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Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p9); Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p34); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p5); Non-structural protein 8 (nsp8) (p23); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); Non-structural protein 11 (nsp11)]

 R1A_CVH22               Reviewed;        4085 AA.
P0C6U2; Q05002;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
23-MAY-2018, entry version 65.
RecName: Full=Replicase polyprotein 1a;
Short=pp1a;
AltName: Full=ORF1a polyprotein;
Contains:
RecName: Full=Non-structural protein 1;
Short=nsp1;
AltName: Full=p9;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p87;
Contains:
RecName: Full=Non-structural protein 3;
Short=nsp3;
EC=3.4.19.12;
EC=3.4.22.-;
AltName: Full=PL1-PRO/PL2-PRO;
AltName: Full=PLP1/PLP2;
AltName: Full=Papain-like proteinases 1/2;
AltName: Full=p195;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
AltName: Full=Peptide HD2;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=M-PRO;
AltName: Full=nsp5;
AltName: Full=p34;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
AltName: Full=p5;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
AltName: Full=p23;
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=p16;
Contains:
RecName: Full=Non-structural protein 11;
Short=nsp11;
ORFNames=1a;
Human coronavirus 229E (HCoV-229E).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Alphacoronavirus.
NCBI_TaxID=11137;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=11369870;
Thiel V., Herold J., Schelle B., Siddell S.G.;
"Infectious RNA transcribed in vitro from a cDNA copy of the human
coronavirus genome cloned in vaccinia virus.";
J. Gen. Virol. 82:1273-1281(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=8337838; DOI=10.1006/viro.1993.1419;
Herold J., Raabe T., Schelle-Prinz B., Siddell S.G.;
"Nucleotide sequence of the human coronavirus 229E RNA polymerase
locus.";
Virology 195:680-691(1993).
[3]
CHARACTERIZATION OF 3CL-PRO, AND MUTAGENESIS OF HIS-3006; HIS-3028;
ASN-3029; GLU-3074; THR-3099; CYS-3109; HIS-3127; HIS-3136 AND
GLN-3267.
PubMed=9094676;
Ziebuhr J., Heusipp G., Siddell S.G.;
"Biosynthesis, purification, and characterization of the human
coronavirus 229E 3C-like proteinase.";
J. Virol. 71:3992-3997(1997).
[4]
ZINC-FINGER DOMAIN OF PL1-PRO, AND MUTAGENESIS OF LYS-1048; GLY-1099;
GLY-1102; CYS-1126; CYS-1128; CYS-1154; LEU-1155; CYS-1157; CYS-1163;
VAL-1175; CYS-1203 AND ASP-1218.
PubMed=10329692; DOI=10.1074/jbc.274.21.14918;
Herold J., Siddell S.G., Gorbalenya A.E.;
"A human RNA viral cysteine proteinase that depends upon a unique
Zn2+-binding finger connecting the two domains of a papain-like
fold.";
J. Biol. Chem. 274:14918-14925(1999).
[5]
ERRATUM.
Herold J., Siddell S.G., Gorbalenya A.E.;
J. Biol. Chem. 274:21490-21490(1999).
[6]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=9847320;
Ziebuhr J., Siddell S.G.;
"Processing of the human coronavirus 229E replicase polyproteins by
the virus-encoded 3C-like proteinase: identification of proteolytic
products and cleavage sites common to pp1a and pp1ab.";
J. Virol. 73:177-185(1999).
[7]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND MUTAGENESIS OF CYS-1054 AND
TRP-1702.
PubMed=11431476; DOI=10.1074/jbc.M104097200;
Ziebuhr J., Thiel V., Gorbalenya A.E.;
"The autocatalytic release of a putative RNA virus transcription
factor from its polyprotein precursor involves two paralogous papain-
like proteases that cleave the same peptide bond.";
J. Biol. Chem. 276:33220-33232(2001).
[8]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=11842254;
Hegyi A., Ziebuhr J.;
"Conservation of substrate specificities among coronavirus main
proteases.";
J. Gen. Virol. 83:595-599(2002).
[9]
MUTAGENESIS OF ASN-3029.
