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Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p28); Non-structural protein 2 (nsp2) (p65); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL1-PRO/PL2-PRO) (PL1/PL2) (Papain-like proteinases 1/2) (p210); Non-structural protein 4 (nsp4) (Peptide HD2) (p44); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p27); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p10); Non-structural protein 8 (nsp8) (p22); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p15); Non-structural protein 11 (nsp11)]

 R1A_CVHOC               Reviewed;        4383 AA.
P0C6U7; Q9WAC3;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
23-MAY-2018, entry version 62.
RecName: Full=Replicase polyprotein 1a;
Short=pp1a;
AltName: Full=ORF1a polyprotein;
Contains:
RecName: Full=Non-structural protein 1;
Short=nsp1;
AltName: Full=p28;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p65;
Contains:
RecName: Full=Non-structural protein 3;
Short=nsp3;
EC=3.4.19.12;
EC=3.4.22.69;
AltName: Full=PL1-PRO/PL2-PRO;
AltName: Full=PL1/PL2;
AltName: Full=Papain-like proteinases 1/2;
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=Non-structural protein 11;
Short=nsp11;
ORFNames=1a;
Human coronavirus OC43 (HCoV-OC43).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=31631;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate 19572 Belgium 2004, and Isolate 87309 Belgium 2003;
PubMed=15914223; DOI=10.1016/j.virol.2005.04.010;
Vijgen L., Keyaerts E., Lemey P., Moes E., Li S., Vandamme A.M.,
Van Ranst M.;
"Circulation of genetically distinct contemporary human coronavirus
OC43 strains.";
Virology 337:85-92(2005).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate ATCC VR-759, and Isolate clinical OC43-Paris;
PubMed=15280490; DOI=10.1128/JVI.78.16.8824-8834.2004;
St Jean J.R., Jacomy H., Desforges M., Vabret A., Freymuth F.,
Talbot P.J.;
"Human respiratory coronavirus OC43: genetic stability and
neuroinvasion.";
J. Virol. 78:8824-8834(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate ATCC VR-759;
PubMed=15650185; DOI=10.1128/JVI.79.3.1595-1604.2005;
Vijgen L., Keyaerts E., Moes E., Thoelen I., Wollants E., Lemey P.,
Vandamme A.M., Van Ranst M.;
"Complete genomic sequence of human coronavirus OC43: molecular clock
analysis suggests a relatively recent zoonotic coronavirus
transmission event.";
J. Virol. 79:1595-1604(2005).
-!- FUNCTION: The papain-like proteinase 1 (PL1-PRO) and papain-like
proteinase 2 (PL2-PRO) are responsible for the cleavages located
at the N-terminus of the replicase polyprotein. In addition, PLP2
possesses a deubiquitinating/deISGylating activity and processes
both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from
cellular substrates. Antagonizes innate immune induction of type I
interferon by blocking the phosphorylation, dimerization and
subsequent nuclear translocation of host IRF-3 (By similarity).
{ECO:0000250}.
-!- FUNCTION: The main proteinase 3CL-PRO is responsible for the
majority of cleavages as it cleaves the C-terminus of replicase
polyprotein at 11 sites. Recognizes substrates containing the core
sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog
Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-
phosphate (ADRP)-binding function (By similarity).
{ECO:0000255|PROSITE-ProRule:PRU00772}.
-!- FUNCTION: Nsp7-nsp8 hexadecamer may possibly confer processivity
to the polymerase, maybe by binding to dsRNA or by producing
primers utilized by the latter. {ECO:0000250}.
-!- FUNCTION: Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
-!- FUNCTION: Non-structural protein 1: binds to the 40S ribosomal
subunit and inhibits host translation. The nsp1-40S ribosome
complex further induces an endonucleolytic cleavage near the 5'UTR
of host mRNAs, targeting them for degradation. By suppressing host
gene expression, nsp1 facilitates efficient viral gene expression
in infected cells and evasion from host immune response (By
similarity). {ECO:0000250}.
-!- 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: 3CL-PRO exists as monomer and homodimer. Eight copies of
nsp7 and eight copies of nsp8 assemble to form a
heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 3: 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 (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=P0C6U7-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6X6-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
-!- 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: The sequence shown is that of isolate 19572 Belgium
2004.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
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EMBL; AY903459; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY903460; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY585228; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY585229; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AY391777; -; NOT_ANNOTATED_CDS; Genomic_RNA.
ProteinModelPortal; P0C6U7; -.
SMR; P0C6U7; -.
PRIDE; P0C6U7; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000007552; Genome.
