Annotations: 2KN4

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Canonical RBD	8064922	4000236	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	RNA-binding domain, RBD	8064923	3000110	SCOP2 (2022-06-29)
A	SCOP2B Superfamily	Immunoglobulin-binding domains-like	8090290	3000399	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	IgG_binding_B	e2kn4A1	A: a+b two layers	X: beta-Grasp	H: Immunoglobulin-binding domains (From Topology)	T: Immunoglobulin-binding domains	F: IgG_binding_B	ECOD (1.6)
A	RRM_1_4	e2kn4A2	A: a+b two layers	X: Alpha-beta plaits	H: RNA-binding domain, RBD (From Topology)	T: RNA-binding domain, RBD	F: RRM_1_4	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.20.10	Alpha Beta	Roll	Ubiquitin-like (UB roll)		CATH (4.3.0)
A	3.30.70.330	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	RRM (RNA recognition motif) domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00076	RNA recognition motif (RRM_1)	RNA recognition motif	The RRM motif (a.k.a. RRM, RBD, or RNP domain) is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and pro ...	The RRM motif (a.k.a. RRM, RBD, or RNP domain) is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins (Swiss:P05455) have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteristic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins (Swiss:P05455) are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.	Domain
A	PF01378	B domain (IgG_binding_B)	B domain	This domain is found as a tandem repeat in Streptococcal cell surface proteins, such as the IgG binding protein G.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Immunoglobulin G-binding protein G,Serine/arginine-rich splicing factor 2	protein-containing complex binding binding immunoglobulin binding IgG binding pre-mRNA binding RNA binding nucleic acid binding transcription corepressor activity transcription regulator activity transcription coregulator activity protein-macromolecule adaptor activity molecular adaptor activity protein binding kinase binding protein-containing complex binding binding immunoglobulin binding IgG binding pre-mRNA binding RNA binding nucleic acid binding transcription corepressor activity transcription regulator activity transcription coregulator activity protein-macromolecule adaptor activity molecular adaptor activity protein binding kinase binding protein kinase C binding enzyme binding protein kinase binding	RNA splicing RNA metabolic process primary metabolic process gene expression nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process nucleic acid biosynthetic process biosynthetic process metabolic process cellular process RNA processing RNA splicing RNA metabolic process primary metabolic process gene expression nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process nucleic acid biosynthetic process biosynthetic process metabolic process cellular process RNA processing macromolecule metabolic process regulation of cellular process alternative mRNA splicing, via spliceosome regulation of mRNA splicing, via spliceosome mRNA processing regulation of primary metabolic process regulation of RNA metabolic process regulation of nucleobase-containing compound metabolic process regulation of biosynthetic process regulation of mRNA processing regulation of biological process biological regulation regulation of macromolecule metabolic process regulation of RNA splicing mRNA metabolic process regulation of gene expression RNA splicing, via transesterification reactions regulation of alternative mRNA splicing, via spliceosome mRNA splicing, via spliceosome RNA splicing, via transesterification reactions with bulged adenosine as nucleophile regulation of macromolecule biosynthetic process regulation of mRNA metabolic process regulation of metabolic process response to nutrient levels response to stimulus response to chemical response to nutrient response to oxygen-containing compound response to vitamin E response to vitamin	cellular anatomical structure extracellular region membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen perichromatin fibrils nuclear chromosome intracellular membraneless organelle chromosome chromatin intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle cellular anatomical structure extracellular region membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen perichromatin fibrils nuclear chromosome intracellular membraneless organelle chromosome chromatin intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle organelle lumen organelle membraneless organelle nuclear lumen nuclear body interchromatin granule nucleoplasm nuclear speck protein-containing complex nuclear protein-containing complex spliceosomal complex ribonucleoprotein complex cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR009063	Immunoglobulin/albumin-binding domain superfamily	Homologous Superfamily
A	IPR019950	M protein-type anchor domain	Domain
A	IPR005877	YSIRK Gram-positive signal peptide	Domain
A	IPR000724	IgG-binding B	Domain
A	IPR035152	GA-like domain	Domain
A	IPR019931	LPXTG cell wall anchor domain	Domain
A	IPR051106	RNA-binding and splicing regulatory protein	Family
A	IPR000504	RNA recognition motif domain	Domain
A	IPR003954	RNA recognition motif domain, eukaryotes	Domain
A	IPR012677	Nucleotide-binding alpha-beta plait domain superfamily	Homologous Superfamily
A	IPR035979	RNA-binding domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: Q01130	progressive supranuclear palsy sarcomatoid carcinoma Mammary Neoplasms, Experimental carcinoma Pick disease B-cell chronic lymphocytic leukemia glioblastoma lung cancer osteosarcoma plasma cell myeloma systemic mastocytosis bone marrow disease congenital anemia large cell medulloblastoma medulloblastoma progressive supranuclear palsy sarcomatoid carcinoma Mammary Neoplasms, Experimental carcinoma Pick disease B-cell chronic lymphocytic leukemia glioblastoma lung cancer osteosarcoma plasma cell myeloma systemic mastocytosis bone marrow disease congenital anemia large cell medulloblastoma medulloblastoma ovarian cancer undifferentiated carcinoma astrocytic tumor lung adenocarcinoma mammary neoplasms, animal myelodysplastic syndrome

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.