Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in target proteins (PubMed:21531333, PubMed:24140420, PubMed:27994012, PubMed:28158808). Catalyzes the formation of monomethylarginine and asymmetric dimethylarginine on histones H2A and H4, a specific tag for epigenetic transcriptional activation (PubMed:21531333). Catalyzes asymmetric arginine dimethylation of mitochondrial proteins necessary for mitochondrial oxidative phosphorylation activity and thus aerobic respiration and ATP synthesis, and the mitochondrial stress response (PubMed:27994012). Methylates arginine residues in P-granule components pgl-1 and pgl-3 to promote P-granule degradation by autophagy in somatic cells to ensure exclusive localization of the P-granules in germ cells (PubMed:24140420). Modulates the interaction of P-granule proteins epg-2 and sepa-1 (PubMed:24140420). Methylates arginine residues in daf-16, which blocks ftt-2 binding to daf-16, prevents akt-mediated phosphorylation and allows for daf-16 to translocate to the nucleus (PubMed:21531333). In turn, association with daf-16 therefore allows for the transcriptional activation of daf-16 and regulation of longevity-related genes (PubMed:21531333). Maintains lifespan by modulating daf-16 activity downstream of the daf-2 signaling pathway (PubMed:21531333, PubMed:28158808). Plays a role in heat and oxidative stress resistance (PubMed:21531333, PubMed:28158808). Role in stress resistance and also fat storage may be in association with the daf-2 signaling pathway (PubMed:21531333). Required for normal feeding behavior (PubMed:27994012). L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine Interacts with daf-16 (PubMed:21531333). Interacts with pgl-1 and pgl-3 (PubMed:24140420). Interacts with alg-1 (PubMed:23516374). Diffuse cytoplasmic localization during embryogenesis. Widely expressed in pharyngeal, body wall muscle, intestinal and vulval cells. Expressed from embryogenesis (PubMed:24140420). Expressed during larval development and adulthood (PubMed:21531333). Viable with a slight decrease in egg-laying (PubMed:28158808). Defective arginine methyltransferase activity with reduced asymmetric dimethylation of targets (PubMed:21531333, PubMed:28158808). Reduced asymmetric arginine dimethylation of mitochondrial proteins which results in defective mitochondrial oxidative phosphorylation activity characterized by a reduced oxygen consumption rate during aerobic respiration as compared to wild-type animals, defective electron chain function and increased reactive oxygen species production (PubMed:27994012). This overall leads to reduced ATP synthesis and increased mitochondrial stress with an up-regulation of stress response genes conferring a food avoidance phenotype (PubMed:27994012). Defective symmetric arginine dimethylation of targets in mitochondria (PubMed:27994012). Increased phosphorylation of daf-16, increased binding of daf-16 to ftt-2 and subsequently increased cytoplasmic retention of daf-16 (PubMed:21531333). Reduced lifespan as a result of reduced expression of longevity-related proteins such as sod-3, mtl-7, sip-1 and lys-7 (PubMed:21531333, PubMed:28158808). Increased sensitivity to heat and oxidative stress (PubMed:28158808). Double knockout with prmt-5 results in prolonged larval development, shorter body size, reduced brood size, decreased egg-laying and 30% of eggs fail to hatch (PubMed:28158808). Double knockout also results in reduced asymmetric and symmetric arginine dimethylation of proteins (PubMed:28158808). Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.