1O9F

Structural view of a fungal toxin acting on a 14-3-3 regulatory complex

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1o9fa_	All alpha proteins	alpha-alpha superhelix	14-3-3 protein	14-3-3 protein	14-3-3-like protein C	COMMON TOBACCO (Nicotiana tabacum ) [TaxId: 4097 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	14-3-3 protein	8033898	3001329	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	14-3-3	e1o9fA1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: 14-3-3	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.20.190.20	Mainly Alpha	Up-down Bundle	Delta-Endotoxin	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00244	14-3-3 protein (14-3-3)	14-3-3 protein	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	14-3-3-LIKE PROTEIN C	-	cellular response to stimulus regulation of biological process regulation of cellular process response to stimulus signaling biological regulation cellular process signal transduction cell communication	intracellular anatomical structure cytoplasm cellular anatomical entity
B [auth P]	PLASMA MEMBRANE H+ ATPASE	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 pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity ATP-dependent activity	-	membrane cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036815	14-3-3 domain superfamily	Homologous Superfamily
A	IPR000308	14-3-3 protein	Family
A	IPR023409	14-3-3 protein, conserved site	Conserved Site
A	IPR023410	14-3-3 domain	Domain
B [auth P]	IPR036412	HAD-like superfamily	Homologous Superfamily
B [auth P]	IPR023214	HAD superfamily	Homologous Superfamily
B [auth P]	IPR023298	P-type ATPase, transmembrane domain superfamily	Homologous Superfamily
B [auth P]	IPR001757	P-type ATPase	Family

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
B [auth P]	TPO	Parent Component: THR RESID: AA0038 PSI-MOD : O-phospho-L-threonine MOD:00047

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.