PubMed=11842253;
Hegyi A., Friebe A., Gorbalenya A.E., Ziebuhr J.;
"Mutational analysis of the active centre of coronavirus 3C-like
proteases.";
J. Gen. Virol. 83:581-593(2002).
[10]
X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 2966-3265.
PubMed=12746549; DOI=10.1126/science.1085658;
Anand K., Ziebuhr J., Wadhwani P., Mesters J.R., Hilgenfeld R.;
"Coronavirus main proteinase (3CLpro) structure: basis for design of
anti-SARS drugs.";
Science 300:1763-1767(2003).
-!- FUNCTION: The papain-like proteinase 1 (PLP1) and papain-like
proteinase 2 (PLP2) 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. PLP2 also antagonizes innate immune induction
of type I interferon by blocking the 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}.
-!- 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=P0C6U2-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6X1-1; 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. {ECO:0000269|PubMed:11431476,
ECO:0000269|PubMed:11842254, ECO:0000269|PubMed:9847320}.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Proteic grace - Issue
77 of December 2006;
URL="https://web.expasy.org/spotlight/back_issues/077";
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EMBL; AF304460; AAG48590.1; -; Genomic_RNA.
EMBL; X69721; CAA49377.1; -; Genomic_RNA.
PIR; S28600; S28600.
RefSeq; NP_073550.1; NC_002645.1. [P0C6U2-1]
PDB; 1P9S; X-ray; 2.54 A; A/B=2966-3265.
PDB; 2ZU2; X-ray; 1.80 A; A/B=2966-3267.
PDB; 3EWQ; X-ray; 2.10 A; A=1269-1436.
PDB; 3EWR; X-ray; 2.01 A; A=1269-1436.
PDBsum; 1P9S; -.
PDBsum; 2ZU2; -.
PDBsum; 3EWQ; -.
PDBsum; 3EWR; -.
ProteinModelPortal; P0C6U2; -.
SMR; P0C6U2; -.
PRIDE; P0C6U2; -.
GeneID; 918764; -.
OrthoDB; VOG09000000; -.
EvolutionaryTrace; P0C6U2; -.
Proteomes; UP000006716; 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: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: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; 2.30.30.1000; -; 1.
Gene3D; 2.40.10.250; -; 1.
InterPro; IPR038634; A-CoV_nsp1_sf.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR002589; Macro_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; IPR011050; Pectin_lyase_fold/virulence.
InterPro; IPR008740; Peptidase_C30.
InterPro; IPR013016; Peptidase_C30/C16.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF08716; nsp7; 1.
Pfam; PF08717; nsp8; 1.
Pfam; PF08710; nsp9; 1.
Pfam; PF05409; Peptidase_C30; 1.
Pfam; PF08715; Viral_protease; 2.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF101816; SSF101816; 1.
SUPFAM; SSF140367; SSF140367; 1.
SUPFAM; SSF143076; SSF143076; 1.
SUPFAM; SSF144246; SSF144246; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF51126; SSF51126; 1.
SUPFAM; SSF81665; SSF81665; 2.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51124; PEPTIDASE_C16; 2.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus;
Complete proteome; Host cytoplasm; Host membrane;
Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host IRF3 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 4085 Replicase polyprotein 1a.
/FTId=PRO_0000338182.
CHAIN 1 111 Non-structural protein 1.
/FTId=PRO_0000338183.
CHAIN 112 897 Non-structural protein 2.
/FTId=PRO_0000338184.
CHAIN 898 2484 Non-structural protein 3.
/FTId=PRO_0000338185.
CHAIN 2485 2965 Non-structural protein 4.
/FTId=PRO_0000338186.
CHAIN 2966 3267 3C-like proteinase.
/FTId=PRO_0000338187.
CHAIN 3268 3546 Non-structural protein 6.
/FTId=PRO_0000338188.
CHAIN 3547 3629 Non-structural protein 7.
/FTId=PRO_0000338189.
CHAIN 3630 3824 Non-structural protein 8.
/FTId=PRO_0000338190.
CHAIN 3825 3933 Non-structural protein 9.
