ID   R1AB_CVMJD              Reviewed;         500 AA.
AC   P26627;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Replicase polyprotein 1ab;
DE            Short=pp1ab;
DE   AltName: Full=ORF1ab polyprotein;
DE   Contains:
DE     RecName: Full=Non-structural protein 1-non-structural protein 3 fusion;
DE              Short=nsp1-nsp3 fusion;
DE   Flags: Fragment;
GN   Name=rep; ORFNames=1a-1b;
OS   Murine coronavirus (strain defective JHM) (MHV) (Murine hepatitis virus).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Embecovirus.
OX   NCBI_TaxID=11143;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2243386; DOI=10.1128/jvi.64.12.6045-6053.1990;
RA   Makino S., Yokomori K., Lai M.M.C.;
RT   "Analysis of efficiently packaged defective interfering RNAs of murine
RT   coronavirus: localization of a possible RNA-packaging signal.";
RL   J. Virol. 64:6045-6053(1990).
CC   -!- FUNCTION: The replicase polyprotein of coronaviruses is a
CC       multifunctional protein: it contains the activities necessary for the
CC       transcription of negative stranded RNA, leader RNA, subgenomic mRNAs
CC       and progeny virion RNA as well as proteinases responsible for the
CC       cleavage of the polyprotein into functional products.
CC   -!- FUNCTION: The papain-like proteinase 1 (PL1-PRO) is responsible for the
CC       cleavages located at the N-terminus of the replicase polyprotein.
CC       Activity of PL1-PRO is strongly dependent on zinc (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: Non-structural protein 1: binds to the 40S ribosomal subunit
CC       and inhibits host translation. The nsp1-40S ribosome complex further
CC       induces an endonucleolytic cleavage near the 5'UTR of host mRNAs,
CC       targeting them for degradation. By suppressing host gene expression,
CC       nsp1 facilitates efficient viral gene expression in infected cells and
CC       evasion from host immune response (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The genome of this defective strain consists of sequences
CC       derived from five discontinuous regions of the genome of the non-
CC       defective virus. Some proteins are thus truncated or absent.
CC       {ECO:0000305}.
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DR   EMBL; M61144; AAA46451.1; -; Genomic_RNA.
DR   PIR; A36388; A36388.
DR   MEROPS; C16.001; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.1190; -; 1.
DR   InterPro; IPR022570; B-CoV_A_NSP1.
DR   InterPro; IPR002705; Pept_C30/C16_B_coronavir.
DR   InterPro; IPR013016; Peptidase_C16_CoV.
DR   InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF11963; DUF3477; 1.
DR   Pfam; PF01831; Peptidase_C16; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51962; COV_NSP1; 1.
DR   PROSITE; PS51124; PEPTIDASE_C16; 1.
PE   3: Inferred from homology;
KW   Decay of host mRNAs by virus;
KW   Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host translation shutoff by virus;
KW   Host gene expression shutoff by virus; Host mRNA suppression by virus;
KW   Host-virus interaction; Hydrolase; Metal-binding; Methyltransferase;
KW   Protease; RNA-binding; Thiol protease; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..>500
FT                   /note="Non-structural protein 1-non-structural protein 3
FT                   fusion"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037353"
FT   DOMAIN          54..196
FT                   /note="CoV Nsp1 globular"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT   DOMAIN          352..500
FT                   /note="Peptidase C16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ZN_FING         466..494
FT                   /note="C4-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   ACT_SITE        389
FT                   /note="For PL1-PRO activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   NON_TER         500
SQ   SEQUENCE   500 AA;  55246 MW;  B24DB851ED951264 CRC64;
     MAKMGKYGLG FKWAPEFPWM LPNASEKLGN PERSEEDGFC PSAAQEPKVK GKTLVNHVRV
     DCSRLPALEC CVQSAIIRDI FVDEDPQKVE ASTMMALQFG SAVLVKPSKR LSVQAWAKLG
     VLPKTPAMGL FKRFCLCNTR ECVCDAHVAF QLFTVQPDGV CLGNGRFIGW FVPVTAIPEY
     AKQWLQPWSI LLRKGGNKGS VTSGHSRRAV TMPVYDFNAT DVVYADENQD DDADDPVVLV
     ADTQEEDGVA KEQVDSADSE ICVAHTVGQE MTEPDAVGSQ TPIASAEETE VGEACDREGI
     AEVKATVCAD ALDACPDQVE AFDIEKVEDS ILSELQTELN APADKTYEDV LAFDAIYSET
     LSAFYAVPSD ETHFKVCGFY SPAIERTNCW LRSTLIVMQS LPLEFKDLGM QKLWLSYKAG
     YDQCFVDKLV KSAPKSIILP QGGYVADFAY FFLSQCSFKV HANWRCLKCG MELKLQGLDA
     VFFYGDVVSH MCKCSFKAYF