Research Article

Duck RIG-I CARD Domain Induces the Chicken IFN-β by Activating NF-κB

Table 2

The features of retinoic acid inducible protein I in the duck.

NameRegion/site (aa)Note

CARD_RIG-I_12–90Caspase activation and recruitment domain found in RIG-I, first repeat
CARD_RIG-I_299–184Caspase activation and recruitment domain found in RIG-I, second repeat
DEXDc261–413DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region
HELICc607–742Helicase superfamily c-terminal domain; associated with DEXDc-, DEAD-, and DEAH-box proteins; this domain is found in a wide variety of helicases and helicase related proteins
RIG-I_C-RD807–926C-terminal domain of RIG-I
ATP binding site270–274, 706, 727, 731, 733Chemical binding
Putative Mg++ binding site375–378Ion binding
RNA binding site511-512, 515, 519Nucleotide binding
RD interface519, 522-523, 536-537, 540Polypeptide binding
Helicase domain interface554-555, 557–560, 563, 567Polypeptide binding
Nucleotide binding region636–639, 663-664, 698–700Chemical binding

Note. Protein_id: “ACA61272.1”; protein full length: 1–933 aa; organism: “Anas platyrhynchos.