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 R1AB_BCHK4              Reviewed;        7119 AA.
P0C6W3; A3EX93;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-APR-2018, entry version 78.
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 HKU4 (BtCoV) (BtCoV/HKU4/2004).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=694007;
NCBI_TaxID=258959; Tylonycteris pachypus (Lesser bamboo bat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate HKU4-1;
PubMed=17121802; DOI=10.1128/JVI.02182-06;
Woo P.C.Y., Wang M., Lau S.K.P., Xu H.F., Poon R.W.S., Guo R.,
Wong B.H.L., Gao K., Tsoi H.-W., Huang Y., Li K.S.M., Lam C.S.F.,
Chan K.-H., Zheng B.-J., Yuen K.-Y.;
"Comparative analysis of twelve genomes of three novel group 2c and
group 2d coronaviruses reveals unique group and subgroup features.";
J. Virol. 81:1574-1585(2007).
-!- 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=P0C6W3-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6T4-1; 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}.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
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EMBL; EF065505; ABN10838.1; -; Genomic_RNA.
RefSeq; YP_001039952.1; NC_009019.1. [P0C6W3-1]
PDB; 4YO9; X-ray; 2.30 A; A/B=3292-3597.
PDB; 4YOG; X-ray; 2.00 A; A/B=3292-3597.
PDB; 4YOI; X-ray; 1.82 A; A/B=3292-3597.
PDB; 4YOJ; X-ray; 1.90 A; A/B=3292-3597.
PDBsum; 4YO9; -.
PDBsum; 4YOG; -.
PDBsum; 4YOI; -.
PDBsum; 4YOJ; -.
ProteinModelPortal; P0C6W3; -.
SMR; P0C6W3; -.
MEROPS; C16.011; -.
PRIDE; P0C6W3; -.
GeneID; 4835998; -.
KEGG; vg:4835998; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000006574; 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; 1.10.150.420; -; 1.
Gene3D; 1.10.8.370; -; 1.
Gene3D; 2.40.10.250; -; 1.
Gene3D; 3.10.20.350; -; 1.
Gene3D; 3.40.220.20; -; 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; IPR036333; NSP10_sf.
InterPro; IPR009466; NSP11.
InterPro; IPR024375; Nsp3_coronavir.
InterPro; IPR038400; Nsp3_coronavir_sf.
InterPro; IPR038123; NSP4_C_sf.
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; IPR038083; pp1a/1ab.
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; 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; PF05409; Peptidase_C30; 1.
Pfam; PF00680; RdRP_1; 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; SSF159936; SSF159936; 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.
1: Evidence at protein level;
3D-structure; 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 1 195 Host translation inhibitor nsp1.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290288.
CHAIN 196 847 Non-structural protein 2.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290289.
CHAIN 848 2784 Papain-like proteinase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290290.
CHAIN 2785 3291 Non-structural protein 4.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290291.
CHAIN 3292 3597 3C-like proteinase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290292.
CHAIN 3598 3889 Non-structural protein 6.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290293.
CHAIN 3890 3972 Non-structural protein 7.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290294.
CHAIN 3973 4171 Non-structural protein 8.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290295.
CHAIN 4172 4281 Non-structural protein 9.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290296.
CHAIN 4282 4420 Non-structural protein 10.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290297.
CHAIN 4421 5354 RNA-directed RNA polymerase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290298.
CHAIN 5355 5952 Helicase. {ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290299.
CHAIN 5953 6475 Guanine-N7 methyltransferase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290300.
CHAIN 6476 6817 Uridylate-specific endoribonuclease.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290301.
CHAIN 6818 7119 2'-O-methyltransferase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290302.
TRANSMEM 2112 2132 Helical. {ECO:0000255}.
TRANSMEM 2145 2165 Helical. {ECO:0000255}.
TRANSMEM 2222 2242 Helical. {ECO:0000255}.
TRANSMEM 2326 2346 Helical. {ECO:0000255}.
TRANSMEM 2350 2370 Helical. {ECO:0000255}.
TRANSMEM 2375 2395 Helical. {ECO:0000255}.
TRANSMEM 2800 2820 Helical. {ECO:0000255}.
TRANSMEM 3072 3092 Helical. {ECO:0000255}.
TRANSMEM 3105 3125 Helical. {ECO:0000255}.
TRANSMEM 3149 3169 Helical. {ECO:0000255}.
TRANSMEM 3603 3623 Helical. {ECO:0000255}.
