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 R1AB_BCHK5              Reviewed;        7182 AA.
P0C6W4; A3EXC9;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-APR-2018, entry version 79.
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 HKU5 (BtCoV) (BtCoV/HKU5/2004).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=694008;
NCBI_TaxID=105295; Pipistrellus abramus (Japanese pipistrelle) (Pipistrellus javanicus abramus).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate HKU5-1;
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=P0C6W4-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6T5-1; 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; EF065509; ABN10874.1; -; Genomic_RNA.
RefSeq; YP_001039961.1; NC_009020.1. [P0C6W4-1]
ProteinModelPortal; P0C6W4; -.
MEROPS; C16.011; -.
PRIDE; P0C6W4; -.
GeneID; 4836003; -.
KEGG; vg:4836003; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000007451; 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.
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 1 195 Host translation inhibitor nsp1.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290303.
CHAIN 196 851 Non-structural protein 2.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290304.
CHAIN 852 2830 Papain-like proteinase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290305.
CHAIN 2831 3338 Non-structural protein 4.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290306.
CHAIN 3339 3644 3C-like proteinase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290307.
CHAIN 3645 3936 Non-structural protein 6.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290308.
CHAIN 3937 4019 Non-structural protein 7.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290309.
CHAIN 4020 4218 Non-structural protein 8.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290310.
CHAIN 4219 4328 Non-structural protein 9.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290311.
CHAIN 4329 4467 Non-structural protein 10.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290312.
CHAIN 4468 5401 RNA-directed RNA polymerase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290313.
CHAIN 5402 5999 Helicase. {ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290314.
CHAIN 6000 6523 Guanine-N7 methyltransferase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290315.
CHAIN 6524 6874 Uridylate-specific endoribonuclease.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290316.
CHAIN 6875 7182 2'-O-methyltransferase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290317.
TRANSMEM 2158 2178 Helical. {ECO:0000255}.
TRANSMEM 2196 2216 Helical. {ECO:0000255}.
TRANSMEM 2268 2288 Helical. {ECO:0000255}.
TRANSMEM 2372 2392 Helical. {ECO:0000255}.
TRANSMEM 2396 2416 Helical. {ECO:0000255}.
TRANSMEM 2421 2441 Helical. {ECO:0000255}.
TRANSMEM 2848 2868 Helical. {ECO:0000255}.
TRANSMEM 3119 3139 Helical. {ECO:0000255}.
TRANSMEM 3152 3172 Helical. {ECO:0000255}.
TRANSMEM 3203 3223 Helical. {ECO:0000255}.
TRANSMEM 3650 3670 Helical. {ECO:0000255}.
TRANSMEM 3684 3704 Helical. {ECO:0000255}.
TRANSMEM 3709 3729 Helical. {ECO:0000255}.
TRANSMEM 3760 3777 Helical. {ECO:0000255}.
TRANSMEM 3782 3802 Helical. {ECO:0000255}.
TRANSMEM 3823 3843 Helical. {ECO:0000255}.
TRANSMEM 3855 3875 Helical. {ECO:0000255}.
DOMAIN 1186 1345 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1628 1902 Peptidase C16. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3339 3644 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
DOMAIN 5081 5243 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 5402 5485 CV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
DOMAIN 5658 5839 (+)RNA virus helicase ATP-binding.
DOMAIN 5840 6014 (+)RNA virus helicase C-terminal.
ZN_FING 1748 1785 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4402 4418 {ECO:0000250}.
ZN_FING 4444 4457 {ECO:0000250}.
NP_BIND 5683 5690 ATP. {ECO:0000250}.
REGION 2158 2441 HD1. {ECO:0000250}.
REGION 2848 3223 HD2. {ECO:0000250}.
REGION 3650 3875 HD3. {ECO:0000250}.
COMPBIAS 964 1066 Glu-rich.
COMPBIAS 5406 5431 Cys-rich.
ACT_SITE 1668 1668 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1838 1838 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3379 3379 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3486 3486 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
METAL 5406 5406 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5409 5409 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5417 5417 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5420 5420 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5427 5427 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5430 5430 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5434 5434 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5440 5440 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5451 5451 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5456 5456 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5473 5473 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5476 5476 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
SITE 195 196 Cleavage. {ECO:0000255}.
SITE 851 852 Cleavage; by PL-PRO. {ECO:0000255}.
SITE 2830 2831 Cleavage; by PL-PRO. {ECO:0000255}.
