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Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Host translation inhibitor nsp1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Papain-like proteinase (PL-PRO) (EC 3.4.19.12) (EC 3.4.22.69) (Non-structural protein 3) (nsp3); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]

 R1A_MERS1               Reviewed;        4391 AA.
K9N638;
29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
06-MAR-2013, sequence version 1.
07-APR-2021, entry version 52.
RecName: Full=Replicase polyprotein 1a;
Short=pp1a;
AltName: Full=ORF1a 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=Non-structural protein 11;
Short=nsp11;
ORFNames=1a;
Middle East respiratory syndrome-related coronavirus (isolate United
Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1).
Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
Betacoronavirus; Merbecovirus.
NCBI_TaxID=1263720;
NCBI_TaxID=9838; Camelus dromedarius (Dromedary) (Arabian camel).
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Nishi O., Iiyama K., Yasunaga-Aoki C., Shimizu S.;
"The phylogenetic status and pathogenicity of a new isolate of Metarhizium
sp. from a fruit beetle larvae in Japan.";
Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
[2]
FUNCTION (PAPAIN-LIKE PROTEINASE).
PubMed=25142582; DOI=10.1128/jvi.01294-14;
Baez-Santos Y.M., Mielech A.M., Deng X., Baker S., Mesecar A.D.;
"Catalytic function and substrate specificity of the papain-like protease
domain of nsp3 from the Middle East respiratory syndrome coronavirus.";
J. Virol. 88:12511-12527(2014).
[3]
FUNCTION (NSP1).
PubMed=26311885; DOI=10.1128/jvi.01352-15;
Lokugamage K.G., Narayanan K., Nakagawa K., Terasaki K., Ramirez S.I.,
Tseng C.T., Makino S.;
"Middle east respiratory syndrome coronavirus nsp1 inhibits host gene
expression by selectively targeting mRNAs transcribed in the nucleus while
sparing mRNAs of cytoplasmic origin.";
J. Virol. 89:10970-10981(2015).
-!- 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]: Promotes the degradation
of host mRNAs by inducing an endonucleolytic RNA cleavage in template
mRNAs, and inhibits of host mRNA translation, a function that is
separable from its RNA cleavage activity. By suppressing host gene
expression, nsp1 facilitates efficient viral gene expression in
infected cells and evasion from host immune response.
{ECO:0000269|PubMed:26311885}.
-!- 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, ECO:0000269|PubMed:25142582}.
-!- 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: [3C-like proteinase]: 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}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
-!- CATALYTIC ACTIVITY:
Reaction=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.; EC=3.4.22.69;
-!- CATALYTIC ACTIVITY:
Reaction=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).; EC=3.4.19.12;
-!- 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. {ECO:0000250|UniProtKB:P0C6X7}.
-!- INTERACTION:
K9N638; PRO_0000037312 [P0C6X7]: rep; Xeno; NbExp=2; IntAct=EBI-25618448, EBI-25487250;
PRO_0000422456; Q64339: Isg15; Xeno; NbExp=2; IntAct=EBI-25635184, EBI-8345781;
PRO_0000422456; Q9GKP4: ISG17; Xeno; NbExp=2; IntAct=EBI-25635184, EBI-25821151;
PRO_0000422461; PRO_0000422460 [K9N638]: 1a; NbExp=2; IntAct=EBI-26366276, EBI-26366263;
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=K9N638-1; Sequence=Displayed;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=K9N7C7-1; Sequence=External;
-!- 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: [Isoform Replicase polyprotein 1a]: Produced by
conventional translation.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
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EMBL; KC164505; AFY13305.1; -; Genomic_RNA.
PDB; 4R3D; X-ray; 2.82 A; A/B=1481-1811.
PDB; 5DUS; X-ray; 1.43 A; A=1110-1273.
PDB; 5HIH; X-ray; 1.66 A; A=1109-1275.
PDB; 5WKJ; X-ray; 2.05 A; A=3248-3553.
PDB; 5WKK; X-ray; 1.55 A; A=3248-3553.
PDB; 5WKL; X-ray; 1.85 A; A=3248-3553.
