palmitoyltransferase ZDHHC6 isoform X1 [Homo sapiens]
Protein Classification
zf-DHHC and SH3 domain-containing protein( domain architecture ID 10479076)
zf-DHHC and SH3 domain-containing protein
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 ... |
91-237 | 2.54e-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: 124.02 E-value: 2.54e-34
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| SH3 super family | cl17036 | Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ... |
313-392 | 1.87e-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: 36.03 E-value: 1.87e-03
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| Name | Accession | Description | Interval | E-value | ||||
| DHHC | pfam01529 | DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ... |
91-237 | 2.54e-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: 124.02 E-value: 2.54e-34
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| COG5273 | COG5273 | Uncharacterized protein containing DHHC-type Zn finger [General function prediction only]; |
66-286 | 2.33e-25 | ||||
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only]; Pssm-ID: 227598 [Multi-domain] Cd Length: 309 Bit Score: 104.83 E-value: 2.33e-25
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| SH3_2 | pfam07653 | Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ... |
313-392 | 1.87e-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: 36.03 E-value: 1.87e-03
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| Name | Accession | Description | Interval | E-value | ||||
| DHHC | pfam01529 | DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ... |
91-237 | 2.54e-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: 124.02 E-value: 2.54e-34
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| COG5273 | COG5273 | Uncharacterized protein containing DHHC-type Zn finger [General function prediction only]; |
66-286 | 2.33e-25 | ||||
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only]; Pssm-ID: 227598 [Multi-domain] Cd Length: 309 Bit Score: 104.83 E-value: 2.33e-25
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| SH3_2 | pfam07653 | Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ... |
313-392 | 1.87e-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: 36.03 E-value: 1.87e-03
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| Blast search parameters | ||||
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