Herpesvirus US11, RNA-binding, N-terminal (IPR020124)

Short name: Herpes_US11_RNA-bd_N

Overlapping homologous superfamilies


Domain relationships



Herpes simplex virus-1 US11 is a RNA-binding protein with a novel RNA-binding domain, which is able to mediate post-transcriptional transactivation of human T-lymphotropic virus type I (HTLV-I) envelope glycoprotein gene expression by interacting with the Rex responsive element (XRE) located at the 3' end of the env mRNA [PMID: 16246910, PMID: 9680120]. The gene product of US11 is one of the most abundant viral proteins present in cells late in infection and is not necessary for virus viability. It is one of the components of the HSV-1 virion, with approximately 600 to 1000 copies per virion. It also binds specifically to UL34 mRNA (in vitro) and seems to regulate the expression of that gene.

The C-terminal half of US11 protein, not covered by this signature, consisting of 20-24 XPR repeats, mediates RNA-binding with a high affinity and specificity. Structural prediction analysis shows the likely conformation of this C-terminal domain to be that of a polyproline type II helix. Localised within the first 40 amino acids of the N-terminal region of US11 protein is the effector domain involved in transport and translation of this mRNA [PMID: 9680120].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.