PDB; 5WKM; X-ray; 2.25 A; A=3248-3553.
PDBsum; 4R3D; -.
PDBsum; 5DUS; -.
PDBsum; 5HIH; -.
PDBsum; 5WKJ; -.
PDBsum; 5WKK; -.
PDBsum; 5WKL; -.
PDBsum; 5WKM; -.
SMR; K9N638; -.
BioGRID; 4383912; 1.
IntAct; K9N638; 10.
DrugBank; DB15797; GC-373.
DrugBank; DB15796; GC-376 free acid.
PRIDE; K9N638; -.
SABIO-RK; K9N638; -.
Proteomes; UP000139997; Genome.
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:0016887; F:ATPase activity; IEA:RHEA.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0002151; F:G-quadruplex RNA binding; IEA:InterPro.
GO; GO:0003727; F:single-stranded RNA binding; IEA:InterPro.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:UniProtKB-EC.
GO; GO:0016740; F:transferase activity; IEA:InterPro.
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:0039548; P:suppression by virus of host IRF3 activity; IEA:UniProtKB-KW.
GO; GO:0039579; P:suppression by virus of host ISG15 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0019079; P:viral genome replication; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
CDD; cd21560; betaCoV-Nsp6; 1.
CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
CDD; cd21517; cv_beta_Nsp2_MERS-like; 1.
CDD; cd21473; cv_Nsp4_TM; 1.
CDD; cd21563; Macro_cv_SUD-M_Nsp3-like; 1.
CDD; cd21557; Macro_X_Nsp3-like; 1.
CDD; cd21523; SUD_C_MERS-CoV_Nsp3; 1.
CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1.
CDD; cd21466; Ubl2_cv_PLpro_N_Nsp3-like; 1.
Gene3D; 1.10.150.420; -; 1.
Gene3D; 1.10.1840.10; -; 1.
Gene3D; 1.10.8.1190; -; 1.
Gene3D; 1.10.8.370; -; 1.
Gene3D; 2.40.10.10; -; 2.
Gene3D; 2.40.10.250; -; 1.
Gene3D; 2.40.10.290; -; 1.
Gene3D; 3.10.20.350; -; 1.
Gene3D; 3.10.20.540; -; 1.
Gene3D; 3.40.220.10; -; 1.
Gene3D; 3.40.220.20; -; 1.
Gene3D; 3.40.50.11020; -; 1.
Gene3D; 3.90.70.90; -; 1.
InterPro; IPR043613; CoV_NSP2_C.
InterPro; IPR043611; CoV_NSP3_C.
InterPro; IPR043612; CoV_NSP4_N.
InterPro; IPR002589; Macro_dom.
InterPro; IPR043472; Macro_dom-like.
InterPro; IPR044371; Macro_X_NSP3-like.
InterPro; IPR042570; NAR_sf.
InterPro; IPR036333; NSP10_sf_CoV.
InterPro; IPR021590; NSP1_bCoV.
InterPro; IPR044388; NSP2_MERS-like.
InterPro; IPR043615; NSP2_N_CoV.
InterPro; IPR024375; NSP3_bCoV.
InterPro; IPR032592; NSP3_NAR_bCoV.
InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
InterPro; IPR044382; NSP3_SUD_C_MERS-CoV.
InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
InterPro; IPR038083; NSP3A-like.
InterPro; IPR032505; NSP4_C_CoV.
InterPro; IPR038123; NSP4_C_sf_CoV.
InterPro; IPR044367; NSP6_betaCoV.
InterPro; IPR043610; NSP6_CoV.
InterPro; IPR014828; NSP7_CoV.
InterPro; IPR037204; NSP7_sf_CoV.
InterPro; IPR014829; NSP8_CoV-like.
InterPro; IPR037230; NSP8_sf_CoV.
InterPro; IPR014822; NSP9_CoV.
InterPro; IPR036499; NSP9_sf_CoV.
InterPro; IPR013016; Peptidase_C16_CoV.
InterPro; IPR008740; Peptidase_C30_CoV.
