANFIMRQISSRLSPERVYKVISSILDNYNDTTFVKMMIQILSTNLITSPEMSSLRNKLR---TCEDGMFFNSLF 649
Cdd:pfam11916   2 RLLERRGSLIIRQLCLLLNAERIYRTLAEILEKEEDLEFASTMVQTLNTILLTSPELAELRNKLRnldSEEDRELFSTLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366065  650 KSWCPNPVSVISLCFVAENYELAYTVLQTYANYELKLNDLVQLDILIQLFESPVFTRMRLQLLEQQKHPFLHKCLFGILM 729
Cdd:pfam11916  82 KSWCHNPVATLSLCLLAQAYEHAYNLLQSFGELEITVEFLVQIDKLVQLLESPVFTYLRLQLLEPEKYPYLYKCLYGLLM 161

                         170
                  ....*....|....*..
gi 398366065  730 IIPQSKAFETLNRRLNS 746
Cdd:pfam11916 162 LLPQSSAFNTLRNRLQS 178
Vac14_Fab1_bd pfam12755
Vacuolar 14 Fab1-binding region; Vac14 is a scaffold for the Fab1 kinase complex, a complex ...
 59-156 5.61e-48

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: 165.08  E-value: 5.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366065   59 MARNAGLMGLAATAIALGiNDVGRYLRNILPPVLACFGDQNDQVRFYACESLYNIAKIAKGEILVYFNEIFDVLCKISAD 138
Cdd:pfam12755   1 NARKGGLIGLAATAIALG-KDIAPYLDDIIPPVLACFSDQDSRVRYYACESLYNIAKVARGEVLPYFNDIFDGLCKLFAD 79

                          90
                  ....*....|....*...
gi 398366065  139 TENSVRGAAELLDRLIKD 156
Cdd:pfam12755  80 SDPSVKNGAELLDRLLKD 97
 
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, ...
 573-746 2.00e-88

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: 278.21  E-value: 2.00e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366065  573 KLVKTRANFIMRQISSRLSPERVYKVISSILDNYNDTTFVKMMIQILSTNLITSPEMSSLRNKLR---TCEDGMFFNSLF 649
Cdd:pfam11916   2 RLLERRGSLIIRQLCLLLNAERIYRTLAEILEKEEDLEFASTMVQTLNTILLTSPELAELRNKLRnldSEEDRELFSTLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366065  650 KSWCPNPVSVISLCFVAENYELAYTVLQTYANYELKLNDLVQLDILIQLFESPVFTRMRLQLLEQQKHPFLHKCLFGILM 729
Cdd:pfam11916  82 KSWCHNPVATLSLCLLAQAYEHAYNLLQSFGELEITVEFLVQIDKLVQLLESPVFTYLRLQLLEPEKYPYLYKCLYGLLM 161

                         170
                  ....*....|....*..
gi 398366065  730 IIPQSKAFETLNRRLNS 746
Cdd:pfam11916 162 LLPQSSAFNTLRNRLQS 178
Vac14_Fab1_bd pfam12755
Vacuolar 14 Fab1-binding region; Vac14 is a scaffold for the Fab1 kinase complex, a complex ...
 59-156 5.61e-48

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: 165.08  E-value: 5.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366065   59 MARNAGLMGLAATAIALGiNDVGRYLRNILPPVLACFGDQNDQVRFYACESLYNIAKIAKGEILVYFNEIFDVLCKISAD 138
Cdd:pfam12755   1 NARKGGLIGLAATAIALG-KDIAPYLDDIIPPVLACFSDQDSRVRYYACESLYNIAKVARGEVLPYFNDIFDGLCKLFAD 79

                          90
                  ....*....|....*...
gi 398366065  139 TENSVRGAAELLDRLIKD 156
Cdd:pfam12755  80 SDPSVKNGAELLDRLLKD 97
HEAT pfam02985
HEAT repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see ...
 87-117 5.89e-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: 5.89e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 398366065   87 ILPPVLACFGDQNDQVRFYACESLYNIAKIA 117
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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