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 R1AB_CVBEN              Reviewed;        7094 AA.
P0C6W7; Q91A28; Q91A29;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-OCT-2017, entry version 75.
RecName: Full=Replicase polyprotein 1ab;
Short=pp1ab;
AltName: Full=ORF1ab polyprotein;
Contains:
RecName: Full=Host translation inhibitor nsp1;
Short=nsp1;
AltName: Full=p28;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p65;
Contains:
RecName: Full=Papain-like proteinase;
Short=PL-PRO;
EC=3.4.19.12;
EC=3.4.22.69;
AltName: Full=Non-structural protein 3;
Short=nsp3;
AltName: Full=p210;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
AltName: Full=Peptide HD2;
AltName: Full=p44;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=M-PRO;
AltName: Full=nsp5;
AltName: Full=p27;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
AltName: Full=p10;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
AltName: Full=p22;
Contains:
RecName: Full=Non-structural protein 9;
Short=nsp9;
AltName: Full=p12;
Contains:
RecName: Full=Non-structural protein 10;
Short=nsp10;
AltName: Full=Growth factor-like peptide;
Short=GFL;
AltName: Full=p15;
Contains:
RecName: Full=RNA-directed RNA polymerase;
Short=Pol;
Short=RdRp;
EC=2.7.7.48;
AltName: Full=nsp12;
AltName: Full=p100;
Contains:
RecName: Full=Helicase;
Short=Hel;
EC=3.6.4.12;
EC=3.6.4.13;
AltName: Full=nsp13;
AltName: Full=p67;
Contains:
RecName: Full=Guanine-N7 methyltransferase;
Short=ExoN;
EC=2.1.1.-;
EC=3.1.13.-;
AltName: Full=nsp14;
Contains:
RecName: Full=Uridylate-specific endoribonuclease;
EC=3.1.-.-;
AltName: Full=NendoU;
AltName: Full=nsp15;
AltName: Full=p35;
Contains:
RecName: Full=2'-O-methyltransferase;
EC=2.1.1.-;
AltName: Full=nsp16;
Name=rep; ORFNames=1a-1b;
Bovine coronavirus (strain 98TXSF-110-ENT) (BCoV-ENT) (BCV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=233262;
NCBI_TaxID=9913; Bos taurus (Bovine).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=11714968;
Chouljenko V.N., Lin X.Q., Storz J., Kousoulas K.G., Gorbalenya A.E.;
"Comparison of genomic and predicted amino acid sequences of
respiratory and enteric bovine coronaviruses isolated from the same
animal with fatal shipping pneumonia.";
J. Gen. Virol. 82:2927-2933(2001).
-!- FUNCTION: The replicase polyprotein of coronaviruses is a
multifunctional protein: it contains the activities necessary for
the transcription of negative stranded RNA, leader RNA, subgenomic
mRNAs and progeny virion RNA as well as proteinases responsible
for the cleavage of the polyprotein into functional products.
{ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: Host translation inhibitor nsp1: Inhibits host
translation by interacting with the 40S ribosomal subunit. The
nsp1-40S ribosome complex further induces an endonucleolytic
cleavage near the 5'UTR of host mRNAs, targeting them for
degradation. Viral mRNAs are not susceptible to nsp1-mediated
endonucleolytic RNA cleavage thanks to the presence of a 5'-end
leader sequence and are therefore protected from degradation. By
suppressing host gene expression, nsp1 facilitates efficient viral
gene expression in infected cells and evasion from host immune
response. {ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: Non-structural protein 2: May play a role in the
modulation of host cell survival signaling pathway by interacting
with host PHB and PHB2. Indeed, these two proteins play a role in
maintaining the functional integrity of the mitochondria and
protecting cells from various stresses.
{ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: Papain-like proteinase: Responsible for the cleavages
located at the N-terminus of the replicase polyprotein. In
addition, PL-PRO possesses a deubiquitinating/deISGylating
activity and processes both 'Lys-48'- and 'Lys-63'-linked
polyubiquitin chains from cellular substrates. Participates
together with nsp4 in the assembly of virally-induced cytoplasmic
double-membrane vesicles necessary for viral replication.
