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 R1AB_CVH22              Reviewed;        6758 AA.
P0C6X1; Q05002; Q9DLN0; Q9DLN1;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
22-NOV-2017, entry version 80.
RecName: Full=Replicase polyprotein 1ab;
Short=pp1ab;
AltName: Full=ORF1ab 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=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=p66;
AltName: Full=p66-HEL;
Contains:
RecName: Full=Exoribonuclease;
Short=ExoN;
EC=3.1.13.-;
AltName: Full=nsp14;
Contains:
RecName: Full=Uridylate-specific endoribonuclease;
EC=3.1.-.-;
AltName: Full=NendoU;
AltName: Full=nsp15;
AltName: Full=p41;
Contains:
RecName: Full=Putative 2'-O-methyl transferase;
EC=2.1.1.-;
AltName: Full=nsp16;
Name=rep; ORFNames=1a-1b;
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] OF 1-4085.
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]
CHARACTERIZATION OF P41, AND SUBCELLULAR LOCATION.
PubMed=9367364; DOI=10.1099/0022-1317-78-11-2789;
Heusipp G., Groetzinger C., Herold J., Siddell S.G., Ziebuhr J.;
"Identification and subcellular localization of a 41 kDa, polyprotein
1ab processing product in human coronavirus 229E-infected cells.";
J. Gen. Virol. 78:2789-2794(1997).
[5]
CHARACTERIZATION OF HELICASE, AND MUTAGENESIS OF LYS-5284.
PubMed=10917600; DOI=10.1017/S1355838200000728;
Seybert A., Hegyi A., Siddell S.G., Ziebuhr J.;
"The human coronavirus 229E superfamily 1 helicase has RNA and DNA
duplex-unwinding activities with 5'-to-3' polarity.";
RNA 6:1056-1068(2000).
[6]
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).
[7]
ERRATUM.
Herold J., Siddell S.G., Gorbalenya A.E.;
J. Biol. Chem. 274:21490-21490(1999).
[8]
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).
[9]
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).
[10]
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).
[11]
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).
[12]
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 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.
-!- 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: The helicase which contains a zinc finger structure
displays RNA and DNA duplex-unwinding activities with 5' to 3'
polarity. Its ATPase activity is strongly stimulated by poly(U),
poly(dT), poly(C), poly(dA), but not by poly(G).
-!- FUNCTION: The exoribonuclease acts on both ssRNA and dsRNA in a 3'
to 5' direction. {ECO:0000250}.
-!- 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: NendoU is a Mn(2+)-dependent, uridylate-specific enzyme,
which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.
{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).
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- 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}.
-!- SUBCELLULAR LOCATION: Helicase: Host endoplasmic reticulum-Golgi
intermediate compartment {ECO:0000305}. Note=The helicase
interacts with the N protein in membranous complexes and
colocalizes with sites of synthesis of new viral RNA.
{ECO:0000250}.
-!- 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=P0C6X1-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6U2-1; 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. {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; AAG48591.1; -; Genomic_RNA.
PIR; S28600; S28600.
RefSeq; NP_073549.1; NC_002645.1. [P0C6X1-1]
PDB; 1P9S; X-ray; 2.54 A; A/B=2966-3265.
PDB; 2J97; X-ray; 1.75 A; A=3825-3933.
PDB; 2J98; X-ray; 1.80 A; A=3825-3933, B=3830-3933.
PDB; 3EJG; X-ray; 1.78 A; A=1270-1434.
PDB; 4RS4; X-ray; 2.96 A; A/B/C/D/E/F=6111-6458.
PDB; 4S1T; X-ray; 2.50 A; A/B/C/D/E/F=6111-6458.
PDBsum; 1P9S; -.
PDBsum; 2J97; -.
PDBsum; 2J98; -.
PDBsum; 3EJG; -.
PDBsum; 4RS4; -.
PDBsum; 4S1T; -.
ProteinModelPortal; P0C6X1; -.
SMR; P0C6X1; -.
GeneID; 918764; -.
KEGG; vg:918764; -.
OrthoDB; VOG09000000; -.