TRANSMEM 3637 3657 Helical. {ECO:0000255}.
TRANSMEM 3662 3682 Helical. {ECO:0000255}.
TRANSMEM 3707 3727 Helical. {ECO:0000255}.
TRANSMEM 3735 3755 Helical. {ECO:0000255}.
TRANSMEM 3784 3804 Helical. {ECO:0000255}.
TRANSMEM 3808 3828 Helical. {ECO:0000255}.
DOMAIN 1152 1321 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1593 1864 Peptidase C16. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3292 3597 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
DOMAIN 5034 5196 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 5355 5438 CV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
DOMAIN 5611 5792 (+)RNA virus helicase ATP-binding.
DOMAIN 5793 5967 (+)RNA virus helicase C-terminal.
ZN_FING 1714 1751 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4355 4371 {ECO:0000250}.
ZN_FING 4397 4410 {ECO:0000250}.
NP_BIND 5636 5643 ATP. {ECO:0000250}.
REGION 2112 2395 HD1. {ECO:0000250}.
REGION 2800 3169 HD2. {ECO:0000250}.
REGION 3603 3828 HD3. {ECO:0000250}.
COMPBIAS 960 1049 Glu-rich.
COMPBIAS 4161 4166 Poly-Ser.
COMPBIAS 5359 5384 Cys-rich.
ACT_SITE 1634 1634 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1800 1800 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3332 3332 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3439 3439 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
METAL 5359 5359 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5362 5362 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5370 5370 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5373 5373 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5380 5380 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5383 5383 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5387 5387 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5393 5393 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5404 5404 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5409 5409 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5426 5426 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5429 5429 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
SITE 195 196 Cleavage. {ECO:0000255}.
SITE 847 848 Cleavage; by PL-PRO. {ECO:0000255}.
SITE 2784 2785 Cleavage; by PL-PRO. {ECO:0000255}.
SITE 3291 3292 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 3597 3598 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 3889 3890 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 3972 3973 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4171 4172 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4281 4282 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4420 4421 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 5354 5355 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 5952 5953 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 6475 6476 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 6817 6818 Cleavage; by 3CL-PRO. {ECO:0000255}.
HELIX 3302 3305 {ECO:0000244|PDB:4YOI}.
STRAND 3308 3313 {ECO:0000244|PDB:4YOI}.
STRAND 3316 3323 {ECO:0000244|PDB:4YOI}.
STRAND 3326 3330 {ECO:0000244|PDB:4YOI}.
HELIX 3331 3334 {ECO:0000244|PDB:4YOI}.
HELIX 3337 3339 {ECO:0000244|PDB:4YOI}.
STRAND 3340 3342 {ECO:0000244|PDB:4YOI}.
HELIX 3345 3351 {ECO:0000244|PDB:4YOI}.
HELIX 3354 3356 {ECO:0000244|PDB:4YOI}.
STRAND 3357 3361 {ECO:0000244|PDB:4YOI}.
STRAND 3363 3365 {ECO:0000244|PDB:4YOI}.
STRAND 3367 3369 {ECO:0000244|PDB:4YOI}.
STRAND 3371 3377 {ECO:0000244|PDB:4YOI}.
STRAND 3380 3387 {ECO:0000244|PDB:4YOI}.
STRAND 3394 3397 {ECO:0000244|PDB:4YOI}.
STRAND 3405 3412 {ECO:0000244|PDB:4YOI}.
STRAND 3415 3423 {ECO:0000244|PDB:4YOI}.
HELIX 3436 3438 {ECO:0000244|PDB:4YOI}.
STRAND 3442 3447 {ECO:0000244|PDB:4YOI}.
STRAND 3450 3462 {ECO:0000244|PDB:4YOI}.
STRAND 3465 3469 {ECO:0000244|PDB:4YOI}.
STRAND 3475 3478 {ECO:0000244|PDB:4YOI}.
STRAND 3481 3484 {ECO:0000244|PDB:4YOI}.
HELIX 3495 3507 {ECO:0000244|PDB:4YOI}.
HELIX 3521 3530 {ECO:0000244|PDB:4YOI}.
HELIX 3540 3549 {ECO:0000244|PDB:4YOI}.
HELIX 3553 3565 {ECO:0000244|PDB:4YOI}.
STRAND 3575 3577 {ECO:0000244|PDB:4YOI}.
