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 R1AB_BCHK3              Reviewed;        7067 AA.
P0C6W2; Q3LZX2;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-OCT-2017, entry version 73.
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 HKU3 (BtCoV) (SARS-like coronavirus HKU3).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=442736;
NCBI_TaxID=89399; Rhinolophus sinicus (Chinese rufous horseshoe bat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate HKU3-1;
PubMed=16169905; DOI=10.1073/pnas.0506735102;
Lau S.K.P., Woo P.C.Y., Li K.S.M., Huang Y., Tsoi H.-W., Wong B.H.L.,
Wong S.S.Y., Leung S.-Y., Chan K.-H., Yuen K.-Y.;
"Severe acute respiratory syndrome coronavirus-like virus in Chinese
horseshoe bats.";
Proc. Natl. Acad. Sci. U.S.A. 102:14040-14045(2005).
-!- 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=P0C6W2-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6F8-1; 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 HKU3 is highly similar to SARS-CoV
(SARS-like).
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
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EMBL; DQ022305; AAY88865.2; -; Genomic_RNA.
ProteinModelPortal; P0C6W2; -.
SMR; P0C6W2; -.
MEROPS; C30.005; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000007450; 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; IPR037227; EndoU-like.
InterPro; IPR002589; Macro_dom.
InterPro; IPR032592; NAR_dom.
InterPro; IPR021590; NSP1.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR009466; NSP11.
InterPro; IPR024375; Nsp3_coronavir.
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; 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; 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; 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_0000291335.
CHAIN 180 818 Non-structural protein 2.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000291336.
CHAIN 819 2734 Papain-like proteinase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000291337.
CHAIN 2735 3234 Non-structural protein 4.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000291338.
CHAIN 3235 3540 3C-like proteinase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000291339.
CHAIN 3541 3830 Non-structural protein 6.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000291340.
CHAIN 3831 3913 Non-structural protein 7.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000291341.
CHAIN 3914 4111 Non-structural protein 8.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000291342.
CHAIN 4112 4224 Non-structural protein 9.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000291343.
CHAIN 4225 4363 Non-structural protein 10.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000291344.
CHAIN 4364 5295 RNA-directed RNA polymerase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000291345.
CHAIN 5296 5896 Helicase. {ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000291346.
CHAIN 5897 6423 Guanine-N7 methyltransferase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000291347.
CHAIN 6424 6769 Uridylate-specific endoribonuclease.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000291348.
CHAIN 6770 7067 2'-O-methyltransferase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000291349.
TRANSMEM 2197 2217 Helical. {ECO:0000255}.
TRANSMEM 2298 2318 Helical. {ECO:0000255}.
TRANSMEM 2345 2365 Helical. {ECO:0000255}.
TRANSMEM 2744 2764 Helical. {ECO:0000255}.
TRANSMEM 2986 3006 Helical. {ECO:0000255}.
TRANSMEM 3016 3036 Helical. {ECO:0000255}.
TRANSMEM 3048 3068 Helical. {ECO:0000255}.
TRANSMEM 3071 3091 Helical. {ECO:0000255}.
TRANSMEM 3099 3119 Helical. {ECO:0000255}.
TRANSMEM 3136 3156 Helical. {ECO:0000255}.
TRANSMEM 3558 3578 Helical. {ECO:0000255}.
TRANSMEM 3580 3600 Helical. {ECO:0000255}.
TRANSMEM 3606 3626 Helical. {ECO:0000255}.
TRANSMEM 3652 3672 Helical. {ECO:0000255}.
TRANSMEM 3679 3698 Helical. {ECO:0000255}.
TRANSMEM 3722 3742 Helical. {ECO:0000255}.
TRANSMEM 3750 3770 Helical. {ECO:0000255}.
DOMAIN 998 1164 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1605 1869 Peptidase C16. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3235 3540 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
DOMAIN 4975 5137 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 5296 5379 CV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
DOMAIN 5552 5733 (+)RNA virus helicase ATP-binding.
DOMAIN 5734 5903 (+)RNA virus helicase C-terminal.
ZN_FING 1723 1760 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4298 4314 {ECO:0000250}.
ZN_FING 4341 4354 {ECO:0000250}.
NP_BIND 5577 5584 ATP. {ECO:0000250}.
REGION 2086 2365 HD1. {ECO:0000250}.
REGION 2749 3156 HD2. {ECO:0000250}.
REGION 3558 3770 HD3. {ECO:0000250}.
REGION 4906 5208 RNA-directed RNA polymerase.
{ECO:0000250}.
