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 R1AB_CVHN2              Reviewed;        7152 AA.
P0C6X3; Q14EB2;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
10-MAY-2017, entry version 72.
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;
Human coronavirus HKU1 (isolate N2) (HCoV-HKU1).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=443240;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16809319; DOI=10.1128/JVI.00509-06;
Woo P.C.Y., Lau S.K.P., Yip C.C.Y., Huang Y., Tsoi H.-W., Chan K.-H.,
Yuen K.-Y.;
"Comparative analysis of 22 coronavirus HKU1 genomes reveals a novel
genotype and evidence of natural recombination in coronavirus HKU1.";
J. Virol. 80:7136-7145(2006).
-!- 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).
-!- 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.
-!- 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.
-!- 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=P0C6X3-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6U4-1; 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}.
-!- MISCELLANEOUS: Isolate N2 belongs to genotype B.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
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EMBL; AY884001; AAX76519.1; -; Genomic_RNA.
ProteinModelPortal; P0C6X3; -.
SMR; P0C6X3; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000006551; 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:0019079; P:viral genome replication; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; 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; IPR002589; Macro_dom.
InterPro; IPR032592; NAR_dom.
InterPro; IPR009466; NSP11.
InterPro; IPR014828; NSP7.
InterPro; IPR014829; NSP8.
InterPro; IPR014822; NSP9.
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; 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; 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; 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; 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; 2.
PROSITE; PS51657; PSRV_HELICASE; 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 1 222 Host translation inhibitor nsp1.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000297773.
CHAIN 223 809 Non-structural protein 2.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000297774.
CHAIN 810 2808 Papain-like proteinase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000297775.
CHAIN 2809 3304 Non-structural protein 4.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000297776.
CHAIN 3305 3607 3C-like proteinase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000297777.
CHAIN 3608 3894 Non-structural protein 6.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000297778.
CHAIN 3895 3986 Non-structural protein 7.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000297779.
CHAIN 3987 4180 Non-structural protein 8.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000297780.
CHAIN 4181 4290 Non-structural protein 9.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000297781.
CHAIN 4291 4427 Non-structural protein 10.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000297782.
CHAIN 4428 5355 RNA-directed RNA polymerase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000297783.
CHAIN 5356 5958 Helicase. {ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000297784.
CHAIN 5959 6479 Guanine-N7 methyltransferase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000297785.
CHAIN 6480 6853 Uridylate-specific endoribonuclease.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000297786.
CHAIN 6854 7152 2'-O-methyltransferase.
{ECO:0000250|UniProtKB:P0C6X7}.
/FTId=PRO_0000297787.
TRANSMEM 2196 2216 Helical. {ECO:0000255}.
TRANSMEM 2257 2277 Helical. {ECO:0000255}.
TRANSMEM 2288 2308 Helical. {ECO:0000255}.
TRANSMEM 2371 2391 Helical. {ECO:0000255}.
TRANSMEM 2413 2433 Helical. {ECO:0000255}.
TRANSMEM 2814 2834 Helical. {ECO:0000255}.
TRANSMEM 3089 3109 Helical. {ECO:0000255}.
TRANSMEM 3121 3141 Helical. {ECO:0000255}.
TRANSMEM 3148 3168 Helical. {ECO:0000255}.
TRANSMEM 3173 3193 Helical. {ECO:0000255}.
TRANSMEM 3621 3641 Helical. {ECO:0000255}.
TRANSMEM 3646 3666 Helical. {ECO:0000255}.
TRANSMEM 3671 3691 Helical. {ECO:0000255}.
TRANSMEM 3714 3734 Helical. {ECO:0000255}.
TRANSMEM 3742 3762 Helical. {ECO:0000255}.
TRANSMEM 3770 3790 Helical. {ECO:0000255}.
TRANSMEM 3813 3833 Helical. {ECO:0000255}.
REPEAT 945 954 1.
REPEAT 955 964 2.
REPEAT 965 974 3.
