Catalysis of the selective cleavage of Lys(or Arg)-Ile bond in complement subcomponent C1s to form the active form of C1s (EC:3.4.21.42).

Catalysis of the cleavage of component C4 to C4a and C4b (Arg-Ala bond), and component C2 to C2a and C2b (Lys-Lys or Arg-Lys bond).

A ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in a polypeptide chain.

Catalysis of the cleavage of component factor B (Arg-Lys) when in complex with C3b or with cobra venom factor (CVF).

The modification of an amino acid to an active form, for incorporation into a peptide, protein or other macromolecule.

Catalysis of the inactivation of complement subcomponents C3b, iC3b and C4b by proteolytic cleavage.

The synthesis of aminoacyl tRNA by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA, usually catalyzed by the cognate aminoacyl-tRNA ligase. A given aminoacyl-tRNA ligase aminoacylates all species of an isoaccepting group of tRNA molecules.

The elicitation by an organism of a defense response by the host.

The chemical reactions involving proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.

Catalysis of the reaction: (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl-amino acid.

The processes by which an organism has an observable effect on an organism of a different species.

The formation from simpler components of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.

Catalysis of the reaction: acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

The process by which the anatomical structures of the eye are generated and organized. Morphogenesis pertains to the creation of form.

The breakdown into simpler components of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.