InterPro; IPR043477; Peptidase_C30_dom3_CoV.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
InterPro; IPR043177; PLpro_N_sf_CoV.
InterPro; IPR043503; PLpro_palm_finger_dom_CoV.
InterPro; IPR043178; PLpro_thumb_sf_CoV.
InterPro; IPR018995; RNA_synth_NSP10_CoV.
Pfam; PF16251; bCoV_NAR; 1.
Pfam; PF11501; bCoV_NSP1; 1.
Pfam; PF11633; bCoV_SUD_M; 1.
Pfam; PF09401; CoV_NSP10; 1.
Pfam; PF19212; CoV_NSP2_C; 1.
Pfam; PF19211; CoV_NSP2_N; 1.
Pfam; PF19218; CoV_NSP3_C; 1.
Pfam; PF16348; CoV_NSP4_C; 1.
Pfam; PF19217; CoV_NSP4_N; 1.
Pfam; PF19213; CoV_NSP6; 1.
Pfam; PF08716; CoV_NSP7; 1.
Pfam; PF08717; CoV_NSP8; 1.
Pfam; PF08710; CoV_NSP9; 1.
Pfam; PF08715; CoV_peptidase; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF05409; Peptidase_C30; 1.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF101816; SSF101816; 1.
SUPFAM; SSF140367; SSF140367; 1.
SUPFAM; SSF143076; SSF143076; 1.
SUPFAM; SSF144246; SSF144246; 1.
SUPFAM; SSF159936; SSF159936; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52949; SSF52949; 1.
PROSITE; PS51942; BCOV_NSP3C_C; 1.
PROSITE; PS51941; BCOV_NSP3C_M; 1.
PROSITE; PS51945; BCOV_NSP3E_NAB; 1.
PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
PROSITE; PS51943; COV_NSP3A_UBL; 1.
PROSITE; PS51944; COV_NSP3D_UBL; 1.
PROSITE; PS51946; COV_NSP4C; 1.
PROSITE; PS51949; COV_NSP7; 1.
PROSITE; PS51950; COV_NSP8; 1.
PROSITE; PS51951; COV_NSP9_SSRNA_BD; 1.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51124; PEPTIDASE_C16; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus;
Decay of host mRNAs by virus;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; 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 IRF3 by virus; Inhibition of host ISG15 by virus;
Inhibition of host RLR pathway by virus; Membrane; Metal-binding;
Modulation of host ubiquitin pathway by viral deubiquitinase;
Modulation of host ubiquitin pathway by virus; Protease; Repeat;
Ribosomal frameshifting; RNA-binding; Thiol protease; Transmembrane;
Transmembrane helix; Ubl conjugation pathway; Viral immunoevasion; Zinc;
Zinc-finger.
CHAIN 1..193
/note="Host translation inhibitor nsp1"
/evidence="ECO:0000250"
/id="PRO_0000422454"
CHAIN 194..853
/note="Non-structural protein 2"
/evidence="ECO:0000250"
/id="PRO_0000422455"
CHAIN 854..2740
/note="Papain-like proteinase"
/evidence="ECO:0000250"
/id="PRO_0000422456"
CHAIN 2741..3247
/note="Non-structural protein 4"
/evidence="ECO:0000255"
/id="PRO_0000422457"
CHAIN 3248..3553
/note="3C-like proteinase"
/evidence="ECO:0000250"
/id="PRO_0000422458"
CHAIN 3554..3845
/note="Non-structural protein 6"
/evidence="ECO:0000250"
/id="PRO_0000422459"
CHAIN 3846..3928
/note="Non-structural protein 7"
