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Conserved domains on  [gi|1039753264|ref|XP_017172896|]
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palmitoyltransferase ZDHHC14 isoform X7 [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

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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 ...
 1-76 3.82e-07

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 pfam01529:

Pssm-ID: 418707  Cd Length: 132  Bit Score: 48.13  E-value: 3.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753264   1 MFILSLSFLTVFIFAFVITHVIH-----RSQQKGFLDALKDSPASVLEAVICFFSVWSIIGLSGFHTYLISSNQTTNEDI 75
Cdd:pfam01529  50 YFILFLLYLTLYLILYLVLSLYYlvkliESSTLFFFLILFLFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFM 129


                  .
gi 1039753264  76 K 76
Cdd:pfam01529 130 K 130
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 140-250 7.34e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.91  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753264 140 QSQSDMCDQDQCIQSTKFVLQAAATPLLQSEPSLTSEELHMPGKPglgTPCASLTLGQPTPPSSMPNLATEATLS----- 214
Cdd:pfam03154 155 ESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGP---TPSAPSVPPQGSPATSQPPNQTQSTAAphtli 231

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039753264 215 ----DIMP--LKDEHGGHQFLTPDEAPS--------PPRMLGAGSPLAHS 250
Cdd:pfam03154 232 qqtpTLHPqrLPSPHPPLQPMTQPPPPSqvspqplpQPSLHGQMPPMPHS 281
 
Name Accession Description Interval E-value
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 1-76 3.82e-07

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: 48.13  E-value: 3.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753264   1 MFILSLSFLTVFIFAFVITHVIH-----RSQQKGFLDALKDSPASVLEAVICFFSVWSIIGLSGFHTYLISSNQTTNEDI 75
Cdd:pfam01529  50 YFILFLLYLTLYLILYLVLSLYYlvkliESSTLFFFLILFLFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFM 129


                  .
gi 1039753264  76 K 76
Cdd:pfam01529 130 K 130
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 140-250 7.34e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.91  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753264 140 QSQSDMCDQDQCIQSTKFVLQAAATPLLQSEPSLTSEELHMPGKPglgTPCASLTLGQPTPPSSMPNLATEATLS----- 214
Cdd:pfam03154 155 ESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGP---TPSAPSVPPQGSPATSQPPNQTQSTAAphtli 231

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039753264 215 ----DIMP--LKDEHGGHQFLTPDEAPS--------PPRMLGAGSPLAHS 250
Cdd:pfam03154 232 qqtpTLHPqrLPSPHPPLQPMTQPPPPSqvspqplpQPSLHGQMPPMPHS 281
PHA03247 PHA03247
large tegument protein UL36; Provisional
 103-275 1.04e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753264  103 ALCGPISPS-LIDRRGYVQPDTPQPAAPSN-------GITMYGATQSQSDMCDQDQCIQSTKFVLQAAATPLLQSEPSLT 174
Cdd:PHA03247  2851 PLGGSVAPGgDVRRRPPSRSPAAKPAAPARppvrrlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ 2930

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753264  175 SEElHMPGKPGLGTPCASLTLGQPTPPSSMPNLATEATLSDIMPLKdehgghQFLTPDEAPSPPRMLGAGSPLAHSRTMH 254
Cdd:PHA03247  2931 PPP-PPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVP------RFRVPQPAPSREAPASSTPPLTGHSLSR 3003

                          170       180
                   ....*....|....*....|.
gi 1039753264  255 MLGLASQDSLHEDSVRGLVKL 275
Cdd:PHA03247  3004 VSSWASSLALHEETDPPPVSL 3024
 
Name Accession Description Interval E-value
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 1-76 3.82e-07

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: 48.13  E-value: 3.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753264   1 MFILSLSFLTVFIFAFVITHVIH-----RSQQKGFLDALKDSPASVLEAVICFFSVWSIIGLSGFHTYLISSNQTTNEDI 75
Cdd:pfam01529  50 YFILFLLYLTLYLILYLVLSLYYlvkliESSTLFFFLILFLFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFM 129


                  .
gi 1039753264  76 K 76
Cdd:pfam01529 130 K 130
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 140-250 7.34e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.91  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753264 140 QSQSDMCDQDQCIQSTKFVLQAAATPLLQSEPSLTSEELHMPGKPglgTPCASLTLGQPTPPSSMPNLATEATLS----- 214
Cdd:pfam03154 155 ESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGP---TPSAPSVPPQGSPATSQPPNQTQSTAAphtli 231

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039753264 215 ----DIMP--LKDEHGGHQFLTPDEAPS--------PPRMLGAGSPLAHS 250
Cdd:pfam03154 232 qqtpTLHPqrLPSPHPPLQPMTQPPPPSqvspqplpQPSLHGQMPPMPHS 281
PHA03247 PHA03247
large tegument protein UL36; Provisional
 103-275 1.04e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753264  103 ALCGPISPS-LIDRRGYVQPDTPQPAAPSN-------GITMYGATQSQSDMCDQDQCIQSTKFVLQAAATPLLQSEPSLT 174
Cdd:PHA03247  2851 PLGGSVAPGgDVRRRPPSRSPAAKPAAPARppvrrlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ 2930

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753264  175 SEElHMPGKPGLGTPCASLTLGQPTPPSSMPNLATEATLSDIMPLKdehgghQFLTPDEAPSPPRMLGAGSPLAHSRTMH 254
Cdd:PHA03247  2931 PPP-PPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVP------RFRVPQPAPSREAPASSTPPLTGHSLSR 3003

                          170       180
                   ....*....|....*....|.
gi 1039753264  255 MLGLASQDSLHEDSVRGLVKL 275
Cdd:PHA03247  3004 VSSWASSLALHEETDPPPVSL 3024
 
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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