Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
6-314
6.92e-162
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.
:
Pssm-ID: 461882 Cd Length: 306 Bit Score: 470.20 E-value: 6.92e-162
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
346-494
1.01e-36
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.
The actual alignment was detected with superfamily member pfam07859:
Pssm-ID: 473884 [Multi-domain] Cd Length: 208 Bit Score: 136.96 E-value: 1.01e-36
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
6-314
6.92e-162
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.
Pssm-ID: 461882 Cd Length: 306 Bit Score: 470.20 E-value: 6.92e-162
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
6-314
6.92e-162
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.
Pssm-ID: 461882 Cd Length: 306 Bit Score: 470.20 E-value: 6.92e-162
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
336-429
5.44e-11
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.
Pssm-ID: 466583 [Multi-domain] Cd Length: 215 Bit Score: 62.97 E-value: 5.44e-11
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
295-429
1.81e-03
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) and fission yeast Mug180. Say1 is a a membrane-anchored deacetylase required for the deacetylation of acetylated sterols. It is involved in the resistance to eugenol and pregnenolone toxicity. Mug180 has a role in meiosis.
Pssm-ID: 313549 Cd Length: 374 Bit Score: 41.36 E-value: 1.81e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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