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Phospholipase A2
This family consists of several phospholipase A2 like proteins mostly from insects [1]. (from Pfam)
Lysophospholipase catalytic domain
This family consists of Lysophospholipase / phospholipase B EC:3.1.1.5 and cytosolic phospholipase A2 EC:3.1.4 which also has a C2 domain Pfam:PF00168. Phospholipase B enzymes catalyse the release of fatty acids from lysophsopholipids and are capable in vitro of hydrolysing all phospholipids extractable form yeast cells [1]. Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids [2], the aligned region corresponds the the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in [2]. (from Pfam)
phospholipase A2 family protein
Phospholipase A2 releases fatty acids from the second carbon group of glycerol. Perhaps the best known members are secreted snake venoms, but also found in secreted pancreatic and membrane-associated forms. Structure is all-alpha, with two core disulfide-linked helices and a calcium-binding loop. This alignment represents the major family of PLA2s. A second minor family, defined by the honeybee venom PLA2 PDB:1POC and related sequences from Gila monsters (Heloderma), is not recognised. This minor family conserves the core helix pair but is substantially different elsewhere. The PROSITE pattern PA2_HIS, specific to the first core helix, recognises both families. (from Pfam)
MAPEG family protein
This family is has been called MAPEG (Membrane Associated Proteins in Eicosanoid and Glutathione metabolism). It includes proteins such as Prostaglandin E synthase. This enzyme catalyses the synthesis of PGE2 from PGH2 (produced by cyclooxygenase from arachidonic acid). Because of structural similarities in the active sites of FLAP, LTC4 synthase and PGE synthase, substrates for each enzyme can compete with one another and modulate synthetic activity. (from Pfam)
cytochrome P450
cytochrome P450 catalyzes the oxidation of organic species by molecular oxygen, by the oxidative addition of atomic oxygen into an unactivated C-H or C-C bond
cytochrome P450 catalyzes the oxidation of organic species by molecular oxygen, by the oxidative addition of atomic oxygen into an unactivated C-H or C-C bond; similar to Homo sapiens thromboxane-A synthase that catalyzes the conversion of prostaglandin H2 (PGH2) to thromboxane A2 (TXA2), a potent inducer of blood vessel constriction and platelet aggregation
patatin-like phospholipase domain-containing protein
patatin-like phospholipase domain-containing protein may function as a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids
PLA2_like domain-containing protein
PLA2c domain-containing protein
B4_12hDH family protein
C2 and cPLA2_Grp-IVA domain-containing protein
C2 and STKc_PKN domain-containing protein
STKc_PKN domain-containing protein
MBOAT and MAPEG domain-containing protein
HR1_PKN_1 and C2_PKN-like domain-containing protein
protein containing domains HR1_PKN_1, HR1, C2_PKN-like, and PKc_like
C2_PKN-like and STKc_PKN domain-containing protein
protein containing domains HR1_PKN_1, HR1_PKN2_2, C2_PKN-like, and STKc_PKN
serine/threonine-protein kinase N1
serine/threonine-protein kinase N1 catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates
serine/threonine-protein kinase N
serine/threonine-protein kinase N catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids
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