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Conserved domains on  [gi|569007658|ref|XP_006527331|]
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palmitoyltransferase ZDHHC6 isoform X1 [Mus musculus]

Protein Classification

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 ...
 95-241 4.04e-32

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: 118.24  E-value: 4.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007658   95 SMYLQYCKVCQAYKAPRSHHCRKCNRCVMKMDHHCPWINNCCGHQNHASFTLFLLLAPLGCTHAAFIFVMTMYTQLYNRL 174
Cdd:pfam01529   2 FDELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESST 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007658  175 SFGWNTVKIDMsaarrdpPPIVPFglaafaatlfalGLALGTTIAVGMLFFIQIKIILRNKTSIESW 241
Cdd:pfam01529  82 LFFFLILFLFS-------ISIILL------------ILSLFFLLFLGILLFFHLYLISRNLTTYEFM 129
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 317-396 3.34e-05

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: 41.04  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007658  317 RYKVIEDYNGACCPLnrgvrtfftspcteeprIRLQKGEFILATRGLrywlygdkilDDSFIEG-TSRVRGWFPRNCVEK 395
Cdd:pfam07653   1 YGRVIFDYVGTDKNG-----------------LTLKKGDVVKVLGKD----------NDGWWEGeTGGRVGLVPSTAVEE 53


                  .
gi 569007658  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 4.04e-32

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: 118.24  E-value: 4.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007658   95 SMYLQYCKVCQAYKAPRSHHCRKCNRCVMKMDHHCPWINNCCGHQNHASFTLFLLLAPLGCTHAAFIFVMTMYTQLYNRL 174
Cdd:pfam01529   2 FDELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESST 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007658  175 SFGWNTVKIDMsaarrdpPPIVPFglaafaatlfalGLALGTTIAVGMLFFIQIKIILRNKTSIESW 241
Cdd:pfam01529  82 LFFFLILFLFS-------ISIILL------------ILSLFFLLFLGILLFFHLYLISRNLTTYEFM 129
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
66-290 6.68e-24

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 100.98  E-value: 6.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007658  66 VMILYNYFNAMFAGPGFVPR-----GWKPEKSQDSMYLQ-----YCKVCQAYKAPRSHHCRKCNRCVMKMDHHCPWINNC 135
Cdd:COG5273   67 VLASFSYLLLLVSDPGYLGEnitlsGYRETISRLLDDGKfgtenFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNC 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007658 136 CGHQNHASFTLFLLLAPLGcthaafIFVMTMYTQLYNRLSFGwntvkidmsaARRDPPPIVPFglaafaATLFALGLALG 215
Cdd:COG5273  147 VGFRNYRFFYQFLLYTILV------ALVVLLSTAYYIAGIFS----------IRHDTSLAICF------LIFGCSLLGVV 204

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569007658 216 TTIAVGMLFFIQIKIILRNKTSIESWIEEKakdriqYYQLDEVFIFPYDMGSKWKNFKQ---VFTWSGVPEGDGLEWP 290
Cdd:COG5273  205 FFIITTLLLLFLIYLILNNLTTIEFIQISR------GGSTLEFFPLCRESNLPFTNIFDsseGALPLDLGIGQNLSTI 276
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 317-396 3.34e-05

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: 41.04  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007658  317 RYKVIEDYNGACCPLnrgvrtfftspcteeprIRLQKGEFILATRGLrywlygdkilDDSFIEG-TSRVRGWFPRNCVEK 395
Cdd:pfam07653   1 YGRVIFDYVGTDKNG-----------------LTLKKGDVVKVLGKD----------NDGWWEGeTGGRVGLVPSTAVEE 53


                  .
gi 569007658  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 4.04e-32

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: 118.24  E-value: 4.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007658   95 SMYLQYCKVCQAYKAPRSHHCRKCNRCVMKMDHHCPWINNCCGHQNHASFTLFLLLAPLGCTHAAFIFVMTMYTQLYNRL 174
Cdd:pfam01529   2 FDELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESST 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569007658  175 SFGWNTVKIDMsaarrdpPPIVPFglaafaatlfalGLALGTTIAVGMLFFIQIKIILRNKTSIESW 241
Cdd:pfam01529  82 LFFFLILFLFS-------ISIILL------------ILSLFFLLFLGILLFFHLYLISRNLTTYEFM 129
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
66-290 6.68e-24

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 100.98  E-value: 6.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007658  66 VMILYNYFNAMFAGPGFVPR-----GWKPEKSQDSMYLQ-----YCKVCQAYKAPRSHHCRKCNRCVMKMDHHCPWINNC 135
Cdd:COG5273   67 VLASFSYLLLLVSDPGYLGEnitlsGYRETISRLLDDGKfgtenFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNC 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007658 136 CGHQNHASFTLFLLLAPLGcthaafIFVMTMYTQLYNRLSFGwntvkidmsaARRDPPPIVPFglaafaATLFALGLALG 215
Cdd:COG5273  147 VGFRNYRFFYQFLLYTILV------ALVVLLSTAYYIAGIFS----------IRHDTSLAICF------LIFGCSLLGVV 204

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569007658 216 TTIAVGMLFFIQIKIILRNKTSIESWIEEKakdriqYYQLDEVFIFPYDMGSKWKNFKQ---VFTWSGVPEGDGLEWP 290
Cdd:COG5273  205 FFIITTLLLLFLIYLILNNLTTIEFIQISR------GGSTLEFFPLCRESNLPFTNIFDsseGALPLDLGIGQNLSTI 276
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 317-396 3.34e-05

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: 41.04  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007658  317 RYKVIEDYNGACCPLnrgvrtfftspcteeprIRLQKGEFILATRGLrywlygdkilDDSFIEG-TSRVRGWFPRNCVEK 395
Cdd:pfam07653   1 YGRVIFDYVGTDKNG-----------------LTLKKGDVVKVLGKD----------NDGWWEGeTGGRVGLVPSTAVEE 53


                  .
gi 569007658  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.
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