BRENDA; 3.6.4.12; 8801.
EvolutionaryTrace; P0C6X1; -.
Proteomes; UP000006716; 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: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:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
Gene3D; 2.40.10.250; -; 1.
InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR009461; Coronavirus_NSP16.
InterPro; IPR027352; CV_ZBD.
InterPro; IPR037227; EndoU-like.
InterPro; IPR002589; Macro_dom.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR009466; NSP11.
InterPro; IPR014828; NSP7.
InterPro; IPR037204; NSP7_sf.
InterPro; IPR014829; NSP8.
InterPro; IPR037230; NSP8_sf.
InterPro; IPR014822; NSP9.
InterPro; IPR036499; NSP9_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008740; Peptidase_C30.
InterPro; IPR013016; Peptidase_C30/C16.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR009469; RNA_pol_N_coronovir.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF06478; Corona_RPol_N; 1.
Pfam; PF01661; Macro; 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; PF05409; Peptidase_C30; 1.
Pfam; PF08715; Viral_protease; 2.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF101816; SSF101816; 1.
SUPFAM; SSF140367; SSF140367; 1.
SUPFAM; SSF142877; SSF142877; 1.
SUPFAM; SSF143076; SSF143076; 1.
SUPFAM; SSF144246; SSF144246; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF53335; SSF53335; 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.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Complete proteome; Endonuclease; Exonuclease; Helicase;
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;
Methyltransferase;
Modulation of host ubiquitin pathway by viral deubiquitinase;
Modulation of host ubiquitin pathway by virus; Nuclease;
Nucleotide-binding; Nucleotidyltransferase; Protease;
Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
RNA-directed RNA polymerase; Thiol protease; Transferase;
Transmembrane; Transmembrane helix; Ubl conjugation pathway;
Viral immunoevasion; Viral RNA replication; Zinc; Zinc-finger.
CHAIN 1 111 Non-structural protein 1.
/FTId=PRO_0000037293.
CHAIN 112 897 Non-structural protein 2.
/FTId=PRO_0000037294.
CHAIN 898 2484 Non-structural protein 3.
/FTId=PRO_0000037295.
CHAIN 2485 2965 Non-structural protein 4.
/FTId=PRO_0000037296.
CHAIN 2966 3267 3C-like proteinase.
/FTId=PRO_0000037297.
CHAIN 3268 3546 Non-structural protein 6.
/FTId=PRO_0000037298.
CHAIN 3547 3629 Non-structural protein 7.
/FTId=PRO_0000037299.
CHAIN 3630 3824 Non-structural protein 8.
/FTId=PRO_0000037300.
CHAIN 3825 3933 Non-structural protein 9.
/FTId=PRO_0000037301.
CHAIN 3934 4068 Non-structural protein 10.
/FTId=PRO_0000037302.
CHAIN 4069 4995 RNA-directed RNA polymerase.
/FTId=PRO_0000037303.
CHAIN 4996 5592 Helicase.
/FTId=PRO_0000037304.
CHAIN 5593 6110 Exoribonuclease. {ECO:0000250}.
/FTId=PRO_0000037305.
CHAIN 6111 6458 Uridylate-specific endoribonuclease.
{ECO:0000250}.
/FTId=PRO_0000037306.
CHAIN 6459 6758 Putative 2'-O-methyl transferase.
{ECO:0000250}.
/FTId=PRO_0000037307.
TRANSMEM 1925 1945 Helical. {ECO:0000255}.
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}.
DOMAIN 4675 4837 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 4996 5079 CV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
DOMAIN 5253 5434 (+)RNA virus helicase ATP-binding.
DOMAIN 5435 5607 (+)RNA virus helicase C-terminal.
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}.
NP_BIND 5278 5285 ATP. {ECO:0000305}.
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.
METAL 5000 5000 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5003 5003 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5011 5011 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5014 5014 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5021 5021 Zinc 1. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5024 5024 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5028 5028 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5034 5034 Zinc 2. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5045 5045 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5050 5050 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5067 5067 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
METAL 5070 5070 Zinc 3. {ECO:0000255|PROSITE-
ProRule:PRU00986}.
