Annotations: 1N1H

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B [auth A]	d1n1ha_	Multi-domain proteins (alpha and beta)	DNA/RNA polymerases	DNA/RNA polymerases	RNA-dependent RNA-polymerase	Reovirus polymerase lambda3	(Mammalian orthoreovirus 3 Dearing ) [TaxId: 10886 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B [auth A]	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8043810	3001272	SCOP2B (2022-06-29)
B [auth A]	SCOP2B Superfamily	Nucleotide cyclase/DNA polymerase palm domain-like	8043810	3001272	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 A]	RdRP_5_3rd	e1n1hA1	A: alpha bundles	X: helical bundle domain in reverse transcriptase-like polymerases (From Topology)	H: helical bundle domain in reverse transcriptase-like polymerases (From Topology)	T: helical bundle domain in reverse transcriptase-like polymerases	F: RdRP_5_3rd	ECOD (1.6)
B [auth A]	RdRP_5_4th	e1n1hA5	A: alpha complex topology	X: C-terminal additional helical subdomain in reovirus polymerase lambda3 (From Topology)	H: C-terminal additional helical subdomain in reovirus polymerase lambda3 (From Topology)	T: C-terminal additional helical subdomain in reovirus polymerase lambda3	F: RdRP_5_4th	ECOD (1.6)
B [auth A]	RdRP_5_1st	e1n1hA2	A: alpha complex topology	X: N-terminal additional helical subdomain in reovirus polymerase lambda3 (From Homology)	H: N-terminal additional helical subdomain in reovirus polymerase lambda3	T: N-terminal additional helical subdomain in reovirus polymerase lambda3	F: RdRP_5_1st	ECOD (1.6)
B [auth A]	RdRP_5_2nd	e1n1hA4	A: a+b two layers	X: Alpha-beta plaits	H: Adenylyl and guanylyl cyclase catalytic domain-like	T: Adenylyl and guanylyl cyclase catalytic domain-like	F: RdRP_5_2nd	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B [auth A]	3.90.1850.10	Alpha Beta	Alpha-Beta Complex	RNA-directed RNA polymerase lambda-3	RNA-directed RNA polymerase lambda-3	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B]	5'-R(APUPUPAPGPC)-3'	-	-	-
B [auth A]	Minor core protein lambda 3	5'-3' RNA polymerase activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid RNA polymerase activity transferase activity RNA-dependent RNA polymerase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups hydrolase activity RNA binding binding organic cyclic compound binding nucleic acid binding 5'-3' RNA polymerase activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid RNA polymerase activity transferase activity RNA-dependent RNA polymerase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups hydrolase activity RNA binding binding organic cyclic compound binding nucleic acid binding nucleoside phosphate binding nucleotide binding heterocyclic compound binding small molecule binding	viral genome replication viral process viral life cycle	viral nucleocapsid viral capsid virion component

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B [auth A]	IPR007097	RNA-directed RNA polymerase, reovirus	Domain
B [auth A]	IPR043502	DNA/RNA polymerase superfamily	Homologous Superfamily
B [auth A]	IPR012915	Reovirus RNA-dependent RNA polymerase lambda 3	Family

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.