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TCIDNameDomainKingdom/PhylumProtein(s)
1.G.18.1.1









The SARS-CoV has two fusion peptides, one of 19 aas (residues 770 - 788) and the other of 16 aas (residues 873 - 888) in the spike glycoprotein precursor of 1255 aas (Apellániz et al. 2014).  The structure of a 34 aa fusion peptide has been determined (PDB 1ZVB). The Spike (S) glycoprotein cytoplasmic domain is palmitoylated and that palmitoylation has two membrane proximal cysteine clusters I and II that are important for S-mediated cell fusion (Petit et al. 2007). The SARS-CoV E protein has transmembrane domains that increase the mamalian cell membrane permeability (Liao et al. 2006).

Viruses
Nidovirales
Spike glycoprotein of SARS coronavirus
1.G.18.1.2









The Coronavirus spike glycoprotein (S-glycoprotein; spike S2 protein of E2peplomer protein of 1363 aas.  The fusion peptide isN-terminal and of 19 aas (Apellániz et al. 2014).  It is a class I fusion protein.

Viruses
Nidovirales
S2 of bovine coronavirus (BCV)
1.G.18.1.3









Spike (S) protein (partial) of 120 aas

Viruses
Nidovirales
S protein of feline coronavirus
1.G.18.1.4









Spike glycoprotein of 1171 aas.

Viruses
Nidovirales
S-protein of Infectious bronchitis virus
1.G.18.1.5









Spike glycoprotein of 1353 aas.

Viruses
Nidovirales
S-protein of Pipistrellus bat coronavirus HKU5
1.G.18.1.6









Surface glycoprotein of 1273 aas and at least two TMSs, N- and C-terminal, but several smaller peaks of hydrophobicity that could be TMSs occur inbetween these two. Wrapp et al. 2020. Cai et al. 2020 determined a 3.5-Å-resolution cryo-EM structure of the 2019-nCoV S trimer in the prefusion conformation. The predominant state of the trimer has one of the three receptor-binding domains (RBDs) rotated up in a receptor-accessible conformation. They also provided biophysical and structural evidence that the 2019-nCoV S protein binds angiotensin-converting enzyme 2 (ACE2) with higher affinity than does severe acute respiratory syndrome (SARS)-CoV S. report two cryo-electron microscopy structures derived from a preparation of the full-length S protein, representing its prefusion (2.9-angstrom resolution) and postfusion (3.0-angstrom resolution) conformations, respectively. The spontaneous transition to the postfusion state is independent of target cells. The prefusion trimer has three receptor-binding domains clamped down by a segment adjacent to the fusion peptide. The postfusion structure is strategically decorated by N-linked glycans, suggesting possible protective roles against host immune responses and harsh external conditions (Cai et al. 2020).

Viruses
Nidovirales
Surface glycoprotein of severe acute respiratory syndrome coronavirus 2
1.G.18.1.7









The surface spike (S) protein of 1353 aas and at least 2 TMSs, N- and C-terminal, but several hydrophobic peaks observed with the central region of this protein could be TMSs.

Viruses
Nidovirales
S protein of betacoronavirus England 1