3I32

Dimeric structure of a Hera helicase fragment including the C-terminal RecA domain, the dimerization domain, and the RNA binding domain

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
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)
A	PF21591	e3i32A4	A: alpha duplicates or obligate multimers	X: RNA helicase Hera dimerization domain (From Topology)	H: RNA helicase Hera dimerization domain (From Topology)	T: RNA helicase Hera dimerization domain	F: PF21591	ECOD (1.6)
A	PF22231	e3i32A5	A: a+b two layers	X: Alpha-beta plaits	H: RNA-binding domain, RBD (From Topology)	T: RNA-binding domain, RBD	F: PF22231	ECOD (1.6)
A	PF00271	e3i32A3	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF00271	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF21591	RNA helicase Hera, dimerization domain (Hera_DD)	RNA helicase Hera, dimerization domain	This domain is found at the C-terminal region of Heat resistant RNA dependent ATPase from Thermus thermophilus (also known as Hera) the first DEAD box helicase that forms a stable dimer in the absence of ligands. This dimerization domain (DD) folds i ...	This domain is found at the C-terminal region of Heat resistant RNA dependent ATPase from Thermus thermophilus (also known as Hera) the first DEAD box helicase that forms a stable dimer in the absence of ligands. This dimerization domain (DD) folds into a single turn of a left-handed super-helix [1,2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Heat resistant RNA dependent 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 hydrolase activity catalytic activity nucleic acid binding catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid helicase activity RNA helicase activity ATP-dependent activity, acting on RNA ATP-dependent activity cation binding metal ion binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR048768	RNA helicase Hera-like, dimerization domain	Domain
A	IPR001650	Helicase, C-terminal domain-like	Domain
A	IPR000629	ATP-dependent RNA helicase DEAD-box, conserved site	Conserved Site
A	IPR014001	Helicase superfamily 1/2, ATP-binding domain	Domain
A	IPR014014	RNA helicase, DEAD-box type, Q motif	Domain
A	IPR011545	DEAD/DEAH box helicase domain	Domain
A	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily

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.