HELIX 3584 3590 {ECO:0000244|PDB:4YOI}.
TURN 3591 3593 {ECO:0000244|PDB:4YOG}.
SEQUENCE 7119 AA; 795200 MW; E85475854586DD79 CRC64;
MLSKASVTTQ GARGKYRAEL YNEKRSDHVA CTVPLCDTDD MACKLTPWFE DGETAFNQVS
SILKEKGKIL FVPMHMQRAM KFLPGPRVYL VERLTGGMLS KHFLVNQLAY KDQVGAAMMR
TTLNAKPLGM FFPYDSSLET GEYTFLLRKN GLGGQLFRER PWDRKETPYV EILDDLEADP
TGKYSQNLLK KLIGGDCIPI DQYMCGKNGK PIADYAKIVA KEGLTTLADI EVDVKSRMDS
DRFIVLNKKL YRVVWNVTRR NVPYPKQTAF TIVSVVQCDD KDSVPEHTFT IGSQILMVSP
LKATNNKNFN LKQRLLYTFY GKDAVQQPGY IYHSAYVDCN ACGRGTWCTG NAIQGFACDC
GANYSANDVD LQSSGLVPRN ALFLANCPCA NNGACSHSAA QVYNILDGKA CVEVGGKSFT
LTFGGVVYAY MGCCDGTMYF VPRAKSCVSR IGDAIFTGCT GTWDKVVETA NLFLEKAQRS
LNFCQQFALT EVVLAILSGT TSTFEELRDL CHNASYEKVR DHLVNHGFVV TIGDYIRDAI
NIGANGVCNA TINAPFIAFT GLGESFKKVS AIPWKICSNL KSALDYYSSN IMFRVFPYDI
PCDVSNFVEL LLDCGKLTVA TSYFVLRYLD EKFDTVLGTV SSACQTALSS FLNACVAASR
ATAGFINDMF KLFKVLMHKL YVYTSCGYVA VAEHSSKIVQ QVLDIMSKAM KLLHTNVSWA
GTKLSAIIYE GREALLFNSG TYFCLSTKAK TLQGQMNLVL PGDYNKKTLG ILDPVPNADT
IDVNANSTVV DVVHGQLEPT NEHGPSMIVG NYVLVSDKLF VRTEDEEFYP LCTNGKVVST
LFRLKGGMPS KKVTFGDVNT VEVTAYRSVS ITYDIHPVLD ALLSSSKLAT FTVEKDLLVE
DFVDVIKDEV LTLLTPLLRG YDIDGFDVED FIDVPCYVYN QDGDCAWSSN MTFSINPVED
VEEVEEFIED DYLSDELPIA DDEEAWARAV EEVMPLDDIL VAEIELEEDP PLETALESVE
AEVVETAEAQ EPSVESIDST PSTSTVVGEN DLSVKPMSRV AETDDVLELE TAVVGGPVSD
VTAIVTNDIV SVEQAQQCGV SSLPIQDEAS ENQVHQVSDL QGNELLCSET KVEIVQPRQD
LKPRRSRKSK VDLSKYKHTV INNSVTLVLG DAIQIASLLP KCILVNAANR HLKHGGGIAG
VINKASGGDV QEESDEYISN NGPLHVGDSV LLKGHGLADA ILHVVGPDAR NNEDAALLKR
CYKAFNKHTI VVTPLISAGI FSVDPKVSFE YLLANVTTTT YVVVNNEDIY NTLATPSKPD
GLVYSFEGWR GTVRTAKNYG FTCFICTEYS ANVKFLRTKG VDTTKKIQTV DGVSYYLYSA
RDALTDVIAA ANGCSGICAM PFGYVTHGLD LAQSGNYVRQ VKVPYVCLLA SKEQIPIMNS
DVAIQTPETA FINNVTSNGG YHSWHLVSGD LIVKDVCYKK LLHWSGQTIC YADNKFYVVK
NDVALPFSDL EACRAYLTSR AAQQVNIEVL VTIDGVNFRT VILNDTTTFR KQLGATFYKG
VDISDAFPTV KMGGESLFVA DNLSESEKVV LKEYYGTSDV TFLQRYYSLQ PLVQQWKFVV
HDGVKSLKLS NYNCYINATI MMIDMLHDIK FVVPALQNAY LRYKGGDPYD FLALIMAYGD