Antagonizes innate immune induction of type I interferon by
blocking the phosphorylation, dimerization and subsequent nuclear
translocation of host IRF3. Prevents also host NF-kappa-B
signaling. {ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: Non-structural protein 4: Participates in the assembly
of virally-induced cytoplasmic double-membrane vesicles necessary
for viral replication. {ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: Proteinase 3CL-PRO: Cleaves the C-terminus of replicase
polyprotein at 11 sites. Recognizes substrates containing the core
sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-
phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7,
ECO:0000255|PROSITE-ProRule:PRU00772}.
-!- FUNCTION: Non-structural protein 6: Plays a role in the initial
induction of autophagosomes from host reticulum endoplasmic.
Later, limits the expansion of these phagosomes that are no longer
able to deliver viral components to lysosomes.
{ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: Non-structural protein 7: Forms a hexadecamer with nsp8
(8 subunits of each) that may participate in viral replication by
acting as a primase. Alternatively, may synthesize substantially
longer products than oligonucleotide primers.
{ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: Non-structural protein 8: Forms a hexadecamer with nsp7
(8 subunits of each) that may participate in viral replication by
acting as a primase. Alternatively, may synthesize substantially
longer products than oligonucleotide primers.
{ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: Non-structural protein 9: May participate in viral
replication by acting as a ssRNA-binding protein.
{ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: Non-structural protein 10: Plays a pivotal role in viral
transcription by stimulating both nsp14 3'-5' exoribonuclease and
nsp16 2'-O-methyltransferase activities. Therefore plays an
essential role in viral mRNAs cap methylation.
{ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: RNA-directed RNA polymerase: Responsible for replication
and transcription of the viral RNA genome.
{ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: Helicase: Multi-functional protein with a zinc-binding
domain in N-terminus displaying RNA and DNA duplex-unwinding
activities with 5' to 3' polarity. Activity of helicase is
dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: Guanine-N7 methyltransferase: Enzyme possessing two
different activities: an exoribonuclease activity acting on both
ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine
methyltransferase activity. {ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: Uridylate-specific endoribonuclease: Mn(2+)-dependent,
uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5'
to the cleaved bond. {ECO:0000250|UniProtKB:P0C6X7}.
-!- FUNCTION: 2'-O-methyltransferase: Methyltransferase that mediates
mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral
mRNAs. N7-methyl guanosine cap is a prerequisite for binding of
nsp16. Therefore plays an essential role in viral mRNAs cap
methylation which is essential to evade immune system.
{ECO:0000250|UniProtKB:P0C6X7}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- CATALYTIC ACTIVITY: TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the
two peptides corresponding to the two self-cleavage sites of the
SARS 3C-like proteinase are the two most reactive peptide
substrates. The enzyme exhibits a strong preference for substrates
containing Gln at P1 position and Leu at P2 position.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
-!- SUBUNIT: Nsp2 interacts with host PHB and PHB2. 3CL-PRO exists as
monomer and homodimer. Nsp4 interacts with PL-PRO and nsp6. Only
the homodimer shows catalytic activity. Eight copies of nsp7 and
eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-
encircling ring structure. Nsp9 is a dimer. Nsp10 forms a
dodecamer and interacts with nsp14 and nsp16; these interactions
enhance nsp14 and nsp16 enzymatic activities. Nsp14 interacts (via
N-terminus) with DDX1. {ECO:0000250|UniProtKB:P0C6X7}.
-!- SUBCELLULAR LOCATION: Papain-like proteinase: Host membrane;
Multi-pass membrane protein. Host cytoplasm
{ECO:0000250|UniProtKB:P0C6X7}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4: Host membrane;
Multi-pass membrane protein. Host cytoplasm. Note=Localizes in
virally-induced cytoplasmic double-membrane vesicles.
{ECO:0000250|UniProtKB:P0C6X7}.
-!- SUBCELLULAR LOCATION: Non-structural protein 6: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 7: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 8: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 9: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 10: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Helicase: Host endoplasmic reticulum-Golgi
intermediate compartment {ECO:0000305}. Note=The helicase
interacts with the N protein in membranous complexes and
colocalizes with sites of synthesis of new viral RNA.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Uridylate-specific endoribonuclease: Host
cytoplasm, host perinuclear region {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6W7-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6T8-1; Sequence=External;
Note=Produced by conventional translation.;
-!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
association of the replication complex and thereby alter the
architecture of the host cell membrane.
