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Conserved domains on  [gi|24307963|ref|NP_037436|]
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palmitoyltransferase ZDHHC1 isoform 1 [Homo sapiens]

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 ...
 129-284 8.02e-27

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: 104.76  E-value: 8.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307963   129 HVIEDLHCNLCNVDVSARSKHCSACNKCVCGFDHHCKWLNNCVGERNYR---LFLHSVASAllgvlllVLVATYVFVEFF 205
Cdd:pfam01529   1 IFDELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKyfiLFLLYLTLY-------LILYLVLSLYYL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24307963   206 VNPMRLRTNRHFEVLKNHTDVWFVFLPAAPVetqapailalaallillgllsTALLGHLLCFHIYLMWHKLTTYEYIVQ 284
Cdd:pfam01529  74 VKLIESSTLFFFLILFLFSISIILLILSLFF---------------------LLFLGILLFFHLYLISRNLTTYEFMKK 131
DPBB_RlpA_EXP_N-like super family cl41724
double-psi beta-barrel fold of RlpA, N-terminal domain of expansins, and similar domains; The ...
 362-400 9.25e-03

double-psi beta-barrel fold of RlpA, N-terminal domain of expansins, and similar domains; The double-psi beta-barrel (DPBB) fold is found in a divergent group of proteins, including endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A), EG45-like domain containing proteins, kiwellins, Streptomyces papain inhibitor (SPI), the N-terminal domain of plant and bacterial expansins, GH45 family of endoglucanases, barwins, cerato-platanins, membrane-bound lytic murein transglycosylase A (MltA) and YuiC-like proteins. RlpA may work in tandem with amidases to degrade peptidoglycan (PG) in the division septum and lateral wall to facilitate daughter cell separation. An EG45-like domain containing protein from Arabidopsis thaliana, called plant natriuretic peptide A (AtPNP-A), functions in cell volume regulation. Kiwellin proteins comprise a widespread family of plant-defense proteins that target pathogenic bacterial/fungal effectors that down-regulate plant defense responses. SPI is a stress protein produced under hyperthermal stress conditions that serves as a glutamine and lysine donor substrate for microbial transglutaminase (MTG, EC 2.3.2.13) from Streptomycetes. Some expansin family proteins display cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. Endoglucanases (EC 3.2.1.4) catalyze the endohydrolysis of (1-4)-beta-D-glucosidic linkages in cellulose, lichenin, and cereal beta-D-glucans. Animal cellulases, such as endoglucanase EG27II, have great potential for industrial applications such as bioethanol production. Barwin is a basic protein from barley seed. It is a probable plant lectin that may be involved in a defense mechanism. Cerato-platanin is a phytotoxin which causes production of phytoalexin in platanus acerifolia, platanus occidentalis, and platanus orientalis. It also induces cell necrosis. MltA, also called murein hydrolase A, is a murein-degrading enzyme that may play a role in recycling of muropeptides during cell elongation and/or cell division. It degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. YuiC is a Firmicute stationary phase survival (Sps) protein.


The actual alignment was detected with superfamily member cd22777:

Pssm-ID: 455124  Cd Length: 119  Bit Score: 36.35  E-value: 9.25e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24307963 362 WDRKKPLPWRSPLLLLAMWGPQAPpclcrkRGRGACIKC 400
Cdd:cd22777  31 WDADKPLSWRSKYGWTAFCGPAGP------RGQASCGKC 63
 
Name Accession Description Interval E-value
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 129-284 8.02e-27

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: 104.76  E-value: 8.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307963   129 HVIEDLHCNLCNVDVSARSKHCSACNKCVCGFDHHCKWLNNCVGERNYR---LFLHSVASAllgvlllVLVATYVFVEFF 205
Cdd:pfam01529   1 IFDELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKyfiLFLLYLTLY-------LILYLVLSLYYL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24307963   206 VNPMRLRTNRHFEVLKNHTDVWFVFLPAAPVetqapailalaallillgllsTALLGHLLCFHIYLMWHKLTTYEYIVQ 284
Cdd:pfam01529  74 VKLIESSTLFFFLILFLFSISIILLILSLFF---------------------LLFLGILLFFHLYLISRNLTTYEFMKK 131
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
136-180 4.84e-17

