1XPI

Crystal structure of the catalytic domain of E. coli pseudouridine synthase RluC

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Pseudouridine synthase	8041225	3001360	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Pseudouridine synthase	8041225	3001360	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	PseudoU_synth_2	e1xpiA1	A: a+b two layers	X: Alpha-beta plaits	H: Pseudouridine synthase (From Topology)	T: Pseudouridine synthase	F: PseudoU_synth_2	ECOD (1.6)
B	PseudoU_synth_2	e1xpiB1	A: a+b two layers	X: Alpha-beta plaits	H: Pseudouridine synthase (From Topology)	T: Pseudouridine synthase	F: PseudoU_synth_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.2350.10	Alpha Beta	2-Layer Sandwich	Pseudouridine synthase	Pseudouridine synthase	CATH (4.3.0)
B	3.30.2350.10	Alpha Beta	2-Layer Sandwich	Pseudouridine synthase	Pseudouridine synthase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00849	RNA pseudouridylate synthase (PseudoU_synth_2)	RNA pseudouridylate synthase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Ribosomal large subunit pseudouridine synthase C	isomerase activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid pseudouridine synthase activity rRNA pseudouridine synthase activity catalytic activity intramolecular transferase activity RNA binding binding organic cyclic compound binding nucleic acid binding	ribonucleoprotein complex biogenesis cellular biosynthetic process RNA metabolic process rRNA processing enzyme-directed rRNA pseudouridine synthesis rRNA modification nucleobase-containing compound metabolic process cellular component biogenesis ribosome biogenesis organic substance metabolic process organic substance biosynthetic process cellular component organization or biogenesis RNA processing rRNA metabolic process ribonucleoprotein complex biogenesis cellular biosynthetic process RNA metabolic process rRNA processing enzyme-directed rRNA pseudouridine synthesis rRNA modification nucleobase-containing compound metabolic process cellular component biogenesis ribosome biogenesis organic substance metabolic process organic substance biosynthetic process cellular component organization or biogenesis RNA processing rRNA metabolic process pseudouridine synthesis rRNA pseudouridine synthesis cellular metabolic process primary metabolic process gene expression macromolecule biosynthetic process nucleic acid metabolic process organic cyclic compound metabolic process RNA modification biosynthetic process macromolecule modification ncRNA metabolic process nucleic acid catabolic process metabolic process cellular process macromolecule metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR020103	Pseudouridine synthase, catalytic domain superfamily	Homologous Superfamily
A, B	IPR006225	Pseudouridine synthase, RluC/RluD	Family
A, B	IPR002942	RNA-binding S4 domain	Domain
A, B	IPR036986	RNA-binding S4 domain superfamily	Homologous Superfamily
A, B	IPR006145	Pseudouridine synthase, RsuA/RluA-like	Domain
A, B	IPR006224	Pseudouridine synthase, RluA-like, conserved site	Conserved Site

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.