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 R1AB_CVMA5              Reviewed;        7176 AA.
P0C6X9; O39225; O39226; P16342; P19750;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
25-OCT-2017, entry version 74.
RecName: Full=Replicase polyprotein 1ab;
Short=pp1ab;
AltName: Full=ORF1ab polyprotein;
Contains:
RecName: Full=Host translation inhibitor nsp1;
Short=nsp1;
AltName: Full=p28;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p65;
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;
AltName: Full=p210;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
AltName: Full=Peptide HD2;
AltName: Full=p44;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=M-PRO;
AltName: Full=nsp5;
AltName: Full=p27;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
AltName: Full=p10;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
AltName: Full=p22;
Contains:
RecName: Full=Non-structural protein 9;
Short=nsp9;
AltName: Full=p12;
Contains:
RecName: Full=Non-structural protein 10;
Short=nsp10;
AltName: Full=Growth factor-like peptide;
Short=GFL;
AltName: Full=p15;
Contains:
RecName: Full=RNA-directed RNA polymerase;
Short=Pol;
Short=RdRp;
EC=2.7.7.48;
AltName: Full=nsp12;
AltName: Full=p100;
Contains:
RecName: Full=Helicase;
Short=Hel;
EC=3.6.4.12;
EC=3.6.4.13;
AltName: Full=nsp13;
AltName: Full=p67;
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;
AltName: Full=p35;
Contains:
RecName: Full=2'-O-methyltransferase;
EC=2.1.1.-;
AltName: Full=nsp16;
Name=rep; ORFNames=1a-1b;
Murine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=11142;
NCBI_TaxID=10090; Mus musculus (Mouse).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] (ORF1B).
PubMed=2159623; DOI=10.1093/nar/18.7.1825;
Bredenbeek P.J., Pachuk C.J., Noten A.F.H., Charite J., Luytjes W.,
Weiss S.R., Spaan W.J.M.;
"The primary structure and expression of the second open reading frame
of the polymerase gene of the coronavirus MHV-A59; a highly conserved
polymerase is expressed by an efficient ribosomal frameshifting
mechanism.";
Nucleic Acids Res. 18:1825-1832(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] (ORF1A).
PubMed=8291254; DOI=10.1006/viro.1994.1088;
Bonilla P.J., Gorbalenya A.E., Weiss S.R.;
"Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a:
heterogeneity among MHV strains.";
Virology 198:736-740(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate C12 mutant;
PubMed=9426441; DOI=10.1006/viro.1997.8877;
Leparc-Goffart I., Hingley S.T., Chua M.M., Jiang X., Lavi E.,
Weiss S.R.;
"Altered pathogenesis of a mutant of the murine coronavirus MHV-A59 is
associated with a Q159L amino acid substitution in the spike
protein.";
Virology 239:1-10(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-597.
PubMed=2545027; DOI=10.1016/0042-6822(89)90520-5;
Pachuk C.J., Bredenbeek P.J., Zoltick P.W., Spaan W.J.M., Weiss S.R.;
"Molecular cloning of the gene encoding the putative polymerase of
mouse hepatitis coronavirus, strain A59.";
Virology 171:141-148(1989).
[5]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND CHARACTERIZATION OF NSP8.
PubMed=9499085;
Lu X.T., Sims A.C., Denison M.R.;
"Mouse hepatitis virus 3C-like protease cleaves a 22-kilodalton
protein from the open reading frame 1a polyprotein in virus-infected
cells and in vitro.";
J. Virol. 72:2265-2271(1998).
[6]
SUBCELLULAR LOCATION OF HELICASE.
PubMed=10400784;
Denison M.R., Spaan W.J.M., van der Meer Y., Gibson C.A., Sims A.C.,
Prentice E., Lu X.T.;
"The putative helicase of the coronavirus mouse hepatitis virus is
processed from the replicase gene polyprotein and localizes in
complexes that are active in viral RNA synthesis.";
J. Virol. 73:6862-6871(1999).
[7]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND MUTAGENESIS OF PHE-3331;
LEU-3332; GLN-3333; SER-3334; GLY-3335; ILE-3336; CYS-3478; LEU-5381;
GLN-5382 AND SER-5383.
PubMed=10544119; DOI=10.1006/viro.1999.9954;
Pinon J.D., Teng H., Weiss S.R.;
"Further requirements for cleavage by the murine coronavirus 3C-like
proteinase: identification of a cleavage site within ORF1b.";
Virology 263:471-484(1999).