SITE 3338 3339 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 3644 3645 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 3936 3937 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4019 4020 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4218 4219 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4328 4329 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4467 4468 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 5401 5402 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 5999 6000 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 6523 6524 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 6874 6875 Cleavage; by 3CL-PRO. {ECO:0000255}.
SEQUENCE 7182 AA; 799932 MW; 455E36D8EF6FD1E1 CRC64;
MSFVAGVAPQ GARGKYRAEL NTEKRTDHVS LKASLCDAGD LVLKISPWFM DGESAYKHVS
EQLSKGSKLL FVPQTLKGFI RHLPGPRVYL VERLTGGTYS DPFMVNQLAY QNAAGEGVIG
TTLQGKRVGM FFPFDADLVT GEFQFLLRKK GFGGNRFRDA PWDYNWTPYS DLMDALEADP
CGKYSQSLLK KLVGGDFTPI DQYMCGKNGK PIAEFAALMA SEGITKLADV EAEVKSRTDS
DRYIVFKNKL YRIVWNVQRK DVAYSKQSAF TMNSIVQLDT MEDVPRHSFT IGSEIQVIAP
STAVQANGHL NLKQRLLYAF YGKQAVSEPN YIYHSAYVDC TSCGKGSWLT GNAVQGFACD
CGAHYCANDV DLQSSGLVRK NAVLLTTCPC NKDGECKHTL PQLVSMMTDK CDVEVVGKTF
ILTYGGVIYA YMGCSGGTMH FIPRAKSCVS KIGDAIFTGC TGTWSKVCET ANLFLERAQH
AINFVNEFVL TETVVALLSG TTSSIEELRD LCRNATFEKV RDYLTPRGWI VTMGSYIEGV
INVGAAGVCN AALNAPFIVL SGLGESFKKV AATPWKLCSS LRETLDHYAD SITYRVFPYD
IPCDVTDYTA LLLDCAVLTG ASAYFVARYV DEKVEQLTNL VFSSCQSAVA AFVQACMSTY
KATAKFISDM FTLIKVVSER LYVYTSVGFV VVGDYSSQLL KQFMHILSKA MQLLHTTVSW
AGSKLPSVVY NGRDSLVFPS GTYYCVSTQG RSLQDQFDLV IPGDLSKKQI GILEPTPNST
TVDKKINTNV VEVVVGQLEP TKEHSPELVV GDYVIISNKI FVRSVEDSET VFYPLCTDGK
IVPTLFRLKG GAPPKGVKFG GEQTKEITAV RSVSVDYDVH PVLDALLAGS ELATFTVEKD
LPVKDFVDVV KDEVIELLSK LLRGYNVDGF DLEDFADTPC YVYNAEGDLA WSSTMTFSVN
PVEEVEEECD DDYVEDEYLS EEMLVEEDEN SWAAAVEAVI PMEDVQLDTL VAEIDVSEPA
DDVAEQASTE EVEVPSACVL EASQVANAAE VESCEAEVSS SIPLHEDANA AKANDCAEGM
PALDSTETVS KLSVDTPVGD VTQDDATSSN ATVISEDVHT ATHSKGLVAV PEVVPEKALG
TSVERMRSTS EWTVVETSLK QETAVIVKND SSAKPQRVKK PKAENPLKNF KHIVLNNDVT
LVFGDAIAVA RATEDCILVN AANTHLKHGG GIAAAIDRAS GGLVQAESDD YVNFYGPLNV
GDSTLLKGHG LATGILHVVG PDARANQDIQ LLKRCYKAFN KYPLVVSPLI SAGIFCVEPR
