R1AB_CVH22
ID R1AB_CVH22 Reviewed; 6758 AA.
AC P0C6X1; Q05002; Q9DLN0; Q9DLN1;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Replicase polyprotein 1ab;
DE Short=pp1ab;
DE AltName: Full=ORF1ab polyprotein;
DE Contains:
DE RecName: Full=Non-structural protein 1;
DE Short=nsp1;
DE AltName: Full=p9;
DE Contains:
DE RecName: Full=Non-structural protein 2;
DE Short=nsp2;
DE AltName: Full=p87;
DE Contains:
DE RecName: Full=Non-structural protein 3;
DE Short=nsp3;
DE EC=3.4.19.12;
DE EC=3.4.22.-;
DE AltName: Full=PL1-PRO/PL2-PRO;
DE AltName: Full=PLP1/PLP2;
DE AltName: Full=Papain-like proteinases 1/2;
DE AltName: Full=p195;
DE Contains:
DE RecName: Full=Non-structural protein 4;
DE Short=nsp4;
DE AltName: Full=Peptide HD2;
DE Contains:
DE RecName: Full=3C-like proteinase;
DE Short=3CL-PRO;
DE Short=3CLp;
DE EC=3.4.22.-;
DE AltName: Full=M-PRO;
DE AltName: Full=nsp5;
DE AltName: Full=p34;
DE Contains:
DE RecName: Full=Non-structural protein 6;
DE Short=nsp6;
DE Contains:
DE RecName: Full=Non-structural protein 7;
DE Short=nsp7;
DE AltName: Full=p5;
DE Contains:
DE RecName: Full=Non-structural protein 8;
DE Short=nsp8;
DE AltName: Full=p23;
DE Contains:
DE RecName: Full=Non-structural protein 9;
DE Short=nsp9;
DE AltName: Full=p12;
DE Contains:
DE RecName: Full=Non-structural protein 10;
DE Short=nsp10;
DE AltName: Full=Growth factor-like peptide;
DE Short=GFL;
DE AltName: Full=p16;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE Short=Pol;
DE Short=RdRp;
DE EC=2.7.7.48;
DE AltName: Full=nsp12;
DE AltName: Full=p100;
DE Contains:
DE RecName: Full=Helicase;
DE Short=Hel;
DE EC=3.6.4.12;
DE EC=3.6.4.13;
DE AltName: Full=nsp13;
DE AltName: Full=p66;
DE AltName: Full=p66-HEL;
DE Contains:
DE RecName: Full=Exoribonuclease;
DE Short=ExoN;
DE EC=3.1.13.-;
DE AltName: Full=nsp14;
DE Contains:
DE RecName: Full=Uridylate-specific endoribonuclease;
DE EC=4.6.1.-;
DE AltName: Full=NendoU;
DE AltName: Full=nsp15;
DE AltName: Full=p41;
DE Contains:
DE RecName: Full=Putative 2'-O-methyl transferase;
DE EC=2.1.1.57;
DE AltName: Full=nsp16;
GN Name=rep; ORFNames=1a-1b;
OS Human coronavirus 229E (HCoV-229E).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Duvinacovirus.
OX NCBI_TaxID=11137;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11369870; DOI=10.1099/0022-1317-82-6-1273;
RA Thiel V., Herold J., Schelle B., Siddell S.G.;
RT "Infectious RNA transcribed in vitro from a cDNA copy of the human
RT coronavirus genome cloned in vaccinia virus.";
RL J. Gen. Virol. 82:1273-1281(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-4085.
RX PubMed=8337838; DOI=10.1006/viro.1993.1419;
RA Herold J., Raabe T., Schelle-Prinz B., Siddell S.G.;
RT "Nucleotide sequence of the human coronavirus 229E RNA polymerase locus.";
RL Virology 195:680-691(1993).
RN [3]
RP CHARACTERIZATION OF 3CL-PRO, AND MUTAGENESIS OF HIS-3006; HIS-3028;
RP ASN-3029; GLU-3074; THR-3099; CYS-3109; HIS-3127; HIS-3136 AND GLN-3267.