[8]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND CHARACTERIZATION OF NSP7;
NSP9 AND NSP10.
PubMed=10708455; DOI=10.1128/JVI.74.7.3379-3387.2000;
Bost A.G., Carnahan R.H., Lu X.T., Denison M.R.;
"Four proteins processed from the replicase gene polyprotein of mouse
hepatitis virus colocalize in the cell periphery and adjacent to sites
of virion assembly.";
J. Virol. 74:3379-3387(2000).
-!- 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
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- 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.
-!- 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.
-!- 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.
-!- 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.
-!- 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:0000269|PubMed:10400784}.
-!- 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=P0C6X9-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6V0-1; 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.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=AAB86818.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAB86820.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAA36202.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; X51939; CAA36202.1; ALT_SEQ; Genomic_RNA.
EMBL; X73559; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AF029248; AAB86818.1; ALT_SEQ; Genomic_RNA.
EMBL; AF029248; AAB86820.1; ALT_SEQ; Genomic_RNA.
EMBL; M27198; AAA74011.1; -; Genomic_RNA.
PIR; A32440; A32440.
PIR; S15760; S15760.
RefSeq; NP_045299.1; NC_001846.1.
PDB; 2GTH; X-ray; 2.70 A; A=6504-6872.
PDB; 2GTI; X-ray; 2.15 A; A=6504-6872.
PDB; 3VC8; X-ray; 2.00 A; A/B=3245-3333.
PDB; 3VCB; X-ray; 2.40 A; A/B=3245-3333.
PDB; 4YPT; X-ray; 2.60 A; A=1525-1911.
PDBsum; 2GTH; -.
PDBsum; 2GTI; -.
PDBsum; 3VC8; -.
PDBsum; 3VCB; -.
PDBsum; 4YPT; -.
ProteinModelPortal; P0C6X9; -.
SMR; P0C6X9; -.
ELM; P0C6X9; -.
GeneID; 1489749; -.
OrthoDB; VOG09000000; -.
EvolutionaryTrace; P0C6X9; -.
Proteomes; UP000007192; Genome.
GO; GO:0039714; C:cytoplasmic viral factory; IDA:UniProtKB.
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; IPR022570; B-CoV_NSP1.
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; 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; IPR002705; Pept_C30/C16_B_coronavir.
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; PF11963; DUF3477; 2.
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; PF01831; Peptidase_C16; 1.
Pfam; PF05409; Peptidase_C30; 1.
Pfam; PF00680; RdRP_1; 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; 2.
PROSITE; PS51653; CV_ZBD; 1.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51124; PEPTIDASE_C16; 2.
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;
Reference proteome; 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 1 247 Host translation inhibitor nsp1.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037338.
CHAIN 248 832 Non-structural protein 2.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037339.
CHAIN 833 2837 Papain-like proteinase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037340.
CHAIN 2838 3333 Non-structural protein 4.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037341.
CHAIN 3334 3635 3C-like proteinase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037342.
CHAIN 3636 3921 Non-structural protein 6.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037343.
CHAIN 3922 4013 Non-structural protein 7.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037344.
CHAIN 4014 4207 Non-structural protein 8.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037345.
CHAIN 4208 4317 Non-structural protein 9.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037346.
CHAIN 4318 4454 Non-structural protein 10.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037347.
CHAIN 4455 5382 RNA-directed RNA polymerase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037348.
CHAIN 5383 5982 Helicase. {ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037349.
CHAIN 5983 6503 Guanine-N7 methyltransferase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037350.
CHAIN 6504 6877 Uridylate-specific endoribonuclease.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037351.
CHAIN 6878 7176 2'-O-methyltransferase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000037352.
TRANSMEM 2225 2245 Helical. {ECO:0000255}.
TRANSMEM 2286 2306 Helical. {ECO:0000255}.
TRANSMEM 2314 2334 Helical. {ECO:0000255}.
TRANSMEM 2400 2420 Helical. {ECO:0000255}.
TRANSMEM 2442 2462 Helical. {ECO:0000255}.
TRANSMEM 2625 2645 Helical. {ECO:0000255}.
TRANSMEM 2847 2867 Helical. {ECO:0000255}.
TRANSMEM 3096 3116 Helical. {ECO:0000255}.
TRANSMEM 3118 3138 Helical. {ECO:0000255}.
