Annotations: 3WRV

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	UPF0261_N	e3wrvA1	A: a/b three-layered sandwiches	X: Resistance protein Tm-1 first domain (From Topology)	H: Resistance protein Tm-1 first domain (From Topology)	T: Resistance protein Tm-1 first domain	F: UPF0261_N	ECOD (1.6)
B	UPF0261_N	e3wrvB1	A: a/b three-layered sandwiches	X: Resistance protein Tm-1 first domain (From Topology)	H: Resistance protein Tm-1 first domain (From Topology)	T: Resistance protein Tm-1 first domain	F: UPF0261_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.12020	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Uncharacterised protein family UPF0261, NN domain	CATH (4.3.0)
B	3.40.50.12020	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Uncharacterised protein family UPF0261, NN domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF06792	Uncharacterised protein family (UPF0261) N-terminal domain (UPF0261)	Uncharacterised protein family (UPF0261) N-terminal domain		Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Tm-1 protein	catalytic activity binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding catalytic activity binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide 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	biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response response to external stimulus response to biotic stimulus defense response to virus defense response to other organism response to stress response to external biotic stimulus response to virus modulation by host of viral RNA genome replication RNA metabolic process viral life cycle biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response response to external stimulus response to biotic stimulus defense response to virus defense response to other organism response to stress response to external biotic stimulus response to virus modulation by host of viral RNA genome replication RNA metabolic process viral life cycle primary metabolic process nucleobase-containing compound biosynthetic process macromolecule biosynthetic process host-mediated perturbation of symbiont process nucleic acid metabolic process modulation by host of viral genome replication RNA biosynthetic process nucleobase-containing compound metabolic process nucleic acid biosynthetic process modulation by host of viral process viral genome replication biosynthetic process viral RNA genome replication viral process metabolic process cellular process macromolecule metabolic process modulation of process of another organism	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR051353	Tobamovirus Resistance UPF0261	Family
A, B	IPR015813	Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily	Homologous Superfamily
A, B	IPR009215	TIM-barrel domain, IGPS-like	Domain
A, B	IPR044122	UPF0261, N-terminal domain	Domain
A, B	IPR013785	Aldolase-type TIM barrel	Homologous Superfamily

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 R01GM157729.