RX PubMed=9094676; DOI=10.1128/jvi.71.5.3992-3997.1997;
RA Ziebuhr J., Heusipp G., Siddell S.G.;
RT "Biosynthesis, purification, and characterization of the human coronavirus
RT 229E 3C-like proteinase.";
RL J. Virol. 71:3992-3997(1997).
RN [4]
RP CHARACTERIZATION OF P41, AND SUBCELLULAR LOCATION.
RX PubMed=9367364; DOI=10.1099/0022-1317-78-11-2789;
RA Heusipp G., Groetzinger C., Herold J., Siddell S.G., Ziebuhr J.;
RT "Identification and subcellular localization of a 41 kDa, polyprotein 1ab
RT processing product in human coronavirus 229E-infected cells.";
RL J. Gen. Virol. 78:2789-2794(1997).
RN [5]
RP CHARACTERIZATION OF HELICASE, AND MUTAGENESIS OF LYS-5284.
RX PubMed=10917600; DOI=10.1017/s1355838200000728;
RA Seybert A., Hegyi A., Siddell S.G., Ziebuhr J.;
RT "The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-
RT unwinding activities with 5'-to-3' polarity.";
RL RNA 6:1056-1068(2000).
RN [6]
RP ZINC-FINGER DOMAIN OF PL1-PRO, AND MUTAGENESIS OF LYS-1048; GLY-1099;
RP GLY-1102; CYS-1126; CYS-1128; CYS-1154; LEU-1155; CYS-1157; CYS-1163;
RP VAL-1175; CYS-1203 AND ASP-1218.
RX PubMed=10329692; DOI=10.1074/jbc.274.21.14918;
RA Herold J., Siddell S.G., Gorbalenya A.E.;
RT "A human RNA viral cysteine proteinase that depends upon a unique Zn2+-
RT binding finger connecting the two domains of a papain-like fold.";
RL J. Biol. Chem. 274:14918-14925(1999).
RN [7]
RP ERRATUM OF PUBMED:10329692.
RA Herold J., Siddell S.G., Gorbalenya A.E.;
RL J. Biol. Chem. 274:21490-21490(1999).
RN [8]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=9847320; DOI=10.1128/jvi.73.1.177-185.1999;
RA Ziebuhr J., Siddell S.G.;
RT "Processing of the human coronavirus 229E replicase polyproteins by the
RT virus-encoded 3C-like proteinase: identification of proteolytic products
RT and cleavage sites common to pp1a and pp1ab.";
RL J. Virol. 73:177-185(1999).
RN [9]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND MUTAGENESIS OF CYS-1054 AND
RP TRP-1702.
RX PubMed=11431476; DOI=10.1074/jbc.m104097200;
RA Ziebuhr J., Thiel V., Gorbalenya A.E.;
RT "The autocatalytic release of a putative RNA virus transcription factor
RT from its polyprotein precursor involves two paralogous papain-like
RT proteases that cleave the same peptide bond.";
RL J. Biol. Chem. 276:33220-33232(2001).
RN [10]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=11842254; DOI=10.1099/0022-1317-83-3-595;
RA Hegyi A., Ziebuhr J.;
RT "Conservation of substrate specificities among coronavirus main
RT proteases.";
RL J. Gen. Virol. 83:595-599(2002).
RN [11]
RP MUTAGENESIS OF ASN-3029.
RX PubMed=11842253; DOI=10.1099/0022-1317-83-3-581;
RA Hegyi A., Friebe A., Gorbalenya A.E., Ziebuhr J.;
RT "Mutational analysis of the active centre of coronavirus 3C-like
RT proteases.";
RL J. Gen. Virol. 83:581-593(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 2966-3265.
RX PubMed=12746549; DOI=10.1126/science.1085658;
RA Anand K., Ziebuhr J., Wadhwani P., Mesters J.R., Hilgenfeld R.;
RT "Coronavirus main proteinase (3CLpro) structure: basis for design of anti-
RT SARS drugs.";
RL Science 300:1763-1767(2003).
CC -!- FUNCTION: The replicase polyprotein of coronaviruses is a
CC multifunctional protein: it contains the activities necessary for the
CC transcription of negative stranded RNA, leader RNA, subgenomic mRNAs
CC and progeny virion RNA as well as proteinases responsible for the
CC cleavage of the polyprotein into functional products.
