1QOJ

Crystal Structure of E.coli UvrB C-terminal domain, and a model for UvrB-UvrC interaction.

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 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	d1qoja_	All alpha proteins	Long alpha-hairpin	C-terminal UvrC-binding domain of UvrB	C-terminal UvrC-binding domain of UvrB	C-terminal UvrC-binding domain of UvrB	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1qojb_	All alpha proteins	Long alpha-hairpin	C-terminal UvrC-binding domain of UvrB	C-terminal UvrC-binding domain of UvrB	C-terminal UvrC-binding domain of UvrB	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	C-terminal UvrC-binding domain of UvrB	8023944	4000619	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	C-terminal UvrC-binding domain of UvrB	8036323	3000775	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	C-terminal UvrC-binding domain of UvrB	8036323	3000775	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	UVR	e1qojA1	A: alpha bundles	X: Long alpha-hairpin	H: C-terminal UvrC-binding domain of UvrB (From Topology)	T: C-terminal UvrC-binding domain of UvrB	F: UVR	ECOD (1.6)
B	UVR	e1qojB1	A: alpha bundles	X: Long alpha-hairpin	H: C-terminal UvrC-binding domain of UvrB (From Topology)	T: C-terminal UvrC-binding domain of UvrB	F: UVR	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	4.10.860.10	Few Secondary Structures	Irregular	DNA Excision Repair, Uvrb	Chain A	CATH (4.3.0)
B	4.10.860.10	Few Secondary Structures	Irregular	DNA Excision Repair, Uvrb	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF02151	UvrB/uvrC motif (UVR)	UvrB/uvrC motif	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	UVRB	excinuclease ABC activity DNA endonuclease activity endonuclease activity catalytic activity, acting on DNA nuclease activity hydrolase activity, acting on ester bonds catalytic activity, acting on a nucleic acid hydrolase activity catalytic activity DNA nuclease activity binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding excinuclease ABC activity DNA endonuclease activity endonuclease activity catalytic activity, acting on DNA nuclease activity hydrolase activity, acting on ester bonds catalytic activity, acting on a nucleic acid hydrolase activity catalytic activity DNA nuclease activity 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 DNA binding nucleic acid binding pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity, acting on acid anhydrides ATP-dependent activity identical protein binding protein binding	nucleotide-excision repair, DNA damage recognition cellular response to stimulus response to stimulus chromosome organization primary metabolic process DNA metabolic process nucleic acid metabolic process cellular component organization nucleobase-containing compound metabolic process organic cyclic compound metabolic process organelle organization organic substance metabolic process cellular response to stress nucleotide-excision repair DNA damage response nucleotide-excision repair, DNA damage recognition cellular response to stimulus response to stimulus chromosome organization primary metabolic process DNA metabolic process nucleic acid metabolic process cellular component organization nucleobase-containing compound metabolic process organic cyclic compound metabolic process organelle organization organic substance metabolic process cellular response to stress nucleotide-excision repair DNA damage response response to stress cellular process metabolic process cellular component organization or biogenesis macromolecule metabolic process DNA repair response to radiation response to abiotic stimulus SOS response cellular component biogenesis protein-DNA complex organization cellular component assembly protein-containing complex assembly protein-containing complex organization nucleotide-excision repair, preincision complex assembly protein-DNA complex assembly	protein-containing complex catalytic complex excinuclease repair complex endodeoxyribonuclease complex intracellular protein-containing complex endonuclease complex DNA repair complex intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR024759	UvrB, YAD/RRR-motif-containing domain	Domain
A, B	IPR006935	Helicase/UvrB, N-terminal	Domain
A, B	IPR041471	UvrB, interaction domain	Domain
A, B	IPR001650	Helicase, C-terminal domain-like	Domain
A, B	IPR036876	UVR domain superfamily	Homologous Superfamily
A, B	IPR014001	Helicase superfamily 1/2, ATP-binding domain	Domain
A, B	IPR001943	UVR domain	Domain
A, B	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
A, B	IPR004807	UvrABC system, subunit B	Family

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.