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 R1AB_BC279              Reviewed;        7079 AA.
P0C6V9; Q0Q476;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
10-MAY-2017, entry version 70.
RecName: Full=Replicase polyprotein 1ab;
Short=pp1ab;
AltName: Full=ORF1ab polyprotein;
Contains:
RecName: Full=Host translation inhibitor nsp1;
Short=nsp1;
AltName: Full=Leader protein;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p65 homolog;
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;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=nsp5;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
Contains:
RecName: Full=Non-structural protein 9;
Short=nsp9;
Contains:
RecName: Full=Non-structural protein 10;
Short=nsp10;
AltName: Full=Growth factor-like peptide;
Short=GFL;
Contains:
RecName: Full=RNA-directed RNA polymerase;
Short=Pol;
Short=RdRp;
EC=2.7.7.48;
AltName: Full=nsp12;
Contains:
RecName: Full=Helicase;
Short=Hel;
EC=3.6.4.12;
EC=3.6.4.13;
AltName: Full=nsp13;
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;
Contains:
RecName: Full=2'-O-methyltransferase;
EC=2.1.1.-;
AltName: Full=nsp16;
Name=rep; ORFNames=1a-1b;
Bat coronavirus 279/2005 (BtCoV) (BtCoV/279/2005).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=389167;
NCBI_TaxID=196889; Rhinolophus macrotis (Big-eared horseshoe bat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16840328; DOI=10.1128/JVI.00697-06;
Tang X.C., Zhang J.X., Zhang S.Y., Wang P., Fan X.H., Li L.F., Li G.,
Dong B.Q., Liu W., Cheung C.L., Xu K.M., Song W.J., Vijaykrishna D.,
Poon L.L.M., Peiris J.S.M., Smith G.J., Chen H., Guan Y.;
"Prevalence and genetic diversity of coronaviruses in bats from
China.";
J. Virol. 80:7481-7490(2006).
-!- 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=P0C6V9-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6F5-1; 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. {ECO:0000250}.
-!- 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}.
-!- MISCELLANEOUS: Bat coronavirus 279/2005 is highly similar to SARS-
CoV (SARS-like).
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABG47068.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; DQ648857; ABG47068.1; ALT_INIT; Genomic_RNA.
ProteinModelPortal; P0C6V9; -.
SMR; P0C6V9; -.
MEROPS; C16.009; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000006573; 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; IPR032505; Corona_NSP4_C.
InterPro; IPR009461; Coronavirus_NSP16.
InterPro; IPR027352; CV_ZBD.
InterPro; IPR002589; Macro_dom.
InterPro; IPR032592; NAR_dom.
InterPro; IPR021590; NSP1.
InterPro; IPR009466; NSP11.
InterPro; IPR024375; Nsp3_coronavir.
InterPro; IPR014828; NSP7.
InterPro; IPR014829; NSP8.
InterPro; IPR014822; NSP9.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008740; Peptidase_C30.
InterPro; IPR013016; Peptidase_C30/C16.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR009469; RNA_pol_N_coronovir.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR024358; SARS-CoV_Nsp3_N.
InterPro; IPR022733; SARS_polyprot_cleavage.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF06478; Corona_RPol_N; 1.
Pfam; PF12379; DUF3655; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF16251; NAR; 1.
Pfam; PF11501; Nsp1; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF06471; NSP11; 1.
Pfam; PF06460; NSP13; 1.
Pfam; PF12124; Nsp3_PL2pro; 1.
Pfam; PF08716; nsp7; 1.
Pfam; PF08717; nsp8; 1.
Pfam; PF08710; nsp9; 1.
Pfam; PF05409; Peptidase_C30; 1.
Pfam; PF11633; SUD-M; 1.
Pfam; PF08715; Viral_protease; 1.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF101816; SSF101816; 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; 1.
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 1 179 Host translation inhibitor nsp1.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000289896.
CHAIN 180 818 Non-structural protein 2.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000289897.
CHAIN 819 2746 Papain-like proteinase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000289898.
CHAIN 2747 3246 Non-structural protein 4.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000289899.
CHAIN 3247 3552 3C-like proteinase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000289900.