/FTId=PRO_0000338191.
CHAIN 3934 4068 Non-structural protein 10.
/FTId=PRO_0000338192.
CHAIN 4069 4085 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338193.
TRANSMEM 1998 2018 Helical. {ECO:0000255}.
TRANSMEM 2068 2088 Helical. {ECO:0000255}.
TRANSMEM 2095 2115 Helical. {ECO:0000255}.
TRANSMEM 2491 2511 Helical. {ECO:0000255}.
TRANSMEM 2731 2751 Helical. {ECO:0000255}.
TRANSMEM 2755 2775 Helical. {ECO:0000255}.
TRANSMEM 2782 2802 Helical. {ECO:0000255}.
TRANSMEM 2809 2829 Helical. {ECO:0000255}.
TRANSMEM 2834 2854 Helical. {ECO:0000255}.
TRANSMEM 3281 3301 Helical. {ECO:0000255}.
TRANSMEM 3304 3324 Helical. {ECO:0000255}.
TRANSMEM 3328 3348 Helical. {ECO:0000255}.
TRANSMEM 3367 3387 Helical. {ECO:0000255}.
TRANSMEM 3401 3421 Helical. {ECO:0000255}.
TRANSMEM 3422 3442 Helical. {ECO:0000255}.
TRANSMEM 3467 3487 Helical. {ECO:0000255}.
DOMAIN 1016 1268 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1269 1436 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1663 1914 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 2966 3267 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1126 1157 C4-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 1780 1815 C4-type 2; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ZN_FING 4007 4023 {ECO:0000250}.
ZN_FING 4049 4062 {ECO:0000250}.
REGION 1925 2115 HD1.
REGION 2491 2854 HD2.
REGION 3281 3487 HD3.
ACT_SITE 1054 1054 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1205 1205 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1701 1701 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1863 1863 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3006 3006 For 3CL-PRO activity.
ACT_SITE 3109 3109 For 3CL-PRO activity.
SITE 111 112 Cleavage; by PL1-PRO.
SITE 897 898 Cleavage; by PL1-PRO.
SITE 2484 2485 Cleavage; by PL2-PRO.
SITE 2965 2966 Cleavage; by 3CL-PRO.
SITE 3267 3268 Cleavage; by 3CL-PRO.
SITE 3546 3547 Cleavage; by 3CL-PRO.
SITE 3629 3630 Cleavage; by 3CL-PRO.
SITE 3824 3825 Cleavage; by 3CL-PRO.
SITE 3933 3934 Cleavage; by 3CL-PRO.
SITE 4068 4069 Cleavage; by 3CL-PRO.
MUTAGEN 1048 1048 K->E: Complete loss of PL1-PRO activity.
{ECO:0000269|PubMed:10329692}.
MUTAGEN 1054 1054 C->A,G,S: Complete loss of PL1-PRO
activity. {ECO:0000269|PubMed:11431476}.
MUTAGEN 1099 1099 G->A: Complete loss of PL1-PRO activity.
{ECO:0000269|PubMed:10329692}.
MUTAGEN 1099 1099 G->P: No effect.
{ECO:0000269|PubMed:10329692}.
MUTAGEN 1102 1102 G->A,S: No effect.
{ECO:0000269|PubMed:10329692}.
MUTAGEN 1126 1126 C->D,H: Complete loss of PL1-PRO
activity. {ECO:0000269|PubMed:10329692}.
MUTAGEN 1128 1128 C->A,D,P: Complete loss of PL1-PRO
activity. {ECO:0000269|PubMed:10329692}.
MUTAGEN 1154 1154 C->A,H,D: Complete loss of PL1-PRO
activity. {ECO:0000269|PubMed:10329692}.
MUTAGEN 1155 1155 Missing: Complete loss of PL1-PRO
activity. {ECO:0000269|PubMed:10329692}.
MUTAGEN 1157 1157 C->A,D,H,P: Complete loss of PL1-PRO
activity. {ECO:0000269|PubMed:10329692}.
MUTAGEN 1163 1163 C->A,D: No effect.
{ECO:0000269|PubMed:10329692}.
