Annotations: 3THG

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PLN00020	e3thgA1	A: alpha arrays	X: Histone-like	H: Histone-related	T: AAA+ ATPase lid domain	F: PLN00020	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.8.1070	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF21228	Ribulose bisphosphate carboxylase/oxygenase activase, AAA, helical (RuBisCO_activase_AAA_helical)	Ribulose bisphosphate carboxylase/oxygenase activase, AAA, helical	This domain is found in Ribulose bisphosphate carboxylase/oxygenase activase from Nicotiana tabacum (RuBisCO activase) and similar proteins from plants and cyanobacteria. This enzyme facilitates the removal of the sugar phosphate inhibitors of RuBisC ...	This domain is found in Ribulose bisphosphate carboxylase/oxygenase activase from Nicotiana tabacum (RuBisCO activase) and similar proteins from plants and cyanobacteria. This enzyme facilitates the removal of the sugar phosphate inhibitors of RuBisCO, the enzyme that catalyses the fixation of atmospheric CO2 in photosynthesis. This protein is organised into an N-terminal, followed by a AAA module and a 23-residue C-terminal extension. The AAA module has an alpha-beta and an alpha-helical subdomains. This entry covers part of the alpha-beta subdomain and the C-terminal extension [1-4].	Domain
A	PF00004	ATPase family associated with various cellular activities (AAA) (AAA)	ATPase family associated with various cellular activities (AAA)	AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Ribulose bisphosphate carboxylase/oxygenase activase 1, chloroplastic	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-bounded organelle intracellular anatomical structure plastid cellular anatomical entity intracellular membrane-bounded organelle intracellular organelle plastid stroma organelle chloroplast stroma cytoplasm chloroplast

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR044960	Ribulose bisphosphate carboxylase/oxygenase activase-like	Family
A	IPR003959	ATPase, AAA-type, core	Domain
A	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
A	IPR048571	Ribulose bisphosphate carboxylase/oxygenase activase, AAA, helical	Domain

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.