CHAIN 3553 3842 Non-structural protein 6.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000289901.
CHAIN 3843 3925 Non-structural protein 7.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000289902.
CHAIN 3926 4123 Non-structural protein 8.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000289903.
CHAIN 4124 4236 Non-structural protein 9.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000289904.
CHAIN 4237 4375 Non-structural protein 10.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000289905.
CHAIN 4376 5307 RNA-directed RNA polymerase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000289906.
CHAIN 5308 5908 Helicase. {ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000289907.
CHAIN 5909 6435 Guanine-N7 methyltransferase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000289908.
CHAIN 6436 6781 Uridylate-specific endoribonuclease.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000289909.
CHAIN 6782 7079 2'-O-methyltransferase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000289910.
TRANSMEM 2209 2229 Helical. {ECO:0000255}.
TRANSMEM 2310 2330 Helical. {ECO:0000255}.
TRANSMEM 2357 2377 Helical. {ECO:0000255}.
TRANSMEM 2761 2781 Helical. {ECO:0000255}.
TRANSMEM 2998 3018 Helical. {ECO:0000255}.
TRANSMEM 3028 3048 Helical. {ECO:0000255}.
TRANSMEM 3060 3080 Helical. {ECO:0000255}.
TRANSMEM 3083 3103 Helical. {ECO:0000255}.
TRANSMEM 3111 3131 Helical. {ECO:0000255}.
TRANSMEM 3148 3168 Helical. {ECO:0000255}.
TRANSMEM 3570 3590 Helical. {ECO:0000255}.
TRANSMEM 3592 3612 Helical. {ECO:0000255}.
TRANSMEM 3618 3638 Helical. {ECO:0000255}.
TRANSMEM 3665 3684 Helical. {ECO:0000255}.
TRANSMEM 3691 3710 Helical. {ECO:0000255}.
TRANSMEM 3734 3754 Helical. {ECO:0000255}.
TRANSMEM 3762 3782 Helical. {ECO:0000255}.
DOMAIN 1001 1167 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1617 1881 Peptidase C16. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3247 3552 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
DOMAIN 4987 5149 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 5308 5391 CV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
DOMAIN 5564 5745 (+)RNA virus helicase ATP-binding.
DOMAIN 5746 5915 (+)RNA virus helicase C-terminal.
ZN_FING 1735 1772 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4310 4326 {ECO:0000250}.
ZN_FING 4353 4366 {ECO:0000250}.
NP_BIND 5589 5596 ATP. {ECO:0000250}.
REGION 2098 2377 HD1. {ECO:0000250}.
REGION 2761 3168 HD2. {ECO:0000250}.
REGION 3570 3782 HD3. {ECO:0000250}.
REGION 4918 5220 RNA-directed RNA polymerase.
{ECO:0000250}.
COMPBIAS 930 999 Glu-rich.
COMPBIAS 2216 2219 Poly-Leu.
COMPBIAS 3772 3775 Poly-Cys.
COMPBIAS 5312 5337 Cys-rich.
ACT_SITE 1657 1657 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1818 1818 For PL-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 5312 5312 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5315 5315 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5323 5323 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5326 5326 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5333 5333 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5336 5336 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5340 5340 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5346 5346 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5357 5357 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5362 5362 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5379 5379 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5382 5382 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
SITE 179 180 Cleavage. {ECO:0000250}.
SITE 818 819 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 3246 3247 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 3552 3553 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3842 3843 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3925 3926 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4123 4124 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4236 4237 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4375 4376 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 5307 5308 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 5908 5909 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6435 6436 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6781 6782 Cleavage; by 3CL-PRO. {ECO:0000250}.
