4RV7

Characterization of an essential diadenylate cyclase

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	DacA-like	8089956	4003884	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	DacA-like	8089957	3001724	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	DacA-like	8089957	3001724	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	DacA-like	8089957	3001724	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	DacA-like	8089957	3001724	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	DisA_N	e4rv7A1	A: a+b three layers	X: DisA nucleotide-binding domain (From Topology)	H: DisA nucleotide-binding domain (From Topology)	T: DisA nucleotide-binding domain	F: DisA_N	ECOD (1.6)
B	DisA_N	e4rv7B1	A: a+b three layers	X: DisA nucleotide-binding domain (From Topology)	H: DisA nucleotide-binding domain (From Topology)	T: DisA nucleotide-binding domain	F: DisA_N	ECOD (1.6)
C	DisA_N	e4rv7C1	A: a+b three layers	X: DisA nucleotide-binding domain (From Topology)	H: DisA nucleotide-binding domain (From Topology)	T: DisA nucleotide-binding domain	F: DisA_N	ECOD (1.6)
D	DisA_N	e4rv7D1	A: a+b three layers	X: DisA nucleotide-binding domain (From Topology)	H: DisA nucleotide-binding domain (From Topology)	T: DisA nucleotide-binding domain	F: DisA_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.1700.10	Alpha Beta	3-Layer(aba) Sandwich	YojJ-like (1	DNA integrity scanning protein, DisA, N-terminal domain	CATH (4.3.0)
B	3.40.1700.10	Alpha Beta	3-Layer(aba) Sandwich	YojJ-like (1	DNA integrity scanning protein, DisA, N-terminal domain	CATH (4.3.0)
C	3.40.1700.10	Alpha Beta	3-Layer(aba) Sandwich	YojJ-like (1	DNA integrity scanning protein, DisA, N-terminal domain	CATH (4.3.0)
D	3.40.1700.10	Alpha Beta	3-Layer(aba) Sandwich	YojJ-like (1	DNA integrity scanning protein, DisA, N-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF02457	DisA bacterial checkpoint controller nucleotide-binding (DAC)	DisA bacterial checkpoint controller nucleotide-binding	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Diadenylate cyclase	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 diadenylate cyclase activity transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups phosphorus-oxygen lyase activity cyclase activity lyase activity adenylate cyclase activity	ribose phosphate metabolic process nucleotide biosynthetic process carbohydrate derivative metabolic process purine ribonucleotide biosynthetic process cAMP biosynthetic process cyclic nucleotide metabolic process nucleobase-containing compound metabolic process ribonucleotide biosynthetic process purine nucleotide metabolic process ribonucleotide metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process cyclic nucleotide biosynthetic process phosphate-containing compound metabolic process ribose phosphate metabolic process nucleotide biosynthetic process carbohydrate derivative metabolic process purine ribonucleotide biosynthetic process cAMP biosynthetic process cyclic nucleotide metabolic process nucleobase-containing compound metabolic process ribonucleotide biosynthetic process purine nucleotide metabolic process ribonucleotide metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process cyclic nucleotide biosynthetic process phosphate-containing compound metabolic process small molecule metabolic process phosphorus metabolic process ribose phosphate biosynthetic process nucleoside phosphate metabolic process carbohydrate derivative biosynthetic process cAMP metabolic process cyclic purine nucleotide metabolic process primary metabolic process nucleotide metabolic process nucleobase-containing compound biosynthetic process purine-containing compound metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleoside phosphate biosynthetic process metabolic process cellular process purine ribonucleotide metabolic process purine nucleotide biosynthetic process	cell periphery cellular anatomical structure plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR045585	Diadenylate cyclase CdaA, N-terminal domain	Domain
A, B, C, D	IPR050338	DNA integrity scanning protein DisA	Family
A, B, C, D	IPR036888	DNA integrity scanning protein, DisA, N-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR014046	Diadenylate cyclase	Family
A, B, C, D	IPR003390	DNA integrity scanning protein, DisA, N-terminal	Domain
A, B, C, D	IPR034701	Diadenylate cyclase CdaA	Family

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.