2L8D

Structure/function of the LBR Tudor domain

External Resource: Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2l8da1	All beta proteins	SH3-like barrel	Tudor/PWWP/MBT	Tudor domain	Lamin-b receptor	bantam,chickens (Gallus gallus ) [TaxId: 9031 ],	SCOPe (2.08)
A	d2l8da2	Artifacts	Tags	Tags	Tags	N-terminal Tags	bantam,chickens (Gallus gallus ) [TaxId: 9031 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Tudor domain	8085038	4003195	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Tudor/PWWP/MBT domain-like	8085039	3000404	SCOP2 (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	LBR_tudor	e2l8dA1	A: beta barrels	X: SH3	H: SH3	T: SH3	F: LBR_tudor	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.30.30.140	Mainly Beta	Roll	SH3 type barrels.		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF09465	Lamin-B receptor of TUDOR domain (LBR_tudor)	Lamin-B receptor of TUDOR domain	The Lamin-B receptor, found on the TUDOR domain Pfam:PF00567, is a chromatin and lamin binding protein in the inner nuclear membrane. It is one of the integral inner Nuclear Envelope membrane proteins responsible for targeting nuclear membranes to ch ...	The Lamin-B receptor, found on the TUDOR domain Pfam:PF00567, is a chromatin and lamin binding protein in the inner nuclear membrane. It is one of the integral inner Nuclear Envelope membrane proteins responsible for targeting nuclear membranes to chromatin, being a downstream effector of Ran, a small Ras-like nuclear GTPase which regulates NE assembly. Lamin-B receptor interacts with Importin beta, a Ran-binding protein, thereby directly contributing to the fusion of membrane vesicles and the formation of the NE [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Lamin-B receptor	DNA binding binding organic cyclic compound binding nucleic acid binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding heterocyclic compound binding NADPH binding NADP binding small molecule binding DNA binding binding organic cyclic compound binding nucleic acid binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding heterocyclic compound binding NADPH binding NADP binding small molecule binding oxidoreductase activity oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on the CH-CH group of donors delta14-sterol reductase activity catalytic activity	developmental process myeloid leukocyte differentiation cellular developmental process hemopoiesis cell development granulocyte differentiation myeloid cell differentiation cell differentiation neutrophil differentiation anatomical structure development cellular process leukocyte differentiation organic hydroxy compound metabolic process sterol metabolic process developmental process myeloid leukocyte differentiation cellular developmental process hemopoiesis cell development granulocyte differentiation myeloid cell differentiation cell differentiation neutrophil differentiation anatomical structure development cellular process leukocyte differentiation organic hydroxy compound metabolic process sterol metabolic process steroid metabolic process cholesterol metabolic process lipid biosynthetic process alcohol metabolic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process steroid biosynthetic process secondary alcohol biosynthetic process small molecule biosynthetic process cholesterol biosynthetic process primary metabolic process organic cyclic compound metabolic process secondary alcohol metabolic process biosynthetic process sterol biosynthetic process organic hydroxy compound biosynthetic process organic cyclic compound biosynthetic process alcohol biosynthetic process metabolic process lipid metabolic process	membrane-bounded organelle intracellular anatomical structure organelle inner membrane nuclear membrane membrane nucleus cellular anatomical entity intracellular membrane-bounded organelle endomembrane system intracellular organelle organelle envelope organelle nuclear inner membrane nuclear envelope membrane-bounded organelle intracellular anatomical structure organelle inner membrane nuclear membrane membrane nucleus cellular anatomical entity intracellular membrane-bounded organelle endomembrane system intracellular organelle organelle envelope organelle nuclear inner membrane nuclear envelope organelle membrane cytoplasm organelle subcompartment endoplasmic reticulum subcompartment nuclear outer membrane-endoplasmic reticulum membrane network endoplasmic reticulum endoplasmic reticulum membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR018083	Sterol reductase, conserved site	Conserved Site
A	IPR002999	Tudor domain	Domain
A	IPR019023	Lamin-B receptor of TUDOR domain	Domain
A	IPR001171	Sterol biosynthesis ERG24/DHCR-like	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.