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.
SITE 4995 4996 Cleavage; by 3CL-PRO.
SITE 5592 5593 Cleavage; by 3CL-PRO.
SITE 6110 6111 Cleavage; by 3CL-PRO.
SITE 6458 6459 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}.
MUTAGEN 5284 5284 K->A: Almost complete loss of helicase
activity. {ECO:0000269|PubMed:10917600}.
CONFLICT 1982 1982 A -> Q (in Ref. 1; Ref/1). {ECO:0000305}.
CONFLICT 4042 4042 F -> S (in Ref. 1; Ref/1). {ECO:0000305}.
STRAND 1275 1278 {ECO:0000244|PDB:3EJG}.
STRAND 1281 1285 {ECO:0000244|PDB:3EJG}.
HELIX 1288 1294 {ECO:0000244|PDB:3EJG}.
STRAND 1298 1304 {ECO:0000244|PDB:3EJG}.
HELIX 1313 1321 {ECO:0000244|PDB:3EJG}.
TURN 1322 1324 {ECO:0000244|PDB:3EJG}.
HELIX 1325 1337 {ECO:0000244|PDB:3EJG}.
STRAND 1345 1350 {ECO:0000244|PDB:3EJG}.
STRAND 1353 1359 {ECO:0000244|PDB:3EJG}.
HELIX 1367 1380 {ECO:0000244|PDB:3EJG}.
STRAND 1381 1383 {ECO:0000244|PDB:3EJG}.
STRAND 1385 1387 {ECO:0000244|PDB:3EJG}.
HELIX 1393 1395 {ECO:0000244|PDB:3EJG}.
HELIX 1399 1409 {ECO:0000244|PDB:3EJG}.
STRAND 1415 1419 {ECO:0000244|PDB:3EJG}.
HELIX 1422 1433 {ECO:0000244|PDB:3EJG}.
HELIX 3829 3831 {ECO:0000244|PDB:2J98}.
STRAND 3834 3842 {ECO:0000244|PDB:2J97}.
HELIX 3843 3845 {ECO:0000244|PDB:2J97}.
STRAND 3847 3855 {ECO:0000244|PDB:2J97}.
STRAND 3858 3860 {ECO:0000244|PDB:2J98}.
STRAND 3862 3869 {ECO:0000244|PDB:2J97}.
STRAND 3873 3878 {ECO:0000244|PDB:2J97}.
STRAND 3881 3883 {ECO:0000244|PDB:2J97}.
STRAND 3885 3889 {ECO:0000244|PDB:2J97}.
STRAND 3893 3897 {ECO:0000244|PDB:2J97}.
STRAND 3904 3911 {ECO:0000244|PDB:2J97}.
HELIX 3916 3930 {ECO:0000244|PDB:2J97}.
HELIX 6112 6122 {ECO:0000244|PDB:4S1T}.
STRAND 6134 6137 {ECO:0000244|PDB:4S1T}.
STRAND 6140 6144 {ECO:0000244|PDB:4S1T}.
STRAND 6149 6154 {ECO:0000244|PDB:4S1T}.
STRAND 6157 6159 {ECO:0000244|PDB:4S1T}.
HELIX 6161 6169 {ECO:0000244|PDB:4S1T}.
STRAND 6174 6176 {ECO:0000244|PDB:4S1T}.
HELIX 6180 6184 {ECO:0000244|PDB:4S1T}.
STRAND 6189 6194 {ECO:0000244|PDB:4S1T}.
TURN 6198 6201 {ECO:0000244|PDB:4S1T}.
STRAND 6202 6211 {ECO:0000244|PDB:4S1T}.
TURN 6213 6215 {ECO:0000244|PDB:4S1T}.
STRAND 6223 6226 {ECO:0000244|PDB:4S1T}.
HELIX 6232 6238 {ECO:0000244|PDB:4S1T}.
STRAND 6240 6248 {ECO:0000244|PDB:4S1T}.
STRAND 6252 6254 {ECO:0000244|PDB:4S1T}.
