Annotations: 2KTL

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Tyrosyl-tRNA synthetase (TyrRS) C-terminal domain	8046024	4002686	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Alpha-L RNA-binding motif	8092723	3001473	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	PF16714	e2ktlA1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Alpha-L RNA-binding motif	F: PF16714	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF16714	Tyrosyl-tRNA synthetase C-terminal domain (TyrRSs_C)	Tyrosyl-tRNA synthetase C-terminal domain	This domain is found at the C-terminus of fungal tyrosyl-tRNA synthetases. It binds to group I introns [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Tyrosyl-tRNA synthetase	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 ligase activity, forming carbon-oxygen bonds aminoacyl-tRNA ligase activity tyrosine-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 RNA binding nucleic acid binding	amino acid activation tRNA aminoacylation RNA metabolic process primary metabolic process amino acid metabolic process nucleic acid metabolic process tRNA metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process organic substance metabolic process ncRNA metabolic process metabolic process macromolecule metabolic process tyrosyl-tRNA aminoacylation amino acid activation tRNA aminoacylation RNA metabolic process primary metabolic process amino acid metabolic process nucleic acid metabolic process tRNA metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process organic substance metabolic process ncRNA metabolic process metabolic process macromolecule metabolic process tyrosyl-tRNA aminoacylation cellular biosynthetic process organonitrogen compound biosynthetic process organic substance biosynthetic process protein metabolic process organonitrogen compound metabolic process cellular metabolic process translation gene expression tRNA aminoacylation for protein translation macromolecule biosynthetic process biosynthetic process cellular process	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR032005	Tyrosyl-tRNA synthetase, C-terminal	Domain
A	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	Homologous Superfamily
A	IPR002307	Tyrosine-tRNA ligase	Family
A	IPR002305	Aminoacyl-tRNA synthetase, class Ic	Family
A	IPR024088	Tyrosine-tRNA ligase, bacterial-type	Family
A	IPR036986	RNA-binding S4 domain superfamily	Homologous Superfamily

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.