REPEAT 975 984 4.
REPEAT 985 994 5.
REPEAT 995 1004 6.
REPEAT 1005 1014 7.
REPEAT 1015 1024 8.
REPEAT 1025 1034 9.
REPEAT 1035 1044 10.
REPEAT 1045 1054 11.
DOMAIN 1093 1343 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1321 1492 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1688 1948 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3305 3607 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
DOMAIN 5035 5197 RdRp catalytic.
DOMAIN 5356 5439 CV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
DOMAIN 5611 5792 (+)RNA virus helicase ATP-binding.
DOMAIN 5793 5962 (+)RNA virus helicase C-terminal.
ZN_FING 1208 1236 C4-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 1805 1841 C4-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4364 4380 {ECO:0000250}.
ZN_FING 4406 4419 {ECO:0000250}.
NP_BIND 5636 5643 ATP. {ECO:0000250}.
REGION 945 1054 11 X 10 AA tandem repeat of N-[DN]-D-E-D-
V-V-T-G-D.
REGION 2196 2433 HD1. {ECO:0000250}.
REGION 2814 3193 HD2. {ECO:0000250}.
REGION 3621 3833 HD3. {ECO:0000250}.
COMPBIAS 934 1086 Asp-rich.
COMPBIAS 2199 2291 Phe-rich.
COMPBIAS 2586 2589 Poly-Val.
COMPBIAS 5360 5385 Cys-rich.
ACT_SITE 1131 1131 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1282 1282 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1727 1727 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1884 1884 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3345 3345 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3449 3449 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
METAL 5360 5360 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5363 5363 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5371 5371 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5374 5374 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5381 5381 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5384 5384 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5388 5388 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5394 5394 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5405 5405 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5410 5410 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5427 5427 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5430 5430 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
