Annotations: 4XJ4

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	EUF07928	e4xj4A1	A: alpha arrays	X: HhH/H2TH	H: SAM/DNA-glycosylase	T: PAP/OAS1 substrate-binding domain	F: EUF07928	ECOD (1.6)
A	NT_2-5OAS_ClassI-CCAase_like	e4xj4A2	A: a+b three layers	X: Nucleotidyltransferase-like	H: Nucleotidyltransferase (From Topology)	T: Nucleotidyltransferase	F: NT_2-5OAS_ClassI-CCAase_like	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF21713	Cyclic GMP-AMP synthase, C-terminal domain (DncV_C)	Cyclic GMP-AMP synthase, C-terminal domain	This domain is found Cyclic GMP-AMP synthase from Vibrio cholerae (DncV), a prokaryotic cGAS-like enzyme that synthesises cyclic GMP- AMP (c-GAMP) and stimulates intestinal colonization. DncV adopts a structure and topology that are typical of the n ...	This domain is found Cyclic GMP-AMP synthase from Vibrio cholerae (DncV), a prokaryotic cGAS-like enzyme that synthesises cyclic GMP- AMP (c-GAMP) and stimulates intestinal colonization. DncV adopts a structure and topology that are typical of the nucleotidyltransferase superfamily. It is organised into two domains: an N-terminal domain that contains the catalytic loop (Pfam:PF21654) and a C- terminal helix bundle that consists of eight helices and one pair of anti-parallel beta-sheets (this entry) [1-3].	Domain
A	PF21654	Cyclic GMP-AMP synthase DncV-like, nucleotidyltransferase domain (DncV-like_NTFase)	Cyclic GMP-AMP synthase DncV-like, nucleotidyltransferase domain	This is the nucleotidyltransferase domain of DncV from Vibrio cholerae (also known as Cyclic GMP-AMP synthase) and related proteins [1-4]. DncV catalyses the synthesis of 3'3'-cyclic GMP-AMP (3'3'-cGAMP) from GTP and ATP. It is part of the CBASS (cyc ...	This is the nucleotidyltransferase domain of DncV from Vibrio cholerae (also known as Cyclic GMP-AMP synthase) and related proteins [1-4]. DncV catalyses the synthesis of 3'3'-cyclic GMP-AMP (3'3'-cGAMP) from GTP and ATP. It is part of the CBASS (cyclic oligonucleotide-based antiphage signaling system) which provides immunity against bacteriophage [1-4]. This protein is required for efficient V.cholerae intestinal colonization and and down-regulates the colonization-influencing process of chemotaxis.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Cyclic AMP-GMP synthase	3',3'-cyclic GMP-AMP synthase activity cyclic GMP-AMP synthase activity transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding 3',3'-cyclic GMP-AMP synthase activity cyclic GMP-AMP synthase activity transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups 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 diguanylate cyclase activity guanyl nucleotide binding GTP binding guanyl ribonucleotide binding cation binding metal ion binding	biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response defense response to symbiont response to external stimulus response to biotic stimulus defense response to virus defense response to other organism response to stress response to external biotic stimulus response to virus nucleoside phosphate metabolic process nucleotide biosynthetic process biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response defense response to symbiont response to external stimulus response to biotic stimulus defense response to virus defense response to other organism response to stress response to external biotic stimulus response to virus nucleoside phosphate metabolic process nucleotide biosynthetic process primary metabolic process nucleobase-containing compound biosynthetic process nucleotide metabolic process cyclic nucleotide metabolic process nucleobase-containing compound metabolic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleobase-containing small molecule metabolic process cyclic nucleotide biosynthetic process nucleoside phosphate biosynthetic process phosphate-containing compound metabolic process metabolic process cellular process small molecule metabolic process phosphorus metabolic process chemotaxis negative regulation of locomotion regulation of biological process regulation of response to external stimulus negative regulation of response to stimulus biological regulation negative regulation of biological process negative regulation of chemotaxis regulation of chemotaxis taxis regulation of response to stimulus response to chemical regulation of locomotion negative regulation of response to external stimulus locomotion	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR048445	Cyclic GMP-AMP synthase DncV-like, nucleotidyltransferase domain	Domain
A	IPR047805	Cyclic GMP-AMP synthase	Family
A	IPR048446	Cyclic GMP-AMP synthase, C-terminal domain	Domain

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.