TRANSMEM 3150 3170 Helical. {ECO:0000255}.
TRANSMEM 3177 3197 Helical. {ECO:0000255}.
TRANSMEM 3202 3222 Helical. {ECO:0000255}.
TRANSMEM 3644 3664 Helical. {ECO:0000255}.
TRANSMEM 3674 3694 Helical. {ECO:0000255}.
TRANSMEM 3699 3719 Helical. {ECO:0000255}.
TRANSMEM 3742 3762 Helical. {ECO:0000255}.
TRANSMEM 3769 3789 Helical. {ECO:0000255}.
TRANSMEM 3796 3816 Helical. {ECO:0000255}.
TRANSMEM 3840 3860 Helical. {ECO:0000255}.
DOMAIN 1084 1333 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1323 1482 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1678 1937 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3334 3635 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
DOMAIN 5062 5224 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 5383 5466 CV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
DOMAIN 5638 5819 (+)RNA virus helicase ATP-binding.
DOMAIN 5820 5989 (+)RNA virus helicase C-terminal.
ZN_FING 1198 1226 C4-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 1794 1830 C4-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4391 4407 {ECO:0000250}.
ZN_FING 4433 4446 {ECO:0000250}.
NP_BIND 5663 5670 ATP. {ECO:0000250}.
REGION 2225 2645 HD1.
REGION 2847 3222 HD2.
REGION 3526 3860 HD3.
ACT_SITE 1121 1121 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1272 1272 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1716 1716 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1873 1873 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3374 3374 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3478 3478 For 3CL-PRO activity.
METAL 5387 5387 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5390 5390 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5398 5398 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5401 5401 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5408 5408 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5411 5411 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5415 5415 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5421 5421 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5432 5432 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5437 5437 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5454 5454 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5457 5457 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
SITE 247 248 Cleavage; by PL1-PRO. {ECO:0000305}.
SITE 832 833 Cleavage; by PL1-PRO. {ECO:0000305}.
SITE 2837 2838 Cleavage; by PL2-PRO.
SITE 3333 3334 Cleavage; by 3CL-PRO.
SITE 3635 3636 Cleavage; by 3CL-PRO.
SITE 3921 3922 Cleavage; by 3CL-PRO.
SITE 4013 4014 Cleavage; by 3CL-PRO.
SITE 4207 4208 Cleavage; by 3CL-PRO.
SITE 4317 4318 Cleavage; by 3CL-PRO.
SITE 4454 4455 Cleavage; by 3CL-PRO.
SITE 5382 5383 Cleavage; by 3CL-PRO.
SITE 5982 5983 Cleavage; by 3CL-PRO. {ECO:0000305}.
SITE 6503 6504 Cleavage; by 3CL-PRO. {ECO:0000305}.
SITE 6877 6878 Cleavage; by 3CL-PRO. {ECO:0000305}.
VARIANT 1699 1699 P -> S (in strain: Isolate C12 mutant).
VARIANT 2196 2196 M -> K (in strain: Isolate C12 mutant).
VARIANT 5773 5773 R -> S (in strain: Isolate C12 mutant).
MUTAGEN 3331 3331 F->A,H,W: No effect.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 3332 3332 L->I,S: No processing between peptide HD2
and 3CL-PRO.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 3333 3333 Q->A,K,R: No processing between peptide
HD2 and 3CL-PRO.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 3334 3334 S->A: No effect.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 3334 3334 S->C: No processing between peptide HD2
and 3CL-PRO.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 3335 3335 G->A: No effect.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 3335 3335 G->P: No processing between peptide HD2
and 3CL-PRO.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 3336 3336 I->L: No effect.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 3478 3478 C->A: Complete loss of 3CL-PRO activity.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 5381 5381 L->I: No processing between RDRP and
helicase. {ECO:0000269|PubMed:10544119}.
MUTAGEN 5381 5381 L->M: No effect.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 5382 5382 Q->K,R: No processing between RDRP and
helicase. {ECO:0000269|PubMed:10544119}.
MUTAGEN 5383 5383 S->A: No effect.
{ECO:0000269|PubMed:10544119}.
MUTAGEN 5383 5383 S->N: No processing between RDRP and
helicase. {ECO:0000269|PubMed:10544119}.
CONFLICT 287 288 WR -> CA (in Ref. 4). {ECO:0000305}.
CONFLICT 311 311 L -> V (in Ref. 4). {ECO:0000305}.