CC -!- FUNCTION: The papain-like proteinase 1 (PLP1) and papain-like
CC proteinase 2 (PLP2) are responsible for the cleavages located at the N-
CC terminus of the replicase polyprotein. In addition, PLP2 possesses a
CC deubiquitinating/deISGylating activity and processes both 'Lys-48'- and
CC 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2
CC also antagonizes innate immune induction of type I interferon by
CC blocking the nuclear translocation of host IRF-3 (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: [3C-like proteinase]: Responsible for the majority of
CC cleavages as it cleaves the C-terminus of replicase polyprotein at 11
CC sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-
CC [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-
CC CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function
CC (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}.
CC -!- FUNCTION: The helicase which contains a zinc finger structure displays
CC RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Its
CC ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C),
CC poly(dA), but not by poly(G).
CC -!- FUNCTION: The exoribonuclease acts on both ssRNA and dsRNA in a 3' to
CC 5' direction. {ECO:0000250}.
CC -!- FUNCTION: Nsp7-nsp8 hexadecamer may possibly confer processivity to the
CC polymerase, maybe by binding to dsRNA or by producing primers utilized
CC by the latter. {ECO:0000250}.
CC -!- FUNCTION: Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
CC -!- FUNCTION: [Uridylate-specific endoribonuclease]: Plays a role in viral
CC transcription/replication and prevents the simultaneous activation of
CC host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By
CC similarity). Acts by degrading the 5'-polyuridines generated during
CC replication of the poly(A) region of viral genomic and subgenomic RNAs.
CC Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-
CC cP) is first generated by 2'-O transesterification, which is then
CC hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded,
CC poly(U) RNA would hybridize with poly(A) RNA tails and activate host
CC dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- CATALYTIC ACTIVITY: [Non-structural protein 3]:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12;
CC -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY: [Helicase]:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- CATALYTIC ACTIVITY: [Helicase]:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- CATALYTIC ACTIVITY: [Putative 2'-O-methyl transferase]:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC EC=2.1.1.57; Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC -!- CATALYTIC ACTIVITY: [Uridylate-specific endoribonuclease]:
CC Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-
CC 2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-
CC RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-
CC COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173079, ChEBI:CHEBI:173080;
CC Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC -!- COFACTOR: [Uridylate-specific endoribonuclease]:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC Note=Likely affects Nsp15 binding to RNA.
CC {ECO:0000250|UniProtKB:P0C6X7};
CC -!- SUBUNIT: 3CL-PRO exists as monomer and homodimer. Eight copies of nsp7
CC and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is
CC a dimer. Nsp10 forms a dodecamer (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC PRO_0000037300; PRO_0000037299 [P0C6X1]: rep; NbExp=4; IntAct=EBI-26366585, EBI-26366570;
CC PRO_0000037301; PRO_0000037301 [P0C6X1]: rep; NbExp=5; IntAct=EBI-25708564, EBI-25708564;
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 9]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Helicase]: Host endoplasmic reticulum-Golgi
CC intermediate compartment {ECO:0000305}. Note=The helicase interacts
CC with the N protein in membranous complexes and colocalizes with sites
CC of synthesis of new viral RNA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease]: Host
CC cytoplasm, host perinuclear region {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=P0C6X1-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6U2-1; Sequence=External;
CC -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC association of the replication complex and thereby alter the
CC architecture of the host cell membrane.
CC -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically
CC processed. {ECO:0000269|PubMed:11431476, ECO:0000269|PubMed:11842254,
CC ECO:0000269|PubMed:9847320}.
CC -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1ab]: Produced by -1
CC ribosomal frameshifting at the 1a-1b genes boundary.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Proteic grace - Issue 77 of
CC December 2006;
CC URL="https://web.expasy.org/spotlight/back_issues/077";
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DR EMBL; AF304460; AAG48591.1; -; Genomic_RNA.
DR PIR; S28600; S28600.
DR RefSeq; NP_073549.1; NC_002645.1. [P0C6X1-1]
DR PDB; 1P9S; X-ray; 2.54 A; A/B=2966-3265.
DR PDB; 2J97; X-ray; 1.75 A; A=3825-3933.
DR PDB; 2J98; X-ray; 1.80 A; A/B=3825-3933.
