squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
77-523
0e+00
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the triterpenes squalene or 2-3-oxidosqualene to a variety of products including hopene, lanosterol, cycloartenol, amyrin, lupeol, and isomultiflorenol.
The actual alignment was detected with superfamily member TIGR01787:
Pssm-ID: 273809 [Multi-domain] Cd Length: 621 Bit Score: 651.43 E-value: 0e+00
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
77-523
0e+00
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the triterpenes squalene or 2-3-oxidosqualene to a variety of products including hopene, lanosterol, cycloartenol, amyrin, lupeol, and isomultiflorenol.
Pssm-ID: 273809 [Multi-domain] Cd Length: 621 Bit Score: 651.43 E-value: 0e+00
Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an ...
78-523
0e+00
Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. This group contains bacterial SQCY which catalyzes the convertion of squalene to hopene or diplopterol and eukaryotic OSQCY which transforms the 2,3-epoxide of squalene to compounds such as, lanosterol in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain.
Pssm-ID: 239222 [Multi-domain] Cd Length: 634 Bit Score: 609.20 E-value: 0e+00
Squalene-hopene cyclase N-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes the cyclization of squalene into hopene in bacteria. This reaction is part of a cationic cyclization cascade, which is homologous to a key step in cholesterol biosynthesis. This family is the N-terminal domain.
Pssm-ID: 433061 [Multi-domain] Cd Length: 290 Bit Score: 155.34 E-value: 3.96e-43
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
77-523
0e+00
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the triterpenes squalene or 2-3-oxidosqualene to a variety of products including hopene, lanosterol, cycloartenol, amyrin, lupeol, and isomultiflorenol.
Pssm-ID: 273809 [Multi-domain] Cd Length: 621 Bit Score: 651.43 E-value: 0e+00
Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an ...
78-523
0e+00
Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. This group contains bacterial SQCY which catalyzes the convertion of squalene to hopene or diplopterol and eukaryotic OSQCY which transforms the 2,3-epoxide of squalene to compounds such as, lanosterol in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain.
Pssm-ID: 239222 [Multi-domain] Cd Length: 634 Bit Score: 609.20 E-value: 0e+00
2,3-oxidosqualene cyclase; This model identifies 2,3-oxidosqualene cyclases from Stigmatella ...
86-523
2.29e-138
2,3-oxidosqualene cyclase; This model identifies 2,3-oxidosqualene cyclases from Stigmatella aurantiaca which produces cycloartenol, and Gemmata obscuriglobus and Methylococcus capsulatus, which each produce the closely related sterol, lanosterol.
Pssm-ID: 274591 [Multi-domain] Cd Length: 634 Bit Score: 414.39 E-value: 2.29e-138
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ...
385-523
4.11e-55
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. Bacterial SQCY catalyzes the convertion of squalene to hopene or diplopterol. Eukaryotic OSQCY transforms the 2,3-epoxide of squalene to compounds such as, lanosterol (a metabolic precursor of cholesterol and steroid hormones) in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain. This group also contains SQCY-like archael sequences and some bacterial SQCY's which lack this minor domain.
Pssm-ID: 239219 [Multi-domain] Cd Length: 348 Bit Score: 188.97 E-value: 4.11e-55
Squalene-hopene cyclase N-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes the cyclization of squalene into hopene in bacteria. This reaction is part of a cationic cyclization cascade, which is homologous to a key step in cholesterol biosynthesis. This family is the N-terminal domain.
Pssm-ID: 433061 [Multi-domain] Cd Length: 290 Bit Score: 155.34 E-value: 3.96e-43
squalene-hopene cyclase; SHC is an essential prokaryotic gene in hopanoid (triterpenoid) ...
82-445
1.36e-20
squalene-hopene cyclase; SHC is an essential prokaryotic gene in hopanoid (triterpenoid) biosynthesis. Squalene hopene cyclase, an integral membrane protein, directly cyclizes squalene into hopanoid products. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273661 [Multi-domain] Cd Length: 635 Bit Score: 95.34 E-value: 1.36e-20
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
363-514
1.40e-16
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two broadly specific proteinase inhibitors alpha2-macroglobulin (alpha (2)-M) and pregnancy zone protein (PZP) and, the C3 C4 and C5 components of vertebrate complement. Class II terpene cyclases include squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY), these integral membrane proteins catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. The protein prenyltransferases include protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II) which catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Alpha (2)-M is a major carrier protein in serum and involved in the immobilization and entrapment of proteases. PZP is a pregnancy associated protein. Alpha (2)-M and PZP are known to bind to and, may modulate, the activity of placental protein-14 in T-cell growth and cytokine production thereby protecting the allogeneic fetus from attack by the maternal immune system.
Pssm-ID: 238362 [Multi-domain] Cd Length: 300 Bit Score: 80.67 E-value: 1.40e-16
Squalene-hopene cyclase C-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes the cyclization of squalene into hopene in bacteria. This reaction is part of a cationic cyclization cascade, which is homologous to a key step in cholesterol biosynthesis. This family is the C-terminal half of the molecule.
Pssm-ID: 433057 [Multi-domain] Cd Length: 319 Bit Score: 49.64 E-value: 2.15e-06
squalene--tetrahymanol cyclase; This enzyme, also called squalene--tetrahymanol cyclase, ...
132-524
1.30e-05
squalene--tetrahymanol cyclase; This enzyme, also called squalene--tetrahymanol cyclase, occurs a small number of eukaryotes, some of them anaerobic. The pathway can occur under anaerobic conditions, and the product is thought to replace sterols, letting organisms with this compound build membrane suitable for performing phagocytosis.
Pssm-ID: 212000 [Multi-domain] Cd Length: 624 Bit Score: 48.09 E-value: 1.30e-05
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ...
78-99
7.73e-03
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. Bacterial SQCY catalyzes the convertion of squalene to hopene or diplopterol. Eukaryotic OSQCY transforms the 2,3-epoxide of squalene to compounds such as, lanosterol (a metabolic precursor of cholesterol and steroid hormones) in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain. This group also contains SQCY-like archael sequences and some bacterial SQCY's which lack this minor domain.
Pssm-ID: 239219 [Multi-domain] Cd Length: 348 Bit Score: 38.74 E-value: 7.73e-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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