1JL2

Crystal structure of TCEO RNase H-a chimera combining the folding core from T. thermophilus RNase H and the remaining region of E. coli RNase H

External Resource: Annotation

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1jl2a_	Alpha and beta proteins (a/b)	Ribonuclease H-like motif	Ribonuclease H-like	Ribonuclease H	RNase H (RNase HI)	(Escherichia coli K-12 ) [TaxId: 83333 ], (Thermus thermophilus HB8 ) [TaxId: 300852 ], (Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
B	d1jl2b_	Alpha and beta proteins (a/b)	Ribonuclease H-like motif	Ribonuclease H-like	Ribonuclease H	RNase H (RNase HI)	(Escherichia coli K-12 ) [TaxId: 83333 ], (Thermus thermophilus HB8 ) [TaxId: 300852 ], (Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
C	d1jl2c_	Alpha and beta proteins (a/b)	Ribonuclease H-like motif	Ribonuclease H-like	Ribonuclease H	RNase H (RNase HI)	(Escherichia coli K-12 ) [TaxId: 83333 ], (Thermus thermophilus HB8 ) [TaxId: 300852 ], (Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
D	d1jl2d_	Alpha and beta proteins (a/b)	Ribonuclease H-like motif	Ribonuclease H-like	Ribonuclease H	RNase H (RNase HI)	(Escherichia coli K-12 ) [TaxId: 83333 ], (Thermus thermophilus HB8 ) [TaxId: 300852 ], (Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00075	e1jl2A1	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: PF00075	ECOD (1.6)
B	PF00075	e1jl2B1	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: PF00075	ECOD (1.6)
C	PF00075	e1jl2C1	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: PF00075	ECOD (1.6)
D	PF00075	e1jl2D1	A: mixed a+b and a/b	X: Ribonuclease H-like	H: Ribonuclease H-like (From Topology)	T: Ribonuclease H-like	F: PF00075	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.420.10	Alpha Beta	2-Layer Sandwich	Nucleotidyltransferase	domain 5	CATH (4.3.0)
B	3.30.420.10	Alpha Beta	2-Layer Sandwich	Nucleotidyltransferase	domain 5	CATH (4.3.0)
C	3.30.420.10	Alpha Beta	2-Layer Sandwich	Nucleotidyltransferase	domain 5	CATH (4.3.0)
D	3.30.420.10	Alpha Beta	2-Layer Sandwich	Nucleotidyltransferase	domain 5	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00075	RNase H (RNase_H)	RNase H	RNase H digests the RNA strand of an RNA/DNA hybrid. Important enzyme in retroviral replication cycle, and often found as a domain associated with reverse transcriptases. Structure is a mixed alpha+beta fold with three a/b/a layers.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Chimera of Ribonuclease HI, Ribonuclease H	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding endonuclease activity RNA endonuclease activity, producing 5'-phosphomonoesters catalytic activity, acting on RNA RNA-DNA hybrid ribonuclease activity catalytic activity, acting on a nucleic acid RNA nuclease activity hydrolase activity nuclease activity cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding endonuclease activity RNA endonuclease activity, producing 5'-phosphomonoesters catalytic activity, acting on RNA RNA-DNA hybrid ribonuclease activity catalytic activity, acting on a nucleic acid RNA nuclease activity hydrolase activity nuclease activity hydrolase activity, acting on ester bonds RNA endonuclease activity endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 5'-phosphomonoesters catalytic activity organic cyclic compound binding nucleic acid binding	DNA replication, removal of RNA primer catabolic process RNA metabolic process primary metabolic process DNA metabolic process nucleic acid metabolic process macromolecule catabolic process organic cyclic compound catabolic process nucleobase-containing compound catabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process DNA replication organic substance metabolic process nucleic acid catabolic process DNA replication, removal of RNA primer catabolic process RNA metabolic process primary metabolic process DNA metabolic process nucleic acid metabolic process macromolecule catabolic process organic cyclic compound catabolic process nucleobase-containing compound catabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process DNA replication organic substance metabolic process nucleic acid catabolic process metabolic process macromolecule metabolic process organic substance catabolic process RNA catabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR036397	Ribonuclease H superfamily	Homologous Superfamily
A, B, C, D	IPR022892	Ribonuclease HI	Family
A, B, C, D	IPR002156	Ribonuclease H domain	Domain
A, B, C, D	IPR012337	Ribonuclease H-like superfamily	Homologous Superfamily
A, B, C, D	IPR036397	Ribonuclease H superfamily	Homologous Superfamily
A, B, C, D	IPR022892	Ribonuclease HI	Family
A, B, C, D	IPR002156	Ribonuclease H domain	Domain
A, B, C, D	IPR012337	Ribonuclease H-like superfamily	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.