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 R1AB_BC133              Reviewed;        7126 AA.
P0C6W1; Q0Q4F3;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-OCT-2017, entry version 76.
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 133/2005 (BtCoV) (BtCoV/133/2005).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=389230;
NCBI_TaxID=258959; Tylonycteris pachypus (Lesser bamboo 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).
[2]
FUNCTION OF NSP1.
PubMed=19264783; DOI=10.1128/JVI.02485-08;
Tohya Y., Narayanan K., Kamitani W., Huang C., Lokugamage K.,
Makino S.;
"Suppression of host gene expression by nsp1 proteins of group 2 bat
coronaviruses.";
J. Virol. 83:5282-5288(2009).
-!- 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,
ECO:0000269|PubMed:19264783}.
-!- 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: 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: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- 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=P0C6W1-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6F7-1; 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; DQ648794; ABG47051.1; -; Genomic_RNA.
ProteinModelPortal; P0C6W1; -.
SMR; P0C6W1; -.
PRIDE; P0C6W1; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000007449; 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; 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; 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; 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_0000290273.
CHAIN 196 847 Non-structural protein 2.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290274.
CHAIN 848 2791 Papain-like proteinase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290275.
CHAIN 2792 3298 Non-structural protein 4.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290276.
CHAIN 3299 3604 3C-like proteinase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290277.
CHAIN 3605 3896 Non-structural protein 6.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290278.
CHAIN 3897 3979 Non-structural protein 7.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290279.
CHAIN 3980 4178 Non-structural protein 8.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290280.
CHAIN 4179 4288 Non-structural protein 9.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290281.
CHAIN 4289 4427 Non-structural protein 10.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290282.
CHAIN 4428 5361 RNA-directed RNA polymerase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290283.
CHAIN 5362 5959 Helicase. {ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290284.
CHAIN 5960 6482 Guanine-N7 methyltransferase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290285.
CHAIN 6483 6824 Uridylate-specific endoribonuclease.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290286.
CHAIN 6825 7126 2'-O-methyltransferase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000290287.
TRANSMEM 2119 2139 Helical. {ECO:0000255}.
TRANSMEM 2152 2172 Helical. {ECO:0000255}.
TRANSMEM 2229 2249 Helical. {ECO:0000255}.
TRANSMEM 2333 2353 Helical. {ECO:0000255}.
TRANSMEM 2357 2377 Helical. {ECO:0000255}.
TRANSMEM 2382 2402 Helical. {ECO:0000255}.
TRANSMEM 2807 2827 Helical. {ECO:0000255}.
TRANSMEM 3079 3099 Helical. {ECO:0000255}.
TRANSMEM 3112 3132 Helical. {ECO:0000255}.
TRANSMEM 3156 3176 Helical. {ECO:0000255}.
TRANSMEM 3610 3630 Helical. {ECO:0000255}.
TRANSMEM 3644 3664 Helical. {ECO:0000255}.
TRANSMEM 3669 3689 Helical. {ECO:0000255}.
TRANSMEM 3714 3734 Helical. {ECO:0000255}.
TRANSMEM 3742 3762 Helical. {ECO:0000255}.
TRANSMEM 3791 3811 Helical. {ECO:0000255}.
TRANSMEM 3815 3835 Helical. {ECO:0000255}.
DOMAIN 1159 1328 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1600 1871 Peptidase C16. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3299 3604 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
DOMAIN 5041 5203 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 5362 5445 CV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
DOMAIN 5618 5799 (+)RNA virus helicase ATP-binding.
DOMAIN 5800 5974 (+)RNA virus helicase C-terminal.
ZN_FING 1721 1758 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4362 4378 {ECO:0000250}.
ZN_FING 4404 4417 {ECO:0000250}.
NP_BIND 5643 5650 ATP. {ECO:0000255}.
REGION 2119 2402 HD1. {ECO:0000250}.
REGION 2807 3176 HD2. {ECO:0000250}.
REGION 3610 3835 HD3. {ECO:0000250}.
COMPBIAS 960 1059 Glu-rich.
COMPBIAS 5366 5391 Cys-rich.
ACT_SITE 1641 1641 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1807 1807 For PL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3339 3339 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3446 3446 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
METAL 5366 5366 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5369 5369 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5377 5377 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5380 5380 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5387 5387 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5390 5390 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5394 5394 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5400 5400 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5411 5411 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5416 5416 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5433 5433 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5436 5436 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
SITE 195 196 Cleavage. {ECO:0000255}.