Proteomes; UP000100580; Genome.
Proteomes; UP000159995; Genome.
Proteomes; UP000161137; 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:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
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:InterPro.
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: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.
Gene3D; 1.10.150.420; -; 1.
Gene3D; 1.10.8.370; -; 1.
Gene3D; 2.40.10.250; -; 1.
Gene3D; 3.10.20.350; -; 1.
InterPro; IPR022570; B-CoV_NSP1.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR002589; Macro_dom.
InterPro; IPR032592; NAR_dom.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR038123; NSP4_C_sf.
InterPro; IPR014828; NSP7.
InterPro; IPR037204; NSP7_sf.
InterPro; IPR014829; NSP8.
InterPro; IPR037230; NSP8_sf.
InterPro; IPR014822; NSP9.
InterPro; IPR036499; NSP9_sf.
InterPro; IPR002705; Pept_C30/C16_B_coronavir.
InterPro; IPR008740; Peptidase_C30.
InterPro; IPR013016; Peptidase_C30/C16.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR038083; pp1a/1ab.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF11963; DUF3477; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF16251; NAR; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF08716; nsp7; 1.
Pfam; PF08717; nsp8; 1.
Pfam; PF08710; nsp9; 1.
Pfam; PF01831; Peptidase_C16; 1.
Pfam; PF05409; Peptidase_C30; 1.
Pfam; PF08715; Viral_protease; 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.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51124; PEPTIDASE_C16; 2.
3: Inferred from homology;
Activation of host autophagy by virus; Complete proteome;
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;
Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
Thiol protease; Transmembrane; Transmembrane helix;
Ubl conjugation pathway; Viral immunoevasion; Zinc; Zinc-finger.
CHAIN 1 4383 Replicase polyprotein 1a.
/FTId=PRO_0000338242.
CHAIN 1 246 Non-structural protein 1. {ECO:0000250}.
/FTId=PRO_0000338243.
CHAIN 247 851 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000338244.
CHAIN 852 2750 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000338245.
CHAIN 2751 3246 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_0000338246.
CHAIN 3247 3549 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000338247.
CHAIN 3550 3836 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000338248.
CHAIN 3837 3925 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000338249.
CHAIN 3926 4122 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000338250.
CHAIN 4123 4232 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000338251.
CHAIN 4233 4369 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000338252.
CHAIN 4370 4383 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338253.
TRANSMEM 2138 2158 Helical. {ECO:0000255}.
TRANSMEM 2199 2219 Helical. {ECO:0000255}.
TRANSMEM 2221 2241 Helical. {ECO:0000255}.
TRANSMEM 2313 2333 Helical. {ECO:0000255}.
TRANSMEM 2343 2363 Helical. {ECO:0000255}.
TRANSMEM 2365 2385 Helical. {ECO:0000255}.
TRANSMEM 2752 2772 Helical. {ECO:0000255}.
TRANSMEM 2824 2844 Helical. {ECO:0000255}.
TRANSMEM 3009 3029 Helical. {ECO:0000255}.
TRANSMEM 3031 3051 Helical. {ECO:0000255}.
TRANSMEM 3063 3083 Helical. {ECO:0000255}.
TRANSMEM 3090 3110 Helical. {ECO:0000255}.
TRANSMEM 3115 3135 Helical. {ECO:0000255}.
TRANSMEM 3558 3578 Helical. {ECO:0000255}.
TRANSMEM 3588 3608 Helical. {ECO:0000255}.
TRANSMEM 3615 3635 Helical. {ECO:0000255}.
TRANSMEM 3657 3677 Helical. {ECO:0000255}.
TRANSMEM 3684 3704 Helical. {ECO:0000255}.
TRANSMEM 3711 3731 Helical. {ECO:0000255}.
TRANSMEM 3755 3775 Helical. {ECO:0000255}.
DOMAIN 1036 1274 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1275 1435 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1631 1892 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3247 3549 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1151 1179 C4-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 1749 1785 C4-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4306 4322 {ECO:0000250}.
ZN_FING 4348 4361 {ECO:0000250}.
REGION 2138 2385 HD1. {ECO:0000250}.
REGION 2752 3135 HD2. {ECO:0000250}.
REGION 3319 3775 HD3. {ECO:0000250}.
ACT_SITE 1074 1074 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1225 1225 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1671 1671 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1828 1828 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3287 3287 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3391 3391 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
SITE 246 247 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 851 852 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 2750 2751 Cleavage; by PL2-PRO. {ECO:0000250}.