COMPBIAS 930 996 Glu-rich.
COMPBIAS 2204 2207 Poly-Leu.
COMPBIAS 3760 3763 Poly-Cys.
ACT_SITE 1645 1645 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1806 1806 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3275 3275 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3379 3379 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
METAL 5300 5300 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5303 5303 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5311 5311 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5314 5314 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5321 5321 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5324 5324 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5328 5328 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5334 5334 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5345 5345 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5350 5350 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5367 5367 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5370 5370 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
SITE 179 180 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 818 819 Cleavage; by PL-PRO. {ECO:0000250}.
SITE 3234 3235 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3540 3541 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3830 3831 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3913 3914 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4111 4112 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4224 4225 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4363 4364 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 5295 5296 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 5896 5897 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6423 6424 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6769 6770 Cleavage; by 3CL-PRO. {ECO:0000250}.
SEQUENCE 7067 AA; 789496 MW; 9EE66BBA1B5E6339 CRC64;
MESLVLGVNE KTHVQLSLPV LQVRDVLVRG FGDSVEEALS EAREHLKNGT CGLVELEKGV
LPQLEQPYVF IKRSDALSTN HGHKVVELVA ELDGIQFGRS GITLGVLVPH VGETPIAYRN
VLLRKNGNKG AGGHSFGIDL KSYDLGDELG TDPIEDYEQN WNTKHGSGAL RELTRELNGG
VVTRYVDNNF CGPDGYPLEC IKDFLARAGK SMCTLSEQLD YIESKRGVYC CREHEHEIVW
FTERSEKSYE HQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
RSVYPVATPQ ECNDMHLSTL MKCNHCDEVS WQTCDFLKAT CEQCGTENLV CEGPTTCGYL
PTNAVVKMPC PACQDPEVGP EHSVADYHNH SNIETRLRKG GRTKCFGGCV FSYVGCYNKR