DR PDB; 3EJG; X-ray; 1.78 A; A=1270-1434.
DR PDB; 4RS4; X-ray; 2.96 A; A/B/C/D/E/F=6111-6458.
DR PDB; 4S1T; X-ray; 2.50 A; A/B/C/D/E/F=6111-6458.
DR PDBsum; 1P9S; -.
DR PDBsum; 2J97; -.
DR PDBsum; 2J98; -.
DR PDBsum; 3EJG; -.
DR PDBsum; 4RS4; -.
DR PDBsum; 4S1T; -.
DR SMR; P0C6X1; -.
DR IntAct; P0C6X1; 41.
DR BindingDB; P0C6X1; -.
DR MEROPS; C30.003; -.
DR PRIDE; P0C6X1; -.
DR DNASU; 918764; -.
DR GeneID; 918764; -.
DR KEGG; vg:918764; -.
DR BRENDA; 3.4.22.B14; 8801.
DR BRENDA; 3.6.4.12; 8801.
DR BRENDA; 3.6.4.13; 8801.
DR SABIO-RK; P0C6X1; -.
DR EvolutionaryTrace; P0C6X1; -.
DR Proteomes; UP000006716; Genome.
DR GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004532; F:exoribonuclease activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd21409; 1B_cv_Nsp13-like; 1.
DR CDD; cd21558; alphaCoV-Nsp6; 1.
DR CDD; cd21660; alphaCoV_Nsp14; 1.
DR CDD; cd21665; alphaCoV_Nsp5_Mpro; 1.
DR CDD; cd21588; alphaCoV_RdRp; 1.
DR CDD; cd21514; cv_alpha_Nsp2_HCoV-229E-like; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR CDD; cd21171; NTD_alpha_beta_cv_Nsp15-like; 1.
DR CDD; cd21466; Ubl2_cv_PLpro_N_Nsp3-like; 1.
DR CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR Gene3D; 1.10.150.420; -; 1.
DR Gene3D; 1.10.1840.10; -; 1.
DR Gene3D; 1.10.8.1190; -; 2.
DR Gene3D; 1.10.8.370; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.40.10.250; -; 1.
DR Gene3D; 3.30.160.820; -; 1.
DR Gene3D; 3.30.70.3540; -; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.50.11580; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR043608; CoV_NSP15_M.
DR InterPro; IPR043606; CoV_NSP15_N.
DR InterPro; IPR043613; CoV_NSP2_C.
DR InterPro; IPR043611; CoV_NSP3_C.
DR InterPro; IPR032505; CoV_NSP4_C.
DR InterPro; IPR043612; CoV_NSP4_N.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR044371; Macro_X_NSP3-like.
DR InterPro; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR036333; NSP10_sf_CoV.
DR InterPro; IPR044343; NSP13_1B_dom_CoV.
DR InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR InterPro; IPR044313; NSP14_alphaCoV.
DR InterPro; IPR009466; NSP14_CoV.
DR InterPro; IPR044330; NSP15_alpha_betaCoV_N.
DR InterPro; IPR043174; NSP15_middle_sf.
DR InterPro; IPR042515; NSP15_N_CoV.
DR InterPro; IPR044401; NSP15_NendoU_CoV.
DR InterPro; IPR009461; NSP16_CoV-like.
DR InterPro; IPR044385; NSP2_HCoV-229E-like.
DR InterPro; IPR043615; NSP2_N_CoV.
DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR044309; NSP5_Mpro_alphaCoV.
DR InterPro; IPR044369; NSP6_alphaCoV.
DR InterPro; IPR043610; NSP6_CoV.
DR InterPro; IPR014828; NSP7_CoV.
DR InterPro; IPR037204; NSP7_sf_CoV.
DR InterPro; IPR014829; NSP8_CoV.
DR InterPro; IPR037230; NSP8_sf_CoV.
DR InterPro; IPR014822; NSP9_CoV.
DR InterPro; IPR036499; NSP9_sf_CoV.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013016; Peptidase_C16_CoV.
DR InterPro; IPR008740; Peptidase_C30_CoV.
DR InterPro; IPR043477; Peptidase_C30_dom3_CoV.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR InterPro; IPR044356; RdRp_alphaCoV.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR009469; RNA_pol_N_CoV.