CTFDNPDDEA KLLHTLLAKA ELTVSAKMVW REWCTVCGIR DIEYTGMRAC VYAGVNSMEE
LQSVFNETCV CGSVKHRQLV EHSAPWLLVS GLNEVKVSTS TDPIYRAFNV FQGVETSVGH
YVHIRVKDGL FYKYDSGSLT KTSDMKCKMT SVWYPTVRYT ADCNVVVYDL DGVTKVEVNP
DLSNYYMKDG KYYTSKPTIK YSPATILPGS VYSNSCLVGV DGTPGSDTIS KFFNDLLGFD
ETKPISKKLT YSLLPNEDGD VLLSEFSNYN PVYKKGVMLK GKPILWVNNG VCDSALNKPN
RASLRQLYDV APIVLDNKYT VLQDNTSQLV EHNVPVVDDV PITTRKLIEV KCKGLNKPFV
KGNFSFVNDP NGVTVVDTLG LTELRALYVD INTRYIVLRD NNWSSLFKLH TVESGDLQIV
AAGGSVTRRA RVLLGASSLF ASFAKITVTA TTAACKTAGR GFCKFVVNYG VLQNMFVFLK
MLFFLPFNYL WPKKQPTVDI GVSGLRTAGI VTTNIVKQCG TAAYYMLLGK FKRVDWKATL
RLFLLLCTTI LLLSSIYHLV LFNQVLSSDV MLEDATGILA IYKEVRSYLG IRTLCDGLVV
EYRNTSFDVM EFCSNRSVLC QWCLIGQDSL TRYSALQMLQ THITSYVLNI DWIWFALEFF
LAYVLYTSSF NVLLLVVTAQ YFFAYTSAFV NWRAYNYIVS GLFFLVTHIP LHGLVRVYNF
LACLWFLRKF YSHVINGCKD TACLLCYKRN RLTRVEASTI VCGTKRTFYI AANGGTSYCC
KHNWNCVECD TAGVGNTFIC TEVANDLTTT LRRLIKPTDQ SHYYVDSVVV KDAVVELHYN
RDGSSCYERY PLCYFTNLEK LKFKEVCKTP TGIPEHNFLI YDTNDRGQEN LARSACVYYS
QVLCKPMLLV DVNLVTTVGD SREIAIKMLD SFINSFISLF SVSRDKLEKL INTARDCVRR
GDDFQNVLKT FTDAARGHAG VESDVETTMV VDALQYAHKN DIQLTTECYN NYVPGYIKPD
SINTLDLGCL IDLKAASVNQ TSMRNANGAC VWNSGDYMKL SDSFKRQIRI ACRKCNIPFR
LTTSKLRAAD NILSVKFSAT KIVGGAPSWL LRVRDLTVKG YCILTLFVFT VAVLSWFCLP
SYSIATVNFN DDRILTYKVI ENGIVRDIAP NDVCFANKYG HFSKWFNENH GGVYRNSMDC
PITIAVIAGV AGARVANVPA NLAWVGKQIV LFVSRVFANT NVCFTPINEI PYDTFSDSGC
VLSSECTLFR DAEGNLNPFC YDPTVLPGAS SYADMKPHVR YDMYDSDMYI KFPEVIVEST
LRITKTLATQ YCRFGSCEES AAGVCISTNG SWALYNQNYS TRPGIYCGDD YFDIVRRLAI
SLFQPVTYFQ LSTSLAMGLV LCVFLTAAFY YINKVKRALA DYTQCAVVAV VAALLNSLCL
CFIVANPLLV APYTAMYYYA TFYLTGEPAF IMHISWYVMF GAVVPIWMLA SYTVGVMLRH
LFWVLAYFSK KHVDVFTDGK LNCSFQDAAS NIFVIGKDTY VALRNAITQD SFVRYLSLFN
KYKYYSGAMD TASYREACAA HLCKALQTYS ETGSDILYQP PNCSVTSSVL QSGLVKMSAP
SGAVENCIVQ VTCGSMTLNG LWLDNTVWCP RHIMCPADQL TDPNYDALLI SKTNHSFIVQ
KHIGAQANLR VVAHSMVGVL LKLTVDVANP STPAYTFSTV KPGASFSVLA CYNGKPTGVF
TVNLRHNSTI KGSFLCGSCG SVGYTENGGV INFVYMHQME LSNGTHTGSS FDGVMYGAFE
DKQTHQLQLT DKYCTINVVA WLYAAVLNGC KWFVKPTRVG IVTYNEWALS NQFTEFVGTQ