CONFLICT 570 570 D -> G (in Ref. 4). {ECO:0000305}.
CONFLICT 3620 3620 E -> EL (in Ref. 3). {ECO:0000305}.
CONFLICT 3711 3711 T -> TL (in Ref. 3). {ECO:0000305}.
CONFLICT 3968 3968 M -> V (in Ref. 3). {ECO:0000305}.
CONFLICT 4464 4464 I -> V (in Ref. 3). {ECO:0000305}.
CONFLICT 6156 6156 V -> A (in Ref. 3). {ECO:0000305}.
HELIX 1537 1545 {ECO:0000244|PDB:4YPT}.
STRAND 1556 1563 {ECO:0000244|PDB:4YPT}.
STRAND 1566 1574 {ECO:0000244|PDB:4YPT}.
TURN 1575 1577 {ECO:0000244|PDB:4YPT}.
STRAND 1578 1583 {ECO:0000244|PDB:4YPT}.
STRAND 1586 1591 {ECO:0000244|PDB:4YPT}.
STRAND 1594 1597 {ECO:0000244|PDB:4YPT}.
HELIX 1600 1607 {ECO:0000244|PDB:4YPT}.
STRAND 1610 1621 {ECO:0000244|PDB:4YPT}.
STRAND 1623 1628 {ECO:0000244|PDB:4YPT}.
HELIX 1633 1637 {ECO:0000244|PDB:4YPT}.
STRAND 1639 1642 {ECO:0000244|PDB:4YPT}.
HELIX 1654 1656 {ECO:0000244|PDB:4YPT}.
STRAND 1660 1663 {ECO:0000244|PDB:4YPT}.
HELIX 1669 1678 {ECO:0000244|PDB:4YPT}.
HELIX 1683 1695 {ECO:0000244|PDB:4YPT}.
STRAND 1700 1703 {ECO:0000244|PDB:4YPT}.
STRAND 1706 1709 {ECO:0000244|PDB:4YPT}.
HELIX 1716 1725 {ECO:0000244|PDB:4YPT}.
HELIX 1735 1745 {ECO:0000244|PDB:4YPT}.
HELIX 1750 1759 {ECO:0000244|PDB:4YPT}.
HELIX 1770 1780 {ECO:0000244|PDB:4YPT}.
STRAND 1787 1794 {ECO:0000244|PDB:4YPT}.
STRAND 1797 1804 {ECO:0000244|PDB:4YPT}.
HELIX 1806 1809 {ECO:0000244|PDB:4YPT}.
STRAND 1810 1813 {ECO:0000244|PDB:4YPT}.
HELIX 1817 1822 {ECO:0000244|PDB:4YPT}.
STRAND 1824 1828 {ECO:0000244|PDB:4YPT}.
STRAND 1831 1841 {ECO:0000244|PDB:4YPT}.
STRAND 1845 1852 {ECO:0000244|PDB:4YPT}.
STRAND 1861 1867 {ECO:0000244|PDB:4YPT}.
TURN 1869 1872 {ECO:0000244|PDB:4YPT}.
STRAND 1873 1878 {ECO:0000244|PDB:4YPT}.
STRAND 1880 1882 {ECO:0000244|PDB:4YPT}.
STRAND 1884 1887 {ECO:0000244|PDB:4YPT}.
STRAND 1890 1893 {ECO:0000244|PDB:4YPT}.
STRAND 1901 1906 {ECO:0000244|PDB:4YPT}.
HELIX 3246 3249 {ECO:0000244|PDB:3VC8}.
STRAND 3254 3256 {ECO:0000244|PDB:3VC8}.
HELIX 3258 3267 {ECO:0000244|PDB:3VC8}.
HELIX 3270 3278 {ECO:0000244|PDB:3VC8}.
HELIX 3280 3284 {ECO:0000244|PDB:3VC8}.
STRAND 3287 3290 {ECO:0000244|PDB:3VCB}.
HELIX 3292 3313 {ECO:0000244|PDB:3VC8}.
STRAND 3318 3320 {ECO:0000244|PDB:3VC8}.
STRAND 3326 3330 {ECO:0000244|PDB:3VCB}.
