Annotations: 1EJ6

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ej6a_	Low resolution protein structures	Reovirus components	Reovirus components	Reovirus components	Reovirus core	(Reovirus sp. ) [TaxId: 10891 ],	SCOPe (2.08)
B	d1ej6b_	Low resolution protein structures	Reovirus components	Reovirus components	Reovirus components	Reovirus core	(Reovirus sp. ) [TaxId: 10891 ],	SCOPe (2.08)
C	d1ej6c_	Low resolution protein structures	Reovirus components	Reovirus components	Reovirus components	Reovirus core	(Reovirus sp. ) [TaxId: 10891 ],	SCOPe (2.08)
D	d1ej6d_	Low resolution protein structures	Reovirus components	Reovirus components	Reovirus components	Reovirus core	(Reovirus sp. ) [TaxId: 10891 ],	SCOPe (2.08)
E	d1ej6e_	Low resolution protein structures	Reovirus components	Reovirus components	Reovirus components	Reovirus core	(Reovirus sp. ) [TaxId: 10891 ],	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	Reovirus_L2_6th	e1ej6A7	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Reovirus_L2_6th	ECOD (1.6)
A	Reovirus_L2_7th	e1ej6A1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Reovirus_L2_7th	ECOD (1.6)
A	Reovirus_L2_8th_1	e1ej6A8	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Reovirus_L2_8th_1	ECOD (1.6)
A	Reovirus_L2_4th	e1ej6A6	A: a+b two layers	X: ferredoxin-like domain in VP1 (From Topology)	H: ferredoxin-like domain in VP1 (From Topology)	T: ferredoxin-like domain in VP1	F: Reovirus_L2_4th	ECOD (1.6)
A	Reovirus_L2_2nd	e1ej6A4	A: a+b three layers	X: HIT-like	H: HIT-related (From Topology)	T: HIT-related	F: Reovirus_L2_2nd	ECOD (1.6)
A	Reovirus_L2_1st	e1ej6A5	A: a+b complex topology	X: Rotavirus NSP2 fragment, N-terminal domain (From Topology)	H: Rotavirus NSP2 fragment, N-terminal domain (From Topology)	T: Rotavirus NSP2 fragment, N-terminal domain	F: Reovirus_L2_1st	ECOD (1.6)
A	Reovirus_L2_3rd	e1ej6A2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: Reovirus_L2_3rd	ECOD (1.6)
A	Reovirus_L2_5th	e1ej6A3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: Reovirus_L2_5th	ECOD (1.6)
B	lambda-1	e1ej6B1	A: a+b complex topology	X: Inner layer core protein p3-related (From Topology)	H: Inner layer core protein p3-related (From Topology)	T: Inner layer core protein p3-related	F: lambda-1	ECOD (1.6)
C	lambda-1,zf-C2H2_6	e1ej6C1	A: a+b complex topology	X: Inner layer core protein p3-related (From Topology)	H: Inner layer core protein p3-related (From Topology)	T: Inner layer core protein p3-related	F: lambda-1,zf-C2H2_6	ECOD (1.6)
D	Sigma_1_2	e1ej6D1	A: alpha complex topology	X: Core protein VP6 (From Topology)	H: Core protein VP6 (From Topology)	T: Core protein VP6	F: Sigma_1_2	ECOD (1.6)
E	Sigma_1_2	e1ej6E1	A: alpha complex topology	X: Core protein VP6 (From Topology)	H: Core protein VP6 (From Topology)	T: Core protein VP6	F: Sigma_1_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.1810.10	Alpha Beta	Alpha-Beta Complex	Reovirus components fold	Reovirus components	CATH (4.3.0)
A	3.55.60.10	Alpha Beta	3-Layer(bab) Sandwich	Reovirus components fold	Reovirus components	CATH (4.3.0)
A	3.40.50.10760	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Reovirus core	CATH (4.3.0)
A	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
A	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)
B	3.90.1830.10	Alpha Beta	Alpha-Beta Complex	Inner capsid protein lambda-1	Inner capsid protein lambda-1	CATH (4.3.0)
C	3.90.1830.10	Alpha Beta	Alpha-Beta Complex	Inner capsid protein lambda-1	Inner capsid protein lambda-1	CATH (4.3.0)
D	1.10.287.1520	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)
E	1.10.287.1520	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF21064	Reovirus core-spike protein lambda-2 (L2), N-terminal (Reovirus_L2_N)	Reovirus core-spike protein lambda-2 (L2), N-terminal	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight dom ...	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight domains with the most N-terminal domain at the base of the turret and the most C-terminal domain at the top [2]. This entry represents the N-terminal domain which adopts an alpha/beta topology.	Domain