VSLEYLLSVV HTKTYVVVNS EKVYNDLAAP KPPTGLTYSH EGWRGIIRNA KSFGFTCFIC
TDQSANAKLL KGRGVDLTKK TQTVDGVKYY LYSSKDPLTD IITAANACKG ICAMPIGYVT
HGLDLAQAGQ QVKKITVPYV CLLASKDQVP ILNSDVAVQT PEQSFINTVI ANGGYHCWHL
VTGELIVKGV SYRKLLNWSD QTICYADNKF YVVKGQIALP FDSLEKCRTY LTSRAAQQKN
VDVLVTIDGV NFRTVVLNNT TTYRVQLGSV FYKGSDISDT IPTEKMSGEA VYLADNLSEA
EKAVLSEVYG TADTAFLHRY YSLLALVKKW KYTVHDGVKS LKLNSNNCYV NVTMLMLDML
KEIKFIVPAL QAAYLKHKGG DSTEFIALIM AYGDCTYGEP DDASRLLHTI LSKAELTTQA
KMVWRQWCNV CGVQDTTTTG LKACIYVGMN SLDELHATHE ECCQCGDVRK RQLVEHNAPW
LLLSGLNEAK VMTPTSQSAG PDYTAFNVFQ GVETSVGHYL HVRVKDNLLY KYDSGSLSKT
SDMKCKMTDV YYPKQRYSAD CNVVVYSLDG NTWADVDPDL SAFYMKDGKY FTKKPVIEYS
PATILSGSVY TNSCLVGHDG TIGSDAISSS FNNLLGFDNS KPVSKKLTYS FFPDFEGDVI
LTEYSTYDPI YKNGAMLHGK PILWVNNSKF DSALNKFNRA TLRQVYDIAP VTLENKYTVL
QDNQIQQVEV EAPKEDAKPQ SPVQVAEDID NKLPIIKCKG LKKPFVKDGY SFVNDPQGVN
VIDTLGIDDL RALYVDRNLR LIVLKENNWS ALFNIHTVEK GDLSVIAASG SITRRVKILL
GASSLFAQFA SVTVNVTTAM GKALGRMTRN VITNTGIIGQ GFALLKMLLI LPFTFWKSKN
QSTVKVEVGA LRTAGIVTTN VVKQCASAAY DVLVVKFKRI DWKSTLRLLF LICTTGLLLS
SLYYLFLFHQ VLTSDVMLDG AEGMLATYRE LRSYLGIHSL CDGMVEAYRN VSYDVNDFCS
NRSALCNWCL IGQDSLTRYS AFQMIQTHVT SYVINIDWVW FVMEFALAYV LYTSTFNVLL
LVVSSQYFFS YTGAFVNWRS YNYLVSGYFF CVTHIPLLGL VRIYNFLACL WFLRRFYNHV
INGCKDTACL LCYKRNRLTR VEASTVVCGS KRTFYIVANG GTSFCCRHNW NCVDCDTAGI
GNTFICEEVA NDLTTSLRRL VKPTDKSHYY VESVTVKDSV VQLHYSREGA SCYERYPLCY
FTNLDKLKFK EVCKTPTGIP EHNFLIYDSS DRGQENLARS ACVYYSQVLS KPMLLVDSNM
VTTVGDSREI ASKMLDSYVN SFISLFGVNR DKLDKLVATA RDCVKRGDDF QTVIKTFTDA
ARGPAGVESD VETSSIVDAL QYAYKHDLQL TTEGFNNYVP SYIKPDSVAT ADLGCLIDLN
AASVNQTSIR NANGACIWNS SDYMKLSDSL KRQIRIACRK CNIPFRLTTS RLRSADNILS
VKFSATKLSG GAPKWLLKLR DFTWKSYCVV TLVVFAMAVL SYLCLPAFNM SQVSFHEDRI
LTYKVVENGI IRDITPSDTC FANKYQSFSK WFNEHYGGLF NNDISCPVTV AVIAGVAGAR
VPNLPANVAW VGRQIVLFVS RVFASSNNVC YTPTAEIPYE RFSDSGCVLA SECTLFRDAE
GKINPYCYDP TVLPGASAYD QMKPHVRYDM YDSDMYIKFP EVVFESTLRI TKTLATRYCR
FGSCEDANEG VCITTNGSWA IYNDHYANKP GVYCGDNYFD IVRRLGLSLF QPVTYFQLST
SLALGVMLCI FLTIAFYYVN KVKRALADYT QCAVVAVAAA LLNSLCLCFV VSNPLLVLPY
TALYYYATFY LTGEPAFVMH VSWFVMFGTV VPIWMVFAYI VGVCLRHLLW VMAYFSKKHV
EVFTDGKLNC SFQDAAANIF VINKDTYVAL RNSITQDSYN RYLSMFNKYK YYSGAMDTAS