-!- PTM: Specific enzymatic cleavages in vivo by its own proteases
yield mature proteins. 3CL-PRO and PL-PRO proteinases are
autocatalytically processed (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK83365.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF391541; AAK83365.1; ALT_SEQ; Genomic_RNA.
RefSeq; NP_150073.2; NC_003045.1.
ProteinModelPortal; P0C6W7; -.
SMR; P0C6W7; -.
MEROPS; C16.006; -.
PRIDE; P0C6W7; -.
GeneID; 921688; -.
KEGG; vg:921688; -.
OrthoDB; VOG09000000; -.
BRENDA; 3.4.22.B14; 8724.
Proteomes; UP000008570; Genome.
GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0016896; F:exoribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
GO; GO:0039579; P:suppression by virus of host ISG15 activity; IEA:UniProtKB-KW.
GO; GO:0039644; P:suppression by virus of host NF-kappaB transcription factor activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
Gene3D; 2.40.10.250; -; 1.
InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR022570; B-CoV_NSP1.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR009461; Coronavirus_NSP16.
InterPro; IPR027352; CV_ZBD.
InterPro; IPR037227; EndoU-like.
InterPro; IPR002589; Macro_dom.
InterPro; IPR032592; NAR_dom.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR009466; NSP11.
InterPro; IPR014828; NSP7.
InterPro; IPR037204; NSP7_sf.
InterPro; IPR014829; NSP8.
InterPro; IPR037230; NSP8_sf.
InterPro; IPR014822; NSP9.
InterPro; IPR036499; NSP9_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR002705; Pept_C30/C16_B_coronavir.
InterPro; IPR008740; Peptidase_C30.
InterPro; IPR013016; Peptidase_C30/C16.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR009469; RNA_pol_N_coronovir.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF06478; Corona_RPol_N; 1.
Pfam; PF11963; DUF3477; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF16251; NAR; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF06471; NSP11; 1.
Pfam; PF06460; NSP13; 1.
Pfam; PF08716; nsp7; 1.
Pfam; PF08717; nsp8; 1.
Pfam; PF08710; nsp9; 1.
Pfam; PF01831; Peptidase_C16; 1.
Pfam; PF05409; Peptidase_C30; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF08715; Viral_protease; 1.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF101816; SSF101816; 1.
SUPFAM; SSF140367; SSF140367; 1.
SUPFAM; SSF142877; SSF142877; 1.
SUPFAM; SSF143076; SSF143076; 1.
SUPFAM; SSF144246; SSF144246; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51653; CV_ZBD; 1.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51124; PEPTIDASE_C16; 2.
PROSITE; PS51657; PSRV_HELICASE; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
3: Inferred from homology;
Activation of host autophagy by virus; ATP-binding; Complete proteome;
Decay of host mRNAs by virus; Endonuclease;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; Exonuclease; Helicase;
Host cytoplasm; Host gene expression shutoff by virus; Host membrane;
Host mRNA suppression by virus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host ISG15 by virus;
Inhibition of host NF-kappa-B by virus; Membrane; Metal-binding;
Methyltransferase;
Modulation of host ubiquitin pathway by viral deubiquitinase;
Modulation of host ubiquitin pathway by virus; Nuclease;
Nucleotide-binding; Nucleotidyltransferase; Protease; Repeat;
Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
Thiol protease; Transferase; Transmembrane; Transmembrane helix;
Ubl conjugation pathway; Viral immunoevasion; Viral RNA replication;
Zinc; Zinc-finger.
CHAIN 1 246 Host translation inhibitor nsp1.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037229.
CHAIN 247 851 Non-structural protein 2.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037230.
CHAIN 852 2750 Papain-like proteinase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037231.
CHAIN 2751 3246 Non-structural protein 4.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037232.
CHAIN 3247 3549 3C-like proteinase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037233.
CHAIN 3550 3836 Non-structural protein 6.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037234.
CHAIN 3837 3925 Non-structural protein 7.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037235.
CHAIN 3926 4122 Non-structural protein 8.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037236.
