7JLU

Structure of the activated Roq1 resistosome directly recognizing the pathogen effector XopQ

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	PF01156	e7jluB1	A: a/b three-layered sandwiches	X: Nucleoside hydrolase (From Topology)	H: Nucleoside hydrolase (From Topology)	T: Nucleoside hydrolase	F: PF01156	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF20160	C-JID domain (C-JID)	C-JID domain	C-terminal jelly roll/Ig-like domain (C-JID) was defined in cryogenic electron microscopy (cryoEM) structures of plant intracellular immune receptors containing Toll/interleukin-1 receptor (TIR, PF01582), nucleotide-binding (NB-ARC, PF00931) and leuc ...	C-terminal jelly roll/Ig-like domain (C-JID) was defined in cryogenic electron microscopy (cryoEM) structures of plant intracellular immune receptors containing Toll/interleukin-1 receptor (TIR, PF01582), nucleotide-binding (NB-ARC, PF00931) and leucine-rich repeat (LRR) domains (TIR-NLRs) [1,2]. Structurally, the C-JID core is represented by a beta-sandwich made up of 8 to 9 beta-strands. C-JID matches the so-called post-LRR or C-terminal non-LRR domain detected earlier via MEME and BLAST searches [3,7]. The domain showed a strong distribution bias towards TIR-NLRs of dicotyledonous plant species despite broader taxonomic distribution of TIR-NLR in plant groups [1-7]. Structure-function analyses of cryoEM structures suggest that C-JID domains play a role in substrate recognition, such as binding to effector proteins from pathogens, and thus are involved in the initiation of signaling by TIR-NLR receptors [1,2]. Presence of C-JID (or post-LRR) and its importance for the function of Arabidopsis TIR-NLR RPS4 that partners with RRS1 for effector recognition suggest that C-JID has additional functions [4-6].	Domain
B	PF01156	Inosine-uridine preferring nucleoside hydrolase (IU_nuc_hydro)	Inosine-uridine preferring nucleoside hydrolase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Disease resistance protein Roq1	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding nucleoside phosphate binding ion binding ADP binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding nucleoside phosphate binding ion binding ADP binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding hydrolase activity, acting on glycosyl bonds NADP+ nucleosidase activity hydrolase activity hydrolase activity, hydrolyzing N-glycosyl compounds catalytic activity NAD+ nucleotidase, cyclic ADP-ribose generating	cellular response to stimulus regulation of biological process regulation of cellular process response to stimulus signaling biological regulation cellular process signal transduction cell communication defense response response to stress	-
B	XopQ	hydrolase activity, acting on glycosyl bonds hydrolase activity hydrolase activity, hydrolyzing N-glycosyl compounds catalytic activity	nucleobase-containing compound metabolic process organic cyclic compound metabolic process organic substance metabolic process metabolic process primary metabolic process organonitrogen compound metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR000157	Toll/interleukin-1 receptor homology (TIR) domain	Domain
A	IPR045344	C-JID domain	Domain
A	IPR042197	Apoptotic protease-activating factors, helical domain	Homologous Superfamily
A	IPR032675	Leucine-rich repeat domain superfamily	Homologous Superfamily
A	IPR035897	Toll/interleukin-1 receptor homology (TIR) domain superfamily	Homologous Superfamily
A	IPR044974	Disease resistance protein, plants	Family
A	IPR002182	NB-ARC	Domain
A	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
B	IPR036452	Ribonucleoside hydrolase-like	Homologous Superfamily
B	IPR001910	Inosine/uridine-preferring nucleoside hydrolase 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.