Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyArginine methyltransferase C-terminal oligomerisation domain-like8053430 3002184 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyS-adenosyl-L-methionine-dependent methyltransferases8034266 3000118 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF22528e1or8A3 A: beta sandwichesX: Arginine methyltransferase oligomerization subdomain (From Topology)H: Arginine methyltransferase oligomerization subdomain (From Topology)T: Arginine methyltransferase oligomerization subdomainF: PF22528ECOD (1.6)
APF13649e1or8A2 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: PF13649ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.40.50.150 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold Vaccinia Virus protein VP39CATH (4.3.0)
A2.70.160.11 Mainly Beta Distorted Sandwich Hnrnp arginine n-methyltransferase1 Hnrnp arginine n-methyltransferase1CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF13649Methyltransferase domain (Methyltransf_25)Methyltransferase domainThis family appears to be a methyltransferase domain.Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Protein arginine N-methyltransferase 1
B, C, D, E
Substrate peptide---

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
type I protein arginine methyltransferase  M-CSA #872

This eukaryotic enzyme catalyses the sequential dimethylation of one of the terminal guanidino nitrogen atoms in arginine residues, resulting in formation of asymmetric dimethylarginine residues.

Defined by 4 residues: ASP:A-38 [auth A-51]GLU:A-131 [auth A-144]GLU:A-140 [auth A-153]HIS:A-280 [auth A-293]
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