SITE 222 223 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 809 810 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 2808 2809 Cleavage; by PL2-PRO. {ECO:0000250}.
SITE 3304 3305 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3607 3608 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3894 3895 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3986 3987 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4180 4181 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4290 4291 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4427 4428 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 5355 5356 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6479 6480 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 6853 6854 Cleavage; by 3CL-PRO. {ECO:0000250}.
SEQUENCE 7152 AA; 807495 MW; 1B6E93484EF69631 CRC64;
MIKTSKYGLG FKWAPEFRWL LPDAAEELAS PMKSDEGGLC PSTGQAMESV GFVYDNHVKI
DCRCILGQEW HVQSNLIRDI FVHEDLHVVE VLTKTAVKSG TAILIKSPLH SLGGFPKGYV
MGLFRSYKTK RYVVHHLSMT TSTTNFGEDF LGWIVPFGFM PSYVHKWFQF CRLYIEESDL
IISNFKFDDY DFSVEDAYAE VHAEPKGKYS QKAYALLRQY RGIKPVLFVD QYGCDYSGKL
ADCLQAYGHY SLQDMRQKQS VWLANCDFDI VVAWHVVRDS RFVMRLQTIA TICGIKYVAQ
PTEDVVDGAV VIREPVHLLS ADAIVLKLPS LMKVMTHMDD FSIKSIYNVD LCDCGFVMQY
GYVDCFNDNC DFYGWVSGNM MDGFSCPLCC TVYDSSEVKA QSSGVIPENP VLFTNSTDTV
NPDSFNLYGY SVTPFGSCIY WSPRPGLWIP IIKSSVKSYD DLVYSGVVGC KSIVKETALI
THALYLDYVQ CKCGNLEQNH ILGVNNSWCR QLLLNRGDYN MLLKNIDLFV KRRADFACKF
AVCGDGFVPF LLDGLIPRSY YLIQSGIFFT SLMSQFSQEV SDMCLKMCIL FMDRVSVATF
YIEHYVNRLV TQFKLLGTTL VNKMVNWFNT MLDASAPATG WLLYQLLNGL FVVSQANFNF
VALIPDYAKI LVNKFYTFFK LLLECVTVDV LKDMPVLKTI NGLVCIVGNK FYNVSTGLIP
GFVLPCNAQE QQIYFFEGVA ESVIVEDDVI ENVKSSLSSY EYCQPPKSVE KICIIDNMYM
GKCGDKFFPI VMNDKNICLL DQAWRFPCAG RKVNFNEKPV VMEIPSLMTV KVMFDLDSTF
DDILGKVCSE FEVEKGVTVD DFVAVVCDAI ENALNSCKDH PVVGYQVRAF LNKLNENVVY
LFDEAGDEAM ASRMYCTFAI EDVEDVISSE AVEDTIDGVV EDTINDDEDV VTGDNDDEDV
VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV
VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEEI VTGDNDDQIV VTGDDVDDIE
SVYDFDTYKA LLVFNDVYND ALFVSYGSSV ETETYFKVNG LWSPTITHTN CWLRSVLLVM