MUTAGEN 1175 1175 V->H,P: Complete loss of PL1-PRO
activity. {ECO:0000269|PubMed:10329692}.
MUTAGEN 1175 1175 V->N,T: No effect.
{ECO:0000269|PubMed:10329692}.
MUTAGEN 1203 1203 C->A: Complete loss of PL1-PRO activity.
{ECO:0000269|PubMed:10329692}.
MUTAGEN 1203 1203 C->D: No effect.
{ECO:0000269|PubMed:10329692}.
MUTAGEN 1218 1218 D->A,E,H,K,N,Q: No effect.
{ECO:0000269|PubMed:10329692}.
MUTAGEN 1702 1702 W->L: Complete loss of PL2-PRO activity.
{ECO:0000269|PubMed:11431476}.
MUTAGEN 3006 3006 H->G,S,T,Y: Complete loss of 3CL-PRO
activity. {ECO:0000269|PubMed:9094676}.
MUTAGEN 3028 3028 H->G,T: No loss of 3CL-PRO activity.
{ECO:0000269|PubMed:9094676}.
MUTAGEN 3029 3029 N->A,D,E,Q: Increase of 3CL-PRO activity.
{ECO:0000269|PubMed:11842253,
ECO:0000269|PubMed:9094676}.
MUTAGEN 3029 3029 N->G: No loss of 3CL-PRO activity.
{ECO:0000269|PubMed:11842253,
ECO:0000269|PubMed:9094676}.
MUTAGEN 3029 3029 N->P: 95% loss of 3CL-PRO activity.
{ECO:0000269|PubMed:11842253,
ECO:0000269|PubMed:9094676}.
MUTAGEN 3074 3074 E->H: No loss of 3CL-PRO activity.
{ECO:0000269|PubMed:9094676}.
MUTAGEN 3099 3099 T->D: Complete loss of 3CL-PRO activity.
{ECO:0000269|PubMed:9094676}.
MUTAGEN 3109 3109 C->P,S,V: Complete loss of 3CL-PRO
activity. {ECO:0000269|PubMed:9094676}.
MUTAGEN 3127 3127 H->S: Complete loss of 3CL-PRO activity.
{ECO:0000269|PubMed:9094676}.
MUTAGEN 3136 3136 H->A: 67% loss of 3CL-PRO activity.
{ECO:0000269|PubMed:9094676}.
MUTAGEN 3136 3136 H->S: 77% loss of 3CL-PRO activity.
{ECO:0000269|PubMed:9094676}.
MUTAGEN 3136 3136 H->T: 93% loss of 3CL-PRO activity.
{ECO:0000269|PubMed:9094676}.
MUTAGEN 3267 3267 Q->A: No loss of 3CL-PRO activity.
{ECO:0000269|PubMed:9094676}.
CONFLICT 1982 1982 A -> Q (in Ref. 1). {ECO:0000305}.
CONFLICT 4042 4042 F -> S (in Ref. 1). {ECO:0000305}.
STRAND 1275 1278 {ECO:0000244|PDB:3EWR}.
STRAND 1281 1285 {ECO:0000244|PDB:3EWR}.
HELIX 1288 1294 {ECO:0000244|PDB:3EWR}.
STRAND 1298 1304 {ECO:0000244|PDB:3EWR}.
HELIX 1313 1321 {ECO:0000244|PDB:3EWR}.
TURN 1322 1324 {ECO:0000244|PDB:3EWR}.
HELIX 1325 1333 {ECO:0000244|PDB:3EWR}.
STRAND 1345 1350 {ECO:0000244|PDB:3EWR}.
STRAND 1353 1359 {ECO:0000244|PDB:3EWR}.
HELIX 1367 1380 {ECO:0000244|PDB:3EWR}.
STRAND 1381 1383 {ECO:0000244|PDB:3EWR}.
STRAND 1385 1387 {ECO:0000244|PDB:3EWR}.
HELIX 1399 1409 {ECO:0000244|PDB:3EWR}.
STRAND 1415 1419 {ECO:0000244|PDB:3EWR}.
HELIX 1422 1433 {ECO:0000244|PDB:3EWR}.