SITE 847 848 Cleavage; by PL-PRO. {ECO:0000255}.
SITE 2791 2792 Cleavage; by PL-PRO. {ECO:0000255}.
SITE 3298 3299 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 3604 3605 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 3896 3897 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 3979 3980 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4178 4179 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4288 4289 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 4427 4428 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 5361 5362 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 5959 5960 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 6482 6483 Cleavage; by 3CL-PRO. {ECO:0000255}.
SITE 6824 6825 Cleavage; by 3CL-PRO. {ECO:0000255}.
SEQUENCE 7126 AA; 795781 MW; 23A0EB77D0CFD96F CRC64;
MLSKAGVTTQ GARGKYRAEL YNEKRSDHVA CTVPLCDTED MASKLTPWFE DGETAFNQVS
SILKEKGKIL FVPMHMQRAM KFLPGPRVYL VERLTGGMLS KHFLVNQLAY KDHVGAAMMR
TTLNVKPLGM FFPYDSSLET GEHTFLLRKN GLGGQLFRER PWDRKETPYV EILDDLEADP
TGKYSQNLLK KLIGGDCIPV DQYMCGKNGK PIADYAKIVA KEGLTTLADI EVDVKSRMDS
DRFIVLNKKL YRVVWNVTRR NVPYSKQTAF TVVSVIQCDD KESVPEHTFT IGSQILMVSP
LKATNNKNFN LKQRLLHTFY GKEAVQQPGY IYHSAYVDCN ACGRGTWCTG NAIQGFACDC
GANYSANDVD LQSSGLVPKN ALFLANCPCA NNGACSHNAA QVYSILDGKA CVEVGGKSFT
LTFGGVVYAY MGCCDGTMYF VPRAKSCVSR IGDAIFTGCT GTWDKVVETA NLFLEKAQHS
LNFCQQFALT EVVLAILSGT TSTFEELRDL CHNASYEKVR DHLVNHGFVV TIGDYIRDAI
NIGANGVCNA TINAPFIAFT GLGESFKKVA AIPWKICSNL KSALDYYCSN IMFRVFPYDI
PCDVNDFVEL LLDCGKLTVA TSYFVLRYLD EKFDTVLGTV SNACQTALSS FLNACVAASR
ATAGFISDMF KLFKVLMHKL YVYTSCGYVA VAEHSSKIVQ QVLDIMSKAM KLLHTNVSWA
GTKLSAIIYE GREALLFNSG TYFCLSTKAK TLQDQMNLVL PGDYNKKTLG ILDPVPNADT
IDVTANSTVV DVVHGQLEPT NEHGPSMIVG NYVLVSDKLF VRTDDEEFYP LCINGKVVST
LFRLKGGMPS KKVTFGDVNT VEVTAYRSVS ITYDIHPVLD ALLSSSKLAT FTVEKDLLVE
DFVDVIKDEV LTLLTPLLRG YDIDGFDVED FIDVPCYVYN QDGDCAWSSN MTFSINPVED
VEEVEEFIED DYLSDELPIA DDEEAWTRAV EEVMPLDDIL VAEIELEEDL PLETALESVE
AEVGESISDE LCVVETAKAQ EPSVESTDST PSTSTVVSEN DLSVKPMSRV AETGDVLEVE
TAVVGGPVSD VTASVVTNDI VSVEQAQQCG VSSLPIQDEA SENQVHQVPD LQCTSETKVE
IVQPRQDLRP RRLRKSKVDL SKYKHTVINN SVTLVLGDAI QIASLLPKCV LVNAANRHLK
