NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1188456573|ref|NP_001338012|]
View 

palmitoyltransferase ZDHHC6 isoform 1 [Homo sapiens]

Protein Classification

zf-DHHC and SH3 domain-containing protein( domain architecture ID 10479076)

zf-DHHC and SH3 domain-containing protein

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 ...
 95-241 2.10e-34

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: 124.40  E-value: 2.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188456573  95 TMYLQYCKVCQAYKAPRSHHCRKCNRCVMKMDHHCPWINNCCGYQNHASFTLFLLLAPLGCIHAAFIFVMTMYTQLYHRL 174
Cdd:pfam01529   2 FDELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESST 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1188456573 175 SFGWNTVKIdmsaarrdplpivpfglaaFATTLFALGLALGTTIAVGMLFFIQMKIILRNKTSIESW 241
Cdd:pfam01529  82 LFFFLILFL-------------------FSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFM 129
SH3 super family cl17036
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 317-396 1.81e-03

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


The actual alignment was detected with superfamily member pfam07653:

Pssm-ID: 473055 [Multi-domain]  Cd Length: 54  Bit Score: 36.42  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188456573 317 RYKVIEDYSGACCPLnkgiktfftspcteeprIQLQKGEFILATRGLrywlygdkilDDSFIEG-VSRIRGWFPRKCVEK 395
Cdd:pfam07653   1 YGRVIFDYVGTDKNG-----------------LTLKKGDVVKVLGKD----------NDGWWEGeTGGRVGLVPSTAVEE 53


                  .
gi 1188456573 396 C 396
Cdd:pfam07653  54 I 54
 
Name Accession Description Interval E-value
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 95-241 2.10e-34

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: 124.40  E-value: 2.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188456573  95 TMYLQYCKVCQAYKAPRSHHCRKCNRCVMKMDHHCPWINNCCGYQNHASFTLFLLLAPLGCIHAAFIFVMTMYTQLYHRL 174
Cdd:pfam01529   2 FDELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESST 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1188456573 175 SFGWNTVKIdmsaarrdplpivpfglaaFATTLFALGLALGTTIAVGMLFFIQMKIILRNKTSIESW 241
Cdd:pfam01529  82 LFFFLILFL-------------------FSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFM 129
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
66-290 5.13e-27

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 109.46  E-value: 5.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188456573  66 VMILYNYFNAMFVGPGFVP-----LGWKPEISQDTMYLQ-----YCKVCQAYKAPRSHHCRKCNRCVMKMDHHCPWINNC 135
Cdd:COG5273    67 VLASFSYLLLLVSDPGYLGenitlSGYRETISRLLDDGKfgtenFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNC 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188456573 136 CGYQNHASFTLFLLLAPLG-CIHAAFIFVMTMYTQLYHRLSFGWNTVKIdmsaarrdplpivpFGLAAFATTLFALGLAL 214
Cdd:COG5273   147 VGFRNYRFFYQFLLYTILVaLVVLLSTAYYIAGIFSIRHDTSLAICFLI--------------FGCSLLGVVFFIITTLL 212

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1188456573 215 gttiavgmLFFIQMkIILRNKTSIESWIEEKakdriqYYQLDEVFVFPYDMGSRWRNFKQ---VFTWSGVPEGDGLEWP 290
Cdd:COG5273   213 --------LLFLIY-LILNNLTTIEFIQISR------GGSTLEFFPLCRESNLPFTNIFDsseGALPLDLGIGQNLSTI 276
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 317-396 1.81e-03

Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 36.42  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188456573 317 RYKVIEDYSGACCPLnkgiktfftspcteeprIQLQKGEFILATRGLrywlygdkilDDSFIEG-VSRIRGWFPRKCVEK 395
Cdd:pfam07653   1 YGRVIFDYVGTDKNG-----------------LTLKKGDVVKVLGKD----------NDGWWEGeTGGRVGLVPSTAVEE 53


                  .
gi 1188456573 396 C 396
Cdd:pfam07653  54 I 54
 
Name Accession Description Interval E-value
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 95-241 2.10e-34

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: 124.40  E-value: 2.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188456573  95 TMYLQYCKVCQAYKAPRSHHCRKCNRCVMKMDHHCPWINNCCGYQNHASFTLFLLLAPLGCIHAAFIFVMTMYTQLYHRL 174
Cdd:pfam01529   2 FDELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESST 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1188456573 175 SFGWNTVKIdmsaarrdplpivpfglaaFATTLFALGLALGTTIAVGMLFFIQMKIILRNKTSIESW 241
Cdd:pfam01529  82 LFFFLILFL-------------------FSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFM 129
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
66-290 5.13e-27

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 109.46  E-value: 5.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188456573  66 VMILYNYFNAMFVGPGFVP-----LGWKPEISQDTMYLQ-----YCKVCQAYKAPRSHHCRKCNRCVMKMDHHCPWINNC 135
Cdd:COG5273    67 VLASFSYLLLLVSDPGYLGenitlSGYRETISRLLDDGKfgtenFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNC 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188456573 136 CGYQNHASFTLFLLLAPLG-CIHAAFIFVMTMYTQLYHRLSFGWNTVKIdmsaarrdplpivpFGLAAFATTLFALGLAL 214
Cdd:COG5273   147 VGFRNYRFFYQFLLYTILVaLVVLLSTAYYIAGIFSIRHDTSLAICFLI--------------FGCSLLGVVFFIITTLL 212

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1188456573 215 gttiavgmLFFIQMkIILRNKTSIESWIEEKakdriqYYQLDEVFVFPYDMGSRWRNFKQ---VFTWSGVPEGDGLEWP 290
Cdd:COG5273   213 --------LLFLIY-LILNNLTTIEFIQISR------GGSTLEFFPLCRESNLPFTNIFDsseGALPLDLGIGQNLSTI 276
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 317-396 1.81e-03

Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 36.42  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1188456573 317 RYKVIEDYSGACCPLnkgiktfftspcteeprIQLQKGEFILATRGLrywlygdkilDDSFIEG-VSRIRGWFPRKCVEK 395
Cdd:pfam07653   1 YGRVIFDYVGTDKNG-----------------LTLKKGDVVKVLGKD----------NDGWWEGeTGGRVGLVPSTAVEE 53


                  .
gi 1188456573 396 C 396
Cdd:pfam07653  54 I 54
 
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