AYWVPRASAN IGANHTGITG ENVETLNEDL LEILNRERVN INIVGDFRFN EEVAIILASF
SASPSAFIET VKGLDYKSFK VIVESCGNYK VTNGKPVTGA WNIGQQRSIL TPLCGFPSQA
AGVIRSIFSR TLDAANHSIL DLQRAAVTTL DGISEQSLRL VDAMVYTSDL LTNSVVVMAY
VTGGLVQQTM QWLSNMLGTA VDKLKPVFTW VEAKLSAGVE FLRDAWEILK FLITGVFDVI
KGQIQVATDN IKECVKIFLG VVNKALEMCL DQVTIAGTKL RALNLGEVFI AQSRGLYRQC
IRGKEQLQLL MPLKAPKEVT FLEGDAHDTV LTSEEVVLKS GELEALETPI DSFTSGAVVG
TPVCINGLML LELENKEQYC ALSPGLLATN NVFRLKGGAP VKGVTFGEDT VLEVQGYKNV
KITFELDVRV DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTPMGIDLDE
WSVATFYLFD DAGEEKLSSR MYCSFYPPDE EEDCEECEDE EETCEHEYGT EDDYKGLPLE
FGASTETPHV EEEEEEEDWL DDAIEAEPEP EPLPEEPVNQ FVGYLKLTDN VAIKCIDIVK
EAQSAKPTVI VNAANTHLKH GGGVAGALNK ATNGAMQNES DEYIRQNGPL TVGGSCLLSG
HNLAEKCLHV VGPNLNAGED VQLLKRAYEN FNSQDVLLAP LLSAGIFGAK PLQSLKMCVE
IVRTQVYLAV NDKSLYDQIV LDYLDSLKPK VESPNKEEEP KLEEPKAVQP VAEKPVDVKP
KIKACIDEVT TTLEETKFLT NKLLLFADIN GKLYQDSQNM LRGEDMSFLE KDAPYIVGDV
ITSGDITCVI IPAKKSGGTT EMLARALKEV PVAEYITTYP GQGCAGYTLE EAKTALKKCK
SAFYVLPSET PNEKEEVLGT VSWNLREMLA HAEETRKLMP ICLDVRAIMA TIQRKYKGIK
VQEGIVDYGV RFFFYTSKEP VASIITKLNS LNEPLVTMPI GYVTHGLNLE EAARCMRSLK
APAVVSVSSP DAVTAYNGYL TSSSKTPEEY FVETTSLAGS YRDWSYSGQR TELGVEFLKR
GDKIVYHTTG SPIEFHLDGE VLPLDKLKSL LSLREVKTIK VFTTVDNTNL HTHIVDMSMT
YGQQFGPTYL DGADVTKIKP HVNHEGKTFF VLPSDDTLRS EAFEYYHTID ESFLGRYMSA
LNHTKKWKFP QVGGLTSIKW ADNNCYLSSV LLALQQVEVK FNAPALQEAY YRARAGDAAN
FCALILAYSN KTVGELGDVR ETMTHLLQHA NLESAKRVLN VVCKHCGQKT TTLKGVEAVM
YMGTLSYDEL KTGVSIPCVC GRNATQYLVQ QESSFVMMSA PPAEYKLQQG AFLCANEYTG
NYQCGHYTHI TAKETLYRVD GAHLTKMSEY KGPVTDVFYK ETSYTTAIKP VSYKLDGVTY
TEIEPKLDGY YKKGNAYYTE QPIDLVPTQP MPNASFDNFK LTCSNTKFAD DLNQMTGFKK
PASRELTVTF FPDLNGDVVA IDYRHYSTSF KKGAKLVHKP ILWHINQTTN KTTYKPNIWC
LRCLWSTKPV DTSNSFEVLV VEDTQGMDNL ACESQTTTSE EVVENPTVQK EIIECDVKTT
EVVGNVILKP SEEGVKVTQE LGHEDLMAAY VEETSITIKK PNELSLALGL KTLATHGAAA
INSVPWSKIL AYVKPFLGQT AVITSNCIKK CVQRVFSNYM PYVITLLFQL CTFTKSTNSR
IKASLPTTIA KNSVKSVAKL CLDVCINYVK SPKFSKLFTI VMWLLLLSIC LGSLTYVTAV
LGVCLSSLGV PSYCDGVREL YINSSNVTTM DFCQGYFPCS VCLSGLDSLD SYPALETIQV
TISSYKLDLT FLGLAAEWLL AYMLFTKFFY LLGLSAIMQA FFGYFASHFI SNSWLMWFII
SIVQMAPVSA MVRMYIFFAS FYYVWKSYVH IMDGCTSSTC MMCYKRNRAT RVECTTIVNG
VKRSFYVYAN GGRGFCKAHN WNCLNCDTFC AGSTFISDEV ARDLSLQFKR PINPTDQSAY
VVDSVTVKNG ALHLYFDKAG QKTYERHPLS HFVNLDNLRA NNTKGSLPIN VIVFDGKSKC
EESAAKSASV YYSQLMCQPI LLLDQALVSD VGDSTEVSVK MFDAYVDTFS ATFSVPMEKL
KALVATAHSE LAKGVALDGV LSTFVSAARQ GVVDTDVDTK DVIECLKLSH HSDIEVTGDS