SITE 3246 3247 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3549 3550 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3836 3837 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3925 3926 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4122 4123 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4232 4233 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4369 4370 Cleavage; by 3CL-PRO. {ECO:0000250}.
VARIANT 88 88 H -> D (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 207 207 C -> R (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 291 291 P -> L (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 317 317 C -> R (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 356 356 F -> V (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 545 545 I -> L (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 762 762 D -> N (in strain: Isolate 87309 Belgium
2003).
VARIANT 953 953 F -> L (in strain: ATCC VR-759, Isolate
clinical OC43-Paris and Isolate 87309
Belgium 2003).
VARIANT 989 989 I -> V (in strain: ATCC VR-759, Isolate
clinical OC43-Paris and Isolate 87309
Belgium 2003).
VARIANT 1305 1305 V -> A (in strain: ATCC VR-759, Isolate
clinical OC43-Paris and Isolate 87309
Belgium 2003).
VARIANT 1328 1328 N -> D (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 1379 1379 F -> L (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 1504 1504 L -> V (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 1740 1740 G -> E (in strain: Isolate 87309 Belgium
2003).
VARIANT 1825 1825 N -> K (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 1936 1936 S -> A (in strain: ATCC VR-759, Isolate
clinical OC43-Paris and Isolate 87309
Belgium 2003).
VARIANT 1965 1965 N -> T (in strain: ATCC VR-759, Isolate
clinical OC43-Paris).
VARIANT 2004 2004 L -> S (in strain: ATCC VR-759, Isolate
clinical OC43-Paris and Isolate 87309
Belgium 2003).
VARIANT 2022 2022 S -> G (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 2138 2140 TSA -> ISV (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 2256 2256 I -> M (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 2257 2257 Q -> H (in strain: Isolate 87309 Belgium
2003).
VARIANT 2386 2386 K -> R (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 2500 2500 I -> T (in strain: ATCC VR-759, Isolate
clinical OC43-Paris and Isolate 87309
Belgium 2003).
VARIANT 2921 2921 D -> E (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 2961 2961 V -> I (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 3086 3086 T -> I (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 3440 3440 P -> L (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 3451 3451 L -> V (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 3466 3466 I -> V (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 4067 4067 I -> V (in strain: ATCC VR-759 and