CHAIN 4123 4232 Non-structural protein 9.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037237.
CHAIN 4233 4369 Non-structural protein 10.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037238.
CHAIN 4370 5297 RNA-directed RNA polymerase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037239.
CHAIN 5298 5900 Helicase. {ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037240.
CHAIN 5901 6421 Guanine-N7 methyltransferase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037241.
CHAIN 6422 6795 Uridylate-specific endoribonuclease.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037242.
CHAIN 6796 7094 2'-O-methyltransferase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037243.
TRANSMEM 2138 2158 Helical. {ECO:0000255}.
TRANSMEM 2199 2219 Helical. {ECO:0000255}.
TRANSMEM 2227 2247 Helical. {ECO:0000255}.
TRANSMEM 2313 2333 Helical. {ECO:0000255}.
TRANSMEM 2343 2363 Helical. {ECO:0000255}.
TRANSMEM 2365 2385 Helical. {ECO:0000255}.
TRANSMEM 2752 2772 Helical. {ECO:0000255}.
TRANSMEM 2824 2844 Helical. {ECO:0000255}.
TRANSMEM 3009 3029 Helical. {ECO:0000255}.
TRANSMEM 3031 3051 Helical. {ECO:0000255}.
TRANSMEM 3063 3083 Helical. {ECO:0000255}.
TRANSMEM 3090 3110 Helical. {ECO:0000255}.
TRANSMEM 3115 3135 Helical. {ECO:0000255}.
TRANSMEM 3558 3578 Helical. {ECO:0000255}.
TRANSMEM 3588 3608 Helical. {ECO:0000255}.
TRANSMEM 3614 3634 Helical. {ECO:0000255}.
TRANSMEM 3657 3677 Helical. {ECO:0000255}.
TRANSMEM 3684 3704 Helical. {ECO:0000255}.
TRANSMEM 3711 3731 Helical. {ECO:0000255}.
TRANSMEM 3755 3775 Helical. {ECO:0000255}.
DOMAIN 1036 1274 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1275 1435 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1631 1892 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3247 3549 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
DOMAIN 4977 5139 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 5298 5381 CV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
DOMAIN 5553 5734 (+)RNA virus helicase ATP-binding.
DOMAIN 5735 5904 (+)RNA virus helicase C-terminal.
ZN_FING 1151 1179 C4-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 1749 1785 C4-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4306 4322 {ECO:0000250}.
ZN_FING 4348 4361 {ECO:0000250}.
NP_BIND 5578 5585 ATP. {ECO:0000250}.
REGION 2138 2385 HD1.
REGION 2752 3135 HD2.
REGION 3558 3775 HD3.
ACT_SITE 1074 1074 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1225 1225 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1671 1671 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1828 1828 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3287 3287 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3391 3391 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
METAL 5302 5302 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5305 5305 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5313 5313 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5316 5316 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5323 5323 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5326 5326 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5330 5330 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5336 5336 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5347 5347 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5352 5352 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5369 5369 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5372 5372 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
SITE 246 247 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 851 852 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 2750 2751 Cleavage; by PL2-PRO. {ECO:0000250}.
SITE 3246 3247 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3549 3550 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3836 3837 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3925 3926 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4122 4123 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4232 4233 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4369 4370 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 5297 5298 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 5900 5901 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6421 6422 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6795 6796 Cleavage; by 3CL-PRO. {ECO:0000250}.
