Annotations: 3IEG

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	PF00515	e3iegB3	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: PF00515	ECOD (1.6)
A	PF00515	e3iegA3	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: PF00515	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	1.25.40.10	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Tetratricopeptide repeat domain	CATH (4.3.0)
A	1.25.40.10	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Tetratricopeptide repeat domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF13181	Tetratricopeptide repeat (TPR_8)	Tetratricopeptide repeat	-	Repeat
A, B	PF00515	Tetratricopeptide repeat (TPR_1)	Tetratricopeptide repeat	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	DnaJ homolog subfamily C member 3	enzyme regulator activity protein kinase inhibitor activity molecular function inhibitor activity molecular function regulator activity enzyme inhibitor activity protein kinase regulator activity kinase inhibitor activity kinase regulator activity protein binding binding kinase binding enzyme binding protein kinase binding misfolded protein binding enzyme regulator activity protein kinase inhibitor activity molecular function inhibitor activity molecular function regulator activity enzyme inhibitor activity protein kinase regulator activity kinase inhibitor activity kinase regulator activity protein binding binding kinase binding enzyme binding protein kinase binding misfolded protein binding protein-folding chaperone binding	cellular response to stimulus regulation of cellular process response to stimulus organonitrogen compound biosynthetic process positive regulation of translation initiation in response to endoplasmic reticulum stress positive regulation of macromolecule biosynthetic process regulation of primary metabolic process positive regulation of translational initiation in response to stress post-transcriptional regulation of gene expression positive regulation of metabolic process organic substance biosynthetic process positive regulation of macromolecule metabolic process translational initiation positive regulation of translation in response to stress cellular response to stimulus regulation of cellular process response to stimulus organonitrogen compound biosynthetic process positive regulation of translation initiation in response to endoplasmic reticulum stress positive regulation of macromolecule biosynthetic process regulation of primary metabolic process positive regulation of translational initiation in response to stress post-transcriptional regulation of gene expression positive regulation of metabolic process organic substance biosynthetic process positive regulation of macromolecule metabolic process translational initiation positive regulation of translation in response to stress response to endoplasmic reticulum stress positive regulation of translation in response to endoplasmic reticulum stress regulation of biological process regulation of translational initiation cellular metabolic process regulation of protein metabolic process regulation of translation initiation in response to endoplasmic reticulum stress regulation of cellular metabolic process primary metabolic process regulation of gene expression biosynthetic process regulation of macromolecule biosynthetic process metabolic process macromolecule metabolic process positive regulation of translational initiation regulation of metabolic process cellular biosynthetic process positive regulation of protein metabolic process positive regulation of biological process positive regulation of translation positive regulation of cellular metabolic process regulation of translation in response to stress organic substance metabolic process cellular response to stress positive regulation of biosynthetic process response to stress protein metabolic process positive regulation of cellular process regulation of biosynthetic process organonitrogen compound metabolic process regulation of translation in response to endoplasmic reticulum stress biological regulation regulation of macromolecule metabolic process gene expression translation macromolecule biosynthetic process regulation of cellular biosynthetic process positive regulation of gene expression regulation of translation regulation of translational initiation in response to stress cellular process positive regulation of cellular biosynthetic process negative regulation of programmed cell death regulation of apoptotic process negative regulation of biological process regulation of programmed cell death cell death negative regulation of apoptotic process negative regulation of cellular process apoptotic process programmed cell death cellular response to cold response to abiotic stimulus response to cold response to temperature stimulus protein maturation protein folding protein folding in endoplasmic reticulum organonitrogen compound catabolic process catabolic process proteolysis involved in protein catabolic process protein catabolic process macromolecule catabolic process proteolysis organic substance catabolic process regulation of translational initiation by eIF2 alpha phosphorylation negative regulation of cellular metabolic process regulation of phosphate metabolic process phosphate-containing compound metabolic process negative regulation of protein modification process protein modification process phosphorus metabolic process negative regulation of protein metabolic process protein phosphorylation phosphorylation negative regulation of metabolic process eiF2alpha phosphorylation in response to endoplasmic reticulum stress negative regulation of protein phosphorylation macromolecule modification regulation of phosphorus metabolic process regulation of protein modification process regulation of protein phosphorylation negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation negative regulation of phosphate metabolic process negative regulation of macromolecule metabolic process negative regulation of phosphorus metabolic process regulation of phosphorylation negative regulation of phosphorylation response to organic substance cellular response to topologically incorrect protein signaling endoplasmic reticulum unfolded protein response cellular response to unfolded protein response to unfolded protein cell communication cellular response to chemical stimulus response to chemical response to topologically incorrect protein signal transduction cellular response to organic substance	membrane-bounded organelle intracellular anatomical structure membrane-enclosed lumen cellular anatomical entity intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen endoplasmic reticulum lumen intracellular organelle organelle lumen organelle endoplasmic reticulum cytoplasm cytosol membrane-bounded organelle intracellular anatomical structure membrane-enclosed lumen cellular anatomical entity intracellular membrane-bounded organelle endomembrane system intracellular organelle lumen endoplasmic reticulum lumen intracellular organelle organelle lumen organelle endoplasmic reticulum cytoplasm cytosol smooth endoplasmic reticulum

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR011990	Tetratricopeptide-like helical domain superfamily	Homologous Superfamily
A, B	IPR036869	Chaperone J-domain superfamily	Homologous Superfamily
A, B	IPR001440	TPR_1	Unknown
A, B	IPR001623	DnaJ domain	Domain
A, B	IPR019734	Tetratricopeptide repeat	Repeat

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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.