/evidence="ECO:0000250"
/id="PRO_0000422460"
CHAIN 3929..4127
/note="Non-structural protein 8"
/evidence="ECO:0000250"
/id="PRO_0000422461"
CHAIN 4128..4237
/note="Non-structural protein 9"
/evidence="ECO:0000250"
/id="PRO_0000422462"
CHAIN 4238..4377
/note="Non-structural protein 10"
/evidence="ECO:0000250"
/id="PRO_0000422463"
CHAIN 4378..4391
/note="Non-structural protein 11"
/evidence="ECO:0000250"
/id="PRO_0000422464"
TRANSMEM 2105..2125
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 2177..2197
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 2281..2301
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 2305..2325
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 2330..2350
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 2757..2777
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3028..3048
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3062..3082
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3104..3124
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3125..3145
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3559..3579
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3593..3613
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3618..3638
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3664..3684
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3691..3711
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3740..3760
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 3765..3785
/note="Helical"
/evidence="ECO:0000255"
DOMAIN 856..966
/note="Ubiquitin-like 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
DOMAIN 1110..1276
/note="Macro 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
DOMAIN 1278..1404
/note="Macro 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
DOMAIN 1404..1477
/note="DPUP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
DOMAIN 1482..1537
/note="Ubiquitin-like 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
DOMAIN 1552..1823
/note="Peptidase C16"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
DOMAIN 1837..1954
/note="Nucleic acid-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
DOMAIN 3151..3247
/note="Nsp4C"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
DOMAIN 3248..3553
/note="Peptidase C30"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
DOMAIN 3846..3928
/note="RdRp Nsp7 cofactor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
DOMAIN 3929..4127
/note="RdRp Nsp8 cofactor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
DOMAIN 4128..4237
/note="Nsp9 ssRNA-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
DOMAIN 4238..4377
/note="ExoN/MTase coactivator"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