A	PF21063	Reovirus core-spike protein lambda-2 (L2), GTase domain (Reovirus_L2_GTase)	Reovirus core-spike protein lambda-2 (L2), GTase domain	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight dom ...	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight domains with the most N-terminal domain at the base of the turret and the most C-terminal domain at the top. This entry represents the second one, which contains the nucleotide-binding histidine triad (HIT)-like motif from the GTase (guanylyltransferase) domain [2].	Domain
A	PF21066	Reovirus core-spike protein lambda-2 (L2), methyltransferase-2 (Reovirus_L2_MT2)	Reovirus core-spike protein lambda-2 (L2), methyltransferase-2	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight dom ...	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight domains with the most N-terminal domain at the base of the turret and the most C-terminal domain at the top. This entry represents the second methyltransferase domain (MT2), which catalyses the last reaction, 2'O-methylation [2].	Domain
A	PF21065	Reovirus core-spike protein lambda-2 (L2), methyltransferase-1 (Reovirus_L2_MT1)	Reovirus core-spike protein lambda-2 (L2), methyltransferase-1	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight dom ...	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight domains with the most N-terminal domain at the base of the turret and the most C-terminal domain at the top. This entry represents the methyltransferase-1 domain [2] which adds a methyl group to the N7 of the guanosine added by the GTase [2].	Domain
A	PF21060	Reovirus core-spike protein lambda-2 (L2), 6th domain (Reovirus_L2_6th)	Reovirus core-spike protein lambda-2 (L2), 6th domain	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight dom ...	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight domains with the most N-terminal domain at the base of the turret and the most C-terminal domain at the top. This entry represents the sixth domain which, together with the seventh and eighth (Pfam:PF06016) domains forms a three-domain flap at the top of the turret, that may serve as a gate to retard exit of the 5' terminus of the mRNA [2]. This domain has a Ig-like fold, resembling the V of an antibody light chain [2].	Domain
A	PF21062	Reovirus core-spike protein lambda-2 (L2), ferredoxin-like domain (Reovirus_L2_4th)	Reovirus core-spike protein lambda-2 (L2), ferredoxin-like domain	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight dom ...	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight domains with the most N-terminal domain at the base of the turret and the most C-terminal domain at the top. This entry represents the fourth domain, which adopts a ferredoxin-like fold consisting of four beta-strands protected by alpha-helices that probably functions as a structural support for the three enzyme domains (two methyltransferase and GTase domains) [2].	Domain
A	PF06016	Reovirus core-spike protein lambda-2 (L2), C-terminal (Reovirus_L2_8th)	Reovirus core-spike protein lambda-2 (L2), C-terminal	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight dom ...	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight domains with the most N-terminal domain at the base of the turret and the most C-terminal domain at the top. This entry represents the C-terminal (eighth) domain which, together with the sixth and seventh domains, forms a three-domain flap at the top of the turret, that may serve as a gate to retard exit of the 5' terminus of the mRNA [2]. This domain has a Ig-like, resembling a truncated V region of an antibody light chain.	Domain