SIDMLAHRTG VSVEQMLAAI QSLHAGFQGK TILGQSTLED EFTPDDVNMQ VMGVVMQSGV
KRISYGFIHW LISTFVLAYV SVMQLTKFTM WTYLFETIPT QMTPLLLGFM ACVMFTVKHK
HTFMSLFLLP VALCLTYANI VYEPQTLISS TLIAVANWLT PTSVYMRTTH FDFGLYISLS
FVLAIIVRRL YRPSMSNLAL ALCSGVMWFY TYVIGDHSSP ITYLMFITTL TSDYTITVFA
TVNLAKFISG LVFFYAPHLG FILPEVKLVL LIYLGLGYMC TMYFGVFSLL NLKLRVPLGV
YDYSVSTQEF RFLTGNGLHA PRNSWEALIL NFKLLGIGGT PCIKVATVQS KLTDLKCTSV
VLLTVLQQLH LESNSKAWSY CVKLHNEILA AVDPTEAFER FVCLFATLMS FSANVDLDAL
ANDLFENSSV LQATLTEFSH LATYAELETA QSSYQKALNS GDASPQVLKA LQKAVNVAKN
AYEKDKAVAR KLERMAEQAM TSMYKQARAE DKKAKIVSAM QTMLFGMIKK LDNDVLNGVI
ANARNGCVPL SIVPLCASNK LRVVIPDISV WNKVVNWPSV SYAGSLWDIT VINNVDNEVV
KPTDVVETNE SLTWPLVIEC SRSSSSAVKL QNNEIHPKGL KTMVITAGVD QVNCNSSAVA
YYEPVQGHRM VMGLLSENAH LKWAKVEGKD GFINIELQPP CKFLIAGPKG PEIRYLYFVK
NLNNLHRGQL LGHIAATVRL QAGANTEFAS NSTVLTLVAF AVDPAKAYLD YVGSGGTPLS
NYVKMLAPKT GTGVAISVKP EATADQETYG GASVCLYCRA HIEHPDVSGV CKYKTRFVQI
PAHVRDPVGF LLKNVPCNVC QYWVGYGCNC DALRNNTVPQ SKDTNFLNRV RGSSVNARLE
PCSSGLTTDV VYRAFDICNF KARVAGIGKY YKTNTCRFVQ VDDEGHKLDS YFIVKRHTMS
NYELEKRCYD LLKDCDAVAI HDFFIFDVDK TKTPHIVRQS LTEYTMMDLV YALRHFDQNN
CEVLKSILVK YGCCEQSYFD NKLWFDFVEN PSVIGVYHKL GERIRQAMLN TVKMCDHMVK
SGLVGVLTLD NQDLNGKWYD FGDFVITQPG AGVAIVDSYY SYLMPVLSMT NCLAAETHKD
CDFNKPLIEW PLLEYDYTDY KIGLFNKYFK YWDQTYHPNC VNCSDDRCIL HCANFNVLFS
MVLPNTSFGP IVRKIFVDGV PFIVSCGYHY KELGLVMNMD FNIHRHRLAL KELMMYAADP
AMHIASASAL WDLRTPCFSV AALTTGLTFQ TVRPGNFNKD FYDFVVSRGF FKEGSSVTLK
HFFFAQDGHA AITDYSYYAY NLPTMVDIKQ MLFCMEVVDK YFDIYDGGCL NASEVIVNNL
DKSAGHPFNK FGKARVYYES MSYQEQDELF AVTKRNVLPT ITQMNLKYAI SAKNRARTVA
GVSILSTMTN RQYHQKMLKS MAATRGATCV IGTTKFYGGW DFMLKTLYKD VESPHLMGWD
YPKCDRAMPN MCRILASLIL ARKHSTCCTN SDRFYRLANE CAQVLSEYVL CGGGYYVKPG
GTSSGDATTA YANSVFNILQ ATTANVSALM SANGNTIIDR EIKDMQFDLY INVYRKVVPD
PKFVDKYYAF LNKHFSMMIL SDDGVVCYNS DYAAKGYVAS IQNFKETLYY QNNVFMSEAK
CWVETNLEKG PHEFCSQHTL YIKDGDDGYF LPYPDPSRIL SAGCFVDDIV KTDGTVMMER
YVSLAIDAYP LTKHDDTEYQ NVFWVYLQYI EKLYKDLTGH MLDSYSVMLC GDDSAKFWEE