ZN_FING 1672..1709
/note="C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
ZN_FING 4311..4327
ZN_FING 4354..4367
REGION 2040..2363
/note="HD1"
REGION 2761..3171
/note="HD2"
REGION 3571..3785
/note="HD3"
ACT_SITE 1592
/note="For PL-PRO activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
ACT_SITE 1759
/note="For PL-PRO activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
ACT_SITE 3288
/note="For 3CL-PRO activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
ACT_SITE 3395
/note="For 3CL-PRO activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
METAL 4311
/note="Zinc"
METAL 4311
/note="Zinc 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
METAL 4314
/note="Zinc"
METAL 4314
/note="Zinc 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
METAL 4320
/note="Zinc"
METAL 4320
/note="Zinc 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
METAL 4327
/note="Zinc"
METAL 4327
/note="Zinc 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
METAL 4354
/note="Zinc"
METAL 4354
/note="Zinc 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
METAL 4357
/note="Zinc"
METAL 4357
/note="Zinc 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
METAL 4365
/note="Zinc"
METAL 4365
/note="Zinc 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
METAL 4367
/note="Zinc 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
SITE 193..194
/note="Cleavage"
/evidence="ECO:0000250"
SITE 853..854
/note="Cleavage; by PL-PRO"
/evidence="ECO:0000250"
SITE 2740..2741
/note="Cleavage; by PL-PRO"
/evidence="ECO:0000250"
SITE 3247..3248
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 3553..3554
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 3845..3846
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 3928..3929
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 4127..4128
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 4237..4238
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
SITE 4377..4378
/note="Cleavage; by 3CL-PRO"
/evidence="ECO:0000250"
HELIX 1110..1113
/evidence="ECO:0007744|PDB:5DUS"
STRAND 1116..1118
/evidence="ECO:0007744|PDB:5DUS"
STRAND 1120..1128
/evidence="ECO:0007744|PDB:5DUS"
HELIX 1130..1134
/evidence="ECO:0007744|PDB:5DUS"
STRAND 1141..1146
/evidence="ECO:0007744|PDB:5DUS"
HELIX 1156..1163
/evidence="ECO:0007744|PDB:5DUS"
TURN 1164..1166
/evidence="ECO:0007744|PDB:5DUS"
HELIX 1167..1179
/evidence="ECO:0007744|PDB:5DUS"
STRAND 1187..1191
/evidence="ECO:0007744|PDB:5DUS"
STRAND 1195..1203
/evidence="ECO:0007744|PDB:5DUS"
HELIX 1207..1209
/evidence="ECO:0007744|PDB:5DUS"
HELIX 1213..1215
/evidence="ECO:0007744|PDB:5DUS"
HELIX 1216..1221
/evidence="ECO:0007744|PDB:5DUS"
