NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568954956|ref|XP_006509548|]
View 

palmitoyltransferase ZDHHC2 isoform X1 [Mus musculus]

Protein Classification

DHHC palmitoyltransferase family protein( domain architecture ID 139791)

DHHC palmitoyltransferase family protein may catalyze the post-translational modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage

EC:  2.3.1.225
Gene Ontology:  GO:0016409
PubMed:  16751107|12370247

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 super family cl19890
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 19-301 4.35e-41

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.


The actual alignment was detected with superfamily member COG5273:

Pssm-ID: 418707 [Multi-domain]  Cd Length: 309  Bit Score: 146.43  E-value: 4.35e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954956  19 WIPVVFISLLLGWSYYAYaiqLCIVSMenigeQVVCLMAYHLLFAMFVWSYWKTIFTLPMNPSKEFHLSYAekellerep 98
Cdd:COG5273   31 FIGLFLLSRIVVYTLLVI---VKSLSL-----VVLFIILFIVILVLASFSYLLLLVSDPGYLGENITLSGY--------- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954956  99 rgeahQEVLRRAAKDLPIYTRtmsgaiRYCDRCQLIKPDRCHHCSVCDKCILKMDHHCPWVNNCVGFSNYKFFLLFLAYS 178
Cdd:COG5273   94 -----RETISRLLDDGKFGTE------NFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954956 179 LLYcLFIAATDLQYFIRFWTNGLPDT-QAKFHIMFLFFAAA-MFSVSLSSLFGYHCWLVSKNKSTLEAF------RNPVF 250
Cdd:COG5273  163 ILV-ALVVLLSTAYYIAGIFSIRHDTsLAICFLIFGCSLLGvVFFIITTLLLLFLIYLILNNLTTIEFIqisrggSTLEF 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568954956 251 R-------------HGTDK--NGFSLGFSKNMRQVFGDEKKYWLLPVFSSQGDGCSFPTCLVNQDP 301
Cdd:COG5273  242 FplcresnlpftniFDSSEgaLPLDLGIGQNLSTIKGSNALYWLTPLHTNYCNSYDFSLRSDTLAE 307
 
Name Accession Description Interval E-value
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
19-301 4.35e-41

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 146.43  E-value: 4.35e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954956  19 WIPVVFISLLLGWSYYAYaiqLCIVSMenigeQVVCLMAYHLLFAMFVWSYWKTIFTLPMNPSKEFHLSYAekellerep 98
Cdd:COG5273   31 FIGLFLLSRIVVYTLLVI---VKSLSL-----VVLFIILFIVILVLASFSYLLLLVSDPGYLGENITLSGY--------- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954956  99 rgeahQEVLRRAAKDLPIYTRtmsgaiRYCDRCQLIKPDRCHHCSVCDKCILKMDHHCPWVNNCVGFSNYKFFLLFLAYS 178
Cdd:COG5273   94 -----RETISRLLDDGKFGTE------NFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954956 179 LLYcLFIAATDLQYFIRFWTNGLPDT-QAKFHIMFLFFAAA-MFSVSLSSLFGYHCWLVSKNKSTLEAF------RNPVF 250
Cdd:COG5273  163 ILV-ALVVLLSTAYYIAGIFSIRHDTsLAICFLIFGCSLLGvVFFIITTLLLLFLIYLILNNLTTIEFIqisrggSTLEF 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568954956 251 R-------------HGTDK--NGFSLGFSKNMRQVFGDEKKYWLLPVFSSQGDGCSFPTCLVNQDP 301
Cdd:COG5273  242 FplcresnlpftniFDSSEgaLPLDLGIGQNLSTIKGSNALYWLTPLHTNYCNSYDFSLRSDTLAE 307
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 126-247 6.16e-41

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: 140.58  E-value: 6.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954956  126 RYCDRCQLIKPDRCHHCSVCDKCILKMDHHCPWVNNCVGFSNYKFFLLFLAYSLLYCLFIAATDLQYFIRFWTN----GL 201
Cdd:pfam01529   6 KYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESstlfFF 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568954956  202 PDTQAKFHIMFLFFAAAMFSVSLSSLFGYHCWLVSKNKSTLEAFRN 247
Cdd:pfam01529  86 LILFLFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFMKK 131
 
Name Accession Description Interval E-value
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
19-301 4.35e-41

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 146.43  E-value: 4.35e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954956  19 WIPVVFISLLLGWSYYAYaiqLCIVSMenigeQVVCLMAYHLLFAMFVWSYWKTIFTLPMNPSKEFHLSYAekellerep 98
Cdd:COG5273   31 FIGLFLLSRIVVYTLLVI---VKSLSL-----VVLFIILFIVILVLASFSYLLLLVSDPGYLGENITLSGY--------- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954956  99 rgeahQEVLRRAAKDLPIYTRtmsgaiRYCDRCQLIKPDRCHHCSVCDKCILKMDHHCPWVNNCVGFSNYKFFLLFLAYS 178
Cdd:COG5273   94 -----RETISRLLDDGKFGTE------NFCSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954956 179 LLYcLFIAATDLQYFIRFWTNGLPDT-QAKFHIMFLFFAAA-MFSVSLSSLFGYHCWLVSKNKSTLEAF------RNPVF 250
Cdd:COG5273  163 ILV-ALVVLLSTAYYIAGIFSIRHDTsLAICFLIFGCSLLGvVFFIITTLLLLFLIYLILNNLTTIEFIqisrggSTLEF 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568954956 251 R-------------HGTDK--NGFSLGFSKNMRQVFGDEKKYWLLPVFSSQGDGCSFPTCLVNQDP 301
Cdd:COG5273  242 FplcresnlpftniFDSSEgaLPLDLGIGQNLSTIKGSNALYWLTPLHTNYCNSYDFSLRSDTLAE 307
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 126-247 6.16e-41

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: 140.58  E-value: 6.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954956  126 RYCDRCQLIKPDRCHHCSVCDKCILKMDHHCPWVNNCVGFSNYKFFLLFLAYSLLYCLFIAATDLQYFIRFWTN----GL 201
Cdd:pfam01529   6 KYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLVKLIESstlfFF 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568954956  202 PDTQAKFHIMFLFFAAAMFSVSLSSLFGYHCWLVSKNKSTLEAFRN 247
Cdd:pfam01529  86 LILFLFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFMKK 131
 
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