HELIX 2976 2979 {ECO:0000244|PDB:2ZU2}.
STRAND 2982 2987 {ECO:0000244|PDB:2ZU2}.
STRAND 2990 2997 {ECO:0000244|PDB:2ZU2}.
STRAND 3000 3004 {ECO:0000244|PDB:2ZU2}.
HELIX 3005 3008 {ECO:0000244|PDB:2ZU2}.
HELIX 3018 3024 {ECO:0000244|PDB:2ZU2}.
HELIX 3027 3029 {ECO:0000244|PDB:2ZU2}.
STRAND 3030 3034 {ECO:0000244|PDB:2ZU2}.
STRAND 3037 3039 {ECO:0000244|PDB:2ZU2}.
STRAND 3041 3047 {ECO:0000244|PDB:2ZU2}.
STRAND 3050 3057 {ECO:0000244|PDB:2ZU2}.
STRAND 3064 3067 {ECO:0000244|PDB:2ZU2}.
STRAND 3075 3093 {ECO:0000244|PDB:2ZU2}.
STRAND 3112 3117 {ECO:0000244|PDB:2ZU2}.
STRAND 3120 3130 {ECO:0000244|PDB:2ZU2}.
STRAND 3136 3139 {ECO:0000244|PDB:2ZU2}.
HELIX 3146 3148 {ECO:0000244|PDB:2ZU2}.
STRAND 3151 3154 {ECO:0000244|PDB:2ZU2}.
HELIX 3165 3177 {ECO:0000244|PDB:2ZU2}.
HELIX 3191 3199 {ECO:0000244|PDB:2ZU2}.
TURN 3200 3202 {ECO:0000244|PDB:2ZU2}.
HELIX 3209 3212 {ECO:0000244|PDB:2ZU2}.
HELIX 3213 3219 {ECO:0000244|PDB:2ZU2}.
HELIX 3223 3233 {ECO:0000244|PDB:2ZU2}.
STRAND 3245 3247 {ECO:0000244|PDB:2ZU2}.
HELIX 3254 3262 {ECO:0000244|PDB:2ZU2}.
SEQUENCE 4085 AA; 454215 MW; EAB38E3D375F36B5 CRC64;
MACNRVTLAV ASDSEISANG CSTIAQAVRR YSEAASNGFR ACRFVSLDLQ DCIVGIADDT
YVMGLHGNQT LFCNIMKFSD RPFMLHGWLV FSNSNYLLEE FDVVFGKRGG GNVTYTDQYL
CGADGKPVMS EDLWQFVDHF GENEEIIING HTYVCAWLTK RKPLDYKRQN NLAIEEIEYV
HGDALHTLRN GSVLEMAKEV KTSSKVVLSD ALDKLYKVFG SPVMTNGSNI LEAFTKPVFI
SALVQCTCGT KSWSVGDWTG FKSSCCNVIS NKLCVVPGNV KPGDAVITTQ QAGAGIKYFC
GMTLKFVANI EGVSVWRVIA LQSVDCFVAS STFVEEEHVN RMDTFCFNVR NSVTDECRLA
MLGAEMTSNV RRQVASGVID ISTGWFDVYD DIFAESKPWF VRKAEDIFGP CWSALASALK
QLKVTTGELV RFVKSICNSA VAVVGGTIQI LASVPEKFLN AFDVFVTAIQ TVFDCAVETC
TIAGKAFDKV FDYVLLDNAL VKLVTTKLKG VRERGLNKVK YATVVVGSTE EVKSSRVERS
TAVLTIANNY SKLFDEGYTV VIGDVAYFVS DGYFRLMASP NSVLTTAVYK PLFAFNVNVM
GTRPEKFPTT VTCENLESAV LFVNDKITEF QLDYSIDVID NEIIVKPNIS LCVPLYVRDY
VDKWDDFCRQ YSNESWFEDD YRAFISVLDI TDAAVKAAES KAFVDTIVPP CPSILKVIDG