HELIX 1222..1225
/evidence="ECO:0007744|PDB:5DUS"
STRAND 1226..1231
/evidence="ECO:0007744|PDB:5DUS"
HELIX 1243..1253
/evidence="ECO:0007744|PDB:5DUS"
STRAND 1256..1263
/evidence="ECO:0007744|PDB:5DUS"
HELIX 1265..1272
/evidence="ECO:0007744|PDB:5DUS"
STRAND 1484..1494
/evidence="ECO:0007744|PDB:4R3D"
STRAND 1496..1505
/evidence="ECO:0007744|PDB:4R3D"
HELIX 1507..1510
/evidence="ECO:0007744|PDB:4R3D"
STRAND 1513..1516
/evidence="ECO:0007744|PDB:4R3D"
HELIX 1528..1530
/evidence="ECO:0007744|PDB:4R3D"
STRAND 1534..1537
/evidence="ECO:0007744|PDB:4R3D"
HELIX 1543..1553
/evidence="ECO:0007744|PDB:4R3D"
HELIX 1560..1570
/evidence="ECO:0007744|PDB:4R3D"
TURN 1571..1573
/evidence="ECO:0007744|PDB:4R3D"
STRAND 1576..1579
/evidence="ECO:0007744|PDB:4R3D"
STRAND 1582..1585
/evidence="ECO:0007744|PDB:4R3D"
TURN 1589..1591
/evidence="ECO:0007744|PDB:4R3D"
HELIX 1592..1603
/evidence="ECO:0007744|PDB:4R3D"
STRAND 1607..1611
/evidence="ECO:0007744|PDB:4R3D"
HELIX 1612..1622
/evidence="ECO:0007744|PDB:4R3D"
HELIX 1627..1636
/evidence="ECO:0007744|PDB:4R3D"
HELIX 1647..1655
/evidence="ECO:0007744|PDB:4R3D"
STRAND 1658..1662
/evidence="ECO:0007744|PDB:4R3D"
STRAND 1665..1672
/evidence="ECO:0007744|PDB:4R3D"
TURN 1673..1675
/evidence="ECO:0007744|PDB:4R3D"
STRAND 1676..1683
/evidence="ECO:0007744|PDB:4R3D"
HELIX 1684..1687
/evidence="ECO:0007744|PDB:4R3D"
STRAND 1689..1692
/evidence="ECO:0007744|PDB:4R3D"
HELIX 1696..1699
/evidence="ECO:0007744|PDB:4R3D"
STRAND 1703..1706
/evidence="ECO:0007744|PDB:4R3D"
STRAND 1710..1740
/evidence="ECO:0007744|PDB:4R3D"
STRAND 1745..1751
/evidence="ECO:0007744|PDB:4R3D"
STRAND 1759..1766
/evidence="ECO:0007744|PDB:4R3D"
STRAND 1769..1773
/evidence="ECO:0007744|PDB:4R3D"
STRAND 1780..1799
/evidence="ECO:0007744|PDB:4R3D"
HELIX 3258..3261
/evidence="ECO:0007744|PDB:5WKK"
STRAND 3264..3269
/evidence="ECO:0007744|PDB:5WKK"
STRAND 3273..3279
/evidence="ECO:0007744|PDB:5WKK"
STRAND 3282..3286
/evidence="ECO:0007744|PDB:5WKK"
HELIX 3287..3290
/evidence="ECO:0007744|PDB:5WKK"
HELIX 3293..3295
/evidence="ECO:0007744|PDB:5WKK"
STRAND 3296..3298
/evidence="ECO:0007744|PDB:5WKL"
HELIX 3301..3307
/evidence="ECO:0007744|PDB:5WKK"
HELIX 3310..3312
/evidence="ECO:0007744|PDB:5WKK"
STRAND 3313..3316
/evidence="ECO:0007744|PDB:5WKK"
STRAND 3327..3333
/evidence="ECO:0007744|PDB:5WKK"
STRAND 3336..3343
/evidence="ECO:0007744|PDB:5WKK"
STRAND 3350..3353
/evidence="ECO:0007744|PDB:5WKK"
STRAND 3361..3368
/evidence="ECO:0007744|PDB:5WKK"
STRAND 3371..3379
/evidence="ECO:0007744|PDB:5WKK"
STRAND 3398..3403
/evidence="ECO:0007744|PDB:5WKK"
STRAND 3406..3416
/evidence="ECO:0007744|PDB:5WKK"
STRAND 3422..3425
/evidence="ECO:0007744|PDB:5WKK"
