Annotations: 4CA9

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF17800	e4ca9A1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF17800	ECOD (1.6)
B	PF17800	e4ca9B1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF17800	ECOD (1.6)
C	PF17800	e4ca9C1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF17800	ECOD (1.6)
D	PF17800	e4ca9D1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF17800	ECOD (1.6)
E	PF17800	e4ca9E1	A: beta sandwiches	X: jelly-roll	H: Nucleoplasmin-like/VP (viral coat and capsid proteins) (From Topology)	T: Nucleoplasmin-like/VP (viral coat and capsid proteins)	F: PF17800	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.120.340	Mainly Beta	Sandwich	Jelly Rolls	Nucleoplasmin core domain	CATH (4.3.0)
B	2.60.120.340	Mainly Beta	Sandwich	Jelly Rolls	Nucleoplasmin core domain	CATH (4.3.0)
C	2.60.120.340	Mainly Beta	Sandwich	Jelly Rolls	Nucleoplasmin core domain	CATH (4.3.0)
D	2.60.120.340	Mainly Beta	Sandwich	Jelly Rolls	Nucleoplasmin core domain	CATH (4.3.0)
E	2.60.120.340	Mainly Beta	Sandwich	Jelly Rolls	Nucleoplasmin core domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E	PF17800	Nucleoplasmin-like domain (NPL)	Nucleoplasmin-like domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E	39 KDA FK506-BINDING NUCLEAR PROTEIN	isomerase activity catalytic activity, acting on a protein peptidyl-prolyl cis-trans isomerase activity catalytic activity cis-trans isomerase activity FK506 binding amide binding binding organic cyclic compound binding macrolide binding DNA binding sequence-specific DNA binding double-stranded DNA binding nucleic acid binding isomerase activity catalytic activity, acting on a protein peptidyl-prolyl cis-trans isomerase activity catalytic activity cis-trans isomerase activity FK506 binding amide binding binding organic cyclic compound binding macrolide binding DNA binding sequence-specific DNA binding double-stranded DNA binding nucleic acid binding RNA polymerase II transcription regulatory region sequence-specific DNA binding cis-regulatory region sequence-specific DNA binding juvenile hormone response element binding sequence-specific double-stranded DNA binding transcription cis-regulatory region binding transcription regulatory region nucleic acid binding RNA polymerase II cis-regulatory region sequence-specific DNA binding	negative regulation of cellular catabolic process negative regulation of catabolic process regulation of biological process catabolic process regulation of cellular process cellular metabolic process negative regulation of metabolic process autophagy biological regulation negative regulation of biological process regulation of cellular metabolic process regulation of catabolic process regulation of autophagy negative regulation of cellular metabolic process cellular catabolic process negative regulation of cellular catabolic process negative regulation of catabolic process regulation of biological process catabolic process regulation of cellular process cellular metabolic process negative regulation of metabolic process autophagy biological regulation negative regulation of biological process regulation of cellular metabolic process regulation of catabolic process regulation of autophagy negative regulation of cellular metabolic process cellular catabolic process negative regulation of autophagy regulation of cellular catabolic process negative regulation of cellular process cellular process metabolic process process utilizing autophagic mechanism regulation of metabolic process macroautophagy negative regulation of macroautophagy regulation of macroautophagy cellular response to stimulus response to organic substance intracellular receptor signaling pathway response to stimulus signaling response to endogenous stimulus hormone-mediated signaling pathway cell communication cellular response to endogenous stimulus cellular response to chemical stimulus response to hormone response to chemical signal transduction cellular response to organic substance juvenile hormone mediated signaling pathway cellular response to hormone stimulus	membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle cellular anatomical entity nucleolus intracellular organelle lumen intracellular organelle organelle lumen organelle intracellular non-membrane-bounded organelle nuclear lumen non-membrane-bounded organelle membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle cellular anatomical entity nucleolus intracellular organelle lumen intracellular organelle organelle lumen organelle intracellular non-membrane-bounded organelle nuclear lumen non-membrane-bounded organelle protein-containing complex protein-DNA complex chromatin chromosome heterochromatin

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E	IPR046357	Peptidyl-prolyl cis-trans isomerase domain superfamily	Homologous Superfamily
A, B, C, D, E	IPR001179	FKBP-type peptidyl-prolyl cis-trans isomerase domain	Domain
A, B, C, D, E	IPR023566	Peptidyl-prolyl cis-trans isomerase Fpr3/Fpr4-like	Family
A, B, C, D, E	IPR041232	Nucleoplasmin-like domain	Domain

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.