QKLPFKFKDL AIENMWLSYK VGYNQSFVDY LLTTIPKAIV LPQGGYVADF AYWFLNQFDI
NAYANWCCLK CGFSFDLNGL DAVFFYGDIV SHVCKCGHNM TLIAADLPCT LHFSLFDDNF
CAFCTPKKIF IAACAVDVNV CHSVAVIGDE QIDGKFVTKF SGDKFDFIVG YGMSFSMSSF
ELAQLYGLCI TPNVCFVKGD IINVARLVKA DVIVNPANGH MLHGGGVAKA IAVAAGKKFS
KETAAMVKSK GVCQVGDCYV STGGKLCKTI LNIVGPDARQ DGRQSYVLLA RAYKHLNNYD
CCLSTLISAG IFSVPADVSL TYLLGVVDKQ VILVSNNKED FDIIQKCQIT SVVGTKALAV
RLTANVGRVI KFETDAYKLF LSGDDCFVSN SSVIQEVLLL RHDIQLNNDV RDYLLSKMTS
LPKDWRLINK FDVINGVKTV KYFECPNSIY ICSQGKDFGY VCDGSFYKAT VNQVCVLLAK
KIDVLLTVDG VNFKSISLTV GEVFGKILGN VFCDGIDVTK LKCSDFYADK ILYQYENLSL
ADISAVQSSF GFDQQQLLAY YNFLTVCKWS VVVNGPFFSF EQSHNNCYVN VACLMLQHIN
LKFNKWQWQE AWYEFRAGRP HRLVALVLAK GHFKFDEPSD ATDFIRVVLK QADLSGAICE
LELICDCGIK QESRVGVDAV MHFGTLAKTD LFNGYKIGCN CAGRIVHCTK LNVPFLICSN
TPLSKDLPDD VVAANMFMGV GVGHYTHLKC GSPYQHYDAC SVKKYTGVSG CLTDCLYLKN
LTQTFTSMLT NYFLDDVEMV AYNPDLSQYY CDNGKYYTKP IIKAQFKPFA KVDGVYTNFK
LVGHDICAQL NDKLGFNVDL PFVEYKVTVW PVATGDVVLA SDDLYVKRYF KGCETFGKPV
IWLCHDEASL NSLTYFNKPS FKSENRYSVL SVDSVSEESQ GNVVTSVMES QISTKEVKLK
GVRKTVKIED AIIVNDENSS IKVVKSLSLV DVWDMYLTGC DYVVWVANEL SRLVKSPTVR
EYIRYGIKPI TIPIDLLCLR DDNQTLLVPK IFKARAIEFY GFLKWLFIYV FSLLHFTNDK
TIFYTTEIAS KFTFNLFCLA LKNAFQTFRW SIFIKGFLVV ATVFLFWFNF LYINVIFSDF
YLPNISVFPI FVGRIVMWIK ATFGLVTICD FYSKLGVGFT SHFCNGSFIC ELCYSGFDML
DTYAAIDFVQ YEVDRRVLFD YVSLVKLIVE LVIGYSLYTV WFYPLFCLIG LQLFTTWLPD
LFMLETMHWL IRFIVFVANM LPAFVLLRFY IVVTAMYKVV GFIRHIVYGC NKAGCLFCYK
RNCSVRVKCS TIVGGVIRYY DITANGGTGF CVKHQWNCFN CHSFKPGNTF ITVEAAIELS
KELKRPVNPT DASHYVVTDI KQVGCMMRLF YDRDGQRVYD DVDASLFVDI NNLLHSKVKV
VPNLYVVVVE SDADRANFLN AVVFYAQSLY RPILLVDKKL ITTACNGISV TQTMFDVYVD
TFMSHFDVDR KSFNNFVNIA HASLREGVQL EKVLDTFVGC VRKCCSIDSD VETRFITKSM
ISAVAAGLEF TDENYNNLVP TYLKSDNIVA ADLGVLIQNG AKHVQGNVAK AANISCIWFI
DTFNQLTADL QHKLKKACVK TGLKLKLTFN KQEASVPILT TPFSLKGGVV LSNLLYILFF
ISLICFILLW ALLPTYSVYK SDIHLPAYAS FKVIDNGVVR DISVNDLCFA NKFFQFDQWY
ESTFGSFYYH NSMDCPIVVA VMDEDIGSTM FNVPTKVLRH GFHVLHFLTY AFASDSVQCY
TPHIQISYND FYASGCVLSS LCTMFKRGDG TPHPYCYSDG VMKNASLYTS LVPHTRYSLA
NSNGFIRFPD VISEGIVRIV RTRSMTYCRV GACEYAEEGI CFNFNSSWVL NNDYYRSMPG
TFCGRDLFDL FYQFFSSLIR PIDFFSLTAS SIFGAILAIV VVLVFYYLIK LKRAFGDYTS
VVVINVIVWC INFLMLFVFQ VYPICACVYA CFYFYVTLYF PSEISVIMHL QWIVMYGAIM