STRAND 3437..3440
/evidence="ECO:0007744|PDB:5WKK"
HELIX 3451..3463
/evidence="ECO:0007744|PDB:5WKK"
HELIX 3477..3485
/evidence="ECO:0007744|PDB:5WKK"
TURN 3486..3488
/evidence="ECO:0007744|PDB:5WKK"
HELIX 3496..3505
/evidence="ECO:0007744|PDB:5WKK"
HELIX 3509..3520
/evidence="ECO:0007744|PDB:5WKK"
STRAND 3531..3533
/evidence="ECO:0007744|PDB:5WKK"
HELIX 3540..3546
/evidence="ECO:0007744|PDB:5WKK"
SEQUENCE 4391 AA; 486059 MW; D0A87AE59773BBB8 CRC64;
MSFVAGVTAQ GARGTYRAAL NSEKHQDHVS LTVPLCGSGN LVEKLSPWFM DGENAYEVVK
AMLLKKEPLL YVPIRLAGHT RHLPGPRVYL VERLIACENP FMVNQLAYSS SANGSLVGTT
LQGKPIGMFF PYDIELVTGK QNILLRKYGR GGYHYTPFHY ERDNTSCPEW MDDFEADPKG
KYAQNLLKKL IGGDVTPVDQ YMCGVDGKPI SAYAFLMAKD GITKLADVEA DVAARADDEG
FITLKNNLYR LVWHVERKDV PYPKQSIFTI NSVVQKDGVE NTPPHYFTLG CKILTLTPRN
KWSGVSDLSL KQKLLYTFYG KESLENPTYI YHSAFIECGS CGNDSWLTGN AIQGFACGCG
ASYTANDVEV QSSGMIKPNA LLCATCPFAK GDSCSSNCKH SVAQLVSYLS ERCNVIADSK
SFTLIFGGVA YAYFGCEEGT MYFVPRAKSV VSRIGDSIFT GCTGSWNKVT QIANMFLEQT
QHSLNFVGEF VVNDVVLAIL SGTTTNVDKI RQLLKGVTLD KLRDYLADYD VAVTAGPFMD
NAINVGGTGL QYAAITAPYV VLTGLGESFK KVATIPYKVC NSVKDTLTYY AHSVLYRVFP
YDMDSGVSSF SELLFDCVDL SVASTYFLVR LLQDKTGDFM STIITSCQTA VSKLLDTCFE
ATEATFNFLL DLAGLFRIFL RNAYVYTSQG FVVVNGKVST LVKQVLDLLN KGMQLLHTKV
SWAGSNISAV IYSGRESLIF PSGTYYCVTT KAKSVQQDLD VILPGEFSKK QLGLLQPTDN
STTVSVTVSS NMVETVVGQL EQTNMHSPDV IVGDYVIISE KLFVRSKEED GFAFYPACTN
GHAVPTLFRL KGGAPVKKVA FGGDQVHEVA AVRSVTVEYN IHAVLDTLLA SSSLRTFVVD
KSLSIEEFAD VVKEQVSDLL VKLLRGMPIP DFDLDDFIDA PCYCFNAEGD ASWSSTMIFS
LHPVECDEEC SEVEASDLEE GESECISETS TEQVDVSHEI SDDEWAAAVD EAFPLDEAED
VTESVQEEAQ PVEVPVEDIA QVVIADTLQE TPVVSDTVEV PPQVVKLPSE PQTIQPEVKE
VAPVYEADTE QTQSVTVKPK RLRKKRNVDP LSNFEHKVIT ECVTIVLGDA IQVAKCYGES
VLVNAANTHL KHGGGIAGAI NAASKGAVQK ESDEYILAKG PLQVGDSVLL QGHSLAKNIL
HVVGPDARAK QDVSLLSKCY KAMNAYPLVV TPLVSAGIFG VKPAVSFDYL IREAKTRVLV
VVNSQDVYKS LTIVDIPQSL TFSYDGLRGA IRKAKDYGFT VFVCTDNSAN TKVLRNKGVD
YTKKFLTVDG VQYYCYTSKD TLDDILQQAN KSVGIISMPL GYVSHGLDLI QAGSVVRRVN
VPYVCLLANK EQEAILMSED VKLNPSEDFI KHVRTNGGYN SWHLVEGELL VQDLRLNKLL
HWSDQTICYK DSVFYVVKNS TAFPFETLSA CRAYLDSRTT QQLTIEVLVT VDGVNFRTVV
LNNKNTYRSQ LGCVFFNGAD ISDTIPDEKQ NGHSLYLADN LTADETKALK ELYGPVDPTF
LHRFYSLKAA VHKWKMVVCD KVRSLKLSDN NCYLNAVIMT LDLLKDIKFV IPALQHAFMK
HKGGDSTDFI ALIMAYGNCT FGAPDDASRL LHTVLAKAEL CCSARMVWRE WCNVCGIKDV
VLQGLKACCY VGVQTVEDLR ARMTYVCQCG GERHRQIVEH TTPWLLLSGT PNEKLVTTST
APDFVAFNVF QGIETAVGHY VHARLKGGLI LKFDSGTVSK TSDWKCKVTD VLFPGQKYSS
DCNVVRYSLD GNFRTEVDPD LSAFYVKDGK YFTSEPPVTY SPATILAGSV YTNSCLVSSD
GQPGGDAISL SFNNLLGFDS SKPVTKKYTY SFLPKEDGDV LLAEFDTYDP IYKNGAMYKG
KPILWVNKAS YDTNLNKFNR ASLRQIFDVA PIELENKFTP LSVESTPVEP PTVDVVALQQ
