3R0Q

A Uniquely Open Conformation Revealed in the Crystal Structure of Arabidopsis Thaliana Protein Arginine Methyltransferase 10

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth C]	d3r0qc_	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	automated matches	automated matches	mouse-ear cress,thale-cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
B [auth G]	d3r0qg_	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	automated matches	automated matches	mouse-ear cress,thale-cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
C [auth A]	d3r0qa_	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	automated matches	automated matches	mouse-ear cress,thale-cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
D [auth E]	d3r0qe_	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	automated matches	automated matches	mouse-ear cress,thale-cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth C]	PF22528	e3r0qC3	A: beta sandwiches	X: Arginine methyltransferase oligomerization subdomain (From Topology)	H: Arginine methyltransferase oligomerization subdomain (From Topology)	T: Arginine methyltransferase oligomerization subdomain	F: PF22528	ECOD (1.6)
A [auth C]	PF06325	e3r0qC2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: PF06325	ECOD (1.6)
B [auth G]	PF22528	e3r0qG3	A: beta sandwiches	X: Arginine methyltransferase oligomerization subdomain (From Topology)	H: Arginine methyltransferase oligomerization subdomain (From Topology)	T: Arginine methyltransferase oligomerization subdomain	F: PF22528	ECOD (1.6)
B [auth G]	PF06325	e3r0qG2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: PF06325	ECOD (1.6)
C [auth A]	PF22528	e3r0qA3	A: beta sandwiches	X: Arginine methyltransferase oligomerization subdomain (From Topology)	H: Arginine methyltransferase oligomerization subdomain (From Topology)	T: Arginine methyltransferase oligomerization subdomain	F: PF22528	ECOD (1.6)
C [auth A]	PF06325	e3r0qA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: PF06325	ECOD (1.6)
D [auth E]	PF22528	e3r0qE3	A: beta sandwiches	X: Arginine methyltransferase oligomerization subdomain (From Topology)	H: Arginine methyltransferase oligomerization subdomain (From Topology)	T: Arginine methyltransferase oligomerization subdomain	F: PF22528	ECOD (1.6)
D [auth E]	PF06325	e3r0qE2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: PF06325	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

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

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth C], B [auth G], C [auth A], D [auth E]	PF06325	Ribosomal protein L11 methyltransferase (PrmA) (PrmA)	Ribosomal protein L11 methyltransferase (PrmA)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth C], B [auth G], C [auth A], D [auth E]	Probable protein arginine N-methyltransferase 4.2	catalytic activity, acting on a protein transferase activity, transferring one-carbon groups transferase activity S-adenosylmethionine-dependent methyltransferase activity protein-arginine N-methyltransferase activity protein-arginine omega-N asymmetric methyltransferase activity arginine N-methyltransferase activity protein methyltransferase activity N-methyltransferase activity methyltransferase activity catalytic activity protein-arginine omega-N monomethyltransferase activity histone methyltransferase activity histone arginine N-methyltransferase activity catalytic activity, acting on a protein transferase activity, transferring one-carbon groups transferase activity S-adenosylmethionine-dependent methyltransferase activity protein-arginine N-methyltransferase activity protein-arginine omega-N asymmetric methyltransferase activity arginine N-methyltransferase activity protein methyltransferase activity N-methyltransferase activity methyltransferase activity catalytic activity protein-arginine omega-N monomethyltransferase activity histone methyltransferase activity histone arginine N-methyltransferase activity histone modifying activity	developmental process multicellular organismal process reproductive system development reproductive process vegetative to reproductive phase transition of meristem developmental process involved in reproduction multicellular organism development anatomical structure development reproductive structure development post-embryonic development system development peptidyl-arginine omega-N-methylation organonitrogen compound metabolic process protein methylation developmental process multicellular organismal process reproductive system development reproductive process vegetative to reproductive phase transition of meristem developmental process involved in reproduction multicellular organism development anatomical structure development reproductive structure development post-embryonic development system development 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	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth C], B [auth G], C [auth A], D [auth E]	IPR025799	Protein arginine N-methyltransferase	Family
A [auth C], B [auth G], C [auth A], D [auth E]	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.