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 81.72  E-value: 4.84e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24307963 136 CNLCNVDVSARSKHCSACNKCVCGFDHHCKWLNNCVGERNYRLFL 180
Cdd:COG5273 112 CSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFY 156
DPBB_barwin-like cd22777
double-psi beta-barrel fold of the barwin family; This family represents a group of double-psi ...
 362-400 9.25e-03

double-psi beta-barrel fold of the barwin family; This family represents a group of double-psi beta-barrel (DPBB) fold proteins similar to Barwin, including Wheatwin-1/-2, pathogenesis-related protein P2, and the C-terminal domains of Pro-hevein, Wound-induced proteins WIN1/WIN2, and hevein-like preproprotein. Barwin is a basic protein from barley seed. It is a probable plant lectin that may be involved in a defense mechanism. Barwin binds weakly to a chitin analog. Pro-hevein, also called major hevein, is a rubber tree N-acetyl-D-glucosamine/N-acetyl-D-neuraminic acid binding lectin that can inhibit fungal growth. WIN1 and WIN2 from potato are cysteine-rich proteins which show striking homology to several chitin-binding proteins. Wheatwin-1 and Wheatwin-2 from bread wheat are also called pathogenesis-related protein 4a and 4b, respectively. They show antifungal activity towards B. cinerea and towards the wheat-specific pathogenic fungi F. culmorum and F. graminearum (groups 1 and 2). Wheatwin-1 has ribonuclease activity. Pathogenesis-related protein P2 (also called PR protein P2) from tomato is homologous to WINs and pro-hevein, but lack the N-terminal, chitin-binding "hevein" domain. Hevein-like preproprotein (also called HEL protein) from Arabidopsis is a fungal growth inhibitor. Neither its N-terminal hevein-like domain (CB-HEL) nor the C-terminal domain (CD-HEL) have chitinase activity, but both have antimicrobial activities. CD-HEL has RNase, but no DNase activity.


Pssm-ID: 439259  Cd Length: 119  Bit Score: 36.35  E-value: 9.25e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24307963 362 WDRKKPLPWRSPLLLLAMWGPQAPpclcrkRGRGACIKC 400
Cdd:cd22777  31 WDADKPLSWRSKYGWTAFCGPAGP------RGQASCGKC 63
 
Name Accession Description Interval E-value
DHHC pfam01529
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ...
 129-284 8.02e-27

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: 104.76  E-value: 8.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307963   129 HVIEDLHCNLCNVDVSARSKHCSACNKCVCGFDHHCKWLNNCVGERNYR---LFLHSVASAllgvlllVLVATYVFVEFF 205
Cdd:pfam01529   1 IFDELKYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKyfiLFLLYLTLY-------LILYLVLSLYYL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24307963   206 VNPMRLRTNRHFEVLKNHTDVWFVFLPAAPVetqapailalaallillgllsTALLGHLLCFHIYLMWHKLTTYEYIVQ 284
Cdd:pfam01529  74 VKLIESSTLFFFLILFLFSISIILLILSLFF---------------------LLFLGILLFFHLYLISRNLTTYEFMKK 131
COG5273 COG5273
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
136-180 4.84e-17

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


Pssm-ID: 227598 [Multi-domain]  Cd Length: 309  Bit Score: 81.72  E-value: 4.84e-17
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24307963 136 CNLCNVDVSARSKHCSACNKCVCGFDHHCKWLNNCVGERNYRLFL 180
Cdd:COG5273 112 CSTCNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFY 156
DPBB_barwin-like cd22777
double-psi beta-barrel fold of the barwin family; This family represents a group of double-psi ...
 362-400 9.25e-03

double-psi beta-barrel fold of the barwin family; This family represents a group of double-psi beta-barrel (DPBB) fold proteins similar to Barwin, including Wheatwin-1/-2, pathogenesis-related protein P2, and the C-terminal domains of Pro-hevein, Wound-induced proteins WIN1/WIN2, and hevein-like preproprotein. Barwin is a basic protein from barley seed. It is a probable plant lectin that may be involved in a defense mechanism. Barwin binds weakly to a chitin analog. Pro-hevein, also called major hevein, is a rubber tree N-acetyl-D-glucosamine/N-acetyl-D-neuraminic acid binding lectin that can inhibit fungal growth. WIN1 and WIN2 from potato are cysteine-rich proteins which show striking homology to several chitin-binding proteins. Wheatwin-1 and Wheatwin-2 from bread wheat are also called pathogenesis-related protein 4a and 4b, respectively. They show antifungal activity towards B. cinerea and towards the wheat-specific pathogenic fungi F. culmorum and F. graminearum (groups 1 and 2). Wheatwin-1 has ribonuclease activity. Pathogenesis-related protein P2 (also called PR protein P2) from tomato is homologous to WINs and pro-hevein, but lack the N-terminal, chitin-binding "hevein" domain. Hevein-like preproprotein (also called HEL protein) from Arabidopsis is a fungal growth inhibitor. Neither its N-terminal hevein-like domain (CB-HEL) nor the C-terminal domain (CD-HEL) have chitinase activity, but both have antimicrobial activities. CD-HEL has RNase, but no DNase activity.


Pssm-ID: 439259  Cd Length: 119  Bit Score: 36.35  E-value: 9.25e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24307963 362 WDRKKPLPWRSPLLLLAMWGPQAPpclcrkRGRGACIKC 400
Cdd:cd22777  31 WDADKPLSWRSKYGWTAFCGPAGP------RGQASCGKC 63
 
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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