NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1699951380|ref|NP_001358221|]
View 

palmitoyltransferase ZDHHC4 isoform a [Homo sapiens]

Protein Classification

DHHC family palmitoyltransferase( domain architecture ID 10479004)

DHHC family palmitoyltransferase may catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes

EC:  2.3.1.-
Gene Ontology:  GO:0016409|GO:0043543|GO:0016747
PubMed:  21388813|32522557|21204476

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 151-307 4.20e-25

DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.


:

Pssm-ID: 396215  Cd Length: 132  Bit Score: 98.59  E-value: 4.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699951380 151 CSTCDLRKPARSKHCSECGSrdssgtsnstcvcnwCVHRFDHHCVWVNNCIGAWNIRYFLIYVLTLTASAATVAIVSTTF 230
Cdd:pfam01529   8 CSTCNIYKPPRSKHCRVCNR---------------CVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYY 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699951380 231 LVHLVVMSDLYQETYIDdlghlhvmdtvfliqylflTFPRIVFMLGFVVVLSFLLGGYLLFVLYLAATNQTTNEWYR 307
Cdd:pfam01529  73 LVKLIESSTLFFFLILF-------------------LFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFMK 130
 
Name Accession Description Interval E-value
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 151-307 4.20e-25

DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.


Pssm-ID: 396215  Cd Length: 132  Bit Score: 98.59  E-value: 4.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699951380 151 CSTCDLRKPARSKHCSECGSrdssgtsnstcvcnwCVHRFDHHCVWVNNCIGAWNIRYFLIYVLTLTASAATVAIVSTTF 230
Cdd:pfam01529   8 CSTCNIYKPPRSKHCRVCNR---------------CVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYY 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699951380 231 LVHLVVMSDLYQETYIDdlghlhvmdtvfliqylflTFPRIVFMLGFVVVLSFLLGGYLLFVLYLAATNQTTNEWYR 307
Cdd:pfam01529  73 LVKLIESSTLFFFLILF-------------------LFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFMK 130
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
109-310 4.90e-19

Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 86.34  E-value: 4.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699951380 109 GVNLFFFTLTCGTNPGIITKANELLflHVYEFDE--VMFPKNVR---CSTCDLRKPARSKHCSECgsrdssgtsnstcvc 183
Cdd:COG5273    67 VLASFSYLLLLVSDPGYLGENITLS--GYRETISrlLDDGKFGTenfCSTCNIYKPPRSHHCSIC--------------- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699951380 184 NWCVHRFDHHCVWVNNCIGAWNIRYFLIYVLTlTASAATVAIVSTtflvhlvvmsdLYQETYIDDLGHlhvmDTVFLIQY 263
Cdd:COG5273   130 NRCVLKFDHHCPWINNCVGFRNYRFFYQFLLY-TILVALVVLLST-----------AYYIAGIFSIRH----DTSLAICF 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1699951380 264 LFLTFPrivfmlGFVVVLSFLLGGYLLFVLYLAATNQTTNEWYRGDW 310
Cdd:COG5273   194 LIFGCS------LLGVVFFIITTLLLLFLIYLILNNLTTIEFIQISR 234
 
Name Accession Description Interval E-value
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 151-307 4.20e-25

DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.


Pssm-ID: 396215  Cd Length: 132  Bit Score: 98.59  E-value: 4.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699951380 151 CSTCDLRKPARSKHCSECGSrdssgtsnstcvcnwCVHRFDHHCVWVNNCIGAWNIRYFLIYVLTLTASAATVAIVSTTF 230
Cdd:pfam01529   8 CSTCNIYKPPRSKHCRVCNR---------------CVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYY 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1699951380 231 LVHLVVMSDLYQETYIDdlghlhvmdtvfliqylflTFPRIVFMLGFVVVLSFLLGGYLLFVLYLAATNQTTNEWYR 307
Cdd:pfam01529  73 LVKLIESSTLFFFLILF-------------------LFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFMK 130
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
109-310 4.90e-19

Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 86.34  E-value: 4.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699951380 109 GVNLFFFTLTCGTNPGIITKANELLflHVYEFDE--VMFPKNVR---CSTCDLRKPARSKHCSECgsrdssgtsnstcvc 183
Cdd:COG5273    67 VLASFSYLLLLVSDPGYLGENITLS--GYRETISrlLDDGKFGTenfCSTCNIYKPPRSHHCSIC--------------- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1699951380 184 NWCVHRFDHHCVWVNNCIGAWNIRYFLIYVLTlTASAATVAIVSTtflvhlvvmsdLYQETYIDDLGHlhvmDTVFLIQY 263
Cdd:COG5273   130 NRCVLKFDHHCPWINNCVGFRNYRFFYQFLLY-TILVALVVLLST-----------AYYIAGIFSIRH----DTSLAICF 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1699951380 264 LFLTFPrivfmlGFVVVLSFLLGGYLLFVLYLAATNQTTNEWYRGDW 310
Cdd:COG5273   194 LIFGCS------LLGVVFFIITTLLLLFLIYLILNNLTTIEFIQISR 234
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH