2M4H

Solution structure of the Core Domain (10-76) of the Feline Calicivirus VPg protein

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Peptidase_C37_like	e2m4hA1	A: alpha arrays	X: Virus VPg protein (From Topology)	H: Virus VPg protein (From Topology)	T: Virus VPg protein	F: Peptidase_C37_like	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.260.110	Mainly Alpha	Orthogonal Bundle	434 Repressor (Amino-terminal Domain)		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF20915	Viral genome-linked protein (VPg)	Viral genome-linked protein	This family represents Viral genome-linked protein (VPg) from Caliciviruses such as Feline calicivirus (FCV). VPg plays a key role in translation initiation from genomic and subgenomic RNAs and is thought to function as a cap substitute for ribosomal ...	This family represents Viral genome-linked protein (VPg) from Caliciviruses such as Feline calicivirus (FCV). VPg plays a key role in translation initiation from genomic and subgenomic RNAs and is thought to function as a cap substitute for ribosomal recruitment. It interacts with the initiation factor eIF4E. This protein shows a compact helical structure flanked by flexible N and C terminal ends [1-3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Feline Calicivirus VPg protein	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 5'-3' RNA polymerase activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid RNA polymerase activity transferase activity RNA-dependent RNA polymerase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups cysteine-type peptidase activity peptidase activity catalytic activity, acting on a protein cysteine-type endopeptidase activity hydrolase activity endopeptidase activity 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 helicase activity RNA helicase activity ATP-dependent activity, acting on RNA RNA binding nucleic acid binding	cellular biosynthetic process cellular metabolic process RNA metabolic process viral life cycle primary metabolic process nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process nucleic acid biosynthetic process organic substance metabolic process viral genome replication biosynthetic process cellular biosynthetic process cellular metabolic process RNA metabolic process viral life cycle primary metabolic process nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process nucleic acid biosynthetic process organic substance metabolic process viral genome replication biosynthetic process viral RNA genome replication organic cyclic compound biosynthetic process viral process organic substance biosynthetic process metabolic process cellular process macromolecule metabolic process symbiont-mediated perturbation of host cellular process symbiont-mediated suppression of host gene expression biological process involved in interspecies interaction between organisms modulation by symbiont of host process symbiont-mediated perturbation of host gene expression modulation of process of another organism biological process involved in interaction with host biological process involved in symbiotic interaction organonitrogen compound metabolic process proteolysis protein metabolic process gene expression DNA-templated transcription	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
A	IPR004004	Helicase/polymerase/peptidase polyprotein, Calicivirus-type	Family
A	IPR001205	RNA-directed RNA polymerase, C-terminal domain	Domain
A	IPR043502	DNA/RNA polymerase superfamily	Homologous Superfamily
A	IPR043128	Reverse transcriptase/Diguanylate cyclase domain	Homologous Superfamily
A	IPR003593	AAA+ ATPase domain	Domain
A	IPR014759	Helicase, superfamily 3, single-stranded RNA virus	Domain
A	IPR007094	RNA-directed RNA polymerase, catalytic domain	Domain
A	IPR049434	VPg	Domain
A	IPR000605	Helicase, superfamily 3, single-stranded DNA/RNA virus	Domain
A	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
A	IPR000317	Peptidase C24, Calicivirus polyprotein Orf1	Domain

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.