3ZLA

Crystal structure of the nucleocapsid protein from Bunyamwera virus bound to RNA

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	SCOP2B Superfamily	PepMV Coat protein-like	8089912	3002401	SCOP2B (2022-06-29)
B	SCOP2 Family	BUNV nucleocapsid protein-like	8048492	4006117	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	PepMV Coat protein-like	8089912	3002401	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	PepMV Coat protein-like	8089912	3002401	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	PepMV Coat protein-like	8089912	3002401	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	PepMV Coat protein-like	8089912	3002401	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	PepMV Coat protein-like	8089912	3002401	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	PepMV Coat protein-like	8089912	3002401	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	PepMV Coat protein-like	8089912	3002401	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	PF00952	e3zlaA1	A: alpha complex topology	X: Leanyer virus nucleoprotein-related (From Topology)	H: Leanyer virus nucleoprotein-related (From Topology)	T: Leanyer virus nucleoprotein-related	F: PF00952	ECOD (1.6)
B	PF00952	e3zlaB1	A: alpha complex topology	X: Leanyer virus nucleoprotein-related (From Topology)	H: Leanyer virus nucleoprotein-related (From Topology)	T: Leanyer virus nucleoprotein-related	F: PF00952	ECOD (1.6)
C	PF00952	e3zlaC1	A: alpha complex topology	X: Leanyer virus nucleoprotein-related (From Topology)	H: Leanyer virus nucleoprotein-related (From Topology)	T: Leanyer virus nucleoprotein-related	F: PF00952	ECOD (1.6)
D	PF00952	e3zlaD1	A: alpha complex topology	X: Leanyer virus nucleoprotein-related (From Topology)	H: Leanyer virus nucleoprotein-related (From Topology)	T: Leanyer virus nucleoprotein-related	F: PF00952	ECOD (1.6)
E	PF00952	e3zlaE1	A: alpha complex topology	X: Leanyer virus nucleoprotein-related (From Topology)	H: Leanyer virus nucleoprotein-related (From Topology)	T: Leanyer virus nucleoprotein-related	F: PF00952	ECOD (1.6)
F	PF00952	e3zlaF1	A: alpha complex topology	X: Leanyer virus nucleoprotein-related (From Topology)	H: Leanyer virus nucleoprotein-related (From Topology)	T: Leanyer virus nucleoprotein-related	F: PF00952	ECOD (1.6)
G	PF00952	e3zlaG1	A: alpha complex topology	X: Leanyer virus nucleoprotein-related (From Topology)	H: Leanyer virus nucleoprotein-related (From Topology)	T: Leanyer virus nucleoprotein-related	F: PF00952	ECOD (1.6)
H	PF00952	e3zlaH1	A: alpha complex topology	X: Leanyer virus nucleoprotein-related (From Topology)	H: Leanyer virus nucleoprotein-related (From Topology)	T: Leanyer virus nucleoprotein-related	F: PF00952	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.20.142.20	Mainly Alpha	Up-down Bundle	Poly(ADP-ribose) Polymerase	domain 1	CATH (4.3.0)
A	1.10.472.180	Mainly Alpha	Orthogonal Bundle	Cyclin A	domain 1	CATH (4.3.0)
B	1.20.142.20	Mainly Alpha	Up-down Bundle	Poly(ADP-ribose) Polymerase	domain 1	CATH (4.3.0)
B	1.10.472.180	Mainly Alpha	Orthogonal Bundle	Cyclin A	domain 1	CATH (4.3.0)
C	1.20.142.20	Mainly Alpha	Up-down Bundle	Poly(ADP-ribose) Polymerase	domain 1	CATH (4.3.0)
C	1.10.472.180	Mainly Alpha	Orthogonal Bundle	Cyclin A	domain 1	CATH (4.3.0)
D	1.20.142.20	Mainly Alpha	Up-down Bundle	Poly(ADP-ribose) Polymerase	domain 1	CATH (4.3.0)
D	1.10.472.180	Mainly Alpha	Orthogonal Bundle	Cyclin A	domain 1	CATH (4.3.0)
E	1.20.142.20	Mainly Alpha	Up-down Bundle	Poly(ADP-ribose) Polymerase	domain 1	CATH (4.3.0)
E	1.10.472.180	Mainly Alpha	Orthogonal Bundle	Cyclin A	domain 1	CATH (4.3.0)
F	1.20.142.20	Mainly Alpha	Up-down Bundle	Poly(ADP-ribose) Polymerase	domain 1	CATH (4.3.0)
F	1.10.472.180	Mainly Alpha	Orthogonal Bundle	Cyclin A	domain 1	CATH (4.3.0)
G	1.20.142.20	Mainly Alpha	Up-down Bundle	Poly(ADP-ribose) Polymerase	domain 1	CATH (4.3.0)
G	1.10.472.180	Mainly Alpha	Orthogonal Bundle	Cyclin A	domain 1	CATH (4.3.0)
H	1.20.142.20	Mainly Alpha	Up-down Bundle	Poly(ADP-ribose) Polymerase	domain 1	CATH (4.3.0)
H	1.10.472.180	Mainly Alpha	Orthogonal Bundle	Cyclin A	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H	PF00952	Bunyavirus nucleocapsid (N) protein (Bunya_nucleocap)	Bunyavirus nucleocapsid (N) protein	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H	NUCLEOPROTEIN	RNA binding binding organic cyclic compound binding nucleic acid binding	symbiont-mediated perturbation of host cellular process symbiont-mediated suppression of host gene expression biological process involved in interspecies interaction between organisms modulation by symbiont of host process symbiont-mediated perturbation of host gene expression cellular process modulation of process of another organism biological process involved in interaction with host biological process involved in symbiotic interaction	protein-containing complex ribonucleoprotein complex viral nucleocapsid viral capsid virion component helical viral capsid
I, J	RNA	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR043011	Bunyavirus nucleocapsid (N) , C-terminal domain	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR043012	Bunyavirus nucleocapsid (N) , N-terminal domain	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR001784	Bunyavirus nucleocapsid (N) protein	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.