SEQUENCE 7094 AA; 797266 MW; 146DC43FE7F6AFD8 CRC64;
MSKINKYGLE LHWAPEFPWM FEDAEEKLDN PSSSEVDIVC STTAQKLETG GICPENHVMV
DCRRLLKQEC CVQSSLIREI VMNTRPYDLE VLLQDALQSR EAVLVTPPLG MSLEACYVRG
CNPNGWTMGL FRRRSVCNTG RCAVNKHVAY QLYMIDPAGV CFGAGQFVGW VIPLAFMPVQ
SRKFIVPWVM YLRKCGEKGA YNKDHKRGGF EHVYNFKVED AYDLVHDEPK GKFSKKAYAL
IRGYRGVKPL LYVDQYGCDY TGGLADGLEA YADKTLQEMK ALFPIWSQEL PFDVTVAWHV
VRDPRYVMRL QSASTIRSVA YVANPTEDLC DGSVVIKEPV HVYADDSIIL RQHNLVDIMS
CFYMEADAVV NAFYGVDLKD CGFVMQFGYI DCEQDLCDFK GWVPGNMIDG FACTTCGHVY
ETGDLLAQSS GVLPVNPVLH TKSAAGYGGF GCKDSFTLYG QTVVYFGGCV YWSPARNIWI
PILKSSVKSY DGLVYTGVVG CKAIVKETNL ICKALYLDYV QHKCGNLHQR ELLGVSDVWH
KQLLLNRGVY KPLLENIDYF NMRRAKFSLE TFTVCADGFM PFLLDDLVPR AYYLAVSGQA
FCDYADKICH AVVSKSKELL DVSLDSLSAA IHYLNSKIVD LAQHFSDFGT SFVSKIVHFF
KTFTTSTALA FAWVLFHVLH GAYIVVESDI YFVKNIPRYA SAVAQAFRSV AKVVLDSLRV
TFIDGLSCFK IGRRRICLSG SKIYEVERGL LHSSQLPLDV YDLTMPSQVQ KAKQKPIYLK
GSGSDFSLAD SVVEVVTTSL TPCGYSEPPK VADKICIVDN VYMAKAGDKY YPVVVDGHVG
LLDQAWRVPC AGRRVTFKEQ PTVNEIASTP KTIKVFYELD KDFNTILNTA CGVFEVDDTV
DMEEFYAVVI DAIEEKLSPC KELEGVGAKV SAFLQKLEDN SLFLFDEAGE EVLASKLYCA
FTAPEDDDFL EESGVEEDDV EGEETDLTVT SAGEPCVASE QEESSEILED TLDDGPCVET
SDSQVEEDVE MSDFADLESV IQDYENVCFE FYTTEPEFVK VLDLYVPKAT RNNCWLRSVL
AVMQKLPCQF KDKNLQDLWV LYKQQYSQLF VDTLVNKIPA NIVVPQGGYV ADFAYWFLTL
CDWQCVAYWK CIKCDLALKL KGLDAMFFYG DVVSHVCKCG ESMVLIDVDV PFTAHFALKD
KLFCAFITKR SVYKAACVVD VNDSHSMAVV DGKQIDDHRV TSITSDKFDF IIGHGMSFSM
TTFEIAQLYG SCITPNVCFV KGDIIKVSKR VKAEVVVNPA NGHMAHGGGV AKAIAVAAGQ
QFVKETTDMV KSKGVCATGD CYVSTGGKLC KTVLNVVGPD ARTQGKQSYA LLERVYKHLN
KYDCVVTTLI SAGIFSVPSD VSLTYLLGTA EKQVVLVSNN QEDFDLISKC QITAVEGTKK
LAERLSFNVG RSIVYETDAN KLILSNDVAF VSTFNVLQDV LSLRHDIALD DDARTFVQSN
VDVVPEGWRV VNKFYQINGV RTVKYFECPG GIDICSQDKV FGYVQQGSFN KATVAQIKAL
FLDKVDILLT VDGVNFTNRF VPVGESFGKS LGNVFCDGVN VTKHKCDINY KGKVFFQFDN
LSSEDLKAVR SSFNFDQKEL LAYYNMLVNC SKWQVVFNGK YFTFKQANNN CFVNVSCLML
QSLNLKFKIV QWQEAWLEFR SGRPARFVSL VLAKGGFKFG DPADSRDFLR VVFSQVDLTG
