Arteriviridae zinc-binding domain (IPR027355)

Short name: AV_ZBD

Overlapping homologous superfamilies


Domain relationships



Nidoviruses (Coronaviridae, Arteriviridae, and Roniviridae) feature the most complex genetic organization among plus-strand RNA viruses. Their replicase genes encode an exceptionally large number of nonstructural protein domains which mediate the key functions required for genomic RNA synthesis (replication) and subgenomic RNA (sgRNA) synthesis (transcription). They encode a nonstructural protein, called nsp10 in arteriviruses (AV) and nsp13 in coronaviruses (CV), that is comprised of a C-terminal nucleoside triphosphate-binding/helicase (Hel) motif and an N-terminal cysteine-rich zinc-binding domain (ZBD). The ZBD is critically involved in nidovirus replication and transcription by modulating the enzymatic activities of the helicase domain and other, yet unknown, mechanisms [PMID: 10799597, PMID: 15613297, PMID: 24369429].

The ZBD is comprised of about 80 to 100 residues, including 12 to 13 conserved Cys/His residues. It consists of a RING-like module and treble-cleft zinc finger, together coordinating three Zn atoms. The N-terminal RING-like module has a notable binuclear structure with a cross-brace topology involving 6 Cys and 2 His residues that coordinate two zinc ions. The C- terminal zinc finger of ZBD adopts a treble-cleft fold distinct from that of the RING module. It coordinates one Zn ion with a C[H/C]C[C/H] pattern [PMID: 24369429].

This entry represents the AV ZBD domain.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0008270 zinc ion binding

Cellular Component

No terms assigned in this category.

Contributing signatures

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