SEQUENCE 7176 AA; 802596 MW; AE90461FA631BED3 CRC64;
MAKMGKYGLG FKWAPEFPWM LPNASEKLGN PERSEEDGFC PSAAQEPKVK GKTLVNHVRV
NCSRLPALEC CVQSAIIRDI FVDEDPQKVE ASTMMALQFG SAVLVKPSKR LSIQAWTNLG
VLPKTAAMGL FKRVCLCNTR ECSCDAHVAF HLFTVQPDGV CLGNGRFIGW FVPVTAIPEY
AKQWLQPWSI LLRKGGNKGS VTSGHFRRAV TMPVYDFNVE DACEEVHLNP KGKYSCKAYA
LLKGYRGVKP ILFVDQYGCD YTGCLAKGLE DYGDLTLSEM KELFPVWRDS LDSEVLVAWH
VDRDPRAAMR LQTLATVRCI DYVGQPTEDV VDGDVVVREP AHLLAANAIV KRLPRLVETM
LYTDSSVTEF CYKTKLCECG FITQFGYVDC CGDTCDFRGW VAGNMMDGFP CPGCTKNYMP
WELEAQSSGV IPEGGVLFTQ STDTVNRESF KLYGHAVVPF GSAVYWSPCP GMWLPVIWSS
VKSYSGLTYT GVVGCKAIVQ ETDAICRSLY MDYVQHKCGN LEQRAILGLD DVYHRQLLVN
RGDYSLLLEN VDLFVKRRAE FACKFATCGD GLVPLLLDGL VPRSYYLIKS GQAFTSMMVN
FSHEVTDMCM DMALLFMHDV KVATKYVKKV TGKLAVRFKA LGVAVVRKIT EWFDLAVDIA
ASAAGWLCYQ LVNGLFAVAN GVITFVQEVP ELVKNFVDKF KAFFKVLIDS MSVSILSGLT
VVKTASNRVC LAGSKVYEVV QKSLSAYVMP VGCSEATCLV GEIEPAVFED DVVDVVKAPL
TYQGCCKPPT SFEKICIVDK LYMAKCGDQF YPVVVDNDTV GVLDQCWRFP CAGKKVEFND
KPKVRKIPST RKIKITFALD ATFDSVLSKA CSEFEVDKDV TLDELLDVVL DAVESTLSPC
KEHDVIGTKV CALLDRLAGD YVYLFDEGGD EVIAPRMYCS FSAPDDEDCV AADVVDADEN
QDDDAEDSAV LVADTQEEDG VAKGQVEADS EICVAHTGSQ EELAEPDAVG SQTPIASAEE
TEVGEASDRE GIAEAKATVC ADAVDACPDQ VEAFEIEKVE DSILDELQTE LNAPADKTYE
DVLAFDAVCS EALSAFYAVP SDETHFKVCG FYSPAIERTN CWLRSTLIVM QSLPLEFKDL
EMQKLWLSYK AGYDQCFVDK LVKSVPKSII LPQGGYVADF AYFFLSQCSF KAYANWRCLE
CDMELKLQGL DAMFFYGDVV SHMCKCGNSM TLLSADIPYT LHFGVRDDKF CAFYTPRKVF
RAACAVDVND CHSMAVVEGK QIDGKVVTKF IGDKFDFMVG YGMTFSMSPF ELAQLYGSCI
TPNVCFVKGD VIKVVRLVNA EVIVNPANGR MAHGAGVAGA IAEKAGSAFI KETSDMVKAQ
GVCQVGECYE SAGGKLCKKV LNIVGPDARG HGKQCYSLLE RAYQHINKCD NVVTTLISAG
IFSVPTDVSL TYLLGVVTKN VILVSNNQDD FDVIEKCQVT SVAGTKALSL QLAKNLCRDV
KFVTNACSSL FSESCFVSSY DVLQEVEALR HDIQLDDDAR VFVQANMDCL PTDWRLVNKF
DSVDGVRTIK YFECPGGIFV SSQGKKFGYV QNGSFKEASV SQIRALLANK VDVLCTVDGV
NFRSCCVAEG EVFGKTLGSV FCDGINVTKV RCSAIYKGKV FFQYSDLSEA DLVAVKDAFG
FDEPQLLKYY TMLGMCKWPV VVCGNYFAFK QSNNNCYINV ACLMLQHLSL KFPKWQWQEA
WNEFRSGKPL RFVSLVLAKG SFKFNEPSDS IDFMRVVLRE ADLSGATCNL EFVCKCGVKQ