PFWFCVTYVA MVIANHVLWL FSYCRKIGVN VCNDSTFEET SLTTFMITKD SYCRLKNSVS
DVAYNRYLSL YNKYRYYSGK MDTAAYREAA CSQLAKAMET FNHNNGNDVL YQPPTASVST
SFLQSGIVKM VSPTSKIEPC IVSVTYGSMT LNGLWLDDKV YCPRHVICLS SNMNEPDYSA
LLCRVTLGDF TIMSGRMSLT VVSYQMQGCQ LVLTVSLQNP YTPKYTFGVV KPGETFTVLA
AYNGRPQGAF HVTMRSSYTI KGSFLCGSCG SVGYVLTGDS VKFVYMHQLE LSTGCHTGTD
FTGNFYGPYR DAQVVQLPVK DYVQTVNVIA WLYAAILNNC AWFVQNDVCS IEDFNVWAMT
NGFSQVKADL VLDALASMTG VSIETLLAAI KRLYMGFQGR QILGSCTFED ELAPSDVYQQ
LAGVKLQSKT KRFIKETIYW ILISTFLFSC IISAFVKWTI FMYINTHMIG VTLCVLCFVS
FMMLLVKHKH FYLTMYIIPV LCTLFYVNYL VVYKEGFRGL TYVWLSYFVP AVNFTYVYEV
FYGCILCVFA IFITMHSINH DIFSLMFLVG RIVTLISMWY FGSNLEEDVL LFITAFLGTY
TWTTILSLAI AKIVANWLSV NIFYFTDVPY IKLILLSYLF IGYILSCYWG FFSLLNSVFR
MPMGVYNYKI SVQELRYMNA NGLRPPRNSF EAILLNLKLL GIGGVPVIEV SQIQSKLTDV
KCANVVLLNC LQHLHVASNS RLWQYCSILH NEILSTSDLS VAFDKLAQLL IVLFANPAAV
DTKCLASIDE VSDDYVQDST VLQALQSEFV NMASFVEYEV AKKNLADAKN SGSVNQQQIK
QLEKACNIAK SVYERDKAVA RKLERMADLA LTNMYKEARI NDKKSKVVSA LQTMLFSMVR
KLDNQALNSI LDNAVKGCVP LNAIPALAAN TLTIIIPDKQ VFDKVVDNVY VAYAGSVWHI
QTVQDADGIN KQLTDISVDS NWPLVIIANR YNEVANAVMQ NNELMPHKLK IQVVNSGSDM
NCNIPTQCYY NNGSSGRIVY AVLSDVDGLK YTKIIKDDGN CVVLELDPPC KFSIQDVKGL
KIKYLYFIKG CNTLARGWVV GTLSSTIRLQ AGVATEYAAN SSILSLCAFS VDPKKTYLDY
IQQGGVPIIN CVKMLCDHAG TGMAITIKPE ATINQDSYGG ASVCIYCRAR VEHPDVDGLC
KLRGKFVQVP LGIKDPILYV LTHDVCQVCG FWRDGSCSCV GSGVAVQSKD LNFLNRVRGT
SVNARLVPCA SGLSTDVQLR AFDICNTNRA GIGLYYKVNC CRFQRIDDDG NKLDKFFVVK
RTNLEVYNKE KTYYELTKSC GVVAEHDFFT FDIDGSRVPH IVRKNLSKYT MLDLCYALRH
FDCNDCSVLC EILCEYADCK ESYFSKKDWY DFVENPDIIN IYKKLGPIFN RALLNTVSFA
DTLVKVGLVG VLTLDNQDLY GQWYDFGDFI QTAPGFGVAV ADSYYSYMMP MLTMCHVLDC
ELFVNDSYRQ FDLVQYDFTD YKLELFNKYF KYWGMKYHPN TVDCDNDRCI IHCANFNILF
SMVLPNTCFG PLVRQIFVDG VPFVVSIGYH YKELGVVMNL DVDTHRYRLS LKDLLLYAAD
PAMHVASASA LLDLRTCCFS VAAITSGIKF QTVKPGNFNQ DFYEFVKSKG LFKEGSTVDL
KHFFFTQDGN AAITDYNYYK YNLPTMVDIK QLLFVLEVVY KYFEIYDGGC IPASQVIVNN
YDKSAGYPFN KFGKARLYYE ALSFEEQNEI YAYTKRNVLP TLTQMNLKYA ISAKNRARTV
AGVSILSTMT GRMFHQKCLK SIAATRGVPV VIGTTKFYGG WDDMLRHLIK DVDNPVLMGW
DYPKCDRAMP NILRIVSSLV LARKHEFCCS HGDRFYRLAN ECAQVLSEIV MCGGCYYVKP
GGTSSGDATT AFANSVFNIC QAVTANVCSL MACNGHKIED LSIRNLQKRL YSNVYRTDYV