AICDFEIACK CGVKQEQRTG VDAVMHFGTL SREDLEIGYT VDCSCGKKLI HCVRFDVPFL
ICSNTPASVK LPKGVGSANI FKGDKVGHYV HVKCEQSYQL YDASNVKKVT DVTGNLSDCL
YLKNLKQTFK SVLTTYYLDD VKKIEYNPDL SQYYCDGGKY YTQRIIKAQF KTFEKVDGVY
TNFKLIGHTI CDILNAKLGF DSSKEFVEYK VTEWPTATGD VVLATDDLYV KRYERGCITF
GKPVIWLSHE QASLNSLTYF NRPLLVDENK FDVLKVDDVD DGGDISESDA KESKEINIIK
LSGVKKPFKV EDSVIVNDDT SEIKYVKSLS IVDVYDMWLT GCRYVVRTAN ALSMAVNVPT
IRKFIKFGMT LVSIPIDLLN LREIKPVFNV VKAVRNKISA CFNFIKWLFV LLFGWIKISA
DNKVIYTTEV ASKLTCKLVA LAFKNAFLTF KWSVVARGAC IIATIFLLWF NFIYANVIFS
DFYLPKIGFL PTFVGKIAQW IKSTFSLVTI CDLYSIQDVG FKNQYCNGSI ACQFCLAGFD
MLDNYKAIDV VQYEADRRAF VDYTGVLKIV IELIVSYALY TAWFYPLFAL ISIQILTTWL
PELFMLSTLH WSVRLLVSLA NMLPAHVFMR FYIIIASFIK LFILFRHVAY GCSKPGCLFC
YKRNRSLRVK CSTIVGGMIR YYDVMANGGT GFCSKHQWNC IDCDSYKPGN TFITVEAALD
LSKELKRPIQ PTDVAYHTVT DVKQVGCYMR LFYERDGQRT YDDVNASLFV DYSNLLHSKV
KGVPNMHVVV VENDADKANF LNAAVFYAQS LFRPILMVDK NLITTANTGT SVTETMFDVY
VDTFLSMFDV DKKSLNALIA TAHSSIKQGT QICKVLDTFL SCARKSCSID SDVDTKCLAD
SVMSAVSAGL ELTDESCNNL VPTYLKGDNI VAADLGVLIQ NSAKHVQGNV AKIAGVSCIW
SVDAFNQLSS DFQHKLKKAC CKTGLKLKLT YNKQMANVSV LTTPFSLKGG AVFSYFVYVC
FLLSLVCFIG LWCLMPTYTV HKSDFQLPVY ASYKVLDNGV IRDVSVEDVC FANKFEQFDQ
WYESTFGLSY YSNSMACPIV VAVVDQDLGS TVFNVPTKVL RYGYHVLHFI THALSADGVQ
CYTPHSQISY SNFYASGCVL SSACTMFAMA DGSPQPYCYT EGLMQNASLY SSLVPHVRYN
LANAKGFIRF PEVLREGLVR IVRTRSMSYC RVGLCEEADE GICFNFNGSW VLNNDYYRSL
PGTFCGRDVF DLIYQLFKGL AQPVDFLALT ASSIAGAILA VIVVLVFYYL IKLKRAFGDY
TSIVFVNVIV WCVNFMMLFV FQVYPTLSCV YAICYFYATL YFPSEISVIM HLQWLVMYGT
IMPLWFCLLY ISVVVSNHAF WVFAYCRRLG TSVRSDGTFE EMALTTFMIT KDSYCKLKNS
LSDVAFNRYL SLYNKYRYYS GKMDTAAYRE AACSQLAKAM DTFTNNNGSD VLYQPPTASV
STSFLQSGIV KMVNPTSKVE PCIVSVTYGN MTLNGLWLDD KVYCPRHVIC SASDMTNPDY
TNLLCRVTSS DFTVLFDRLS LTVMSYQMQG CMLVLTVTLQ NSRTPKYTFG VVKPGETFTV
LAAYNGKPQG AFHVTMRSSY TIKGSFLCGS CGSVGYVLMG DCVKFVYMHQ LELSTGCHTG
TDFNGDFYGP YKDAQVVQLP VQDYIQSVNF VAWLYAAILN NCNWFVQSDK CSVEDFNVWA
LSNGFSQVKS DLVIDALASM TGVSLETLLA AIKRLKNGFQ GRQIMGSCSF EDELTPSDVY
