Annotations: 4LWO

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth B]	PRMT5_C_1	e4lwoB2	A: beta sandwiches	X: Arginine methyltransferase oligomerization subdomain (From Topology)	H: Arginine methyltransferase oligomerization subdomain (From Topology)	T: Arginine methyltransferase oligomerization subdomain	F: PRMT5_C_1	ECOD (1.6)
A [auth B]	PrmA	e4lwoB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: PrmA	ECOD (1.6)
B [auth A]	PRMT5_C_1	e4lwoA2	A: beta sandwiches	X: Arginine methyltransferase oligomerization subdomain (From Topology)	H: Arginine methyltransferase oligomerization subdomain (From Topology)	T: Arginine methyltransferase oligomerization subdomain	F: PRMT5_C_1	ECOD (1.6)
B [auth A]	PrmA	e4lwoA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: PrmA	ECOD (1.6)
C [auth E]	PRMT5_C_1	e4lwoE2	A: beta sandwiches	X: Arginine methyltransferase oligomerization subdomain (From Topology)	H: Arginine methyltransferase oligomerization subdomain (From Topology)	T: Arginine methyltransferase oligomerization subdomain	F: PRMT5_C_1	ECOD (1.6)
C [auth E]	PrmA	e4lwoE1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: PrmA	ECOD (1.6)
D [auth G]	PRMT5_C_1	e4lwoG3	A: beta sandwiches	X: Arginine methyltransferase oligomerization subdomain (From Topology)	H: Arginine methyltransferase oligomerization subdomain (From Topology)	T: Arginine methyltransferase oligomerization subdomain	F: PRMT5_C_1	ECOD (1.6)
D [auth G]	PrmA	e4lwoG2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: PrmA	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth B]	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
A [auth B]	2.70.160.11	Mainly Beta	Distorted Sandwich	Hnrnp arginine n-methyltransferase1	Hnrnp arginine n-methyltransferase1	CATH (4.3.0)
B [auth A]	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
B [auth A]	2.70.160.11	Mainly Beta	Distorted Sandwich	Hnrnp arginine n-methyltransferase1	Hnrnp arginine n-methyltransferase1	CATH (4.3.0)
C [auth E]	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
C [auth E]	2.70.160.11	Mainly Beta	Distorted Sandwich	Hnrnp arginine n-methyltransferase1	Hnrnp arginine n-methyltransferase1	CATH (4.3.0)
D [auth G]	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
D [auth G]	2.70.160.11	Mainly Beta	Distorted Sandwich	Hnrnp arginine n-methyltransferase1	Hnrnp arginine n-methyltransferase1	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], B [auth A], C [auth E], D [auth G]	Arginine N-methyltransferase, putative	protein-arginine C-methyltransferase activity C-methyltransferase activity catalytic activity, acting on a protein transferase activity, transferring one-carbon groups protein methyltransferase activity transferase activity methyltransferase activity catalytic activity S-adenosylmethionine-dependent methyltransferase activity protein-arginine N-methyltransferase activity histone methyltransferase activity histone arginine N-methyltransferase activity arginine N-methyltransferase activity histone modifying activity protein-arginine C-methyltransferase activity C-methyltransferase activity catalytic activity, acting on a protein transferase activity, transferring one-carbon groups protein methyltransferase activity transferase activity methyltransferase activity catalytic activity S-adenosylmethionine-dependent methyltransferase activity protein-arginine N-methyltransferase activity histone methyltransferase activity histone arginine N-methyltransferase activity arginine N-methyltransferase activity histone modifying activity N-methyltransferase activity	peptidyl-arginine omega-N-methylation organonitrogen compound metabolic process protein methylation peptidyl-arginine methylation primary metabolic process peptidyl-arginine N-methylation macromolecule methylation protein alkylation organic substance metabolic process methylation peptidyl-arginine methylation, to asymmetrical-dimethyl arginine macromolecule modification peptidyl-amino acid modification peptidyl-arginine modification peptidyl-arginine omega-N-methylation organonitrogen compound metabolic process protein methylation peptidyl-arginine methylation primary metabolic process peptidyl-arginine N-methylation macromolecule methylation protein alkylation organic substance metabolic process methylation peptidyl-arginine methylation, to asymmetrical-dimethyl arginine macromolecule modification peptidyl-amino acid modification peptidyl-arginine modification metabolic process protein metabolic process macromolecule metabolic process protein modification process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth A], C [auth E], D [auth G]	IPR025799	Protein arginine N-methyltransferase	Family
A [auth B], B [auth A], C [auth E], D [auth G]	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily	Homologous Superfamily

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.