1WG8 | pdb_00001wg8

Crystal structure of a predicted S-adenosylmethionine-dependent methyltransferase TT1512 from Thermus thermophilus HB8.

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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	d1wg8a1	All alpha proteins	SAM domain-like	Putative methyltransferase TM0872, insert domain	Putative methyltransferase TM0872, insert domain	Putative methyltransferase TM0872, insert domain	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)
A	d1wg8a2	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	MraW-like putative methyltransferases	TM0872, methyltransferase domain	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)
B	d1wg8b1	All alpha proteins	SAM domain-like	Putative methyltransferase TM0872, insert domain	Putative methyltransferase TM0872, insert domain	Putative methyltransferase TM0872, insert domain	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)
B	d1wg8b2	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	MraW-like putative methyltransferases	TM0872, methyltransferase domain	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Putative methyltransferase TM0872, insert domain	8031131	4002372	SCOP2 (2022-06-29)
A	SCOP2 Family	MraW-like putative methyltransferases	8031133	4003089	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Putative methyltransferase TM0872, insert domain	8043509	3001172	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	S-adenosyl-L-methionine-dependent methyltransferases	8043511	3000118	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	S-adenosyl-L-methionine-dependent methyltransferases	8043511	3000118	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Putative methyltransferase TM0872, insert domain	8043509	3001172	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)
A	Methyltransf_5_2nd	e1wg8A1	A: alpha arrays	X: HhH/H2TH	H: SAM/DNA-glycosylase	T: SAM domain-like	F: Methyltransf_5_2nd	ECOD (1.6)
A	Methyltransf_5_1st	e1wg8A2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: Methyltransf_5_1st	ECOD (1.6)
B	Methyltransf_5_2nd	e1wg8B1	A: alpha arrays	X: HhH/H2TH	H: SAM/DNA-glycosylase	T: SAM domain-like	F: Methyltransf_5_2nd	ECOD (1.6)
B	Methyltransf_5_1st	e1wg8B2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: Methyltransf_5_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
A	1.10.150.170	Mainly Alpha	Orthogonal Bundle	DNA polymerase	domain 1	CATH (4.3.0)
B	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
B	1.10.150.170	Mainly Alpha	Orthogonal Bundle	DNA polymerase	domain 1	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	predicted S-adenosylmethionine-dependent methyltransferase	RNA methyltransferase activity rRNA methyltransferase activity catalytic activity, acting on RNA transferase activity, transferring one-carbon groups catalytic activity, acting on a nucleic acid transferase activity catalytic activity, acting on a rRNA S-adenosylmethionine-dependent methyltransferase activity rRNA (cytosine-N4-)-methyltransferase activity N-methyltransferase activity methyltransferase activity catalytic activity rRNA (cytosine) methyltransferase activity	ribonucleoprotein complex biogenesis rRNA methylation RNA metabolic process rRNA processing rRNA modification nucleobase-containing compound metabolic process cellular component biogenesis RNA biosynthetic process ribosome biogenesis nucleic acid biosynthetic process cellular component organization or biogenesis RNA processing rRNA metabolic process primary metabolic process ribonucleoprotein complex biogenesis rRNA methylation RNA metabolic process rRNA processing rRNA modification nucleobase-containing compound metabolic process cellular component biogenesis RNA biosynthetic process ribosome biogenesis nucleic acid biosynthetic process cellular component organization or biogenesis RNA processing rRNA metabolic process primary metabolic process gene expression nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process macromolecule methylation RNA modification biosynthetic process methylation macromolecule modification metabolic process cellular process macromolecule metabolic process rRNA base methylation RNA methylation	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily	Homologous Superfamily
A, B	IPR002903	Ribosomal RNA small subunit methyltransferase H	Family
A, B	IPR023397	S-adenosyl-L-methionine-dependent methyltransferase, MraW, recognition domain superfamily	Homologous Superfamily

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.