1G6Q

CRYSTAL STRUCTURE OF YEAST ARGININE METHYLTRANSFERASE, HMT1

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 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)
B [auth 2]	d1g6q2_	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	Arginine methyltransferase	Arginine methyltransferase, HMT1	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
C [auth 3]	d1g6q3_	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	Arginine methyltransferase	Arginine methyltransferase, HMT1	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
D [auth 4]	d1g6q4_	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	Arginine methyltransferase	Arginine methyltransferase, HMT1	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
E [auth 5]	d1g6q5_	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	Arginine methyltransferase	Arginine methyltransferase, HMT1	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
A [auth 1]	d1g6q1_	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	Arginine methyltransferase	Arginine methyltransferase, HMT1	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
F [auth 6]	d1g6q6_	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	Arginine methyltransferase	Arginine methyltransferase, HMT1	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B [auth 2]	SCOP2B Superfamily	S-adenosyl-L-methionine-dependent methyltransferases	8032284	3000118	SCOP2B (2022-06-29)
B [auth 2]	SCOP2B Superfamily	Arginine methyltransferase C-terminal oligomerisation domain-like	8053428	3002184	SCOP2B (2022-06-29)
C [auth 3]	SCOP2B Superfamily	S-adenosyl-L-methionine-dependent methyltransferases	8032284	3000118	SCOP2B (2022-06-29)
C [auth 3]	SCOP2B Superfamily	Arginine methyltransferase C-terminal oligomerisation domain-like	8053428	3002184	SCOP2B (2022-06-29)
D [auth 4]	SCOP2B Superfamily	Arginine methyltransferase C-terminal oligomerisation domain-like	8053428	3002184	SCOP2B (2022-06-29)
D [auth 4]	SCOP2B Superfamily	S-adenosyl-L-methionine-dependent methyltransferases	8032284	3000118	SCOP2B (2022-06-29)
E [auth 5]	SCOP2B Superfamily	Arginine methyltransferase C-terminal oligomerisation domain-like	8053428	3002184	SCOP2B (2022-06-29)
E [auth 5]	SCOP2B Superfamily	S-adenosyl-L-methionine-dependent methyltransferases	8032284	3000118	SCOP2B (2022-06-29)
A [auth 1]	SCOP2 Family	Arginine methyltransferase	8019904	4000665	SCOP2 (2022-06-29)
A [auth 1]	SCOP2 Superfamily	Arginine methyltransferase C-terminal oligomerisation domain-like	8053428	3002184	SCOP2 (2022-06-29)
A [auth 1]	SCOP2 Superfamily	S-adenosyl-L-methionine-dependent methyltransferases	8032284	3000118	SCOP2 (2022-06-29)
F [auth 6]	SCOP2B Superfamily	Arginine methyltransferase C-terminal oligomerisation domain-like	8053428	3002184	SCOP2B (2022-06-29)
F [auth 6]	SCOP2B Superfamily	S-adenosyl-L-methionine-dependent methyltransferases	8032284	3000118	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B [auth 2]	PRMT5_C_1	e1g6q23	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 2]	PrmA	e1g6q22	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 3]	PRMT5_C_1	e1g6q33	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 3]	PrmA	e1g6q32	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 4]	PRMT5_C_1	e1g6q43	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 4]	PrmA	e1g6q42	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: PrmA	ECOD (1.6)
E [auth 5]	PRMT5_C_1	e1g6q53	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)
E [auth 5]	PrmA	e1g6q52	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: PrmA	ECOD (1.6)
A [auth 1]	PRMT5_C_1	e1g6q13	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 1]	PrmA	e1g6q12	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: PrmA	ECOD (1.6)
F [auth 6]	PRMT5_C_1	e1g6q63	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)
F [auth 6]	PrmA	e1g6q62	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)
B [auth 2]	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
B [auth 2]	2.70.160.11	Mainly Beta	Distorted Sandwich	Hnrnp arginine n-methyltransferase1	Hnrnp arginine n-methyltransferase1	CATH (4.3.0)
C [auth 3]	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
C [auth 3]	2.70.160.11	Mainly Beta	Distorted Sandwich	Hnrnp arginine n-methyltransferase1	Hnrnp arginine n-methyltransferase1	CATH (4.3.0)
D [auth 4]	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
D [auth 4]	2.70.160.11	Mainly Beta	Distorted Sandwich	Hnrnp arginine n-methyltransferase1	Hnrnp arginine n-methyltransferase1	CATH (4.3.0)
E [auth 5]	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
E [auth 5]	2.70.160.11	Mainly Beta	Distorted Sandwich	Hnrnp arginine n-methyltransferase1	Hnrnp arginine n-methyltransferase1	CATH (4.3.0)
A [auth 1]	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
A [auth 1]	2.70.160.11	Mainly Beta	Distorted Sandwich	Hnrnp arginine n-methyltransferase1	Hnrnp arginine n-methyltransferase1	CATH (4.3.0)
F [auth 6]	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
F [auth 6]	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 1], B [auth 2], C [auth 3], D [auth 4], E [auth 5], A [auth 1], B [auth 2], C [auth 3], D [auth 4], E [auth 5], F [auth 6]	PF22528	Arginine methyltransferase oligomerization subdomain (PRMT_C)	Arginine methyltransferase oligomerization subdomain	This entry represents a domain found C-terminal in protein arginine methyltransferases. This domain is involved in oligomerisation.	Domain