GFYRDLYSSP TTLQAVGSCV VCHSQTSLRC GTCIRRPFLC CKCCYDHVIA TPHKMVLSVS
PYVCNAPGCD VSDVTKLYLG GMSYYCNDHR PVCSFPLCAN GLVFGLYKNM CTGSSSIMEF
NRLATCDWSD SGDYTLANTT TEPLKLFAAE TLRATEEASK QSYAIATIKE IVGERELILV
WEVGKSKPPL NRNYVFTGYH LTKNSKVQLG EYVFERIDYS DAVSYKSSTT YKLAVGDIFV
LTSHSVATLS APTIVNQERY LKITGIYPTI TVPEEFANHV VNFQKAGFSK YVTVQGPPGT
GKSHFAIGLA IYYPTARIVY TACSHAAVDA LCEKAFKYLN IAKCSRIIPA KARVECYDRF
KVNDTNSQYL FSTVNALPEI SVDILVVDEV SMCTNYDLSI INSRVKAKHI VYVGDPAQLP
APRTLLIRGT LEPENFNSVT RLMCNLGPDI FLSVCYRCPK EIVSTVSALV YNNKLSAKKD
ASGQCFKILF KGSVTHDASS AINRPQLNFV KTFIAANPNW SKAVFISPYN SQNAVARSML
GLTTQTVDSS QGSEYPYVIF CQTADTAHAN NLNRFNVAVT RAQKGILCVM TSQVLFDSLE
FAELSLNNYK LQSQIVTGLF KDCSREDTGL PPAYAPTYLS VDAKYKTTDE LCVNLNITPN
VTYSRVISRM GFKLDATIPG YPKLFITRDE AIRQVRSWVG FDVEGAHASR NACGTNVPLQ
LGFSTGVNFV VQPVGVVDTE WGSMLTTISA RPPPGEQFKH LVPLMNKGAT WPIVRRRIVQ
MLSDTLDKLS DYCTFVCWAH GFELTSASYF CKIGKEQRCS MCSRRASTFS SPLQSYACWS
HSSGYDYVYN PFFVDVQQWG YVGNLATNHD RYCGIHAGAH VASSDAIMTR CLAIYDCFIE
RVDWDVTYPY ISHEQKLNSC CRTVERNVVR SAVLSGKFEK IYDIGNPKGI AIISEPVEWH
FYDAQPLSNK VKKLFYTDDV SKQFEDGLCL FWNCNVSKYP SNAVVCRFDT RVHSEFNLPG
CNGGSLYVNK HAFHTPAYDI NAFRDLKPLP FFYYSTTPCE VHGSGNMLED IDYVPLKSAV
CITACNLGGA VCRKHAAEYR DYMEAYNIVS AAGFRLWVYK TFDIYNLWST FVKVQGLENI
AFNVIKQGHF TGVDGELPVA VVNDKIFTKN GTDDVCIFKN ETALPTNVAF ELYAKRAVRS
HPDLNLLRNL EVDVCYNFVL WDYDRNNIYG TTTIGVCKYT DIDVNPNLNM CFDIRDKGSL
ERFMSMPNGV LISDRKIKNY PCISGPKHAY FNGAILRNID AKQPVIFYLY KKVNNEFVSF
SDTFYTCGRT VGDFTVLTPM EEDFLVLDSD VFIKKYGLED YAFEHVVYGD FSHTTLGGLH
LLIGLYKKMR EGHILMEEML KDRATVHNYF ITDSNTASYK AVCSVIDLRL DDFVTIIKEM
DLDVVSKVVK VPIDLTMIEF MLWCRDGKVQ TFYPRLQATN DWKPGLTMPS LFKVQQMNLE
PCLLANYKQS IPMPNGVHMN VAKYMQLCQY LNTCTLAVPA NMRVIHFGAG CEKGVAPGTS
VLRQWLPLDA VLIDNDLNEF VSDADITIFG DCVTVHVGQQ VDLLISDMYD PCTKAVGEVN
QTKALFFVYL CNFIKNNLAL GGSVAIKITE HSWSADLYKI MGRFAYWTVF CTNANASSSE
GFLIGINFLG ELKEEIDGNV MHANYIFWRN STPMNLSTYS LFDLSRFPLK LKGTPVLQLK
ESQINELVIS LLSQGKLLIR DNDTLNVSTD VLVNFRKRL


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