EQRKGVDAVM HFGTLDKGDL VRGYNIACTC GSKLVHCTQF NVPFLICSNT PEGRKLPDDV
VAANIFTGGS VGHYTHVKCK PKYQLYDACN VNKVSEAKGN FTDCLYLKNL KQTFSSVLTT
FYLDDVKCVE YKPDLSQYYC ESGKYYTKPI IKAQFRTFEK VDGVYTNFKL VGHSIAEKLN
AKLGFDCNSP FVEYKITEWP TATGDVVLAS DDLYVSRYSS GCITFGKPVV WLGHEEASLK
SLTYFNRPSV VCENKFNVLP VDVSEPTDKG PVPAAVLVTG VPGADASAGA GIAKEQKACA
SASVEDQVVT EVRQEPSVSA ADVKEVKLNG VKKPVKVEGS VVVNDPTSET KVVKSLSIVD
VYDMFLTGCK YVVWTANELS RLVNSPTVRE YVKWGMGKIV TPAKLLLLRD EKQEFVAPKV
VKAKAIACYC AVKWFLLYCF SWIKFNTDNK VIYTTEVASK LTFKLCCLAF KNALQTFNWS
VVSRGFFLVA TVFLLWFNFL YANVILSDFY LPNIGPLPTF VGQIVAWFKT TFGVSTICDF
YQVTDLGYRS SFCNGSMVCE LCFSGFDMLD NYDAINVVQH VVDRRLSFDY ISLFKLVVEL
VIGYSLYTVC FYPLFVLIGM QLLTTWLPEF FMLETMHWSA RLFVFVANML PAFTLLRFYI
VVTAMYKVYC LCRHVMYGCS KPGCLFCYKR NRSVRVKCST VVGGSLRYYD VMANGGTGFC
TKHQWNCLNC NSWKPGNTFI THEAAADLSK ELKRPVNPTD SAYYSVTEVK QVGCSMRLFY
ERDGQRVYDD VNASLFVDMN GLLHSKVKGV PETHVVVVEN EADKAGFLGA AVFYAQSLYR
PMLMVEKKLI TTANTGLSVS RTMFDLYVDS LLNVLDVDRK SLTSFVNAAH NSLKEGVQLE
QVMDTFIGCA RRKCAIDSDV ETKSITKSVM SAVNAGVDFT DESCNNLVPT YVKSDTIVAA
DLGVLIQNNA KHVQANVAKA ANVACIWSVD AFNQLSADLQ HRLRKACSKT GLKIKLTYNK
QEANVPILTT PFSLKGGAVF SRMLQWLFVA NLICFIVLWA LMPTYAVHKS DMQLPLYASF
KVIDNGVLRD VSVTDACFAN KFNQFDQWYE STFGLAYYRN SKACPVVVAV IDQDIGHTLF
NVPTTVLRYG FHVLHFITHA FATDSVQCYT PHMQIPYDNF YASGCVLSSL CTMLAHADGT
PHPYCYTGGV MHNASLYSSL APHVRYNLAS SNGYIRFPEV VSEGIVRVVR TRSMTYCRVG
LCEEAEEGIC FNFNRSWVLN NPYYRAMPGT FCGRNAFDLI HQVLGGLVRP IDFFALTASS
VAGAILAIIV VLAFYYLIKL KRAFGDYTSV VVINVIVWCI NFLMLFVFQV YPTLSCLYAC
FYFYTTLYFP SEISVVMHLQ WLVMYGAIMP LWFCIIYVAV VVSNHALWLF SYCRKIGTEV
RSDGTFEEMA LTTFMITKES YCKLKNSVSD VAFNRYLSLY NKYRYFSGKM DTAAYREAAC
SQLAKAMETF NHNNGNDVLY QPPTASVTTS FLQSGIVKMV SPTSKVEPCI VSVTYGNMTL
NGLWLDDKVY CPRHVICSSA DMTDPDYPNL LCRVTSSDFC VMSGRMSLTV MSYQMQGCQL
VLTVTLQNPN TPKYSFGVVK PGETFTVLAA YNGRPQGAFH VTLRSSHTIK GSFLCGSCGS
VGYVLTGDSV RFVYMHQLEL STGCHTGTDF SGNFYGPYRD AQVVQLPVQD YTQTVNVVAW
LYAAIFNRCN WFVQSDSCSL EEFNVWAMTN GFSSIKADLV LDALASMTGV TVEQVLAAIK
