Annotations: 1NI5

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ni5a3	All beta proteins	PheT/TilS domain	PheT/TilS domain	tRNA-Ile-lysidine synthetase, TilS, C-terminal domain	tRNA-Ile-lysidine synthetase, TilS, C-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1ni5a1	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Adenine nucleotide alpha hydrolases-like	PP-loop ATPase	tRNA-Ile-lysidine synthetase, TilS, N-terminal domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1ni5a4	Alpha and beta proteins (a+b)	MesJ substrate recognition domain-like	MesJ substrate recognition domain-like	MesJ substrate recognition domain-like	tRNA-Ile-lysidine synthetase, TilS, substrate-binding domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1ni5a5	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	PP-loop ATPase	8031456	4002958	SCOP2 (2022-06-29)
A	SCOP2 Family	MesJ substrate recognition domain-like	8029768	4003359	SCOP2 (2022-06-29)
A	SCOP2 Family	tRNA-Ile-lysidine synthetase TilS C-terminal domain	8029767	4002775	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Adenine nucleotide alpha hydrolases-like	8043834	3001593	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	MesJ substrate recognition domain-like	8042147	3000685	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PheT/TilS domain	8042146	3000688	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	PF11734	e1ni5A1	A: beta complex topology	X: PheT/TilS domain (From Topology)	H: PheT/TilS domain (From Topology)	T: PheT/TilS domain	F: PF11734	ECOD (1.6)
A	PF09179	e1ni5A2	A: a+b two layers	X: MesJ substrate recognition domain-like (From Topology)	H: MesJ substrate recognition domain-like (From Topology)	T: MesJ substrate recognition domain-like	F: PF09179	ECOD (1.6)
A	PF01171	e1ni5A3	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: PF01171	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
A	1.20.59.20	Mainly Alpha	Up-down Bundle	Chorismate Mutase Domain, subunit A		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF09179	TilS substrate binding domain (TilS)	TilS substrate binding domain	This domain is found in the tRNA(Ile) lysidine synthetase (TilS) protein.	Domain
A	PF01171	PP-loop family (ATP_bind_3)	PP-loop family	-	Family
A	PF11734	TilS substrate C-terminal domain (TilS_C)	TilS substrate C-terminal domain	This domain is found in the tRNA(Ile) lysidine synthetase (TilS) protein.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Putative cell cycle protein mesJ	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 catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid tRNA(Ile)-lysidine synthase activity catalytic activity, acting on a tRNA catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity identical protein binding protein binding	cellular biosynthetic process RNA metabolic process nucleobase-containing compound metabolic process organic substance metabolic process tRNA processing organic substance biosynthetic process RNA processing cellular metabolic process tRNA modification primary metabolic process gene expression macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process cellular biosynthetic process RNA metabolic process nucleobase-containing compound metabolic process organic substance metabolic process tRNA processing organic substance biosynthetic process RNA processing cellular metabolic process tRNA modification primary metabolic process gene expression macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process organic cyclic compound metabolic process RNA modification biosynthetic process ncRNA metabolic process macromolecule modification nucleic acid catabolic process metabolic process cellular process macromolecule metabolic process tRNA wobble base lysidine biosynthesis tRNA wobble cytosine modification tRNA wobble base modification	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR015262	tRNA(Ile)-lysidine synthase, substrate-binding domain	Domain
A	IPR011063	tRNA(Ile)-lysidine/2-thiocytidine synthase, N-terminal	Domain
A	IPR012795	tRNA(Ile)-lysidine synthase, N-terminal	Domain
A	IPR012796	Lysidine-tRNA(Ile) synthetase, C-terminal	Domain
A	IPR012094	tRNA(Ile)-lysidine synthase	Family
A	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	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.