DR InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF06471; CoV_ExoN; 1.
DR Pfam; PF06460; CoV_Methyltr_2; 1.
DR Pfam; PF09401; CoV_NSP10; 1.
DR Pfam; PF19215; CoV_NSP15_C; 1.
DR Pfam; PF19216; CoV_NSP15_M; 1.
DR Pfam; PF19219; CoV_NSP15_N; 1.
DR Pfam; PF19212; CoV_NSP2_C; 2.
DR Pfam; PF19211; CoV_NSP2_N; 1.
DR Pfam; PF19218; CoV_NSP3_C; 1.
DR Pfam; PF16348; CoV_NSP4_C; 1.
DR Pfam; PF19217; CoV_NSP4_N; 1.
DR Pfam; PF19213; CoV_NSP6; 1.
DR Pfam; PF08716; CoV_NSP7; 1.
DR Pfam; PF08717; CoV_NSP8; 1.
DR Pfam; PF08710; CoV_NSP9; 1.
DR Pfam; PF08715; CoV_peptidase; 2.
DR Pfam; PF06478; CoV_RPol_N; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF101816; SSF101816; 1.
DR SUPFAM; SSF140367; SSF140367; 1.
DR SUPFAM; SSF142877; SSF142877; 1.
DR SUPFAM; SSF143076; SSF143076; 1.
DR SUPFAM; SSF144246; SSF144246; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
DR PROSITE; PS51954; COV_N7_MTASE; 1.
DR PROSITE; PS51962; COV_NSP1; 1.
DR PROSITE; PS51948; COV_NSP12_RDRP; 1.
DR PROSITE; PS51960; COV_NSP15_NTD; 1.
DR PROSITE; PS51991; COV_NSP2_C; 1.
DR PROSITE; PS51990; COV_NSP2_M; 1.
DR PROSITE; PS51989; COV_NSP2_N; 1.
DR PROSITE; PS51992; COV_NSP3_Y3; 1.
DR PROSITE; PS51943; COV_NSP3A_UBL; 1.
DR PROSITE; PS51944; COV_NSP3D_UBL; 1.
DR PROSITE; PS51946; COV_NSP4C; 1.
DR PROSITE; PS51949; COV_NSP7; 1.
DR PROSITE; PS51950; COV_NSP8; 1.
DR PROSITE; PS51951; COV_NSP9_SSRNA_BD; 1.
DR PROSITE; PS51653; CV_ZBD; 1.
DR PROSITE; PS51442; M_PRO; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51958; NENDOU; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS51955; NIV_2_O_MTASE; 1.
DR PROSITE; PS51953; NIV_EXON; 1.
DR PROSITE; PS51124; PEPTIDASE_C16; 2.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Endonuclease; Exonuclease; Helicase; Host cytoplasm; Host membrane;
KW Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host IRF3 by virus; Inhibition of host RLR pathway by virus;
KW Lyase; Membrane; Metal-binding; Methyltransferase;
KW Modulation of host ubiquitin pathway by viral deubiquitinase;
KW Modulation of host ubiquitin pathway by virus; Nuclease;
KW Nucleotide-binding; Nucleotidyltransferase; Protease; Reference proteome;
KW Repeat; Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
KW Thiol protease; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Viral immunoevasion; Viral RNA replication; Zinc;
KW Zinc-finger.
