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. 2007 Aug 13;369(1):92–104. doi: 10.1016/j.virol.2007.06.035

Table 2.

Predicted end-products of proteolytic processing of the ECoV replicase polyproteins pp1a and pp1ab

Cleavage product Nucleotide positiona Polyprotein Position in pp1a/pp1ab (aa) Length (aa) Putative funcitional domain(s)b Putative proteases predicted to release protein from polyproteins
nsp1 210–941 pp1a/pp1ab 1Met-Gly244 244 PL1pro
nsp2 942–2744 pp1a/pp1ab 245Val-Ala845 601 PL1pro
nsp3 2745–8597 pp1a/pp1ab 846Gly-Gly2796 1951 Ac, PL1pro, ADRP, PL2pro, TM1, Y PL2pro
nsp4 8598–10,085 pp1a/pp1ab 2797Ala-Gln3292 496 TM2 PL2pro + 3CLpro
nsp5 10,086–10,994 pp1a/pp1ab 3293Ser-Gln3595 303 3CLpro 3CLpro
nsp6 10,995–11,855 pp1a/pp1ab 3596Ser-Gln3882 287 TM3 3CLpro
nsp7 11,856–12,122 pp1a/pp1ab 3883Ser-Gln3971 89 Part of RNA binding hexadecameric supercomplex 3CLpro
nsp8 12,123–12,713 pp1a/pp1ab 3972Ala-Gln4168 197 Part of RNA binding hexadecameric supercomplex 3CLpro
nsp9 12,714–13,043 pp1a/pp1ab 4169Asn-Gln4278 110 ssRNA-binding protein 3CLpro
nsp10 13,044–13,454 pp1a/pp1ab 4279Ala-Gln4415 137 2 zinc fingers 3CLpro
nsp11 13,455–13,496 pp1a 4416Ser-Ser4429 14 3CLpro
nsp12 13,455–16,237 pp1ab 4416Ser-Gln5343 928 RdRp 3CLpro
nsp13 16,238–18,034 pp1ab 5344Ser-Gln5942 599 ZBD, HEL 3CLpro
nsp14 18,035–19,597 pp1ab 5943Cys-Gln6463 521 Exonuclease (ExoN) 3CLpro
nsp15 19,598–20,695 pp1ab 6464Ser-Gln6829 366 NendoU 3CLpro
nsp16 20,696–21,592 pp1ab 6830Ala-Ile7128 299 2′-O-MT 3CLpro

Domains Ac and Y are described by Ziebuhr et al. (2001).

a

Nucleotide position means the location of the nucleotides encoding corresponding proteins in the entire genome of equine coronavirus-NC99 strain.

b

PL1pro, papain-like proteinase 1; PL2pro, papain-like proteinase 2; ADRP, adenosine diphosphate-ribose 1ʺ-phosphatase (formerly known as ‘X-domain’); 3CLpro, 3C-like proteinase; TM, transmembrane domain; GFL, growth factor-like domain; RdRp, RNA-dependent RNA polymerase; ZBD, zinc-binding domain; HEL, helicase domain; NendoU, nidoviral uridylate-specific endoribonuclease; 2′-O-MT, 2′-O-ribose methyltransferase.