STRAND 6262 6267 {ECO:0000244|PDB:4S1T}.
STRAND 6270 6273 {ECO:0000244|PDB:4S1T}.
STRAND 6287 6293 {ECO:0000244|PDB:4S1T}.
TURN 6311 6313 {ECO:0000244|PDB:4S1T}.
HELIX 6319 6326 {ECO:0000244|PDB:4S1T}.
HELIX 6329 6336 {ECO:0000244|PDB:4S1T}.
TURN 6339 6342 {ECO:0000244|PDB:4S1T}.
HELIX 6343 6346 {ECO:0000244|PDB:4S1T}.
STRAND 6352 6355 {ECO:0000244|PDB:4S1T}.
HELIX 6362 6371 {ECO:0000244|PDB:4S1T}.
STRAND 6374 6380 {ECO:0000244|PDB:4S1T}.
STRAND 6386 6394 {ECO:0000244|PDB:4S1T}.
TURN 6395 6398 {ECO:0000244|PDB:4S1T}.
STRAND 6399 6407 {ECO:0000244|PDB:4S1T}.
HELIX 6411 6418 {ECO:0000244|PDB:4S1T}.
STRAND 6423 6434 {ECO:0000244|PDB:4S1T}.
STRAND 6437 6446 {ECO:0000244|PDB:4S1T}.
STRAND 6449 6455 {ECO:0000244|PDB:4S1T}.
SEQUENCE 6758 AA; 754163 MW; B7EC2ABD7FE4EC1A 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 DNSYLNRVRG
SSAARLEPCN GTDIDYCVRA FDVYNKDASF IGKNLKSNCV RFKNVDKDDA FYIVKRCIKS
VMDHEQSMYN LLKGCNAVAK HDFFTWHEGR TIYGNVSRQD LTKYTMMDLC FALRNFDEKD
CEVFKEILVL TGCCSTDYFE MKNWFDPIEN EDIHRVYAAL GKVVANAMLK CVAFCDEMVL
KGVVGVLTLD NQDLNGNFYD FGDFVLCPPG MGIPYCTSYY SYMMPVMGMT NCLASECFMK
SDIFGQDFKT FDLLKYDFTE HKEVLFNKYF KYWGQDYHPD CVDCHDEMCI LHCSNFNTLF
ATTIPNTAFG PLCRKVFIDG VPVVATAGYH FKQLGLVWNK DVNTHSTRLT ITELLQFVTD
PTLIVASSPA LVDKRTVCFS VAALSTGLTS QTVKPGHFNK EFYDFLRSQG FFDEGSELTL
KHFFFTQKGD AAIKDFDYYR YNRPTMLDIG QARVAYQVAA RYFDCYEGGC ITSREVVVTN
LNKSAGWPLN KFGKAGLYYE SISYEEQDAI FSLTKRNILP TMTQLNLKYA ISGKERARTV
GGVSLLATMT TRQFHQKCLK SIVATRNATV VIGTTKFYGG WDNMLKNLMA DVDDPKLMGW
DYPKCDRAMP SMIRMLSAMI LGSKHVTCCT ASDKFYRLSN ELAQVLTEVV YSNGGFYFKP
GGTTSGDATT AYANSVFNIF QAVSSNINCV LSVNSSNCNN FNVKKLQRQL YDNCYRNSNV
DESFVDDFYG YLQKHFSMMI LSDDSVVCYN KTYAGLGYIA DISAFKATLY YQNGVFMSTA
KCWTEEDLSI GPHEFCSQHT MQIVDENGKY YLPYPDPSRI ISAGVFVDDI TKTDAVILLE
RYVSLAIDAY PLSKHPKPEY RKVFYALLDW VKHLNKTLNE GVLESFSVTL LDEHESKFWD
ESFYASMYEK STVLQAAGLC VVCGSQTVLR CGDCLRRPML CTKCAYDHVF GTDHKFILAI