HGGGIAGAIN KASGGDVQEE SDEYISNSGP LHVGDSVLLK GYGLADAILR VVGPDARNNE
DAALLKRCYK TFNKHTIVVT PLISSGIFSV DPKVSFEYLL ANVTTTTYVV VNNEDIYNTL
ATPSKPDGLV YSFEGWRGTV RTAKNYGFTC FICTEYSANV KFLRTKGVDT TKKIQTVDGV
SYYLYSARDA LTDVIAAANG CPGICAMPFG YVTHGLDLAQ SGNYVRQVKV PYVCLLASKE
QIPIMNSDVA IQTPETAFIN NVTSNGGYHS WHLVSGDLIV KDVCYKKLLH WSGQTICYAD
NKFYVVKNDV ALPFSDLEAC RAYLTSRAAQ QVNIEVLVTI DGVNFRTVIL NDATTFRKQL
GATFYKGVDI SDALPTVKMG GESLFVADNL SESEEVVLKE YYGTSDVTFL QRYYSLQPLV
QQWKFVVHDG VKSLKLSNYN CYINATIMMI DMLHDIKFVV PALQNAYLRY KGGDPYDFLA
LIMAYGDCTF DNPDDEAKLL HTLLAKAELT VSAKMVWREW CTVCGIRDIE YTGMRACVYA
GVNSMEELQS VFNETCVCGS VKHRQLVEHS TPWLLVSGLN EVKVSTSTDP VYRAFNVFQG
VETSVGHYVH VRVKDGLFYK YDSGSLTKTS DMKCKMTSVW YPKVRYTADC NVVVYDLDGV
TKVEVNPDLS NYYMKDGKYY TSKPTIKYSP ATILPGSVYS NSCLVGVDGT PGSDTISKFF
NDLLGFDETK PISKKLTYSL LPNEDGDVLL SEFNNYNPVY KKGVMLKGKP ILWVNNGVCD
SALNKPNRAS LRQLYDVAPI VLDNKYTVLQ DNTSQLIEPN VPVVEDVSIT TRKLIEVKCK
GLNKPFVKGN FSFVNDPNGV TVVDTLGLTE LRALYVDINT RYIVLRDNNW SSLFKLHTVE
SGDLQIVANG GSVTRRARVL LGASSLFASF AKITVTATTA ACKTAGRSFC KFVVNYGVLQ
NMFLFLKMLF FLPFNYLWPK KQPTVDVGVS GLRTAGVVTT NIVKQCGTAA YYMLLGKFKR
VDWKATLRLF LLLCTTILLL SSIYHLVIFN QVLSSDVMLE DATGILAMYK EVRSYLGIRT
LCDGLAVEYR NTSFDVVDFC SNRSVLCQWC LIGQDSLTRY SALQMLQTHI TSYVLNIDWI
WFALEFFLAY VLYTSSFNVL LLVVTAQYFF AYTSAFVNWR AYNYIVSGLF FLVTHIPLHG
LVRVYNFLAC LWFLRKFYSH VINGCKDTAC LLCYKRNRLT RVEASTIVCG TKRTFYIAAN
GGTSYCCKHN WNCVECDTAG VGNTFICTEV ANDLTTTLRR LIKPTDQSHY YVDSVVVKDA
VVELHYNRDG SSCYERYPLC YFTNLEKLKF KEVCKTPTGI PEHNFLIYDT NDRGQENLAR
SACVYYSQVL CKPMLLVDVN LVTTVGDSRE IAIKMLDSFI NSFISLFSVS RDKLEKLINT
ARDCVRRGDD FQTVLKTFTD AARGHAGVES DVETTMVVDA LQYAHKNDIQ LTTECYNNYV
PGYIKPDSIN TLDLGCLIDL KAASVNQTSM RNANGACVWN SGDYMKLSDS FKRQIRIACR
KCNIPFRLTT SKLRAADNIL SVKFSATKIV GGAPSWLLRV RDLTVKGYCI LTLFVFTVAV
LSWFCLPSYS IATVNFNDDR ILTYKVIENG IVRDIAPNDA CFANKYGHFS KWFNENHGGV
YRNSVDCPIT IAVIAGVAGA RVANVPATLA WVGRQIVLFV SRVFANTNVC FTPTNEIPYD
TFSDSGCVLS SECTLFRDAE GNLNPFCYDP TVLPGASSYA DMKPHVRYDM YDSDMYIKFP
EVIFESTLRI TKTLATQYCR FGSCEESAAG VCISTNGSWA LYNQNYSTRP GIYCGDDYFD
IVRRLAVSLF QPVTYFQLST SLAMGLVLCV FLTAAFYYIN KVKRALADYT QCAVVAVVAA
LLNSLCLCFI VANPLLVAPY TAMYYYATFY LTGEPAFIMH ISWYVMFGTV VPIWMLASYT
VGVMLRHLFW VLAYFSKKHV DVFTDGKLNC SFQDAASNIF VIGKDTYVAL RNAITQDSFV