EMTIVKCKGL NKPFVKDNVS FVADDSGTPV VEYLSKEDLH TLYVDPKYQV IVLKDNVLSS
MLRLHTVESG DINVVAASGS LTRKVKLLFR ASFYFKEFAT RTFTATTAVG SCIKSVVRHL
GVTKGILTGC FSFVKMLFML PLAYFSDSKL GTTEVKVSAL KTAGVVTGNV VKQCCTAAVD
LSMDKLRRVD WKSTLRLLLM LCTTMVLLSS VYHLYVFNQV LSSDVMFEDA QGLKKFYKEV
RAYLGISSAC DGLASAYRAN SFDVPTFCAN RSAMCNWCLI SQDSITHYPA LKMVQTHLSH
YVLNIDWLWF AFETGLAYML YTSAFNWLLL AGTLHYFFAQ TSIFVDWRSY NYAVSSAFWL
FTHIPMAGLV RMYNLLACLW LLRKFYQHVI NGCKDTACLL CYKRNRLTRV EASTVVCGGK
RTFYITANGG ISFCRRHNWN CVDCDTAGVG NTFICEEVAN DLTTALRRPI NATDRSHYYV
DSVTVKETVV QFNYRRDGQP FYERFPLCAF TNLDKLKFKE VCKTTTGIPE YNFIIYDSSD
RGQESLARSA CVYYSQVLCK SILLVDSSLV TSVGDSSEIA TKMFDSFVNS FVSLYNVTRD
KLEKLISTAR DGVRRGDNFH SVLTTFIDAA RGPAGVESDV ETNEIVDSVQ YAHKHDIQIT
NESYNNYVPS YVKPDSVSTS DLGSLIDCNA ASVNQIVLRN SNGACIWNAA AYMKLSDALK
RQIRIACRKC NLAFRLTTSK LRANDNILSV RFTANKIVGG APTWFNALRD FTLKGYVLAT
IIVFLCAVLM YLCLPTFSMV PVEFYEDRIL DFKVLDNGII RDVNPDDKCF ANKHRSFTQW
YHEHVGGVYD NSITCPLTVA VIAGVAGARI PDVPTTLAWV NNQIIFFVSR VFANTGSVCY
TPIDEIPYKS FSDSGCILPS ECTMFRDAEG RMTPYCHDPT VLPGAFAYSQ MRPHVRYDLY
DGNMFIKFPE VVFESTLRIT RTLSTQYCRF GSCEYAQEGV CITTNGSWAI FNDHHLNRPG
VYCGSDFIDI VRRLAVSLFQ PITYFQLTTS LVLGIGLCAF LTLLFYYINK VKRAFADYTQ
CAVIAVVAAV LNSLCICFVA SIPLCIVPYT ALYYYATFYF TNEPAFIMHV SWYIMFGPIV
PIWMTCVYTV AMCFRHFFWV LAYFSKKHVE VFTDGKLNCS FQDAASNIFV INKDTYAALR
NSLTNDAYSR FLGLFNKYKY FSGAMETAAY REAAACHLAK ALQTYSETGS DLLYQPPNCS
ITSGVLQSGL VKMSHPSGDV EACMVQVTCG SMTLNGLWLD NTVWCPRHVM CPADQLSDPN
YDALLISMTN HSFSVQKHIG APANLRVVGH AMQGTLLKLT VDVANPSTPA YTFTTVKPGA
AFSVLACYNG RPTGTFTVVM RPNYTIKGSF LCGSCGSVGY TKEGSVINFC YMHQMELANG
THTGSAFDGT MYGAFMDKQV HQVQLTDKYC SVNVVAWLYA AILNGCAWFV KPNRTSVVSF
NEWALANQFT EFVGTQSVDM LAVKTGVAIE QLLYAIQQLY TGFQGKQILG STMLEDEFTP
EDVNMQIMGV VMQSGVRKVT YGTAHWLFAT LVSTYVIILQ ATKFTLWNYL FETIPTQLFP
LLFVTMAFVM LLVKHKHTFL TLFLLPVAIC LTYANIVYEP TTPISSALIA VANWLAPTNA
YMRTTHTDIG VYISMSLVLV IVVKRLYNPS LSNFALALCS GVMWLYTYSI GEASSPIAYL
VFVTTLTSDY TITVFVTVNL AKVCTYAIFA YSPQLTLVFP EVKMILLLYT CLGFMCTCYF
GVFSLLNLKL RAPMGVYDFK VSTQEFRFMT ANNLTAPRNS WEAMALNFKL IGIGGTPCIK
VAAMQSKLTD LKCTSVVLLS VLQQLHLEAN SRAWAFCVKC HNDILAATDP SEAFEKFVSL
FATLMTFSGN VDLDALASDI FDTPSVLQAT LSEFSHLATF AELEAAQKAY QEAMDSGDTS
PQVLKALQKA VNIAKNAYEK DKAVARKLER MADQAMTSMY KQARAEDKKA KIVSAMQTML
FGMIKKLDND VLNGIISNAR NGCIPLSVIP LCASNKLRVV IPDFTVWNQV VTYPSLNYAG
ALWDITVINN VDNEIVKSSD VVDSNENLTW PLVLECTRAS TSAVKLQNNE IKPSGLKTMV
VSAGQEQTNC NTSSLAYYEP VQGRKMLMAL LSDNAYLKWA RVEGKDGFVS VELQPPCKFL
IAGPKGPEIR YLYFVKNLNN LHRGQVLGHI AATVRLQAGS NTEFASNSSV LSLVNFTVDP
QKAYLDFVNA GGAPLTNCVK MLTPKTGTGI AISVKPESTA DQETYGGASV CLYCRAHIEH
PDVSGVCKYK GKFVQIPAQC VRDPVGFCLS NTPCNVCQYW IGYGCNCDSL RQAALPQSKD
SNFLNESGVL L


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