Isolate clinical OC43-Paris).
VARIANT 4071 4071 I -> V (in strain: ATCC VR-759, Isolate
clinical OC43-Paris and Isolate 87309
Belgium 2003).
CONFLICT 426 426 I -> M (in Ref. 3). {ECO:0000305}.
CONFLICT 813 813 D -> A (in Ref. 3). {ECO:0000305}.
CONFLICT 4376 4377 LN -> FK (in Ref. 2). {ECO:0000305}.
SEQUENCE 4383 AA; 491305 MW; 264040B0DDCDF54E CRC64;
MSKINKYGLE LHWAPEFPWM FEDAEEKLDN PSSSEVDMIC STTAQKLETD GICPENHVMV
DCRRLLKQEC CVQSSLIREI VMNASPYHLE VLLQDALQSR EAVLVTTPLG MSLEACYVRG
CNPKGWTMGL FRRRSVCNTG RCTVNKHVAY QLYMIDPAGV CLGAGQFVGW VIPLAFMPVQ
SRKFIVPWVM YLRKRGEKGA YNKDHGCGGF GHVYDFKVED AYDQVHDEPK GKFSKKAYAL
IRGYRGVKPL LYVDQYGCDY TGSLADGLEA YADKTLQEMK ALFPTWSQEL PFDVIVAWHV
VRDPRYVMRL QSAATICSVA YVANPTEDLC DGSVVIKEPV HVYADDSIIL RQYNLFDIMS
HFYMEADTVV NAFYGVALKD CGFVMQFGYI DCEQDSCDFK GWIPGNMIDG FACTTCGHVY
EVGDLIAQSS GVLPVNPVLH TKSAAGYGGF GCKDSFTLYG QTVVYFGGCV YWSPARNIWI
PILKSSVKSY DSLVYTGVLG CKAIVKETNL ICKALYLDYV QHKCGNLHQR ELLGVSDVWH
KQLLINRGVY KPLLENIDYF NMRRAKFSLE TFTVCADGFM PFLLDDLVPR AYYLAVSGQA
FCDYADKLCH AVVSKSKELL DVSLDSLGAA IHYLNSKIVD LAQHFSDFGT SFVSKIVHFF
KTFTTSTALA FAWVLFHVLH GAYIVVESDI YFVKNIPRYA SAVAQAFQSV AKVVLDSLRV
TFIDGLSCFK IGRRRICLSG RKIYEVERGL LHSSQLPLDV YDLTMPSQVQ KAKQKPIYLK
GSGSDFSLAD SVVEVVTTSL TPCGYSEPPK VADKICIVDN VYMAKAGDKY YPVVVDDHVG
LLDQAWRVPC AGRRVTFKEQ PTVKEIISMP KIIKVFYELD NDFNTILNTA CGVFEVDDTV
DMEEFYAVVI DAIEEKLSPC KELEGVGAKV SAFLQKLEDN PLFLFDEAGE EVFAPKLYCA
FTAPEDDDFL EESDVEEDDV EGEETDLTIT SAGQPCVASE QEESSEVLED TLDDGPSVET
SDSQVEEDVE MSDFVDLESV IQDYENVCFE FYTTEPEFVK VLGLYVPKAT RNNCWLRSVL
AVMQKLPCQF KDKNLQDLWV LYKQQYSQLF VDTLVNKIPA NIVLPQGGYV ADFAYWFLTL
CDWQCVAYWK CIKCDLALKL KGLDAMFFYG DVVSHICKCG ESMVLIDVDV PFTAHFALKD
KLFCAFITKR IVYKAACVVD VNDSHSMAVV DGKQIDDHRI TSITSDKFDF IIGHGMSFSM
TTFEIAQLYG SCITPNVCFV KGDIIKVSKL VKAEVVVNPA NGHMVHGGGV AKAIAVAAGQ
QFVKETTNMV KSKGVCATGD CYVSTGGKLC KTVLNVVGPD ARTQGKQSYV LLERVYKHFN
NYDCVVTTLI SAGIFSVPSD VSLTYLLGTA KKQVVLVSNN QEDFDLISKC QITAVEGTKK
LAARLSFNVG RSIVYETDAN KLILINDVAF VSTFNVLQDV LSLRHDIALD DDARTFVQSN
VDVLPEGWRV VNKFYQINGV RTVKYFECTG GIDICSQDKV FGYVQQGIFN KATVAQIKAL
FLDKVDILLT VDGVNFTNRF VPVGESFGKS LGNVFCDGVN VTKHKCDINY KGKVFFQFDN
LSSEDLKAVR SSFNFDQKEL LAYYNMLVNC FKWQVVVNGK YFTFKQANNN CFVNVSCLML
QSLHLTFKIV QWQEAWLEFR SGRPARFVAL VLAKGGFKFG DPADSRDFLR VVFSQVDLTG
AICDFEIACK CGVKQEQRTG LDAVMHFGTL SREDLEIGYT VDCSCGKKLI HCVRFDVPFL
ICSNTPASVK LPKGVGSANI FIGDNVGHYV HVKCEQSYQL YDASNVKKVT DVTGKLSDCL
YLKNLKQTFK SVLTTYYLDD VKKIEYKPDL SQYYCDGGKY YTQRIIKAQF KTFEKVDGVY
TNFKLIGHTV CDSLNSKLGF DSSKEFVEYK ITEWPTATGD VVLANDDLYV KRYERGCITF
