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serine aminopeptidase domain-containing protein
This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with Pfam:PF00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2. (from Pfam)
alpha/beta fold hydrolase
This family contains alpha/beta hydrolase enzymes of diverse specificity. (from Pfam)
PGAP1-like protein
The sequences found in this family are similar to PGAP1 (Swiss:Q765A7). This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body [1]. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts [2]. [1]. 14734546. Inositol deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p. Tanaka S, Maeda Y, Tashima Y, Kinoshita T;. J Biol Chem. 2004;279:14256-14263. [2]. 19959834. The TGL2 gene of Saccharomyces cerevisiae encodes an active acylglycerol lipase located in the mitochondria. Ham HJ, Rho HJ, Shin SK, Yoon HJ;. J Biol Chem. 2010;285:3005-3013. (from Pfam)
thioesterase domain-containing protein
Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa. [1]. 9560421. Genetic evidence for a role of thioesterase domains, integrated in or associated with peptide synthetases, in non-ribosomal peptide biosynthesis in Bacillus subtilis. Schneider A, Marahiel MA;. Arch Microbiol 1998;169:404-410. (from Pfam)
This catalytic domain is found in a very wide range of enzymes. [1]. 1409539. The alpha/beta hydrolase fold. Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, Sussman JL, Verschueren KHG, Goldman A;. Protein Eng 1992;5:197-211. (from Pfam)
esterase
esterase similar esterase YbfF, which belongs to alpha/beta hydrolase family and cleaves an ester bond utilizing a water molecule; may have broad substrate specificity for long-chain substrates as well as substrates of small molecular weight
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