QQLAGIKLQS KRTRLVKGIV CWIMASTFLF SCIITAFVKW TMFMYVTTNM LSITFCALCV
ISLAMLLVKH KHLYLTMYII PVLFTLLYNN YLVVYKQTFR GYVYAWLSYY VPSVEYTYTD
EVIYGMLLLI GMVFVTLRSI NHDLFSFIMF VGRVISVVSL WYMGSNLEEE ILLMLASLFG
TYTWTTALSM AAAKVIAKWV AVNVLYFTDI PQIKIVLVCY LFIGYIISCY WGLFSLMNSL
FRMPLGVYNY KISVQELRYM NANGLRPPKN SFEALMLNFK LLGIGGVPII EVSQFQSKLT
DVKCANVVLL NCLQHLHVAS NSKLWQYCST LHNEILATSD LGVAFEKLAQ LLIVLFANPA
AVDSKCLTSI EEVCDDYAKD NTVLQALQSE FVNMASFVEY EVAKKNLDEA RSSGSANQQQ
LKQLEKACNI AKSAYERDRA VARKLERMAD LALTNMYKEA RINDKKSKVV SALQTMLFSM
VRKLDNQALN SILDNAVKGC VPLNAIPSLA ANTLTIIVPD KSVYDQVVDN VYVTYAGNVW
QIQTIQDSDG TNKQLNEISD DCNWPLVIIA NRHNEVSATV LQNNELMPAK LKTQVVNSGP
DQTCNTPTQC YYNNSNNGKI VYAILSDVDG LKYTKILKDD GNFVVLELDP PCKFTVQDVK
GLKIKYLYFV KGCNTLARGW VVGTISSTVR LQAGTATEYA SNSSILSLCA FSVDPKKTYL
DFIQQGGTPI ANCVKMLCDH AGTGMAITVK PDATTNQDSY GGASVCIYCR ARVEHPDVDG
LCKLRGKFVQ VPVGIKDPVS YVLTHDVCQV CGFWRDGSCS CVSTDTTVQS KDTNFLNRVR
GTSVDARLVP CASGLSTDVQ LRAFDICNAS VAGIGLHLKV NCCRFQRVDE NGDKLDQFFV
VKRTDLTIYN REMECYERVK DCKFVAEHDF FTFDVEGSRV PHIVRKDLTK YTMLDLCYAL
RHFDRNDCML LCDILSIYAG CEQSYFTKKD WYDFVENPDI INVYKKLGPI FNRALVSATE
FADKLVEVGL VGILTLDNQD LNGKWYDFGD YVIAAPGCGV AIADSYYSYM MPMLTMCHAL
DCELYVNNAY RLFDLVQYDF TDYKLELFNK YFKHWSMPYH PNTVDCQDDR CIIHCANFNI
LFSMVLPNTC FGPLVRQIFV DGVPFVVSIG YHYKELGIVM NMDVDTHRYR LSLKDLLLYA
ADPALHVASA SALYDLRTCC FSVAAITSGV KFQTVKPGNF NQDFYDFILS KGLLKEGSSV
DLKHFFFTQD GNAAITDYNY YKYNLPTMVD IKQLLFVLEV VYKYFEIYDG GCIPASQVIV
NNYDKSAGYP FNKFGKARLY YEALSFEEQD EIYAYTKRNV LPTLTQMNLK YAISAKNRAR
TVAGVSILST MTGRMFHQKC LKSIAATRGV PVVIGTTKFY GGWDDMLRRL IKDVDNPVLM
GWDYPKCDRA MPNILRIVSS LVLARKHEAC CSQSDRFYRL ANECAQVLSE IVMCGGCYYV
KPGGTSSGDA TTAFANSVFN ICQAVSANVC ALMSCNGNKI EDLSIRALQK RLYSHVYRSD
MVDSTFVTEY YEFLNKHFSM MILSDDGVVC YNSDYASKGY IANISAFQQV LYYQNNVFMS
ESKCWVENDI NNGPHEFCSQ HTMLVKMDGD DVYLPYPDPS RILGAGCFVD DLLKTDSVLL
IERFVSLAID AYPLVYHENE EYQKVFRVYL EYIKKLYNDL GNQILDSYSV ILSTCDGQKF
TDESFYKNMY LRSAVMQSVG ACVVCSSQTS LRCGSCIRKP LLCCKCCYDH VMATDHKYVL
