PROSITE documentation PDOC51994
Betacoronavirus Nsp3e group 2-specific marker (G2M) domain profile


Coronaviruses (CoVs) are enveloped positive-strand RNA viruses that infect many species, including humans, other mammals, and birds. After infection, the host may develop respiratory, bowel, liver, and neurological diseases. Coronaviruses are divided into four genera: αcoronavirus, βcoronavirus, γcoronavirus, and Deltacoronavirus. SARS, SARS-CoV-2, BatCoV RaTG13 and Bat-SARS-like coronavirus (BATSL-CoVZXC21 and BAT-SL-CoVZC45) belong to the Sarbecovirus subgenus of βcoronavirus [E1].

The CoV replicase gene encodes two overlapping polyproteins, termed pp1a and pp1ab, which mediate viral replication and transcription. The polypeptides pp1a and pp1ab are processed by the action of a main protease (Nsp5) (see <PDOC51442>) and of one or two papain-like proteases (PLpro) (see <PDOC51124>) found in Nsp3 into non-structural proteins (Nsps) to form the replication/ transcription complex (RTC). Among these, Nsp3 is a glycosylated, multidomain, integral membrane protein. Nsp3 plays many roles in the viral life cycle. It can act as a scaffold protein to interact with itself and to bind other viral Nsps or host proteins. In particular, Nsp3 is essential for RTC formation. Nsp3 comprises various domains, the organization of which differs between CoV genera, due to duplication or absence of some domains. Nsp3e is unique to βcoronaviruses and consists of a nucleic acid-binding domain (NAB) (see <PDOC51945>) and the so-called group 2-specific marker (G2M) or βcoronavirus-specific marker (βSM). The corresponding region is absent in αcoronaviruses and Deltacoronaviruses [1,2,3,4].

The Nsp3e G2M domain possesses an α/β fold (see <PDB:7T9W>).

The profile we developed covers the entire Nsp3e G2M domain.

Last update:

January 2021 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

BCOV_NSP3E_G2M, PS51994; Betacoronavirus Nsp3e group 2-specific marker (G2M) domain profile  (MATRIX)


1AuthorsNeuman B.W. Joseph J.S. Saikatendu K.S. Serrano P. Chatterjee A. Johnson M.A. Liao L. Klaus J.P. Yates J.R. III Wuethrich K. Stevens R.C. Buchmeier M.J. Kuhn P.
TitleProteomics analysis unravels the functional repertoire of coronavirus nonstructural protein 3.
SourceJ. Virol. 82:5279-5294(2008).
PubMed ID18367524

2AuthorsNeuman B.W.
TitleBioinformatics and functional analyses of coronavirus nonstructural proteins involved in the formation of replicative organelles.
SourceAntiviral. Res. 135:97-107(2016).
PubMed ID27743916

3AuthorsLei J. Kusov Y. Hilgenfeld R.
TitleNsp3 of coronaviruses: Structures and functions of a large multi-domain protein.
SourceAntiviral. Res. 149:58-74(2018).
PubMed ID29128390

4AuthorsKorn S.M. Dhamotharan K. Fuertig B. Hengesbach M. Loehr F. Qureshi N.S. Richter C. Saxena K. Schwalbe H. Tants J.-N. Weigand J.E. Woehnert J. Schlundt A.
Title(1)H, (13)C, and (15)N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e.
SourceBiomol. NMR. Assign. 14:329-333(2020).
PubMed ID32770392


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