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. 2012 Nov 20;3(6):e00473-12. doi: 10.1128/mBio.00473-12

TABLE 1 .

Cleavage products of the replicase polyproteins of HCoV-EMC/2012

Cleavage product Position in polyprotein
pp1a/pp1aba
Protein size
(no. of amino acids)
Putative functional domain(s)b
nsp1 1Met-Gly193 193
nsp2 194Asp-Gly853 660
nsp3 854Ala-Gly2740 1887 ADRP, PL2pro, TM1
nsp4 2741Ala-Gln3247 507 TM-2
nsp5 3248Ser-Gln3553 306 3CLpro
nsp6 3554Ser-Gln3845 292 TM-3
nsp7 3846Ser-Gln3928 83
nsp8 3929Ala-Gln4127 199 Putative primase
nsp9 4128Asn-Gln4237 110
nsp10 4238Ala-Gln4377 140
nsp11 4378Ser-Leu4391 14
nsp12 4378Ser-Gln5310 933 RdRp
nsp13 5311Ala-Gln5908 598 ZD, HEL1
nsp14 5909Ser-Gln6432 524 ExoN, NMT
nsp15 6433Gly-Gln6775 343 NendoU
nsp16 6776Ala-Arg7078 303 OMT
a

 Amino acids of the replicase proteins pp1a and pp1ab were numbered with the assumption that a −1 ribosomal frameshift occurs to express ORF1b, as in other coronaviruses (see text); the use of the slippery sequence UUUAAAC is predicted to result in a peptide bond between Asn4385 and Arg4386 in pp1ab.

b

 The major transmembrane domains and a selection of the most conserved domains with enzymatic activities that have been characterized functionally and/or structurally in coronaviruses are listed. Abbreviations: PL2pro, papain-like proteinase 2; ADRP, ADP-ribose 1″-phosphatase; TM, transmembrane domain; 3CLpro, 3C-like cysteine proteinase; RdRp, RNA-dependent RNA polymerase; ZD, putative zinc-binding domain; HEL1, superfamily 1 helicase; ExoN, 3′-to-5′ exonuclease; NMT, N7-methyltransferase; NendoU, nidoviral endoribonuclease specific for U; OMT, S-adenosylmethionine-dependent ribose 2′-O-methyltransferase.