A [auth 1], B [auth 2], C [auth 3], D [auth 4], E [auth 5], A [auth 1], B [auth 2], C [auth 3], D [auth 4], E [auth 5], F [auth 6]	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 1], B [auth 2], C [auth 3], D [auth 4], E [auth 5], A [auth 1], B [auth 2], C [auth 3], D [auth 4], E [auth 5], F [auth 6]	HNRNP ARGININE N-METHYLTRANSFERASE	catalytic activity, acting on a protein transferase activity, transferring one-carbon groups protein methyltransferase activity histone modifying activity transferase activity methyltransferase activity catalytic activity histone methyltransferase activity arginine N-methyltransferase activity N-methyltransferase activity S-adenosylmethionine-dependent methyltransferase activity protein-arginine N-methyltransferase activity protein-arginine omega-N monomethyltransferase activity protein-arginine omega-N asymmetric methyltransferase activity catalytic activity, acting on a protein transferase activity, transferring one-carbon groups protein methyltransferase activity histone modifying activity transferase activity methyltransferase activity catalytic activity histone methyltransferase activity arginine N-methyltransferase activity N-methyltransferase activity S-adenosylmethionine-dependent methyltransferase activity protein-arginine N-methyltransferase activity protein-arginine omega-N monomethyltransferase activity protein-arginine omega-N asymmetric methyltransferase activity identical protein binding protein binding binding	cellular localization nitrogen compound transport nucleocytoplasmic transport transport nuclear transport mRNA transport localization mRNA export from nucleus establishment of localization in cell RNA localization nuclear export nucleobase-containing compound transport RNA transport nucleic acid transport cellular localization nitrogen compound transport nucleocytoplasmic transport transport nuclear transport mRNA transport localization mRNA export from nucleus establishment of localization in cell RNA localization nuclear export nucleobase-containing compound transport RNA transport nucleic acid transport intracellular transport gene expression establishment of localization macromolecule biosynthetic process RNA export from nucleus establishment of RNA localization biosynthetic process macromolecule localization cellular process metabolic process macromolecule metabolic process transcription elongation by RNA polymerase II regulation of cellular process positive regulation of DNA-templated transcription positive regulation of transcription elongation by RNA polymerase II positive regulation of biological process RNA metabolic process positive regulation of macromolecule biosynthetic process regulation of primary metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process DNA-templated transcription nucleic acid biosynthetic process positive regulation of metabolic process regulation of RNA metabolic process transcription by RNA polymerase II positive regulation of biosynthetic process positive regulation of DNA-templated transcription, elongation positive regulation of macromolecule metabolic process regulation of nucleobase-containing compound metabolic process positive regulation of cellular process regulation of RNA biosynthetic process regulation of biosynthetic process regulation of transcription by RNA polymerase II regulation of DNA-templated transcription elongation regulation of biological process positive regulation of nucleobase-containing compound metabolic process regulation of transcription elongation by RNA polymerase II biological regulation primary metabolic process regulation of macromolecule metabolic process nucleobase-containing compound biosynthetic process positive regulation of transcription by RNA polymerase II nucleic acid metabolic process positive regulation of RNA metabolic process regulation of gene expression DNA-templated transcription elongation positive regulation of RNA biosynthetic process regulation of macromolecule biosynthetic process regulation of DNA-templated transcription regulation of metabolic process negative regulation of termination of DNA-templated transcription negative regulation of biological process protein-containing complex disassembly regulation of protein-containing complex disassembly negative regulation of RNA biosynthetic process negative regulation of nucleobase-containing compound metabolic process cellular component disassembly negative regulation of DNA-templated transcription negative regulation of cellular component organization negative regulation of metabolic process negative regulation of macromolecule biosynthetic process regulation of termination of DNA-templated transcription negative regulation of RNA metabolic process regulation of cellular component organization DNA-templated transcription termination cellular component organization negative regulation of protein-containing complex disassembly negative regulation of cellular process cellular component organization or biogenesis negative regulation of macromolecule metabolic process protein-containing complex organization negative regulation of biosynthetic process oxoacid metabolic process modified amino acid biosynthetic process vitamin biosynthetic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process small molecule metabolic process amide metabolic process water-soluble vitamin metabolic process folic acid metabolic process dicarboxylic acid biosynthetic process folic acid biosynthetic process folic acid-containing compound biosynthetic process water-soluble vitamin biosynthetic process small molecule biosynthetic process dicarboxylic acid metabolic process modified amino acid metabolic process carboxylic acid metabolic process amide biosynthetic process vitamin metabolic process folic acid-containing compound metabolic process pteridine-containing compound biosynthetic process pteridine-containing compound metabolic process protein methylation peptidyl-arginine methylation macromolecule methylation protein alkylation methylation macromolecule modification peptidyl-amino acid modification peptidyl-arginine modification protein metabolic process protein modification process chromatin organization chromatin remodeling	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth 1], B [auth 2], C [auth 3], D [auth 4], E [auth 5], A [auth 1], B [auth 2], C [auth 3], D [auth 4], E [auth 5], F [auth 6]	IPR025799	Protein arginine N-methyltransferase	Family
A [auth 1], B [auth 2], C [auth 3], D [auth 4], E [auth 5], A [auth 1], B [auth 2], C [auth 3], D [auth 4], E [auth 5], F [auth 6]	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily	Homologous Superfamily
A [auth 1], B [auth 2], C [auth 3], D [auth 4], E [auth 5], A [auth 1], B [auth 2], C [auth 3], D [auth 4], E [auth 5], F [auth 6]	IPR055135	Protein arginine N-methyltransferase domain	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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 R01GM157729.