RLHSGFQGKQ ILGSCVLEDE TPSDVYQQLA GVKLQSKRTR VIKGTCCWIL ASTFLFCSII
SAFVKWTMFM YVTTHMLGVT LCALCFVSFA MLLIKHKHLY LTMYIMPVLC TFYTNYLVVY
KQSFRGLAYA WLSHFVPAVD YTYMDEVLYG VVLLVAMVFV TMRSINHDVF SIMFLVGRLV
SLVSMWYFGA NLEEEVLLFL TSLFGTYTWT TMLSLATAKV IAKWLAVNVL YFTDVPQIKL
VLLSYLCIGY VCCCYWGILS LLNSIFRMPL GVYNYKISVQ ELRYMNANGL RPPRNSFEAL
MLNFKLLGIG GVPVIEVSQI QSRLTDVKCA NVVLLNCLQH LHIASNSKLW QYCSTLHNEI
LATSDLSMAF DKLAQLLVVL FANPAAVDSK CLASIEEVSD DYVRDNTVLQ ALQSEFVNMA
SFVEYELAKK NLDEAKASGS ANQQQIKQLE KACNIAKSAY ERDRAVARKL ERMADLALTN
MYKEARINDK KSKVVSALQT MLFSMVRKLD NQALNSILDN AVKGCVPLNA IPSLTSNTLT
IIVPDKQVFD QVVDNVYVTY AGNVWHIQFI QDADGAVKQL NEIDVNSTWP LVIAANRHNE
VSTVVLQNNE LMPQKLRTQV VNSGSDMNCN TPTQCYYNTT GTGKIVYAIL SDCDGLKYTK
IVKEDGNCVV LELDPPCKFS VQDVKGLKIK YLYFVKGCNT LARGWVVGTL SSTVRLQAGT
ATEYASNSAI LSLCAFSVDP KKTYLDYIKQ GGVPVTNCVK MLCDHAGTGM AITIKPEATT
NQDSYGGASV CIYCRSRVEH PDVDGLCKLR GKFVQVPLGI KDPVSYVLTH DVCQVCGFWR
DGSCSCVGTG SQFQSKDTNF LNRIRGTSVN ARLVPCASGL DTDVQLRAFD ICNANRAGIG
LYYKVNCCRF QRVDEDGNKL DKFFVVKRTN LEVYNKEKEC YELTKECGVV AEHEFFTFDV
EGSRVPHIVR KDLSKFTMLD LCYALRHFDR NDCSTLKEIL LTYAECEESY FQKKDWYDFV
ENPDIINVYK KLGPIFNRAL LNTAKFADAL VEAGLVGVLT LDNQDLYGQW YDFGDFVKTV
PGCGVAVADS YYSYMMPMLT MCHALDSELF VNGTYREFDL VQYDFTDFKL ELFTKYFKHW
SMTYHPNTCE CEDDRCIIHC ANFNILFSMV LPKTCFGPLV RQIFVDGVPF VVSIGYHYKE
LGVVMNMDVD THRYRLSLKD LLLYAADPAL HVASASALLD LRTCCFSVAA ITSGVKFQTV
KPGNFNQDFY EFILSKGLLK EGSSVDLKHF FFTQDGNAAI TDYNYYKYNL PTMVDIKQLL
FVLEVVNKYF EIYEGGCIPA TQVIVNNYDK SAGYPFNKFG KARLYYEALS FEEQDEIYAY
TKRNVLPTLT QMNLKYAISA KNRARTVAGV SILSTMTGRM FHQKCLKSIA ATRGVPVVIG
TTKFYGGWDD MLRRLIKDVD SPVLMGWDYP KCDRAMPNIL RIVSSLVLAR KHDSCCSHTD
RFYRLANECA QVLSEIVMCG GCYYVKPGGT SSGDATTAFA NSVFNICQAV SANVCSLMAC
NGHKIEDLSI RELQKRLYSN VYRADHVDPA FVSEYYEFLN KHFSMMILSD DGVVCYNSEF
ASKGYIANIS AFQQVLYYQN NVFMSEAKCW VETDIEKGPH EFCSQHTMLV KMDGDEVYLP
YPDPSRILGA GCFVDDLLKT DSVLLIERFV SLAIDAYPLV YHENPEYQNV FRVYLEYIKK
LYNDLGNQIL DSYSVILSTC DGQKFTDETF YKNMYLRSAV LQSVGACVVC SSQTSLRCGS