SEQUENCE 7079 AA; 791654 MW; CE92AE7AE019B902 CRC64;
MESLALGVSE KTHVQLSLPV LQVRDVLVRG FGDSVEEALA EAREHLKNGT CGLVELEKGV
LPQLEQPYVF IKRSDAQGTN HGYKVVELVA ELDGIQYGRS GTTLGVLVPH VGETPVAYRN
VLLRKNGNKG AGGHSYGIDL KSYDLGVELG TDPIEDYEQN WNTKHGGGVL RELIRELNGG
AFTRYVDNNF CGPDGYPLEC IKDLLARAGK SMCTLSEQLD YIESKRGVYC CREHEHEIVW
FTERSEKSYE RQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
RSVYPVATPQ ECNDMHLSTL MKCNHCDEVS WQTCDFLKAT CEQCGTENLV CEGPTTCGYL
PANAVVKMPC PACQDPEVGP EHSVADYHNH SNIETRLRKG GRTKCFGGCV FAYVGCYNKR
AYWVPRASAN IGASHTGITG DNVETLNEDL MEILNRDRVN INIVGDFHLN EEVAIILASF
SASTCAFVDT VKGLDYKTFK DIVESCGNFK VTRGRAKKGA WNIGQEKSIL TPLYGFPSQA
AGVIRSIFTR ALDTANHSIP DLQRAAITIL DGISEQSLRL IDAMVYTSDL LTNSVIVMAY
VTGGLVQQIT QWLSNMLGTT VDKLKPVFTW VEAKLSAGIE FLRDAWEILK FLVTGVFDIV
KGQIQVASDN LKECVKAFLD VLNKALEMCI DQVIIAGAKL RTLNLGEVFI AQSKGLYRQC
IRGKEQLQLL MPLRAPKEVT FFEGDSHDTV FTSEEVVLKN GELEALETPV DSFTNGAVIG
TPVCVNGLML LELKDKEQYC ALSPGLLATN NVFSLKGGAP VKGVTFGEDT VLEVQGYKNV
KITFELDERV DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTNMGIDLDE
WSVATFYLFD DAGEEKLSSR MYCSFYPPDE EEDCEEYEDE EEIPEETCEH EYGTEDDYKG
LPLEFGASTE IQQVDEEEEE DWLEEAIAAK PEPEPLPEEP VNQFTGYLKL TDNVAIKCVD
IVKEAQHAKP TVIVNAANVH LKHGGGVAGA LNKATNGAMQ QESDDYIKKN GPLTVGGSCL
LSGHNLAKKC MHVVGPNLNA GEDVQLLKAA YANFNSQDVL LAPLLSAGIF GAKPLQSLKM
CVETVRTQVY FAVNDQDLYD HVVLGYLDSL KPKVETPTQE NLELKEQPAV ETLTQENLEL
EELPVIEKPV DVKFKARIEE VNTSLEETKF LTSRLLLFAD INGKLYQDSQ NMLRGEDMFF
LEKDAPYIVG DVISSGDITC VIIPAKKAGG TTEMLAKALK KVPVSEYITT YPGQGCAGYT
LEEAKTALRK CKSVFYVLPS KTPNDKEEIL GTVSWNLREM LAHAEETRKL MLICMDVKAL
MSTIHRRYKG IKVQEGIVDY GVRFFFYTSK EPVASIITKL NLLNEPLVTM PIGYVTHGLN
LEEAARCMRS LKAPAVVSVS SPDAVTTYNG YLTSSSKTSE EHFIETVSLA GMYRDWSYSG
QRTELGVEFL KRGDKVVYHT VGSPIQFHLD GEVLLLDKLK SLLSLREVRT IKVFTTVDNT
NLHTQIVDMS MTYGQQFGPT YLDGADVTKI KPHAKHEGKT FFVLPSDDTL RSEAFEYYHT
LDESFLGRYM SALNHTKKWK FPQIGGLTSI KWADNNCYLS SVLLALQQIE VKFNAPALQE
AYYRARAGDA ANFCALILAY SNRTVGELGD VRETMTHLLQ HANLESAKRV LNVVCKTCGQ