GKIWNGVIKN VNSVRDWLKS LKLNLTQQGL LGTCAKRFKR WLGILLEAYN AFLDTVVSTV
KIGGLTFKTY AFDKPYIVIR DIVCKVENKT EAEWIELFPH NDRIKSFSTF ESAYMPIADP
THFDIEEVEL LDAEFVEPGC GGILAVIDEH VFYKKDGVYY PSNGTNILPV AFTKAAGGKV
SFSDDVEVKD IEPVYRVKLC FEFEDEKLVD VCEKAIGKKI KHEGDWDSFC KTIQSALSVV
SCYVNLPTYY IYDEEGGNDL SLPVMISEWP LSVQQAQQEA TLPDIAEDVV DQVEEVNSIF
DIETVDVKHD VSPFEMPFEE LNGLKILKQL DNNCWVNSVM LQIQLTGILD GDYAMQFFKM
GRVAKMIERC YTAEQCIRGA MGDVGLCMYR LLKDLHTGFM VMDYKCSCTS GRLEESGAVL
FCTPTKKAFP YGTCLNCNAP RMCTIRQLQG TIIFVQQKPE PVNPVSFVVK PVCSSIFRGA
VSCGHYQTNI YSQNLCVDGF GVNKIQPWTN DALNTICIKD ADYNAKVEIS VTPIKNTVDT
TPKEEFVVKE KLNAFLVHDN VAFYQGDVDT VVNGVDFDFI VNAANENLAH GGGLAKALDV
YTKGKLQRLS KEHIGLAGKV KVGTGVMVEC DSLRIFNVVG PRKGKHERDL LIKAYNTINN
EQGTPLTPIL SCGIFGIKLE TSLEVLLDVC NTKEVKVFVY TDTEVCKVKD FVSGLVNVQK
VEQPKIEPKP VSVIKVAPKP YRVDGKFSYF TEDLLCVADD KPIVLFTDSM LTLDDRGLAL
DNALSGVLSA AIKDCVDINK AIPSGNLIKF DIGSVVVYMC VVPSEKDKHL DNNVQRCTRK
LNRLMCDIVC TIPADYILPL VLSSLTCNVS FVGELKAAEA KVITIKVTED GVNVHDVTVT
TDKSFEQQVG VIADKDKDLS GAVPSDLNTS ELLTKAIDVD WVEFYGFKDA VTFATVDHSA
FAYESAVVNG IRVLKTSDNN CWVNAVCIAL QYSKPHFISQ GLDAAWNKFV LGDVEIFVAF
VYYVARLMKG DKGDAEDTLT KLSKYLANEA QVQLEHYSSC VECDAKFKNS VASINSAIVC
ASVKRDGVQV GYCVHGIKYY SRVRSVRGRA IIVSVEQLEP CAQSRLLSGV AYTAFSGPVD
KGHYTVYDTA KKSMYDGDRF VKHDLSLLSV TSVVMVGGYV APVNTVKPKP VINQLDEKAQ
KFFDFGDFLI HNFVIFFTWL LSMFTLCKTA VTTGDVKIMA KAPQRTGVVL KRSLKYNLKA
SAAVLKSKWW LLAKFTKLLL LIYTLYSVVL LCVRFGPFNF CSETVNGYAK SNFVKDDYCD
GSLGCKMCLF GYQELSQFSH LDVVWKHITD PLFSNMQPFI VMVLLLIFGD NYLRCFLLYF
VAQMISTVGV FLGYKETNWF LHFIPFDVIC DELLVTVIVI KVISFVRHVL FGCENPDCIA
CSKSARLKRF PVNTIVNGVQ RSFYVNANGG SKFCKKHRFF CVDCDSYGYG STFITPEVSR
ELGNITKTNV QPTGPAYVMI DKVEFENGFY RLYSCETFWR YNFDITESKY SCKEVFKNCN
VLDDFIVFNN NGTNVTQVKN ASVYFSQLLC RPIKLVDSEL LSTLSVDFNG VLHKAYIDVL
RNSFGKDLNA NMSLAECKRA LGLSISDHEF TSAISNAHRC DVLLSDLSFN NFVSSYAKPE
