9KTW

Cryo-EM structure of wild type RIG-I with 5'p-RNA

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0000166	molecular_function	nucleotide binding
B	0002230	biological_process	positive regulation of defense response to virus by host
B	0002376	biological_process	immune system process
B	0002684	biological_process	positive regulation of immune system process
B	0002735	biological_process	positive regulation of myeloid dendritic cell cytokine production
B	0002753	biological_process	cytoplasmic pattern recognition receptor signaling pathway
B	0003690	molecular_function	double-stranded DNA binding
B	0003723	molecular_function	RNA binding
B	0003724	molecular_function	RNA helicase activity
B	0003725	molecular_function	double-stranded RNA binding
B	0003727	molecular_function	single-stranded RNA binding
B	0004386	molecular_function	helicase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005856	cellular_component	cytoskeleton
B	0005886	cellular_component	plasma membrane
B	0005923	cellular_component	bicellular tight junction
B	0008270	molecular_function	zinc ion binding
B	0009597	biological_process	detection of virus
B	0009615	biological_process	response to virus
B	0010467	biological_process	gene expression
B	0010628	biological_process	positive regulation of gene expression
B	0015629	cellular_component	actin cytoskeleton
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0030334	biological_process	regulation of cell migration
B	0031625	molecular_function	ubiquitin protein ligase binding
B	0032587	cellular_component	ruffle membrane
B	0032725	biological_process	positive regulation of granulocyte macrophage colony-stimulating factor production
B	0032727	biological_process	positive regulation of interferon-alpha production
B	0032728	biological_process	positive regulation of interferon-beta production
B	0032755	biological_process	positive regulation of interleukin-6 production
B	0032757	biological_process	positive regulation of interleukin-8 production
B	0032760	biological_process	positive regulation of tumor necrosis factor production
B	0034344	biological_process	regulation of type III interferon production
B	0038187	molecular_function	pattern recognition receptor activity
B	0039529	biological_process	RIG-I signaling pathway
B	0042802	molecular_function	identical protein binding
B	0043330	biological_process	response to exogenous dsRNA
B	0045087	biological_process	innate immune response
B	0045944	biological_process	positive regulation of transcription by RNA polymerase II
B	0046872	molecular_function	metal ion binding
B	0051607	biological_process	defense response to virus
B	0060760	biological_process	positive regulation of response to cytokine stimulus
B	0071360	biological_process	cellular response to exogenous dsRNA
B	0140374	biological_process	antiviral innate immune response
B	1990904	cellular_component	ribonucleoprotein complex

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	179
Details	Domain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	166
Details	Domain: {"description":"Helicase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	3
Details	Motif: {"description":"DECH box"}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	7
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01125","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"(Microbial infection) Deamidated asparagine; by herpes simplex virus 1/HHV-1 UL37","evidences":[{"source":"PubMed","id":"27866900","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by CK2","evidences":[{"source":"PubMed","id":"21068236","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"26746851","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI10
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"Q6Q899","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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