KSTTLTGVEA VMYMGTLSYE ELKTGVTIPC ICGRDATQYL VQQESSFVMM SAPPSEYTLQ
QGAFLCANEY TGSYQCGHYT HVTVKETLYR IDGAYLTKMS EYKGPVTDVF YKEISYTTTI
KPVSYKLDGV IYTEIQPKLD EYYKKDNAYY TEQPIDLVPT QPLPNASFDN FKLTCSNTKF
ADDLNQMTGF KKPASRELSV TFFPDLNGDV VAIDYRHYSA SFKKGAKLLH KPIIWHINQT
TNKTTYKPNT WCLRCLWSTK PVETSNSFEV LEVEDTQGMD NLACESQTPT SEEVVENPTI
QKEVIECDVK TIEVVGNVIL KPSEEGVKVT QELGHEDLMA AYVEETSITI KKPNELSLAL
GLRTLATHGA AAINSVPWSK ILAYVKPFLG QAAVTTTNCI KRCVQRVFNN YMPYVITLLF
QLCTFTRSTN SRIRASLPTT IAKNSVKSVA KLCLDVCINY VKSPKFSKLF TIAMWLLLLS
ICLGSLIYVT AAFGVLLSNL GIPSYCDGVR ESYVNSSNVT TMDFCEGSFL CSVCLNGLDS
LDSYPALETI QVTISSYKLD LTSLGLAAEW FLAYMLFTKF FYLLGLSAIM QVFFGYFASH
FISNSWLMWF IISIVQMAPV SAMVRMYIFF AFCYYVWKSY VHIMDGCTSS TCMMCYKRNR
ATRVECTTIV NGMKRSFYVY ANGGRGFCKA HNWNCLNCDT FCAGSTFISD EVARDLSLQF
KRPINPTDQS SYVVDSVAVK NGALHLYFDK AGQKTYERHP LSHFVNLDNL RANNTKGSLP
INVIVFDGKS KCDESAAKSA SVYYSQLMCQ PILLLDQALV SDVGDSTEVS VKMFDAYVDT
FSATFSVPME KLKALVATAH SELAKGVALD GVLSTFVSAA RQGVVDTDVD TKDVIECLKL
SHHSDLEVTG DSCNNFMLTY NKVENMTPRD LGACIDCNAR HINAQVAKSH NVSLIWNVKD
YMSLSEQLRK QIRSAAKKNN IPFRLTCATT RQVVNAITTK ISLKGGKIVS TWFKLMLKAT
LLCVLAALFC YIIMPVHSLS VHDGYTNEII GYKAIQDGVT RDIMATDDCF ANKHAGFDSW
FSQRGGSYRN DKSCPVVAAI ITREIGFIVP GLPGTVLRAI NGDFLHFLPR VFSAVGNICY
TPSKLIEYSD FATSACVLAA ECTIFKDAMG KPVPYCYDTN LLEGSISYSE LRPDTRYVLM
DGSIIQFPNT YLEGSVRVVT TFDAEYCRHG TCERSEAGVC LSTSGRWVLN NEHYRALPGV
FCGVDAMNLI ANIFTPLVQP VGALDVSASV VAGGIIAILV TCAAYYFMKF RRAFGEYNHV
VAANALLFLM SFTILCLAPA YSFLPGVYSI FYLYLTFYFT NDVSFLAHLQ WFAMFSPIVP
FWITAIYVFC ISLKHCHWFF NNYLRKRVMF NGVTFSTFEE AALCTFLLNK EMYLKLRSET
LLPLTQYNRY LALYNKYKYF SGALDTTSYR EAACCHLAKA LNDFSNSGAD VLYQPPQTSI
TSAVLQSGFR KMAFPSGKVE GCMVQVTCGT TTLNGLWLDD TVYCPRHVIC TAEDMLNPNY
EDLLIRKSNH SFLVQAGNVQ LRVIGHSMQN CLLRLKVDTS NPKTPKYKFV RIQPGQTFSV
LACYNGSPSG VYQCAMRPNY TIKGSFLNGS CGSVGFNIDY DCVSFCYMHH MELPTGVHAG
TDLEGKFYGP FVDRQTAQAA GTDTTITLNV LAWLYAAVIN GDRWFLNRFT TTLNDFNLVA
MKYNYEPLTQ DHVDILGPLS AQTGIAVLDM CAALKELLQN GMNGRTILGS TILEDEFTPF
