NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1046880349|ref|XP_017447385|]
View 

palmitoyltransferase ZDHHC5 isoform X1 [Rattus norvegicus]

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 ...
 99-224 4.21e-42

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: 149.05  E-value: 4.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046880349  99 IQVRMKWCATCRFYRPPRCSHCSVCDNCVEEFDHHCPWVNNCIGRRNYRYFFLFLLSLT--AHIMGVFGFGLLYVLCHIE 176
Cdd:pfam01529   1 IFDELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTlyLILYLVLSLYYLVKLIESS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1046880349 177 ELSGVRTAVTMA----VMCVAGLFFIPVAGLTGFHVVLVARGRTTNEQVTGK 224
Cdd:pfam01529  81 TLFFFLILFLFSisiiLLILSLFFLLFLGILLFFHLYLISRNLTTYEFMKKK 132
 
Name Accession Description Interval E-value
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 99-224 4.21e-42

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: 149.05  E-value: 4.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046880349  99 IQVRMKWCATCRFYRPPRCSHCSVCDNCVEEFDHHCPWVNNCIGRRNYRYFFLFLLSLT--AHIMGVFGFGLLYVLCHIE 176
Cdd:pfam01529   1 IFDELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTlyLILYLVLSLYYLVKLIESS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1046880349 177 ELSGVRTAVTMA----VMCVAGLFFIPVAGLTGFHVVLVARGRTTNEQVTGK 224
Cdd:pfam01529  81 TLFFFLILFLFSisiiLLILSLFFLLFLGILLFFHLYLISRNLTTYEFMKKK 132
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
29-231 1.32e-34

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 134.11  E-value: 1.32e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046880349  29 TLFFAFtcpgLSLDVSPAVPIYNAImfLFVLANFSM--ATFMDPGIFPRAEEDEDKEDDFRAPLYKTVEIkgiqvRMKWC 106
Cdd:COG5273    44 TLLVIV----KSLSLVVLFIILFIV--ILVLASFSYllLLVSDPGYLGENITLSGYRETISRLLDDGKFG-----TENFC 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046880349 107 ATCRFYRPPRCSHCSVCDNCVEEFDHHCPWVNNCIGRRNYRYFFLFLLSLTAHIMGVFgfglLYVLCHIEELSGVRTAVT 186
Cdd:COG5273   113 STCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYTILVALVVL----LSTAYYIAGIFSIRHDTS 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1046880349 187 MAV-------MCVAGLFFIPVAGLTGFHVVLVARGRTTnEQVTGKFRGGVNP 231
Cdd:COG5273   189 LAIcflifgcSLLGVVFFIITTLLLLFLIYLILNNLTT-IEFIQISRGGSTL 239
 
Name Accession Description Interval E-value
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 99-224 4.21e-42

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: 149.05  E-value: 4.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046880349  99 IQVRMKWCATCRFYRPPRCSHCSVCDNCVEEFDHHCPWVNNCIGRRNYRYFFLFLLSLT--AHIMGVFGFGLLYVLCHIE 176
Cdd:pfam01529   1 IFDELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTlyLILYLVLSLYYLVKLIESS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1046880349 177 ELSGVRTAVTMA----VMCVAGLFFIPVAGLTGFHVVLVARGRTTNEQVTGK 224
Cdd:pfam01529  81 TLFFFLILFLFSisiiLLILSLFFLLFLGILLFFHLYLISRNLTTYEFMKKK 132
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
29-231 1.32e-34

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 134.11  E-value: 1.32e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046880349  29 TLFFAFtcpgLSLDVSPAVPIYNAImfLFVLANFSM--ATFMDPGIFPRAEEDEDKEDDFRAPLYKTVEIkgiqvRMKWC 106
Cdd:COG5273    44 TLLVIV----KSLSLVVLFIILFIV--ILVLASFSYllLLVSDPGYLGENITLSGYRETISRLLDDGKFG-----TENFC 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046880349 107 ATCRFYRPPRCSHCSVCDNCVEEFDHHCPWVNNCIGRRNYRYFFLFLLSLTAHIMGVFgfglLYVLCHIEELSGVRTAVT 186
Cdd:COG5273   113 STCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYTILVALVVL----LSTAYYIAGIFSIRHDTS 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1046880349 187 MAV-------MCVAGLFFIPVAGLTGFHVVLVARGRTTnEQVTGKFRGGVNP 231
Cdd:COG5273   189 LAIcflifgcSLLGVVFFIITTLLLLFLIYLILNNLTT-IEFIQISRGGSTL 239
 
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