3T5Q

3A structure of Lassa virus nucleoprotein in complex with ssRNA

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Arenavirus nucleoprotein N-terminal domain-like	8048310	4006049	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Arenavirus nucleoprotein N-terminal domain-like	8053519	3002201	SCOP2 (2022-06-29)
E	SCOP2B Superfamily	Arenavirus nucleoprotein N-terminal domain-like	8053519	3002201	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	Arenavirus nucleoprotein N-terminal domain-like	8053519	3002201	SCOP2B (2022-06-29)
C [auth B]	SCOP2B Superfamily	Arenavirus nucleoprotein N-terminal domain-like	8053519	3002201	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Arenavirus nucleoprotein N-terminal domain-like	8053519	3002201	SCOP2B (2022-06-29)
K	SCOP2B Superfamily	Arenavirus nucleoprotein N-terminal domain-like	8053519	3002201	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	PF00843	e3t5qA2	A: alpha complex topology	X: N-terminal domain in Lassa fever virus nucleoprotein (From Topology)	H: N-terminal domain in Lassa fever virus nucleoprotein (From Topology)	T: N-terminal domain in Lassa fever virus nucleoprotein	F: PF00843	ECOD (1.6)
E	PF00843	e3t5qE1	A: alpha complex topology	X: N-terminal domain in Lassa fever virus nucleoprotein (From Topology)	H: N-terminal domain in Lassa fever virus nucleoprotein (From Topology)	T: N-terminal domain in Lassa fever virus nucleoprotein	F: PF00843	ECOD (1.6)
I	PF00843	e3t5qI2	A: alpha complex topology	X: N-terminal domain in Lassa fever virus nucleoprotein (From Topology)	H: N-terminal domain in Lassa fever virus nucleoprotein (From Topology)	T: N-terminal domain in Lassa fever virus nucleoprotein	F: PF00843	ECOD (1.6)
C [auth B]	PF00843	e3t5qB1	A: alpha complex topology	X: N-terminal domain in Lassa fever virus nucleoprotein (From Topology)	H: N-terminal domain in Lassa fever virus nucleoprotein (From Topology)	T: N-terminal domain in Lassa fever virus nucleoprotein	F: PF00843	ECOD (1.6)
G	PF00843	e3t5qG2	A: alpha complex topology	X: N-terminal domain in Lassa fever virus nucleoprotein (From Topology)	H: N-terminal domain in Lassa fever virus nucleoprotein (From Topology)	T: N-terminal domain in Lassa fever virus nucleoprotein	F: PF00843	ECOD (1.6)
K	PF00843	e3t5qK1	A: alpha complex topology	X: N-terminal domain in Lassa fever virus nucleoprotein (From Topology)	H: N-terminal domain in Lassa fever virus nucleoprotein (From Topology)	T: N-terminal domain in Lassa fever virus nucleoprotein	F: PF00843	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
G	1.10.150.550	Mainly Alpha	Orthogonal Bundle	DNA polymerase	domain 1	CATH (4.3.0)
G	6.10.250.1200	Special	Helix non-globular	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C [auth B], E, G, I, A, C [auth B], E, G, I, K	PF00843	Arenavirus nucleocapsid N-terminal domain (Arena_nucleocap)	Arenavirus nucleocapsid N-terminal domain	This N-terminal domain folds into a novel structure with a deep cavity for binding the m7GpppN cap structure that is required for viral RNA transcription [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C [auth B], E, G, I, A, C [auth B], E, G, I, K	Nucleoprotein	hydrolase activity catalytic activity RNA binding binding organic cyclic compound binding nucleic acid binding cation binding ion binding metal ion binding small molecule binding	symbiont-mediated perturbation of host cellular process biological process involved in interspecies interaction between organisms response to stimulus symbiont-mediated suppression of host pathogen-associated molecular pattern receptor signaling pathway response to biotic stimulus biological process involved in symbiotic interaction symbiont-mediated suppression of host immune response symbiont-mediated suppression of host innate immune response response to host immune response symbiont-mediated suppression of host defenses symbiont-mediated perturbation of host innate immune response response to host response to external biotic stimulus symbiont-mediated perturbation of host signal transduction pathway symbiont-mediated perturbation of host cellular process biological process involved in interspecies interaction between organisms response to stimulus symbiont-mediated suppression of host pathogen-associated molecular pattern receptor signaling pathway response to biotic stimulus biological process involved in symbiotic interaction symbiont-mediated suppression of host immune response symbiont-mediated suppression of host innate immune response response to host immune response symbiont-mediated suppression of host defenses symbiont-mediated perturbation of host innate immune response response to host response to external biotic stimulus symbiont-mediated perturbation of host signal transduction pathway modulation of process of another organism symbiont-mediated perturbation of host defense response response to host defenses response to other organism symbiont-mediated perturbation of host immune response response to defenses of other organism symbiont-mediated perturbation of host defenses response to external stimulus biological process involved in interaction with host symbiont-mediated suppression of host signal transduction pathway modulation by symbiont of host process cellular process symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IKBKE activity symbiont-mediated suppression of cytoplasmic pattern recognition receptor signaling pathway viral gene expression viral process viral transcription RNA-templated viral transcription cellular biosynthetic process RNA metabolic process viral life cycle RNA biosynthetic process nucleobase-containing compound metabolic process nucleic acid biosynthetic process organic substance metabolic process viral RNA genome replication organic substance biosynthetic process cellular metabolic process primary metabolic process nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process organic cyclic compound metabolic process negative stranded viral RNA replication viral genome replication biosynthetic process organic cyclic compound biosynthetic process metabolic process macromolecule metabolic process	protein-containing complex ribonucleoprotein complex viral nucleocapsid viral capsid virion component host cellular component host intracellular part host cell cytoplasm host cell part host intracellular region cellular anatomical entity helical viral capsid
B [auth C], F	RNA (5'-R(PUPUPAPUPCPUPCPA)-3')	-	-	-
D	RNA (5'-R(PUPAPUPCPUPCP*A)-3')	-	-	-
H, L	RNA (5'-R(PUPAPUPCPUPC)-3')	-	-	-
J	RNA (5'-R(PUPUPAPUPCPUPCPC)-3')	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C [auth B], E, G, I, A, C [auth B], E, G, I, K	IPR038115	Nucleocapsid, C-terminal superfamily	Homologous Superfamily
A, C [auth B], E, G, I, A, C [auth B], E, G, I, K	IPR001680	WD40 repeat	Repeat
A, C [auth B], E, G, I, A, C [auth B], E, G, I, K	IPR000229	Nucleocapsid protein, arenaviridae	Family
A, C [auth B], E, G, I, A, C [auth B], E, G, I, K	IPR035083	Nucleocapsid, N-terminal, Arenaviridae	Domain
A, C [auth B], E, G, I, A, C [auth B], E, G, I, K	IPR035084	Nucleocapsid, C-terminal, Arenaviridae	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 R01GM133198.