TPYVCNTSGC NVNDVTKLYL GGLNYYCVDH KPHLSFPLCS AGNVFGLYKS SALGSMDIDV
FNKLSTSDWS DIRDYKLAND AKESLRLFAA ETVKAKEESV KSSYAYATLK EIVGPKELLL
LWESGKAKPP LNRNSVFTCF QITKDSKFQV GEFVFEKVDY GSDTVTYKST ATTKLVPGML
FILTSHNVAP LRAPTMANQE KYSTIYKLHP SFNVSDAYAN LVPYYQLIGK QRITTIQGPP
GSGKSHCSIG IGVYYPGARI VFTACSHAAV DSLCAKAVTA YSVDKCTRII PARARVECYS
GFKPNNNSAQ YVFSTVNALP EVNADIVVVD EVSMCTNYDL SVINQRISYK HIVYVGDPQQ
LPAPRVLISK GVMEPIDYNV VTQRMCAIGP DVFLHKCYRC PAEIVNTVSE LVYENKFVPV
KEASKQCFKI FERGSVQVDN GSSINRRQLD VVKRFIHKNS TWSKAVFISP YNSQNYVAAR
LLGLQTQTVD SAQGSEYDYV IFAQTSDTAH ACNANRFNVA ITRAKKGIFC IMSDRTLFDA
LKFFEITMTD LQSESSCGLF KDCARNPIDL PPSHATTYLS LSDRFKTSGD LAVQIGNNNV
CTYEHVISYM GFRFDVSMPG SHSLFCTRDF AMRHVRGWLG MDVEGAHVTG DNVGTNVPLQ
VGFSNGVDFV AQPEGCVLTN TGSVVKPVRA RAPPGEQFTH IVPLLRKGQP WSVLRKRIVQ
MIADFLAGSS DVLVFVLWAG GLELTTMRYF VKIGAVKHCQ CGTVATCYNS VSNDYCCFKH
ALGCDYVYNP YVIDIQQWGY VGSLSTNHHA ICNVHRNEHV ASGDAIMTRC LAVYDCFVKN
VDWSITYPMI ANENAINKGG RTVQSHIMRA AIKLYNPKAI HDIGNPKGIR CAVTDAKWYC
YDKNPINSNV KTLEYDYMTH GQMDGLCLFW NCNVDMYPEF SIVCRFDTRT RSTLNLEGVN
GGSLYVNNHA FHTPAYDKRA MAKLKPAPFF YYDDGSCEVV HDQVNYVPLR ATNCITKCNI
GGAVCSKHAN LYRAYVESYN IFTQAGFNIW VPTTFDCYNL WQTFTEVNLQ GLENIAFNVV
NKGSFVGADG ELPVAISGDK VFVRDGNTDN LVFVNKTSLP TNIAFELFAK RKVGLTPPLS
ILKNLGVVAT YKFVLWDYEA ERPLTSFTKS VCGYTDFAED VCTCYDNSIQ GSYERFTLST
NAVLFSATAV KTGGKSLPAI KLNFGMLNGN AIATVKSEDG NIKNINWFVY VRKDGKPVDH
YDGFYTQGRN LQDFLPRSTM EEDFLNMDIG VFIQKYGLED FNFEHVVYGD VSKTTLGGLH
LLISQVRLSK MGILKAEEFV AASDITLKCC TVTYLNDPSS KTVCTYMDLL LDDFVSVLKS
LDLTVVSKVH EVIIDNKPWR WMLWCKDNAV ATFYPQLQSA EWKCGYSMPG IYKTQRMCLE
PCNLYNYGAG LKLPSGIMFN VVKYTQLCQY FNSTTLCVPH NMRVLHLGAG SDYGVAPGTA
VLKRWLPHDA IVVDNDVVDY VSDADFSVTG DCATVYLEDK FDLLISDMYD GRTKAIDGEN
VSKEGFFTYI NGFICEKLAI GGSIAIKVTE YSWNKKLYEL VQRFSFWTMF CTSVNTSSSE
AFVVGINYLG DFAQGPFIDG NIIHANYVFW RNSTVMSLSY NSVLDLSKFN CKHKATVVVQ
LKDSDINEMV LSLVRSGKLL VRGNGKCLSF SNHLVSTK


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