DVVRQCSGVT FQGKFKKIVK GTHHWMLLTF LTSLLILVQS TQWSLFFFVY ENAFLPFTLG
IMAIAACAML LVKHKHAFLC LFLLPSLATV AYFNMVYMPA SWVMRIMTWL ELADTSLSGY
RLKDCVMYAS ALVLLVLMTA RTVYDDAARR VWTLMNVITL VYKVYYGNSL DQAISMWALV
ISVTSNYSGV VTTIMFLARA IVFVCVEYYP LLFITGNTLQ CIMLVYCFLG YCCCCYFGLF
CLLNRYFRLT LGVYDYLVST QEFRYMNSQG LLPPKSSIDA FKLNIKLLGI GGKPCIKVAT
VQSKMSDVKC TSVVLLSVLQ QLRVESSSKL WAQCVQLHND ILLAKDTTEA FEKMVSLLSV
LLSMQGAVDI NKLCEEMLDN RATLQAIASE FSSLPSYAAY ATAQEAYEQA VANGDSEVVL
KKLKKSLNVA KSEFDRDAAM QRKLEKMADQ AMTQMYKQAR SEDKRAKVTS AMQTMLFTML
RKLDNDALNN IINNARDGCV PLNIIPLTTA AKLMVVVPDY GTYKNTCDGN TFTYASALWE
IQQVVDADSK IVQLSEINMD NSQNLAWPLI VTALRANSAV KLQNNELSPV ALRQMSCAAG
TTQTACTDDN ALAYYNNSKG GRFVLALLSD HQDLKWARFP KSDGTGTIYT ELEPPCRFVT
DTPRGPKVKY LYFIKGLNNL NRGMVLGSLA ATVRLQAGNA TEVPANSAVL SFCAFAVDPA
KAYKDYLASG GQPITNCVKM LCTHTGTGQA ITVTPEANMD QESFGGASCC LYCRCHIDHP
NPKGFCDLKG KYVQIPATCA NDPVGFTLKN TVCTVCGTWK GYGCSCDQLR EPMMQSADAS
TFLNRVCGVS AARLTPCGTG TSTDVVYRAF DIYNERVAGF AKFLKTNCCR FQEKDEEGNL
LDSYFVVKRH TMSNYQHEET IYNLVKECPA VAVHDFFKFR VDGDMVPHIS RQRLTKYTMA
DLVYALRHFD EGNCDTLKEI LVTYNCCDDD YFNKKDWYDF VENPDILRVY ANLGERVRQA
LLKTVQFCDA MRDAGIVGVL TLDNQDLNGN WYDFGDFVQV APGCGVPIVD SYYSLLMPIL
TLTKALAAES HMDADLAKPL IKWDLLKYDF TEERLCLFDR YFKYWDQTYH PNCINCLDDR
CILHCANFNV LFSTVFPPTS FGPLVRKIFV DGVPFVVSTG YHFRELGVVH NQDVNLHSSR
LSFKELLVYA ADPAMHAASG NLLLDKRTTC FSVAALTNNV AFQTVKPGNF NKDFYDFAVS
KGFFKEGSSV ELKHFFFAQD GNAAISDYDY YRYNLPTMCD IRQLLFVVEV VDKYFDCYDG
GCINANQVIV NNLDKSAGFP FNKWGKARLY YDSMSYEDQD VLFAYTKRNV IPTITQMNLK
YAISAKNRAR TVAGVSICST MTNRQFHQKL LKSIAATRGA TVVIGTSKFY GGWHNMLKTV
YSDVETPHLM GWDYPKCDRA MPNMLRIMAS LVLARKHSTC CNLSHRFYRL ANECAQVLSE
MVMCGGSLYV KPGGTSSGDA TTAYANSVFN ICQAVTANVN ALLSTDGNKI ADKYVRNLQH
RLYECLYRNR DVDHEFVDEF YAYLRKHFSM MILSDDAVVC YNSNYAAQGL VASIKNFKAV
HYYQNNVFMS EAKCWTETDL TKGPHEFCSQ HTMLVKQGDD YVYLPYPDPS RILGAGCFVD
DIVKTDGTLM IERFVSLAID AYPLTKHPNQ EYADVFHLYL QYIRKLHDEL TGHMLDMYSV
MLTNDNTSRY WEPEFYEAMY TPHTVLQAVG ACVLCNSQTS LRCGACIRRP FLCCKCCYDH
