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palmitoyltransferase ZDHHC17 isoform 1 [Homo sapiens]
ankyrin repeat domain-containing DHHC palmitoyltransferase family protein( domain architecture ID 12790884)
DHHC family palmitoyltransferase may catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes; contains N-terminal ankyrin repeats;
List of domain hits
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Name | Accession | Description | Interval | E-value | |||||
ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
52-307 | 9.85e-46 | |||||
Ankyrin repeat [Signal transduction mechanisms]; : Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 163.97 E-value: 9.85e-46
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DHHC | pfam01529 | DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ... |
438-568 | 1.64e-40 | |||||
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: 144.05 E-value: 1.64e-40
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Name | Accession | Description | Interval | E-value | |||||
ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
52-307 | 9.85e-46 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 163.97 E-value: 9.85e-46
|
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DHHC | pfam01529 | DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ... |
438-568 | 1.64e-40 | |||||
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: 144.05 E-value: 1.64e-40
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COG5273 | COG5273 | Uncharacterized protein containing DHHC-type Zn finger [General function prediction only]; |
358-557 | 1.53e-33 | |||||
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only]; Pssm-ID: 227598 [Multi-domain] Cd Length: 309 Bit Score: 130.64 E-value: 1.53e-33
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Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
161-255 | 3.30e-22 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 91.33 E-value: 3.30e-22
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PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
52-277 | 2.83e-16 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 81.25 E-value: 2.83e-16
|
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ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
224-253 | 1.58e-04 | |||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.11 E-value: 1.58e-04
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TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
92-281 | 1.38e-03 | |||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 41.54 E-value: 1.38e-03
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Name | Accession | Description | Interval | E-value | |||||
ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
52-307 | 9.85e-46 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 163.97 E-value: 9.85e-46
|
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ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
54-295 | 1.18e-44 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 160.89 E-value: 1.18e-44
|
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DHHC | pfam01529 | DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ... |
438-568 | 1.64e-40 | |||||
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: 144.05 E-value: 1.64e-40
|
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COG5273 | COG5273 | Uncharacterized protein containing DHHC-type Zn finger [General function prediction only]; |
358-557 | 1.53e-33 | |||||
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only]; Pssm-ID: 227598 [Multi-domain] Cd Length: 309 Bit Score: 130.64 E-value: 1.53e-33
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Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
161-255 | 3.30e-22 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 91.33 E-value: 3.30e-22
|
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ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
110-277 | 2.19e-20 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 91.94 E-value: 2.19e-20
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Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
128-221 | 3.35e-18 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.77 E-value: 3.35e-18
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Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
94-187 | 4.60e-17 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.69 E-value: 4.60e-17
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Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
64-154 | 5.27e-17 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.31 E-value: 5.27e-17
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PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
52-277 | 2.83e-16 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 81.25 E-value: 2.83e-16
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PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
71-265 | 1.34e-15 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 79.62 E-value: 1.34e-15
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PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
54-273 | 6.69e-14 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 75.10 E-value: 6.69e-14
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PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
76-275 | 5.62e-13 | |||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 71.59 E-value: 5.62e-13
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PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
104-268 | 5.63e-13 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 71.45 E-value: 5.63e-13
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PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
53-265 | 3.14e-11 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 66.24 E-value: 3.14e-11
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PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
82-250 | 3.40e-11 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 65.40 E-value: 3.40e-11
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PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
99-267 | 9.42e-11 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 64.21 E-value: 9.42e-11
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PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
133-264 | 1.19e-10 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 64.70 E-value: 1.19e-10
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PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
88-314 | 1.79e-10 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 63.47 E-value: 1.79e-10
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PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
74-295 | 4.23e-10 | |||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 62.35 E-value: 4.23e-10
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PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
63-189 | 8.14e-10 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 61.22 E-value: 8.14e-10
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PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
103-262 | 3.00e-09 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 59.62 E-value: 3.00e-09
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Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
124-177 | 3.97e-09 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 3.97e-09
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PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
135-307 | 1.55e-08 | |||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 57.96 E-value: 1.55e-08
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PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
74-194 | 8.41e-08 | |||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 55.03 E-value: 8.41e-08
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PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
126-271 | 9.84e-08 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 54.61 E-value: 9.84e-08
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PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
74-265 | 1.25e-07 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.50 E-value: 1.25e-07
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Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
209-265 | 1.45e-07 | |||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.50 E-value: 1.45e-07
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Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
159-202 | 2.29e-07 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.65 E-value: 2.29e-07
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Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
90-140 | 2.56e-07 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.65 E-value: 2.56e-07
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PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
74-187 | 2.19e-06 | |||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 50.41 E-value: 2.19e-06
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PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
120-190 | 7.33e-06 | |||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.13 E-value: 7.33e-06
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Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
224-255 | 7.61e-06 | |||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 43.05 E-value: 7.61e-06
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Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
226-265 | 2.60e-05 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 2.60e-05
|
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PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
122-279 | 3.34e-05 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 46.88 E-value: 3.34e-05
|
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PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
143-194 | 8.85e-05 | |||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.66 E-value: 8.85e-05
|
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PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
126-256 | 1.36e-04 | |||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 45.24 E-value: 1.36e-04
|
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ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
224-253 | 1.58e-04 | |||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.11 E-value: 1.58e-04
|
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Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
229-286 | 2.18e-04 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 40.48 E-value: 2.18e-04
|
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Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
109-164 | 2.45e-04 | |||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 2.45e-04
|
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PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
208-267 | 2.59e-04 | |||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.12 E-value: 2.59e-04
|
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PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
94-270 | 2.72e-04 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 43.72 E-value: 2.72e-04
|
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PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
70-194 | 3.73e-04 | |||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 43.70 E-value: 3.73e-04
|
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Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
126-154 | 5.79e-04 | |||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.65 E-value: 5.79e-04
|
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PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
135-281 | 6.75e-04 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 42.67 E-value: 6.75e-04
|
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Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
224-253 | 7.03e-04 | |||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 37.24 E-value: 7.03e-04
|
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Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
156-187 | 8.75e-04 | |||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.27 E-value: 8.75e-04
|
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PHA02859 | PHA02859 | ankyrin repeat protein; Provisional |
122-269 | 8.88e-04 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 40.96 E-value: 8.88e-04
|
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Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
189-222 | 1.05e-03 | |||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.88 E-value: 1.05e-03
|
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ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
126-150 | 1.09e-03 | |||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.80 E-value: 1.09e-03
|
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PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
209-296 | 1.15e-03 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 41.97 E-value: 1.15e-03
|
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Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
92-117 | 1.26e-03 | |||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.47 E-value: 1.26e-03
|
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TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
92-281 | 1.38e-03 | |||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 41.54 E-value: 1.38e-03
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Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
148-194 | 1.38e-03 | |||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 1.38e-03
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ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
156-185 | 3.63e-03 | |||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.26 E-value: 3.63e-03
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PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
64-188 | 5.81e-03 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 39.56 E-value: 5.81e-03
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Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
176-232 | 7.11e-03 | |||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.01 E-value: 7.11e-03
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Blast search parameters | ||||
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