A	PF21061	Reovirus core-spike protein lambda-2 (L2), 7th domain (Reovirus_L2_7th)	Reovirus core-spike protein lambda-2 (L2), 7th domain	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight dom ...	Reovirus core-spike protein VP1/lambda-2 (VP1/L2) forms a pentamer that mediates enzymatic reactions in 5' capping of the viral plus-strand transcripts [1]. It forms a hollow cylinder with projecting turrets. Each VP1/L2 monomer consists of eight domains with the most N-terminal domain at the base of the turret and the most C-terminal domain at the top. This entry represents the seventh domain which, together with the sixth (Pfam:PF21060) and eighth (Pfam:PF06016) domains forms a three-domain flap at the top of the turret, that may serve as a gate to retard exit of the 5' terminus of the mRNA [2]. This domain has a Ig-like fold, resembling the C region of an antibody light chain [2].	Domain
D, E	PF03084	Reoviral Sigma1/Sigma2 family (Sigma_1_2)	Reoviral Sigma1/Sigma2 family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	LAMBDA2	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding guanylyltransferase activity mRNA guanylyltransferase activity RNA guanylyltransferase activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid transferase activity catalytic activity nucleotidyltransferase activity transferase activity, transferring phosphorus-containing groups RNA methyltransferase activity transferase activity, transferring one-carbon groups S-adenosylmethionine-dependent methyltransferase activity mRNA 5'-cap (guanine-N7-)-methyltransferase activity N-methyltransferase activity methyltransferase activity mRNA methyltransferase activity guanyl nucleotide binding GTP binding guanyl ribonucleotide binding	-	viral capsid icosahedral viral capsid virion component viral outer capsid
B, C	LAMBDA1	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity ATP-dependent activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid helicase activity RNA helicase activity ATP-dependent activity, acting on RNA cation binding metal ion binding	cellular biosynthetic process RNA metabolic process 7-methylguanosine RNA capping RNA capping mRNA processing nucleobase-containing compound metabolic process nucleic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process RNA processing 7-methylguanosine mRNA capping cellular metabolic process primary metabolic process gene expression cellular biosynthetic process RNA metabolic process 7-methylguanosine RNA capping RNA capping mRNA processing nucleobase-containing compound metabolic process nucleic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process RNA processing 7-methylguanosine mRNA capping cellular metabolic process primary metabolic process gene expression macromolecule biosynthetic process mRNA metabolic process nucleic acid metabolic process organic cyclic compound metabolic process biosynthetic process RNA 5'-end processing metabolic process cellular process macromolecule metabolic process	viral capsid icosahedral viral capsid virion component viral inner capsid
D, E	SIGMA2	-	-	viral capsid icosahedral viral capsid virion component viral inner capsid

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR048601	Reovirus core-spike protein lambda-2-like, GTase domain	Domain
A	IPR048602	Reovirus core-spike protein lambda-2-like, 7th domain	Domain
A	IPR048604	Reovirus core-spike protein lambda-2-like, ferredoxin-like domain	Domain
A	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily	Homologous Superfamily
A	IPR048598	Reovirus core-spike protein lambda-2-like, first methyltransferase domain	Domain
A	IPR048596	Reovirus core-spike protein lambda-2-like, N-terminal domain	Domain
A	IPR013783	Immunoglobulin-like fold	Homologous Superfamily
A	IPR048603	Reovirus core-spike protein lambda-2-like, 6th domain	Domain
A	IPR010311	Reovirus core-spike lambda-2	Family
A	IPR048597	Reovirus core-spike protein lambda-2-like, second methyltransferase domain	Domain
A	IPR048294	Reovirus core-spike protein lambda-2-like, C-terminal domain	Domain
B, C	IPR013087	Zinc finger C2H2-type	Domain
B, C	IPR044949	Inner capsid protein lambda-1/ VP3	Homologous Superfamily
D, E	IPR004317	Sigma1/sigma2, reoviral	Family

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.