VISTSHKLVL SVNPYVCNAP GCDVTDVTQL YLGGMSYYCK LHKPPISFPL CANGQVFGLY
KNTCVGSDNV TDFNAIATCD WTNAGDYILA NTCTERLKLF AAETLKATEE TFKLSYGIAT
VREVLSDREL HLSWEVGKPR PPLNRNYVFT GYRVTKNSKV QIGEYTFEKG DYGDAVVYRG
TTTYKLNVGD YFVLTSHTVM PLSAPTLVPQ EHYVRITGLY PTLNISDEFS SNVANYQKVG
MQKYSTLQGP PGTGKSHFAI GLALYYPSAR IVYTACSHAA VDALCEKALK YLPIDKCSRI
IPARARVECF DKFKVNSTLE QYVFCTVNAL PETTADIVVF DEISMATNYD LSVVNARLRA
KHYVYIGDPA QLPAPRTLLT KGTLEPEYFN SVCRLMKTIG PDMFLGTCRR CPAEIVDTVS
ALVYDNKLKA HKEKSAQCFK MFYKGVITHD VSSAINRPQI GVVREFLTRN PAWRKAVFIS
PYNSQNAVAS KILGLPTQTV DSSQGSEYDY VIFTQTTETA HSCNVNRFNV AITRAKIGIL
CIMSDRDLYD KLQFTSLEVP RRNVATLQAE NVTGLFKDCS KIITGLHPTQ APTHLSVDTK
FKTEGLCVDI PGIPKDMTYR RLISMMGFKM NYQVNGYPNM FITREEAIRH VRAWIGFDVE
GCHATRDAVG TNLPLQLGFS TGVNLVAVPT GYVDTENNTE FTRVNAKPPP GDQFKHLIPL
MYKGLPWNVV RIKIVQMLSD TLKGLSDRVV FVLWAHGFEL TSMKYFVKIG PERTCCLCDR
RATCFSTSSD TYACWNHSVG FDYVYNPFMI DVQQWGFTGN LQSNHDQHCQ VHGNAHVASC
DAIMTRCLAV HECFVKRVDW SVEYPIIGDE LKINAACRKV QHMVVKSALL ADKFSVLHDI
GNPKAIKCVP QAEVDWKFYD AQPCSDKAYK IEELFYSYAT HHDKFTDGVC LFWNCNVDRY
PANAIVCRFD TRVLSNLNLP GCDGGSLYVN KHAFHTPAFD KSAFTYLKQL PFFYYSDSPC
ESHGKQVVSD IDYVPLKSAT CITRCNLGGA VCRRHANEYR QYLDAYNMMI SAGFSLWIYK
QFDTYNLWNT FTRLQSLENV AYNVVNKGHF DGQIGEAPVS IINNAVYTKV DGNDVEIFEN
KTTLPVNVAF ELWAKRNIKP VPEIKILNNL GVDIAANTVI WDYKREAPAH VSTIGVCTMT
DIAKKPTESA CSSLTVLFDG RVEGQVDLFR NARNGVLITE GSVKGLTPSK GPAQASVNGV
TLIGESVKTQ FNYFKKVDGI IQQLPETYFT QSRDLEDFKP RSKMETDFLE LAMDEFIQRY
KLEGYAFEHI VYGDFSHGQL GGLHLMIGLA KRSQDSPLKL EDFIPTDSTV KNYFITDAQT
GSSKCVCSVI DLLLDDFVEI IKSQDLSVIS KVVKVTIDYA EISFMLWCKD GHVETFYPKL
QASQAWQPGV AMPNLYKMQR MLLEKCDLQN YGENAVIPKG IMMNVAKYTQ LCQYLNTLTL
AVPYNMRVIH FGAGSDKGVA PGTAVLRQWL PTGALLVDSD LNDFVSDADS TLIGDCATVH
TANKWDLIIS DMYDPKTKHV TKENDSKEGF FTYLCGFIKQ KLALGGSVAV KITEHSWNAD
LYKLMGHFSW WTAFVTNVNA SSSEAFLIGV NYLGKLREQI DGYTMHANYI FWRNTNPIQL
SSYSLFDMSK FPLKLRGTAV MSLKENQIND MIYSLLENGR LIIRENNRVV VSSDILVNN


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