GKPVIWLSHE KASLNSLTYF NRPLLVDDNK FDVLKVDDVD DSGDSSESGA KETKEINIIK
LSGVKKPFKV EDSVIVNDDT SETKYVKSLS IVDVYDMWLT GCKYVVRTAN ALSRAVNVPT
IRKFIKFGMT LVSIPIDLLN LREIKPAVNV VKAVRNKTSA CFNFIKWLFV LLFGWIKISA
DNKVIYTTEI ASKLTCKLVA LAFKNAFLTF KWSMVARGAC IIATIFLLWF NFIYANVIFS
DFYLPKIGFL PTFVGKIAQW IKNTFSLVTI CDLYSIQDVG FKNQYCNGSI ACQFCLAGFD
MLDNYKAIDV VQYEADRRAF VDYTGVLKIV IELIVSYALY TAWFYPLFAL ISIQILTTWL
PELFMLSTLH WSFRLLVALA NMLPAHVFMR FYIIIASFIK LFSLFKHVAY GCSKSGCLFC
YKRNRSLRVK CSTIVGGMIR YYDVMANGGT GFCSKHQWNC IDCDSYKPGN TFITVEAALD
LSKELKRPIQ PTDVAYHTVT DVKQVGCSMR LFYDRDGQRI YDDVNASLFV DYSNLLHSKV
KSVPNMHVVV VENDADKANF LNAAVFYAQS LFRPILMVDK NLITTANTGT SVTETMFDVY
VDTFLSMFDV DKKSLNALIA TAHSSIKQGT QIYKVLDTFL SCARKSCSID SDVDTKCLAD
SVMSAVSAGL ELTDESCNNL VPTYLKSDNI VAADLGVLIQ NSAKHVQGNV AKIAGVSCIW
SVDAFNQFSS DFQHKLKKAC CKTGLKLKLT YNKQMANVSV LTTPFSLKGG AVFSYFVYVC
FVLSLVCFIG LWCLMPTYTV HKSDFQLPVY ASYKVLDNGV IRDVSVEDVC FANKFEQFDQ
WYESTFGLSY YSNSMACPIV VAVIDQDFGS TVFNVPTKVL RYGYHVLHFI THALSADGVQ
CYTPHSQISY SNFYASGCVL SSACTMFTMA DGSPQPYCYT DGLMQNASLY SSLVPHVRYN
LANAKGFIRF PEVLREGLVR VVRTRSMSYC RVGLCEEADE GICFNFNGSW VLNNDYYRSL
PGTFCGRDVF DLIYQLFKGL AQPVDFLALT ASSIAGAILA VIVVLVFYYL IKLKRAFGDY
TSVVFVNVIV WCVNFMMLFV FQVYPTLSCV YAICYFYATL YFPSEISVIM HLQWLVMYGT
IMPLWFCLLY IAVVVSNHAF WVFSYCRKLG TSVRSDGTFE EMALTTFMIT KDSYCKLKNS
LSDVAFNRYL SLYNKYRYYS GKMDTAAYRE AACSQLAKAM DTFTNNNGSD VLYQPPTASV
STSFLQSGIV KMVNPTSKVE PCVVSVTYGN MTLNGLWLDD KVYCPRHVIC SASDMTNPDY
TNLLCRVTSS DFTVLFDRLS LTVMSYQMRG CMLVLTVTLQ NSRTPKYTFG VVKPGETFTV
LAAYNGKPQG AFHVTMRSSY TIKGSFLCGS CGSVGYVIMG DCVKFVYMHQ LELSTGCHTG
TDFNGDFYGP YKDAQVVQLP IQDYIQSVNF LAWLYAAILN NCNWFIQSDK CSVEDFNVWA
LSNGFSQVKS DLVIDALASM TGVSLETLLA AIKRLKNGFQ GRQIMGSCSF EDELTPSDVY
QQLAGIKLQS KRTRLFKGTV CWIMASTFLF SCIITAFVKW TMFMYVTTNM FSITFCALCV
ISLAMLLVKH KHLYLTMYIT PVLFTLLYNN YLVVYKHTFR GYVYAWLSYY VPSVEYTYTD
EVIYGMLLLV GMVFVTLRSI NHDLFSFIMF VGRLISVFSL WYKGSNLEEE ILLMLASLFG
TYTWTTVLSM AVAKVIAKWV AVNVLYFTDI PQIKIVLLCY LFIGYIISCY WGLFSLMNSL
FRMPLGVYNY KISVQELRYM NANGLRPPKN SFEALMLNFK LLGIGGVPII EVSQFQSKLT
DVKCANVVLL NCLQHLHVAS NSKLWHYCST LHNEILATSD LSVAFEKLAQ LLIVLFANPA
AVDSKCLTSI EEVCDDYAKD NTVLQALQSE FVNMASFVEY EVAKKNLDEA RFSGSANQQQ
LKQLEKACNI AKSAYERDRA VAKKLERMAD LALTNMYKEA RINDKKSKVV SALQTMLFSM
VRKLDNQALN SILDNAVKGC VPLNAIPSLA ANTLNIIVPD KSVYDQIVDN IYVTYAGNVW
QIQTIQDSDG TNKQLNEISD DCNWPLVIIA NRYNEVSATV LQNNELMPAK LKIQVVNSGP
DQTCNTPTQC YYNNSNNGKI VYAILSDVDG LKYTKILKDD GNFVVLELDP PCKFTVQDAK
GLKIKYLYFV KGCNTLARGW VVGTISSTVR LQAGTATEYA SNSSILSLCA FSVDPKKTYL
DFIQQGGTPI ANCVKMLCDH AGTGMAITVK PDATTSQDSY GGASVCIYCR ARVEHPDVDG
LCKLRGKFVQ VPVGIKDPVS YVLTHDVCRV CGFWRDGSCS CVSTDTTVQS KDTNFLNGFG
VRV


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