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Conserved domains on  [gi|1622198061|ref|XP_028571791|]
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palmitoyltransferase ZDHHC9 isoform X1 [Podarcis muralis]

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

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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 ...
 138-261 9.04e-43

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: 145.59  E-value: 9.04e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622198061 138 LKYCYTCKIFRPPRASHCSICDNCVERFDHHCPWVGNCVGKRNYRYFYLFILSLSLLTIY--IFSFNIVYVALKSLKIGF 215
Cdd:pfam01529   5 LKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILylVLSLYYLVKLIESSTLFF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622198061 216 LNTLKETPGTVLEVLICFFTLWSVVGLTGFHTFLVALNQTTNEDIK 261
Cdd:pfam01529  85 FLILFLFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFMK 130
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 289-371 5.39e-04

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622198061  289 GPLPPSVLDRRGILQQESAALESSAGPEPNTqEEGTTEKPSAQETSGDSALP----EESALPVPTGKVPQETAQPPSAAE 364
Cdd:PHA03307   125 SPPPSPAPDLSEMLRPVGSPGPPPAASPPAA-GASPAAVASDAASSRQAALPlsspEETARAPSSPPAEPPPSTPPAAAS 203


                   ....*..
gi 1622198061  365 PSVPSLD 371
Cdd:PHA03307   204 PRPPRRS 210
 
Name Accession Description Interval E-value
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 138-261 9.04e-43

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: 145.59  E-value: 9.04e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622198061 138 LKYCYTCKIFRPPRASHCSICDNCVERFDHHCPWVGNCVGKRNYRYFYLFILSLSLLTIY--IFSFNIVYVALKSLKIGF 215
Cdd:pfam01529   5 LKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILylVLSLYYLVKLIESSTLFF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622198061 216 LNTLKETPGTVLEVLICFFTLWSVVGLTGFHTFLVALNQTTNEDIK 261
Cdd:pfam01529  85 FLILFLFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFMK 130
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
17-268 3.52e-40

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 144.51  E-value: 3.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622198061  17 LPGRNTFCCDGRIMMARqkGIFYLTLFLIVGTCalFFAFECRYLAVHLSPTIPV-FGAVLFLfAMATLLRTSFSDPGVIP 95
Cdd:COG5273    11 LGFIVFLVRLLRTGLYA--YKMFIGLFLLSRIV--VYTLLVIVKSLSLVVLFIIlFIVILVL-ASFSYLLLLVSDPGYLG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622198061  96 RalpdeaafiemeieatNGTVPPGQRPPPRIKNFQINNQIvklKYCYTCKIFRPPRASHCSICDNCVERFDHHCPWVGNC 175
Cdd:COG5273    86 E----------------NITLSGYRETISRLLDDGKFGTE---NFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNC 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622198061 176 VGKRNYRYFYLFILSLSLLTIYIFSFNIVYvalkslkIGFLNTLKETPGTVLEVLIC------FFTLWSVVGLTGFHTFL 249
Cdd:COG5273   147 VGFRNYRFFYQFLLYTILVALVVLLSTAYY-------IAGIFSIRHDTSLAICFLIFgcsllgVVFFIITTLLLLFLIYL 219

                         250
                  ....*....|....*....
gi 1622198061 250 VALNQTTNEDIKGSWTGKN 268
Cdd:COG5273   220 ILNNLTTIEFIQISRGGST 238
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 289-371 5.39e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622198061  289 GPLPPSVLDRRGILQQESAALESSAGPEPNTqEEGTTEKPSAQETSGDSALP----EESALPVPTGKVPQETAQPPSAAE 364
Cdd:PHA03307   125 SPPPSPAPDLSEMLRPVGSPGPPPAASPPAA-GASPAAVASDAASSRQAALPlsspEETARAPSSPPAEPPPSTPPAAAS 203


                   ....*..
gi 1622198061  365 PSVPSLD 371
Cdd:PHA03307   204 PRPPRRS 210
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 304-370 1.85e-03

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 40.15  E-value: 1.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622198061 304 QESAALESSAGPEPNTQEEGTTEKPSAQETSGDSALPEESALPVPTGKVPQETAQPPSAAEPSVPSL 370
Cdd:pfam13254 241 ADTLSTDKEQSPAPTSASEPPPKTKELPKDSEEPAAPSKSAEASTEKKEPDTESSPETSSEKSAPSL 307
 
Name Accession Description Interval E-value
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 138-261 9.04e-43

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: 145.59  E-value: 9.04e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622198061 138 LKYCYTCKIFRPPRASHCSICDNCVERFDHHCPWVGNCVGKRNYRYFYLFILSLSLLTIY--IFSFNIVYVALKSLKIGF 215
Cdd:pfam01529   5 LKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILylVLSLYYLVKLIESSTLFF 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622198061 216 LNTLKETPGTVLEVLICFFTLWSVVGLTGFHTFLVALNQTTNEDIK 261
Cdd:pfam01529  85 FLILFLFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFMK 130
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
17-268 3.52e-40

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 144.51  E-value: 3.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622198061  17 LPGRNTFCCDGRIMMARqkGIFYLTLFLIVGTCalFFAFECRYLAVHLSPTIPV-FGAVLFLfAMATLLRTSFSDPGVIP 95
Cdd:COG5273    11 LGFIVFLVRLLRTGLYA--YKMFIGLFLLSRIV--VYTLLVIVKSLSLVVLFIIlFIVILVL-ASFSYLLLLVSDPGYLG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622198061  96 RalpdeaafiemeieatNGTVPPGQRPPPRIKNFQINNQIvklKYCYTCKIFRPPRASHCSICDNCVERFDHHCPWVGNC 175
Cdd:COG5273    86 E----------------NITLSGYRETISRLLDDGKFGTE---NFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNC 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622198061 176 VGKRNYRYFYLFILSLSLLTIYIFSFNIVYvalkslkIGFLNTLKETPGTVLEVLIC------FFTLWSVVGLTGFHTFL 249
Cdd:COG5273   147 VGFRNYRFFYQFLLYTILVALVVLLSTAYY-------IAGIFSIRHDTSLAICFLIFgcsllgVVFFIITTLLLLFLIYL 219

                         250
                  ....*....|....*....
gi 1622198061 250 VALNQTTNEDIKGSWTGKN 268
Cdd:COG5273   220 ILNNLTTIEFIQISRGGST 238
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 289-371 5.39e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622198061  289 GPLPPSVLDRRGILQQESAALESSAGPEPNTqEEGTTEKPSAQETSGDSALP----EESALPVPTGKVPQETAQPPSAAE 364
Cdd:PHA03307   125 SPPPSPAPDLSEMLRPVGSPGPPPAASPPAA-GASPAAVASDAASSRQAALPlsspEETARAPSSPPAEPPPSTPPAAAS 203


                   ....*..
gi 1622198061  365 PSVPSLD 371
Cdd:PHA03307   204 PRPPRRS 210
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 304-370 1.85e-03

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 40.15  E-value: 1.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622198061 304 QESAALESSAGPEPNTQEEGTTEKPSAQETSGDSALPEESALPVPTGKVPQETAQPPSAAEPSVPSL 370
Cdd:pfam13254 241 ADTLSTDKEQSPAPTSASEPPPKTKELPKDSEEPAAPSKSAEASTEKKEPDTESSPETSSEKSAPSL 307
 
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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