EKLSAYDLAC CMRAGAKVVN ANVLTKDQTP IVWHAKDFNS LSAEGRKYIV KTSKAKGLTF
LLTINENQAV TQIPATSIVA KQGAGDAGHS LTWLWLLCGL VCLIQFYLCF FMPYFMYDIV
SSFEGYDFKY IENGQLKNFE APLKCVRNVF ENFEDWHYAK FGFTPLNKQS CPIVVGVSEI
VNTVAGIPSN VYLVGKTLIF TLQAAFGNAG VCYDIFGVTT PEKCIFTSAC TRLEGLGGNN
VYCYNTALME GSLPYSSIQA NAYYKYDNGN FIKLPEVIAQ GFGFRTVRTI ATKYCRVGEC
VESNAGVCFG FDKWFVNDGR VANGYVCGTG LWNLVFNILS MFSSSFSVAA MSGQILLNCA
LGAFAIFCCF LVTKFRRMFG DLSVGVCTVV VAVLLNNVSY IVTQNLVTMI AYAILYFFAT
RSLRYAWIWC AAYLIAYISF APWWLCAWYF LAMLTGLLPS LLKLKVSTNL FEGDKFVGTF
ESAAAGTFVI DMRSYEKLAN SISPEKLKSY AASYNRYKYY SGNANEADYR CACYAYLAKA
MLDFSRDHND ILYTPPTVSY GSTLQAGLRK MAQPSGFVEK CVVRVCYGNT VLNGLWLGDI
VYCPRHVIAS NTTSAIDYDH EYSIMRLHNF SIISGTAFLG VVGATMHGVT LKIKVSQTNM
HTPRHSFRTL KSGEGFNILA CYDGCAQGVF GVNMRTNWTI RGSFINGACG SPGYNLKNGE
VEFVYMHQIE LGSGSHVGSS FDGVMYGGFE DQPNLQVESA NQMLTVNVVA FLYAAILNGC
TWWLKGEKLF VEHYNEWAQA NGFTAMNGED AFSILAAKTG VCVERLLHAI QVLNNGFGGK
QILGYSSLND EFSINEVVKQ MFGVNLQSGK TTSMFKSISL FAGFFVMFWA ELFVYTTTIW
VNPGFLTPFM ILLVALSLCL TFVVKHKVLF LQVFLLPSII VAAIQNCAWD YHVTKVLAEK
FDYNVSVMQM DIQGFVNIFI CLFVALLHTW RFAKERCTHW CTYLFSLIAV LYTALYSYDY
VSLLVMLLCA ISNEWYIGAI IFRICRFGVA FLPVEYVSYF DGVKTVLLFY MLLGFVSCMY
YGLLYWINRF CKCTLGVYDF CVSPAEFKYM VANGLNAPNG PFDALFLSFK LMGIGGPRTI
KVSTVQSKLT DLKCTNVVLM GILSNMNIAS NSKEWAYCVE MHNKINLCDD PETAQELLLA
LLAFFLSKHS DFGLGDLVDS YFENDSILQS VASSFVGMPS FVAYETARQE YENAVANGSS
PQIIKQLKKA MNVAKAEFDR ESSVQKKINR MAEQAAAAMY KEARAVNRKS KVVSAMHSLL
FGMLRRLDMS SVDTILNMAR NGVVPLSVIP ATSAARLVVV VPDHDSFVKM MVDGFVHYAG
VVWTLQEVKD NDGKNVHLKD VTKENQEILV WPLILTCERV VKLQNNEIMP GKMKVKATKG
EGDGGITSEG NALYNNEGGR AFMYAYVTTK PGMKYVKWEH DSGVVTVELE PPCRFVIDTP
TGPQIKYLYF VKNLNNLRRG AVLGYIGATV RLQAGKQTEF VSNSHLLTHC SFAVDPAAAY
LDAVKQGAKP VGNCVKMLTN GSGSGQAITC TIDSNTTQDT YGGASVCIYC RAHVAHPTMD
GFCQYKGKWV QVPIGTNDPI RFCLENTVCK VCGCWLNHGC TCDRTAIQSF DNSYLNESGA
LVPLD


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