4U0Z

Eukaryotic Fic Domain containing protein with bound APCPP

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF02661	e4u0zA2	A: alpha bundles	X: Fic-like (From Topology)	H: Fic-like (From Topology)	T: Fic-like	F: PF02661	ECOD (1.6)
A	F_UNCLASSIFIED	e4u0zA1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: F_UNCLASSIFIED	ECOD (1.6)
B	PF02661	e4u0zB1	A: alpha bundles	X: Fic-like (From Topology)	H: Fic-like (From Topology)	T: Fic-like	F: PF02661	ECOD (1.6)
B	F_UNCLASSIFIED	e4u0zB2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: F_UNCLASSIFIED	ECOD (1.6)
C	PF02661	e4u0zC2	A: alpha bundles	X: Fic-like (From Topology)	H: Fic-like (From Topology)	T: Fic-like	F: PF02661	ECOD (1.6)
C	F_UNCLASSIFIED	e4u0zC1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: F_UNCLASSIFIED	ECOD (1.6)
D	PF02661	e4u0zD1	A: alpha bundles	X: Fic-like (From Topology)	H: Fic-like (From Topology)	T: Fic-like	F: PF02661	ECOD (1.6)
D	F_UNCLASSIFIED	e4u0zD2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: F_UNCLASSIFIED	ECOD (1.6)
E	PF02661	e4u0zE1	A: alpha bundles	X: Fic-like (From Topology)	H: Fic-like (From Topology)	T: Fic-like	F: PF02661	ECOD (1.6)
E	F_UNCLASSIFIED	e4u0zE2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: F_UNCLASSIFIED	ECOD (1.6)
F	PF02661	e4u0zF1	A: alpha bundles	X: Fic-like (From Topology)	H: Fic-like (From Topology)	T: Fic-like	F: PF02661	ECOD (1.6)
F	F_UNCLASSIFIED	e4u0zF2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: F_UNCLASSIFIED	ECOD (1.6)
G	PF02661	e4u0zG1	A: alpha bundles	X: Fic-like (From Topology)	H: Fic-like (From Topology)	T: Fic-like	F: PF02661	ECOD (1.6)
G	F_UNCLASSIFIED	e4u0zG2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: F_UNCLASSIFIED	ECOD (1.6)
H	PF02661	e4u0zH1	A: alpha bundles	X: Fic-like (From Topology)	H: Fic-like (From Topology)	T: Fic-like	F: PF02661	ECOD (1.6)
H	F_UNCLASSIFIED	e4u0zH2	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: F_UNCLASSIFIED	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.25.40.10	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Tetratricopeptide repeat domain	CATH (4.3.0)
A	1.10.3290.10	Mainly Alpha	Orthogonal Bundle	Fic-like fold	Fido-like domain	CATH (4.3.0)
B	1.25.40.10	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Tetratricopeptide repeat domain	CATH (4.3.0)
B	1.10.3290.10	Mainly Alpha	Orthogonal Bundle	Fic-like fold	Fido-like domain	CATH (4.3.0)
C	1.25.40.10	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Tetratricopeptide repeat domain	CATH (4.3.0)
C	1.10.3290.10	Mainly Alpha	Orthogonal Bundle	Fic-like fold	Fido-like domain	CATH (4.3.0)
D	1.25.40.10	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Tetratricopeptide repeat domain	CATH (4.3.0)
D	1.10.3290.10	Mainly Alpha	Orthogonal Bundle	Fic-like fold	Fido-like domain	CATH (4.3.0)
E	1.25.40.10	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Tetratricopeptide repeat domain	CATH (4.3.0)
E	1.10.3290.10	Mainly Alpha	Orthogonal Bundle	Fic-like fold	Fido-like domain	CATH (4.3.0)
F	1.25.40.10	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Tetratricopeptide repeat domain	CATH (4.3.0)
F	1.10.3290.10	Mainly Alpha	Orthogonal Bundle	Fic-like fold	Fido-like domain	CATH (4.3.0)
G	1.25.40.10	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Tetratricopeptide repeat domain	CATH (4.3.0)
G	1.10.3290.10	Mainly Alpha	Orthogonal Bundle	Fic-like fold	Fido-like domain	CATH (4.3.0)
H	1.25.40.10	Mainly Alpha	Alpha Horseshoe	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat	Tetratricopeptide repeat domain	CATH (4.3.0)
H	1.10.3290.10	Mainly Alpha	Orthogonal Bundle	Fic-like fold	Fido-like domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H	PF02661	Fic/DOC family (Fic)	Fic/DOC family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H	Adenosine monophosphate-protein transferase FICD	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 identical protein binding protein binding protein homodimerization activity protein dimerization activity Hsp70 protein binding protein-folding chaperone binding heat shock protein binding adenylyltransferase activity transferase activity nucleotidyltransferase activity catalytic activity AMPylase activity transferase activity, transferring phosphorus-containing groups phosphoric ester hydrolase activity catalytic activity, acting on a protein hydrolase activity, acting on ester bonds phosphoric diester hydrolase activity protein adenylylhydrolase activity hydrolase activity	cellular response to stimulus response to organic substance regulation of cellular process response to stimulus signaling regulation of cellular response to stress endoplasmic reticulum unfolded protein response regulation of response to endoplasmic reticulum stress regulation of signal transduction cell communication regulation of endoplasmic reticulum unfolded protein response cellular response to stress response to stress regulation of response to stress cellular response to stimulus response to organic substance regulation of cellular process response to stimulus signaling regulation of cellular response to stress endoplasmic reticulum unfolded protein response regulation of response to endoplasmic reticulum stress regulation of signal transduction cell communication regulation of endoplasmic reticulum unfolded protein response cellular response to stress response to stress regulation of response to stress signal transduction cellular response to organic substance regulation of IRE1-mediated unfolded protein response response to endoplasmic reticulum stress regulation of biological process regulation of signaling cellular response to topologically incorrect protein biological regulation cellular response to unfolded protein response to unfolded protein cellular response to chemical stimulus regulation of response to stimulus response to chemical response to topologically incorrect protein IRE1-mediated unfolded protein response regulation of cell communication cellular process organic substance metabolic process organonitrogen compound metabolic process protein denucleotidylation macromolecule modification protein deadenylylation metabolic process primary metabolic process protein metabolic process macromolecule metabolic process protein modification process protein nucleotidylation protein adenylylation negative regulation of hydrolase activity negative regulation of GTPase activity regulation of catalytic activity negative regulation of molecular function negative regulation of biological process negative regulation of catalytic activity regulation of GTPase activity regulation of molecular function regulation of hydrolase activity	membrane-bounded organelle intracellular anatomical structure organelle subcompartment membrane cellular anatomical entity intracellular membrane-bounded organelle endomembrane system endoplasmic reticulum subcompartment intracellular organelle organelle nuclear outer membrane-endoplasmic reticulum membrane network endoplasmic reticulum cytoplasm organelle membrane membrane-bounded organelle intracellular anatomical structure organelle subcompartment membrane cellular anatomical entity intracellular membrane-bounded organelle endomembrane system endoplasmic reticulum subcompartment intracellular organelle organelle nuclear outer membrane-endoplasmic reticulum membrane network endoplasmic reticulum cytoplasm organelle membrane endoplasmic reticulum membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR011990	Tetratricopeptide-like helical domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR036597	Fido-like domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR003812	Fido domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR040198	Fido domain-containing protein	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR019734	Tetratricopeptide repeat	Repeat

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F, G, H	Pharos: Q9BVA6	interstitial cystitis osteosarcoma spina bifida lung carcinoma pituitary cancer medulloblastoma psoriasis

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.