YREASAAHLC KALQVYSETG SDVLFQPPNC SVTSSVLQSG LVKMAAPSGV VENCMVQVTC
GSMTLNGLWL DNYVWCPRHV MCPADQLSDP NYDALLVSKT NLSFIVQKNV GAPANLRVVG
HTMVGTLLKL TVESANPQTP AYTFTTVKPG ASFSVLACYN GRPTGVFMVN MRQNSTIKGS
FLCGSCGSVG YTQEGNVINF CYMHQMELSN GTHTGCAFDG VMYGAFEDRQ VHQVQLSDKY
CTINIVAWLY AAILNGCNWF VKPNKTGIAT FNEWAMSNQF TEFIGTQSVD MLAHKTGVSV
EQLLYAIQTL HKGFQGKTIL GNSMLEDEFT PDDVNMQVMG VVMQSGVKRI SYGLVHWLFT
TLLLAYVATL QLTKFTIWNY LFEVIPLQLT PLVLCVMACV MLTVKHKHTF LTLFLLPTAI
CLTYANIVYE PQTPVSSALI AVANWLNPAS VYMRTTHTDL GVYLSLCFAL AVVVRRLYRP
NASNLALALG SAMVWFYTYT TGDCSSPLTY LMFLTTLTSD YTVTVFLAVN VAKFFARVVF
LYAPHAGFIF PEVKLVLLMY LAVGYFCTVY FGVFSLLNLK LRVPLGVYDY TVSTQEFRYL
TGNGLHAPRN SWEALRLNMK LIGIGGTPCI KIASVQSKLT DLKCTSVVLL SVLQQLHLEA
NSKAWAHCVK LHNDILAATD PTEAFDNFVC LFATLMSFSA NVDLEALASD LLDHPSVLQA
TLSEFSHLAS YAELEAAQSS YQKALNSGDA SPQVLKALQK AVNIAKNAYE KDKAVARKLE
RMAEQAMTSM YKQARAEDKK AKIVSAMQTM LFGMIKKLDN DVLNGVISNA RNGCVPLSVV
PLCASNKLRV VIPDITIWNK VVTWPSLSYA GALWDISLIN NVDGEVVKSS DVTETNESLT
WPLVLECTRA ASSAVTLQNN EIRPSGLKTM VVSAGIDHAN CNTSSLAYYE PVEGRKMLMG
ILSENAHLKW AKVEGRDGFV NIELQPPCKF LIAGPKGPEV RYLYFVKNLN NLHRGQLLGH
IAATVRLQAG SNTEFAINSS VLSAVTFSVD PGKAYLDFVN AGGAPLTNCV KMLTPKTGTG
IAVSVKPEAN ADQDTYGGAS VCLYCRAHIE HPDVTGVCKF KGKFVQVPLH IRDPVGFCLQ
NTPCNVCQFW IGHGCNCDAL RGTTIPQSKD SNFLNRVRGS IVNARIEPCA SGLTTDVVFR
AFDICNYKAK VAGIGKYYKT NTCRFVEVDD EGHRLDSFFV VKRHTMENYE LEKRCYDLVK
DCDAVAVHDF FIFDVDKVKT PHIVRQRLTE YTMMDLVYAL RHFDQNNCEV LKSILVKYGC
CDASYFDNKL WFDFVENPNV ISVYHKLGER IRQAVLNTVK FCDQMVKSGL VGVLTLDNQD
LNGKWYDFGD FVITQPGAGV AIVDSYYSYL MPVLSMTNCL AAETHRDCDL TKPLIEWPLL
EYDYTDYKIG LFEKYFKXWD QQYHPNCVNC TDDRCVLHCA NFNVLFSMTL PGTSFGPIVR
KIFVDGVPFV ISCGYHYKEL GLVMNMDVSL HRHRLSLKEL MMYAADPAMH IASASALWDL
RTPCFSVAAL TTGLTFQTVR PGNFNKDFYD FVVSKGFFKE GSSVTLRHFF FAQDGHAAIT
DYSYYAYNLP TMCDIKQMLF CMEVVDRYFE IYDGGCLNAS EVIVNNLDKS AGHPFNKFGK
ARVYYESLSY QEQDELFAMT KRNVLPTITQ MNLKYAISAK NRARTVAGVS ILSTMTNRQY
HQKMLKSMAA TRGSTCVIGT TKFYGGWDFM LKTLYKDVDN PHLMGWDYPK CDRAMPNMCR
IFASLILARK HSTCCTNTDR FYRLANECAQ VLSEYVLCGG GYYVKPGGTS SGDATTAYAN
SVFNILQATT ANVSALMGAN GNTIVDEEVK DMQFELYVNV YRKSQPDPKF VDRYYAFLNK
HFSMMILSDD GVVCYNSDYA TKGYIASIQN FKETLYYQNN VFMSEAKCWV ETDLKKGPHE
