Arteriviridae metal-binding domain (IPR027355)

Short name: AV_MBD_dom

Domain relationships



Nidoviruses (Coronaviridae, Arteriviridae, and Roniviridae) feature the most complex genetic organisation among plus-strand RNA viruses [E1,E2,E3]. 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 and nsp13 in coronaviruses, that is comprised of a C-terminal nucleoside triphosphate-binding/helicase (Hel) motif and an N-terminal cysteine-rich metal-binding domain (MBD). The MBD is critically involved in nidovirus replication and transcription by modulating the enzymatic activities of the helicase domain and other, yet unknown, mechanisms. It is comprised of about 80 to 100 residues, including 12 to 13 conserved Cys/His residues. The MBD may adopt a unique multinuclear organisation and bind four Zn(2+)s [PMID: 10799597, PMID: 15613297].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0046872 metal 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