CNNFMLTYNK VENMTPRDLG ACIDCNARHI NAQVAKSHNV SLVWNVKDYM SLSEQLRKQI
RSAAKKNNIP FRLTCATTRQ VVNVITTKIS LKGGKVVSTW FKLLLKVTLL CVLAALFCYV
IMPVHSLSVH DGYTNEIIGY KAIQDGVTRD IVSTDDCFAN KHAGFDSWFS QRGGSYRNDK
NCPVVAAIIT REIGFIVPGL PGTVLRALNG DFLHFLPRVF SAVGNICYTP SKLIEYSDFA
TSACVLAAEC TIFKDAMGKP VPYCYDTNLL EGSISYSELR PDTRYVLMDG SIIQFPNTYL
EGSVRVVTTF DAEYCRHGTC ERSEVGVCLS TSGRWVLNNE HYRALPGVFC GVDAMNLIAN
IFTPLVQPVG ALDVSASVVA GGIIAILVTC AAYYFMKFRR AFGEYNHVVA ANALLFLMSF
TILCLAPAYS FLPGVYSIFY LYLTFYFTND VSFLAHLQWF AMFSPIVPFW ITAIYVFCIS
LKHFHWFFSN YLKKRVMFNG VTFSTFEEAA LCTFLLNKEM YLRLRSETLL PLTQYNRYLA
LYNKYKYFSG ALDTTSYREA ACCHLAKALN DFSNSGADVL YQPPQTSITS AVLQSGFRKM
AFPSGKVEGC MVQVTCGTTT LNGLWLDDTV YCPRHVVCTA EDMLNPNYDD LLIRKSNHSF
LVQAGNVQLR VIGHSMQNCL LRLKVDTSNP KTPKYKFVRI QPGQTFSVLA CYNGSPSGVY
QCAMRPNHTI KGSFLNGSCG SVGFNIDYDC VSFCYMHHME LPTGVHAGTD LEGKFYGPFV
DRQTAQAAGT DTTITLNVLA WLYAAVINGD RWFLNRFTTT LNDFNLVAMK YNYEPLTQDH
VDILGPLSAQ TGIAVLDMCA ALKELLQNGM NGRTILGSTI LEDEFTPFDV VRQCSGVTFQ
GKFKKIVKGT HHWMLLTFLT SLLILVQSTQ WSLFFFVYEN AFLPFALGIM AVAACAMLLV
KHKHAFLCLF LLPSLATVAY FNMVYMPASW VMRIMTWLEL ADTSLSGYRL KDCVMYASAL
VLLILMTART VYDDAARRVW TLMNVITLVY KVYYGNSLDQ AISMWALVIS VTSNYSGVVT
TIMFLARAIV FVCVEYYPLL FITGNTLQCI MLVYCFLGYC CCCYFGLFCL LNRYFRLTLG
VYDYLVSTQE FRYMNSQGLL PPKSSIDAFK LNIKLLGIGG KPCIKVATVQ SKMSDVKCTS
VVLLSVLQQL RVESSSKLWA QCVQLHNDIL LAKDTTEAFE KMVSLLSVLL SMQGAVDINK
LCEEMLDNRA TLQAIASEFS SLPSYAAYAT AQEAYEQAVS NGDSEVVLKK LKKSLNVAKS
EFDHDAAMQR KLEKMADQAM TQMYKQARSE DKRAKVTSAM QTMLFTMLRK LDNDALNNII
NNARDGCVPL NIIPLTTAAK LMVVVPDYGT YKNTCDGNTF TYASALWEIQ QVVDADSKIV
QLSEINMDNS PNLAWPLIVT ALRANSAVKL QNNELSPVAL RQMSCAAGTT QTACTDDNAL
AYYNNAKGGR FVLALLSDHQ DLKWARFPKS DGTGTIYTEL EPPCRFVTDT PKGPKVKYLY
FIKGLNNLNR GMVLGSLAAT VRLQAGNATE VPANSTVLSF CAFAVDPAKA YKDYLASGGQ
PITNCVKMLC THTGTGQAIT VTPEANMDQE SFGGASCCLY CRCHIDHPNP KGFCDLKGKY
VQIPTTCAND PVGFTLRNTV CTVCGMWKGY GCSCDQLREP MMQSADASTF LNRVCGVSAA
RLTPCGTGTS TDVVYRAFDI YNEKVAGFAK FLKTNCCRFQ EKDEEGNLLD SYFVVKRHTM
SNYQHEETIY NLIKECPAVA VHDFFKFRVD GDMVPHISRQ RLTKYTMADL VYALRHFDEG
NCDTLKEILV TYNCCDDNYF NKKDWYDFVE NPDVLRVYAN LGERVRRALL KTVQFCDAMR
DAGIVGVLTL DNQDLNGNWY DFGDFVQVAP GCGVPIVDSY YSLLMPILTL TKALAAESHM
DADLAKPLVK WDLLKYDFTE ERLCLFDRYF KYWDQTYHPN CINCLDDRCI LHCANFNVLF
STVFPPTSFG PLVRKIFVDG VPFVVSTGYH FRELGVVHNQ DVNLHSSRLS FKELLVYAAD
PAMHAASGNL LLDKRTTCFS VAALTNNVAF QTVKPGNFNK DFYDFAVSKG FFKEGSSVEL
KHFFFAQDGN AAISDYDYYR YNLPTMCDIR QLLFVVEVVD KYFDCYDGGC INANQVIVNN
LDKSAGFPFN KWGKARLYYD SMSYEDQDAL FAYTKRNVIP TITQMNLKYA ISAKNRARTV