CIRKPLLCCK CAYDHVMSTD HKYVLSVSPY VCNSPGCDVN DVTKLYLGGM SYYCEDHKPQ
YSFKLVMNGM VFGLYKQSCT GSPYIEDFNK IASCKWTEVD DYVLANECTE RLKLFAAETQ
KATEEAFKQC YASATIREIV SDRELILSWE IGKVRPPLNK NYVFTGYHFT NNGKTVLGEY
VFDKSELTNG VYYRATTTYK LSVGDVFILT SHAVSSLSAP TLVPQENYTS IRFASVYSVP
ETFQNNVPNY QHIGMKRYCT VQGPPGTGKS HLAIGLAVYY CTARVVYTAA SHAAVDALCE
KAHKFLNIND CTRIVPAKVR VDCYDKFKVN DTTRKYVFTT INALPELVTD IIVVDEVSML
TNYELSVINS RVRAKHYVYI GDPAQLPAPR VLLNKGTLEP RYFNSVTKLM CCLGPDIFLG
TCYRCPKEIV DTVSALVYNN KLKAKNDNSS MCFKVYYKGQ TTHESSSAVN MQQIHLISKF
LKANPSWSNA VFISPYNSQN YVAKRVLGLQ TQTVDSAQGS EYDFVIYSQT AETAHSVNVN
RFNVAITRAK KGILCVMSSM QLFESLNFTT LTLDKINNPR LQCTTNLFKD CSRSYVGYHP
AHAPSFLAVD DKYKVGGDLA VCLNVADSAV TYSRLISLMG FKLDLTLDGY CKLFITRDEA
IKRVRAWVGF DAEGAHAIRD SIGTNFPLQL GFSTGIDFVV EATGMFAERD GYVFKKAAAR
APPGEQFKHL IPLMSRGQKW DVVRIRIVQM LSDHLVDLAD SVVLVTWAAS FELTCLRYFA
KVGREVVCSV CTKRATCFNS RTGYYGCWRH SYSCDYLYNP LIVDIQQWGY TGSLTSNHDP
ICSVHKGAHV ASSDAIMTRC LAVHDCFCKS VNWNLEYPII SNEVSVNTSC RLLQRVMFRA
AMLCNRYDVC YDIGNPKGLA CVKGYDFKFY DASPVVKSVK QFVYKYEAHK DQFLDGLCMF
WNCNVDKYPA NAVVCRFDTR VLNKLNLPGC NGGSLYVNKH AFHTSPFTRA AFENLKPMPF
FYYSDTPCVY MEGMESKQVD YVPLRSATCI TRCNLGGAVC LKHAEEYREY LESYNTATTA
GFTFWVYKTF DFYNLWNTFT RLQSLENVVY NLVNAGHFDG RAGELPCAVI GEKVIAKIQN
EDVVVFKNNT PFPTNVAVEL FAKRSIRPHP ELKLFRNLNI DVCWSHVLWD YAKDSVFCSS
TYKVCKYTDL QCIESLNVLF DGRDNGALEA FKKCRNGVYI NTTKIKSLSM IKGPQRADLN
GVVVEKVGDS DVEFWFAVRK DGDDVIFSRT GSLEPSHYRS PQGNPGGNRV GDLSGNEALA
RGTIFTQSRL LSSFTPRSEM EKDFMDLDDD VFIAKYSLQD YAFEHVVYGS FNQKIIGGLH
LLIGLARRQQ KSNLVIQEFV TYDSSIHSYF ITDENSGSSK SVCTVIDLLL DDFVDIVKSL
NLKCVSKVVN VNVDFKDFQF MLWCNEEKVM TFYPRLQAAA DWKPGYVMPV LYKYLESPLE
RVNLWNYGKP ITLPTGCMMN VAKYTQLCQY LSTTTLAVPA NMRVLHLGAG SDKGVAPGSA
VLRQWLPAGS ILVDNDVNPF VSDSVASYYG NCITLPFDCQ WDLIISDMYD PLTKNIGEYN
VSKDGFFTYL CHLIRDKLAL GGSVAIKITE FSWNAELYSL MGKFAFWTIF CTNVNASSSE
GFLIGINWLN KTRTEIDGKT MHANYLFWRN STMWNGGAYS LFDMSKFPLK AAGTAVVSLK
PDQINDLVLS LIEKGKLLVR DTRKEVFVGD SLVNVK


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