SVSPYVCNAP GCDVNDVTKL YLGGMSYYCE DHKPQYSFKL VMNGMVFGLY KQSCTGSPYI
DDFNRIASCK WTDVDDYILA NECTERLKLF AAETQKATEE AFKQSYASAT IQEIVSEREL
ILSWEIGKVK PPLNKNYVFT GYHFTKNGKT VLGEYVFDKS ELTNGVYYRA TTTYKLSVGD
VFVLTSHSVA NLSAPTLVPQ ENYSSIRFAS VYSVLETFQN NVVNYQHIGM KRYCTVQGPP
GTGKSHLAIG LAVYYCTARV VYTAASHAAV DALCEKAYKF LNINDCTRIV PAKVRVECYD
KFKINDTTRK YVFTTINALP EMVTDIVVVD EVSMLTNYEL SVINARIRAK HYVYIGDPAQ
LPAPRVLLSK GTLEPKYFNT VTKLMCCLGP DIFLGTCYRC PKEIVDTVSA LVYENKLKAK
NESSSLCFKV YYKGVTTHES SSAVNMQQIY LINKFLKANP LWHKAVFISP YNSQNFAAKR
VLGLQTQTVD SAQGSEYDYV IYSQTAETAH SVNVNRFNVA ITRAKKGILC VMSNMQLFEA
LQFTTLTLDK VPQAVETRVQ CSTNLFKDCS KSYSGYHPAH APSFLAVDDK YKATGDLAVC
LGIGDSAVTY SRLISLMGFK LDVTLDGYCK LFITKEEAVK RVRAWVGFDA EGAHATRDSI
GTNFPLQLGF STGIDFVVEA TGLFADRDGY SFKKAVAKAP PGEQFKHLIP LMTRGQRWDV
VRPRIVQMFA DHLIDLSDCV VLVTWAANFE LTCLRYFAKV GREISCNVCT KRATAYNSRT
GYYGCWRHSV TCDYLYNPLI VDIQQWGYIG SLSSNHDLYC SVHKGAHVAS SDAIMTRCLA
VYDCFCNNIN WNVEYPIISN ELSINTSCRV LQRVMLKAAM LCNRYTLCYD IGNPKAIACV
KDFDFKFYDA QPIVKSVKTL LYSFEAHKDS FKDGLCMFWN CNVDKYPPNA VVCRFDTRVL
NNLNLPGCNG GSLYVNKHAF HTKPFSRAAF EHLKPMPFFY YSDTPCVYMD GMDAKQVDYV
PLKSATCITR CNLGGAVCLK HAEEYREYLE SYNTATTAGF TFWVYKTFDF YNLWNTFTKL
QSLENVVYNL VKTGHYTGQA GEMPCAIIND KVVAKIDKED VVIFINNTTY PTNVAVELFA
KRSIRHHPEL KLFRNLNIDV CWKHVIWDYA RESIFCSNTY GVCMYTDLKF IDKLNVLFDG
RDNGALEAFK RSNNGVYIST TKVKSLSMIK GPPRAELNGV VVDKVGDTDC VFYFAVRKEG
QDVIFSQFDS LRVSSNQSPQ GNLGSNEPGN VGGNDALATS TIFTQSRVIS SFTCRTDMEK
DFIALDQDLF IQKYGLEDYA FEHIVYGNFN QKIIGGLHLL IGLYRRQQTS NLVIQEFVSY
DSSIHSYFIT DEKSGGSKSV CTVIDILLDD FVALVKSLNL NCVSKVVNVN VDFKDFQFML
WCNDEKVMTF YPRLQAASDW KPGYSMPVLY KYLNSPMERV SLWNYGKPVT LPTGCMMNVA
KYTQLCQYLN TTTLAVPVNM RVLHLGAGSE KGVAPGSAVL RQWLPAGTIL VDNDLYPFVS
DSVATYFGDC ITLPFDCQWD LIISDMYDPI TKNIGEYNVS KDGFFTYICH MIRDKLALGG
SVAIKITEFS WNAELYKLMG YFAFWTVFCT NANASSSEGF LIGINYLGKP KVEIDGNVMH
ANYLFWRNST VWNGGAYSLF DMAKFPLKLA GTAVINLRAD QINDMVYSLL EKGKLLVRDT
NKEVFVGDSL VNVI


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