1XMX

Crystal structure of protein VC1899 from Vibrio cholerae

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	d1xmxa1	Alpha and beta proteins (a/b)	Restriction endonuclease-like	Restriction endonuclease-like	Hypothetical protein VC1899	Hypothetical protein VC1899	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)
A	d1xmxa2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Vibrio cholerae ) [TaxId: 666 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Hypothetical protein VC1899	8031656	4003490	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Restriction endonuclease-like	8044034	3000104	SCOP2 (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	F_UNCLASSIFIED	e1xmxA2	A: alpha arrays	X: HTH	H: HTH	T: winged	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF09002	e1xmxA3	A: a/b three-layered sandwiches	X: Restriction endonuclease-like	H: Restriction endonuclease-like (From Topology)	T: Restriction endonuclease-like	F: PF09002	ECOD (1.6)
A	F_UNCLASSIFIED	e1xmxA4	A: a/b three-layered sandwiches	X: CARF (CRISPR-associated Rossmann fold) domains (From Topology)	H: CARF (CRISPR-associated Rossmann fold) domains (From Topology)	T: CARF (CRISPR-associated Rossmann fold) domains	F: F_UNCLASSIFIED	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.10770	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Hypothetical protein VC1899 like domain (Restriction endonuclease-like)	CATH (4.3.0)
A	3.40.1350.10	Alpha Beta	3-Layer(aba) Sandwich	Trna Endonuclease	Chain: A, domain 1	CATH (4.3.0)
A	1.10.10.680	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Hypothetical protein VC1899 (Restriction endonuclease-like)	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF09002	Card1-like, endonuclease domain (Card1_endonuc)	Card1-like, endonuclease domain	This is the endonuclease domain found in a set of bacterial proteins, including Card1 (cyclic-oligoadenylate-activated single-stranded ribonuclease and single-stranded deoxyribonuclease 1) from Treponema succinifaciens (Swiss:F2NWD3), a protein that ...	This is the endonuclease domain found in a set of bacterial proteins, including Card1 (cyclic-oligoadenylate-activated single-stranded ribonuclease and single-stranded deoxyribonuclease 1) from Treponema succinifaciens (Swiss:F2NWD3), a protein that is part of type III CRISPR-Cas immune response system. This protein consists of a CARF (CRISPR-associated Rossman fold) domain at the N-terminal, an helical hinge domain and a C-terminal endonuclease domain [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	hypothetical protein VC1899	binding organic cyclic compound binding nucleic acid binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR011335	Restriction endonuclease type II-like	Homologous Superfamily
A	IPR011856	tRNA endonuclease-like domain superfamily	Homologous Superfamily
A	IPR015093	Card1 endonuclease 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 R01GM133198.