FCSQHTLFIK DGDDGYFLPY PDPSRILSAG CFVDDIVKTD GTLMVERFVS LAIDAYPLTK
HDDPEYQNVF WVYLQYIEKL YKDLTGHMLD SYSVMLCGDN SAKFWEESFY RDLYTAPTTL
QAVGSCVVCH SQTSLRCGTC IRRPFLCCKC CYDHVIATPH KMVLSVSPYV CNAPGCDVAD
VTKLYLGGMS YFCIDHRPVC SFPLCANGLV FGLYKNMCTG SPSVTEFNRL ATCDWTESGD
YTLANTTTEP LKLFAAETLR ATEEASKQSY AIATIKEIVG ERELLLVWEA GKAKPPLNRN
YVFTGYHITK NSKVQLGEYV FERIDYSDAV SYKSSTTYKL AVGDIFVLTS HSVATLQAPT
IVNQERYVKI TGLYPTLTVP EEFANHVANF QKAGFSKFVT VQGPPGTGKS HFAIGLAIYY
PTARVVYTAC SHAAVDALCE KAFKYLNIAK CSRIIPAKAR VECYDQFKVN ETNSQYLFST
INALPETSAD ILVVDEVSMC TNYDLSVINA RIKAKHIVYV GDPAQLPAPR TLLTRGTLEP
ENFNSVTRLM CNLGPDIFLS VCYRCPEEIV NTVSALVYNN KLVAKKPASG QCFKILYKGS
VTHDASSAIN RPQLNFVKSF IAANPNWSKA VFISPYNSQN AVARSVLGLT TQTVDSSQGS
EYPYVIFCQT ADTAHANNIN RFNVAVTRAQ KGILCVMTSQ ALFDSLEFAE VSLNNYKLQS
QIVTGLYKDC SRESSGLHPA YAPTYVSVDD KYKTSDELCV NLNVPANVPY SRVISRMGFK
LDASIPNYPK LFITRDEAIR QVRSWIGFDV EGAHASRNAC GTNVPLQLGF STGVNFVVQP
VGVVDTEWGS MLTSIAARPP PGEQFKHLVP LMNKGAAWPI VRRRIVQMLS DTLDKLSDYC
TFVCWAHGFE LTSASYFCKI GKEQRCCMCN RRASTYSSPL HSYACWSHSS GYDYVYNPFF
VDVQQWGYIG NLATNHDRYC SVHQGAHVAS NDAVMTRCLA IHDCFIERVE WDITYPYISH
EKRLNSCCRA VERNVVRAAL LAGRFERVYD IGNPKGIPIV DDPVVDWHYY DAQPLSKKVQ
QLFYTEDCAK NFSDGLCLFW NCNVPRYPNN AIVCRFDTRV HSEFNLPGCD GGSLYVNKHA
FHTPAYDASA FRDLKPLPFF YYSTTPCEVH GNGNMLEDID YVPLKSAVCI TACNLGGAVC
RKHAAEYRDY MEAYNLVSAS GFRLWCYKTF DVYNLWSTFT KIQGLENIAY NVIKQGHFTG
VEGELPVAVV NDKIYTKSDV NDVCIFENKT TLPTNIAFEL YAKRAVRSHP DFNLLRNLEV
DVCYKFVLWD YERSNIYGSA TIGVCKYTDI DVNSALNICF DIRDNGSLER FMSLPNGILI
SDRKVKNYPC IVSSNYAYFN GTLIRDNTGN SQSSDGEVKQ PVTFYIYKKV NNEFVQFTDT
YYTLGRTVSD FTPVSEMEKD FLALDSDVFI KKYKLEAYAF EHVVYGDFSR TTLGGLHLLI
GLYKKHQEGH IIMEEMLKER ATVHNYFVTE SNTASFKAVC SVIDLKLDDF VDIIKAMDLS
VVSKVVKIPI DLTMIEFMLW CKDGQVQTFY PRLQAINDWK PGLAMPSLFK VQNSNLEPCM
LPNYKQSIPM PQGVHMNIAK YMQLCQYLNT CTIAVPANMR VMHFGAGSDK GVAPGSSVLR
QWLPTDAILI DNDLNEYVSD ADITLFGDCV TVRVGQQVDL LISDMYDPST KVVGETNEAK
ALFFVYLCNF IKNNLALGGS VAIKITEHSW SAELYELMGR FAWWTVFCTN ANASSSEGFL
IGINYLGELK EVIDGNVMHA NYIFWRNTTL MNLSTYSLFD LSRFPLKLKG TPVLQLKESQ
INELVISLLS QGKLIIRDND TLSVSTDVLV NFYRKPHKRS KC


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