2KQR

Solution structure of the N-terminal domain (residues 1-111) of Brugia malayi asparaginyl-tRNA synthetase

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	KOG0555	e2kqrA1	A: a+b two layers	X: Asparaginal-tRNA synthetase N-terminal domain (From Topology)	H: Asparaginal-tRNA synthetase N-terminal domain (From Topology)	T: Asparaginal-tRNA synthetase N-terminal domain	F: KOG0555	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.1910.20	Alpha Beta	2-Layer Sandwich	so0334 like fold	asparaginyl-tRNA synthetase, N-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF20917	Asparaginal-tRNA synthetase, N-terminal domain (AsnRS_N)	Asparaginal-tRNA synthetase, N-terminal domain	This domain is found at the N-terminal domain of the eukaryotic protein Asparaginal-tRNA synthetase (AsnRS, also known as NARS1). AsnRS is essential for protein translation and has been related to autoimmune and neurological diseases. Unlike its bact ...	This domain is found at the N-terminal domain of the eukaryotic protein Asparaginal-tRNA synthetase (AsnRS, also known as NARS1). AsnRS is essential for protein translation and has been related to autoimmune and neurological diseases. Unlike its bacterial homologs, this protein has a conserved N-terminal extension (this entry) connected by an unstructured tether to the part of the enzyme that has homologues within eukaryotes and prokaryotes: an anticodon-binding domain (Pfam:PF01336), a hinge region (HR), and a catalytic domain (Pfam:PF00152). This domain folds into two alpha-helices and three beta-strands form a parallel/antiparallel mixed beta-sheet and has a characteristic lysine-rich helical motif that interacts with tRNA. It also shows chemokine activity through its interaction with C-C chemokine receptor 3 (CCR3) and the promotion of NRS-CCR3-mediated proinflammatory signaling [1-3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Asparaginyl-tRNA synthetase, cytoplasmic	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding nucleic acid binding asparagine-tRNA ligase activity ligase activity, forming carbon-oxygen bonds aminoacyl-tRNA ligase activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid catalytic activity, acting on a tRNA catalytic activity ligase activity	amino acid activation tRNA aminoacylation cellular biosynthetic process organonitrogen compound biosynthetic process RNA metabolic process amino acid metabolic process nucleobase-containing compound metabolic process organic substance metabolic process organic substance biosynthetic process protein metabolic process organonitrogen compound metabolic process cellular metabolic process primary metabolic process translation amino acid activation tRNA aminoacylation cellular biosynthetic process organonitrogen compound biosynthetic process RNA metabolic process amino acid metabolic process nucleobase-containing compound metabolic process organic substance metabolic process organic substance biosynthetic process protein metabolic process organonitrogen compound metabolic process cellular metabolic process primary metabolic process translation gene expression tRNA aminoacylation for protein translation macromolecule biosynthetic process asparaginyl-tRNA aminoacylation nucleic acid metabolic process tRNA metabolic process organic cyclic compound metabolic process biosynthetic process ncRNA metabolic process metabolic process cellular process macromolecule metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)	Homologous Superfamily
A	IPR002312	Aspartyl/Asparaginyl-tRNA synthetase, class IIb	Family
A	IPR048952	Asparagine--tRNA ligase, N-terminal domain	Domain
A	IPR004522	Asparagine-tRNA ligase	Family
A	IPR004365	OB-fold nucleic acid binding domain, AA-tRNA synthetase-type	Domain
A	IPR006195	Aminoacyl-tRNA synthetase, class II	Domain
A	IPR012340	Nucleic acid-binding, OB-fold	Homologous Superfamily
A	IPR004364	Aminoacyl-tRNA synthetase, class II (D/K/N)	Domain

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.