AGVSICSTMT NRQFHQKLLK SIAATRGATV VIGTSKFYGG WHNMLKTVYS DVESPHLMGW
DYPKCDRAMP NMLRIMASLI LARKHSTCCN LSHRFYRLAN ECAQVLSEMV MCGGSLYVKP
GGTSSGDATT AYANSVFNIC QAVTANVNAL LSTDGNKIAD KYVRNLQHRL YECLYRNRDV
DHEFVDEFYA YLRKHFSMMI LSDDAVVCYN SNYAAQGLVA SIKNFKAVLY YQNNVFMSEA
KCWTETDLTR GPHEFCSQHT MLVKQGDDYV YLPYPDPSRI LGAGCFVDDI VKTDGTLMIE
RFVSLAIDAY PLTKHPNQEY ADVFHLYLQY IRKLHDELTG HMLDMYSVML TNDNTSRYWE
PEFYEAMYTP HTVLQAVGAC VLCNSQTSLR CGACIRRPFL CCKCCYDHVI STSHKLVLSV
NPYVCNAPGC DVTDVTQLYL GGMSYYCKSH KPPISFPLCA NGQVFGLYKN TCVGSDNVTD
FNAIATCDWT NAGDYILANT CTERLKLFAA ETLKATEETF KLSYGIATVR EVLSDRELYL
SWEVGKPRPP LNRNYVFTGY RVTKNSKVQI GEYTFEKGDY GDAVVYRGTT TYKLNVGDYF
VLTSHTVMPL SAPTLVPQEH YVRITGLYPT LNISNEFSSN VANYQKIGMQ KYSTLQGPPG
TGKSHFAIGL ALYYPSARIV YTACSHAAVD ALCEKALKYL PIDKCSRIIP ARARVECFDK
FKVNSTLEQY VFCTVNALPE TTADIVVFDE ISMATNYDLS VVNARLRAKH YVYIGDPAQL
PAPRTLLTKG TLEPEYFNSV CRLMKTIGPD MFLGTCRRCP AEIVDTVSAL VYDNKLKAHK
EKSAQCFKMY YKGVITHDVS SAINRPQIGV VREFLTRNPA WRKAVFISPY NSQNAVASKI
LGLPTQTVDS SQGSEYDYVI FTQTTETAHS CNVNRFNVAI TRAKIGILCI MSDRDLYDKL
QFTSLEVPRR NVATLQAENV TGLFKDCSKI ITGLHPTQAP THLSVDTKFK TEGLCVDIPG
IPKDMTYRRL ISMMGFKMNY QVNGYPNMFI TREEAIRHVR AWIGFDVEGC HATRDAVGTN
LPLQLGFSTG VNLVAVPTGY VDTENSTEFT RVNAKPPPGD QFKHLIPLMY KGLPWNVVRI
KIVQMLSDTL KGLSDRVVFV LWAHGFELTS MKYFVKIGPE RTCCLCDKRA TCFSTSSDTY
ACWNHSVGFD YVYNPFMIDV QQWGFTGNLQ SNHDQHCQVH GNAHVASCDA IMTRCLAVHE
CFVKRVDWSV EYPIIGDELK INAACRKVQH MVVKSALLAD KFTVLHDIGN PKAIRCVPQA
EVDWKFYDAQ PCSDKAYKIE ELFYSYATHH DKFTDGVCLF WNCNVDRYPA NAIVCRFDTR
VLSNLNLPGC DGGSLYVNKH AFHTPAFDKS AFTHLKQLPF FYYSDSPCES HGKQVVSDID
YVPLKSATCI TRCNLGGAVC RHHANEYRQY LDAYNMMISA GFSLWIYKQF DTYNLWNTFT
KLQSLENVAY NVVNKGHFDG QSGEAPVSII NNAVYTKVDG IDVEIFENKT TLPVNVAFEL
WAKRNIKPVP EIKILNNLGV DIAANNVIWD YKREAPAHVS TIGVCTMTDI AKKPTESACS
SLIVLFDGRV EGQVDFFRNA RNGVLITEGS VKGLTPSKGP AQASVNGVTL IGESVKTQFN
YFKKVDGIIQ QLPETYFTQS RDLEDFKPRS QMETDFLELA MDEFIQRYKL EGYAFEHIVY
GDFSHGQLGG LHLMIGLAKR SQDSLLKLED FIPMDSTVKN YFITDAQTGS SKCVCSVIDL
LLDDFVEIIK SQDLSVVSKV VKVTIDYAEI SFMLWCKDGH VETFYPKLQA SQAWQPGVAM
PNLYKMQRML LEKCDLQNYG ENAVIPKGIM MNVAKYTQLC QYLNTLTLAV PYNMRVIHFG
AGSDKGVAPG TAVLRQWLPT GTLLVDSDLN DFVSDADSTL IGDCATVHTA NKWDLIISDM
YDPKTKHVLK DNDSKEGFFT YLCGFIKQKL ALGGSVAVKI TEHSWNADLY KLMGHFSWWT
AFVTNVNASS SEAFLIGVNY LGKPKEQIDG YTMHANYIFW RNTNPIQLSS YSLFDMSKFP
LKLRGTAVMS LKENQINDMI YSLLEKGRLI IRENNRVVVS SDILVNN


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