DYTFVNEYYE FLCKHFSMMI LSDDGVVCYN SDYASKGYIA NISVFQQVLY YQNNVFMSES
KCWVENDITN GPHEFCSQHT MLVKIDGDYV YLPYPDPSRI LGAGCFVDDL LKTDSVLLIE
RFVSLAIDAY PLVHHENEEY QKVFRVYLEY IKKLYNDLGN QILDSYSVIL STCDGLKFTD
ESFYKNMYLK SAVMQSVGAC VVCSSQTSLR CGSCIRKPLL CCKCCYDHVM ATNHKYVLSV
SPYVCNAPNC DVSDVTKLYL GGMSYYCENH KPHYSFKLVM NGMVFGLYKQ SCTGSPYIDD
FNKIASCKWT EVDDYVLANE CIERLKLFAA ETQKATEEAF KQSYASATIQ EIVSDREIIL
CWETGKVKPP LNKNYVFTGY HFTSTGKTVL GEYVFDKSEL TNGVYYRATT TYKLSIGDVF
VLTSHSVANL SAPTLVPQEN YASIRFSSVY SVPLLFQTNV ANYQHIGMKR YCTVQGPPGT
GKSHLAIGLA VYYYTARVVY TAASHAAVDA LCEKAYKFLN INDCTRIIPA KVRVDCYDKF
KINDTTCKYV FTTINALPEL VTDIVVVDEV SMLTNYELSV INARVKAKHY VYIGDPAQLP
APRVLLSKGS LEPRHFNSIT KIMCCLGPDI FLGNCYRCPK EIVETVSALV YDNKLKAKND
NSSLCFKVYF KGQTTHESSS AVNIQQIYLI SKFLKANPVW NSAVFISPYN SQNYVAKRIL
GVQTQTVDSA QGSEYDYVIY SQTAETAHSI NVNRFNVAIT RAKKGIFCVM SNMQLFESLN
FITLPLDKIQ NQTLSRLHCT TNLFKDCSKN FLGYHPAHAP SFLSVDDKYK VNEDLAVCLN
ICEPVLTYSR LISLMGFKLD LTLDGYSKFF ITKDEAIKRV RGWVGFDVEG AHATRDNIGT
NFPLQIGFST GVDFVVEATG LFAERDCYIF KRTVAKAPPG DNFKHLIPLM SKGQKWDVVR
IRIVQMLSDY LLDLSDSVVF ITWSASFELT CLRYFAKLGR ELNCDVCPNR ATCYNSRTGY
YGCWRHSYTC DYVYNPLIVD IQQWGYTGSL TSNHDIICNV HKGAHVASSD AIMTRCLAIY
DCFCKSVNWN LEYPIISNEV SINTSCRLLQ RVMLKAAMLC NRYNLCYDIG NPKGIACVKD
YEFKFYDASP VVKSVKQLFY VYDVHKDNFK DGLCMFWNCN VDKYPSNSIV CRFDTRVLNK
LNLPGCNGGS LYVNKHAFHT NPFTRTVFEN LKPMPFFYYS DTPCVYVDGL ESKQVDYVPL
RSATCITRCN LGGAVCSKHA EDYCKYLESY NVATTAGFTF WVYKTFDFYN LWNTFTMLQS
LENVIYNLVN AGHYDGRIGE LPCAIMNDKV VVKINNVDTV IFKNNTSLPT NIAVELFTKR
SIRHHPELKI LRNLNIDICW KHVLWDYVKD SLFCSSTYGV CKYTDLNFIE NLNVLFDGRD
NGALEAFRKA RNGVFISTGK LSSLSMIKGP QRADLNGVIV DKVGELNVEF WFAMRKDGDD
VIFSRADSLS PSHYWSPQGN LGGNCAGNAS GNDALARFTI FTQSRVLSTF EPRSDLERDF
IDMEDSLFIA KYGLEDYAFD HIVYGSFNYK VIGGLHLLIG LFRRLKKSNL VIQEFLQYDS
SIHSYFITDQ ECGSSKSVCT VIDLLLDDFV VIVKSLNLNC VSKVVNINVD FKDFQFMLWC
NDNKIMTFYP KMQATSDWKP GYSMPVLYKY LNVPLERVSL WNYGKAINLP TGCMMNVAKY
TQLCQYLNTT TLAVPVNMRV LHLGAGSDKE VAPGSAVLRQ WLPSGSILVD NDLNPFVSDS
LVTYFGDCMT LPFDCHWDLI ISDMYDPLTK NIGDYNVSKD GFFTYICYLI RDKLSLGGSV
AIKITEFSWN ADLYKLMSYF AFWTVFCTNV NASSSEGFLI GINYLGKSCF EIDGNVMHAN
YLFWRNSTTW NGGAYSLFDM SKFSLKLAGT AVVNLRPDQL NDLVYSLIER GKLLVRDTRK
EIFVGDSLVN TC


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