RYLSLFNKYK YYSGAMDTAS YREACAAHLC KALQTYSETG SDILYQPPNC SVTSSVLQSG
LVKMSAPSGA VENCIVQVTC GSMTLNGLWL DNTVWCPRHI MCPADQLTDP NYDALLISKT
NHSFIVQKHI GAQANLRVVA HSMVGVLLKL TVDVANPSTP AYTFSTVKPG ASFSVLACYN
GKPTGVFTVN LRHNSTIKGS FLCGSCGSVG YTENGGVLNF VYMHQMELSN GTHTGSSFDG
VMYGAFEDKQ THQLQLTDKY CTINVVAWLY AAVLNGCKWF VKPTRVGIVT YNEWALSNQF
TEFVGTQSID MLAHRTGVSV EQMLAAIQSL HAGFQGKTIL GQSTLEDEFT PDDVNMQVMG
VVMQSGVKRI SYGFMHWLMS TLVLAYVSVM QLTKFTMWTY LFETIPTQMT PLLFGFMACV
MFTVKHKHTF LSLFLLPVAL CLTYANIVYE PQTLVSSTLI AVANWLTPTS VYMRTTHLDF
GLYISLSFVL AIIVRRLYRP SMSNLALALC SGVMWFYTYV IGDHSSPITY LMFITTLTSD
YTITVFATVN LAKFISGLVF LYAPHLGFIL PEVKLVLLIY LCLGYMCTMY FGVFSLLNLK
LRVPLGVYDY SVSTQEFRFL TGNGLHAPRN SWEALILNFK LLGIGGTPCI KVATVQSKLT
DLKCTSVVLL TVLQQLHLES NSKAWSYCVK LHNEILAAVD PTEAFERFVC LFATLMSFSA
NVDLDALAND LFENSSVLQA TLTEFSHLAT YAELETAQSS YQKALNSGDA SPQVLKALQK
AVNVAKNAYE KDKAVARKLE RMAEQAMTSM YKQARAEDKK AKIVSAMQTM LFGMIKKLDN
DVLNGVIANA RNGCVPLSIV PLCASNKLRV VIPDISVWNK VVNWPSVSYA GSLWDVTVIN
NVDNEVVKPT DVVETNESLT WPLVIECSRA SSSAVKLQNN EIHPKGLKTM VVTAGIDQVN
CSSSAVAYYE PVQGHRMVMG LLSENAHLKW AKVEGKDGFI NIELQPPCKF LIAGPKGPEI
RYLYFVKNLN NLHRGQLLGH IAATVRLQAG ANTEFASNST VLTLVAFAVD PAKAYLDYVG
SGGTPLSNYV KMLAPKTGTG VAISVKPEAT ADQETYGGAS VCLYCRAHIE HPDVSGVCKY
KTRFVQIPAH VRDPVGFLLK NVPCNVCQYW VGYGCNCDAL RNNTVPQSKD TNFLNRVRGS
SVNARLEPCS SGLTTDVVYR AFDICNFKAR VAGIGKYYKT NTCRFVQVDD EGHKLDSYFI
VKRHTMSNYE LEKRCYDLLK DCDAVAIHDF FIFDVDKTKT PHIVRQSLTE YTMMDLVYAL
RHFDQNNCEV LKSILVKYGC CEQSYFDNKL WFDFVENPSV IGVYHKLGER IRQAMLNTVK
MCDHMVKSGL VGVLTLDNQD LNGKWYDFGD FVITQPGAGV AIVDSYYSYL MPVLSMTNCL
AAETHKDCDF NKPLIEWLLL EYDYTDYKIG LFNKYFKHWD QTYHPNCVNC GDDRCILHCA
NFNVLFSMVL PNTSFGPIVR KIFVDGVPFI VSCGYHYKEL GLVMNMDVNI HRHRLALKEL
MMYAADPAMH IASASALWDL RTPCFSVAAL TTGLTFQTVR PGNFNKDFYD FVVSRGFFKE
GSSVTLKHFF FAQDGHAAIT DYSYYAYNLP TMVDIKQMLF CMEVVDKYFD IYDGGCLNAS
EVIVNNLDKS AGHPFNKFGK ARVYYESMSY QEQDELFAVT KRNVLPTITQ MNLKYAISAK
NRARTVAGVS ILSTMTNRQY HQKMLKSMAA TRGATCVIGT TKFYGGWDFM LKTLYKDVES
PHLMGWDYPK CDRAMPNMCR ILASLILARK HSTCCTNSDR FYRLANECAQ VLSEYVLCGG
GYYVKPGGTS SGDATTAYAN SVFNILQATT ANVSALMSAN GNTIIDREIK DMQFDLYINV
YRKVVPDPKF VDKYYAFLNK HFSMMILSDD GVVCYNSDYA AKGYVASIQN FKETLYYQNN
VFMSEAKCWV ETNLEKGPHE FCSQHTLYIK DGDDGYFLPY PDPSRILSAG CFVDDIVKTD
GTVMMERYVS LAIDAYPLTK HDDTEYQNVF WVYLQYIEKL YKDLTGHMLD SYSVMLCGDD
SAKFWEEGFY RDLYSSPTTL QAVGSCVVCH SQTSLRCGTC IRRPFLCCKC CYDHVIATTH
KMVLSVSPYV CNAPGCDVSD VTKLYLGGMS YYCNDHRPVC SFPLCANGLV FGLYKNMCTG
SSSIMEFNRL ATCDWSDSGD YTLANTTTEP LKLFAAETLR ATEEASKQSY AIATIKEIVG
ERELILVWEV GKSKPPLNRN YVFTGYHLTK NSKVQLGEYV FERIDYSDAV SYKSSTTYKL
AVGDIFVLTS HSVATLSAPT IVNQERYLKI TGIYPTITVP EEFANHVVNF QKAGFSKYVT
VQGPPGTGKS HFAIGLAIYY PTARIVYTAC SHAAVDALCA KAFKYLNIAK CSRIIPAKAR
VECYDRFKVN DTNAQYLFST VNALPEISVD ILVVDEVSMC TNYDLSIINS RVKAKHIVYV
GDPAQLPAPR TLLTRGTLEP ENFNSVTRLM CNLGPDIFLS VCYRCPKEIV NTVSALVYNN
KLSAKKDASG QCFKILFKGS VTHDASSAIN RPQLNFVKTF IAANPNWSKA VFISPYNSQN
AVARSMLGLT TQTVDSSQGS EYPYVIFCQT ADTAHANNLN RFNVAVTRAQ KGILCVMTSQ
VLFDSLEFAE LSLNNYKLQS QIVTGLFKDC SREDVGLPPA YAPTYLSVDA KYKTTDELCV
NLNITPNVTY SRVISRMGFK LDATIPGYPK LFITRDEAIR QVRSWIGFDV EGAHASRNAC
GTNVPLQLGF STGVNFVVQP VGVVDTEWGS MLTTISARPP PGEQFKHLVP LMNKGATWPI
VRRRIVQMLS DTLDKLSDYC TFVCWAHGFE LTSASYFCKI GKEQRCCMCS RRASTFSSPL
QSYACWSHSS GYDYVYNPFF VDVQQWGYVG NLATNHDRYC GIHAGAHVAS SDAIMTRCLA
IYDCFIERVD WDVTYPYISH EQKLNSCCRT VERNVVRSAV LSGKFDKIYD IGNPKGIPII
SEPVEWHFYD AQPLSNKVKK LFYTDDVAKQ FEDGLCLFWN CNVSKYPSNA VVCRFDTRVH
SEFNLPGCNG GSLYVNKHAF HTPAYDINAF RDLKPLPFFY YSTTPCEVHG SGNMLEDIDY
VPLKSAVCIT ACNLGGAVCR KHAAEYRDYM EAYNIVSAAG FRLWVYKTFD IYNLWSTFVK
VQGLENIAFN VIKQGHFTGV DGELPVAVVN DKIFTKNGTD DVCIFKNETA LPTNVAFELY
AKRAVRSHPD LNLLRNLEVD VCYNFVLWDY DRNNIYGTTT IGVCKYTDID VNPNLNMCFD
IRDKGSLERF MSMPNGVLIS DRKIKNYPCI IGPKHAYFNG AILRNIDAKQ PITFYLYKKV
NNEFVSFSDT FYTCGRTVND FTALTPMEED FLVLDSDVFI KKYSLEDYAF EHVVYGDFSH
TTLGGLHLLI GLYKKMRDGH ILMEEMLKDR ATVHNYFITD SNTASYKAVC SVIDLRLDDF
VNIIKEMDLD VVSKVVKVPI DLTMIEFMLW CKDGKVQTFY PRLQATNDWK PGLTMPSLFK
VQQMNLEPCL LANYKQSIPM PNGVHMNVAK YMQLCQYLNT CTLAVPANMR VIHFGAGCEK
GVAPGTSVLR QWLPLDAVLI DNDLNEFVSD ADITIFGDCV TVHVGQQVDL LISDMYDPCT
KAVGEVNQTK ALFFVYLCNF IKNNLALGGS VAIKITEHSW SADLYKIMGR FAYWTVFCTN
ANASSSEGFL IGINFLGELK EEIDGNVMHA NYIFWRNSTP MNLSTYSLFD LSRFPLKLKG
TPVLQLKESQ INELVISLLS QGKLLIRDND TLNVSTDVLV NFRKRL


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