FT CHAIN 1..111
FT /note="Non-structural protein 1"
FT /id="PRO_0000037293"
FT CHAIN 112..897
FT /note="Non-structural protein 2"
FT /id="PRO_0000037294"
FT CHAIN 898..2484
FT /note="Non-structural protein 3"
FT /id="PRO_0000037295"
FT CHAIN 2485..2965
FT /note="Non-structural protein 4"
FT /id="PRO_0000037296"
FT CHAIN 2966..3267
FT /note="3C-like proteinase"
FT /id="PRO_0000037297"
FT CHAIN 3268..3546
FT /note="Non-structural protein 6"
FT /id="PRO_0000037298"
FT CHAIN 3547..3629
FT /note="Non-structural protein 7"
FT /id="PRO_0000037299"
FT CHAIN 3630..3824
FT /note="Non-structural protein 8"
FT /id="PRO_0000037300"
FT CHAIN 3825..3933
FT /note="Non-structural protein 9"
FT /id="PRO_0000037301"
FT CHAIN 3934..4068
FT /note="Non-structural protein 10"
FT /id="PRO_0000037302"
FT CHAIN 4069..4995
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000037303"
FT CHAIN 4996..5592
FT /note="Helicase"
FT /id="PRO_0000037304"
FT CHAIN 5593..6110
FT /note="Exoribonuclease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037305"
FT CHAIN 6111..6458
FT /note="Uridylate-specific endoribonuclease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037306"
FT CHAIN 6459..6758
FT /note="Putative 2'-O-methyl transferase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037307"
FT TRANSMEM 1925..1945
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1998..2018
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2068..2088
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2095..2115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2491..2511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2731..2751
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2755..2775
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2782..2802
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2809..2829
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2834..2854
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3281..3301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3304..3324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3328..3348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3367..3387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3401..3421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3422..3442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3467..3487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 2..109
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT DOMAIN 113..359
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 389..775
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 773..897
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 898..993
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1016..1268
FT /note="Peptidase C16 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1269..1436
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1600..1655
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1663..1914
FT /note="Peptidase C16 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 2379..2483
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 2870..2965
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 2966..3267
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3547..3629
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3630..3824
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 3825..3933
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 3934..4072
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT DOMAIN 4074..4323
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 4428..4995
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT DOMAIN 4675..4837
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 4996..5079
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT DOMAIN 5253..5434
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 5435..5607
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 5664..5878
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 5887..6108
FT /note="N7-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT DOMAIN 6111..6171
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT DOMAIN 6172..6298
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 6315..6455
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6459..6755
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ZN_FING 1126..1157
FT /note="C4-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 1780..1815
FT /note="C4-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4007..4023
FT /evidence="ECO:0000250"
FT ZN_FING 4049..4062
FT /evidence="ECO:0000250"
FT REGION 246..266
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 1925..2115
FT /note="HD1"
FT REGION 2491..2854
FT /note="HD2"
FT REGION 3281..3487
FT /note="HD3"
FT REGION 5999..6013
FT /note="GpppA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT ACT_SITE 1054
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1205
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1701
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1863
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3006
FT /note="For 3CL-PRO activity"
FT ACT_SITE 3109
FT /note="For 3CL-PRO activity"
FT ACT_SITE 4822
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 4823
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 4824
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5682
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5684
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5783
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5859
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5864
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6345
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6587
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6627
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6660
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 4007
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4010
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4016
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4023
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4049
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4052
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4060
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4062
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 5000
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5003
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5011
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5014
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5021
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5024
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5028
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5034
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5045
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5050
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5067
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5070
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5278..5285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 5799
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5801
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5817
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5820
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5848
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5852
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5855
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5870
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5922..5928
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6037
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6054
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6065
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6068
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT SITE 111..112
FT /note="Cleavage; by PL1-PRO"
FT SITE 897..898
FT /note="Cleavage; by PL1-PRO"
FT SITE 2484..2485
FT /note="Cleavage; by PL2-PRO"
FT SITE 2965..2966
FT /note="Cleavage; by 3CL-PRO"
FT SITE 3267..3268
FT /note="Cleavage; by 3CL-PRO"
FT SITE 3546..3547
FT /note="Cleavage; by 3CL-PRO"
FT SITE 3629..3630
FT /note="Cleavage; by 3CL-PRO"
FT SITE 3824..3825
FT /note="Cleavage; by 3CL-PRO"
FT SITE 3933..3934
FT /note="Cleavage; by 3CL-PRO"
FT SITE 4068..4069
FT /note="Cleavage; by 3CL-PRO"
FT SITE 4995..4996
FT /note="Cleavage; by 3CL-PRO"
FT SITE 5592..5593
FT /note="Cleavage; by 3CL-PRO"
FT SITE 6110..6111
FT /note="Cleavage; by 3CL-PRO"
FT SITE 6458..6459
FT /note="Cleavage; by 3CL-PRO"
FT MUTAGEN 1048
FT /note="K->E: Complete loss of PL1-PRO activity."
FT /evidence="ECO:0000269|PubMed:10329692"
FT MUTAGEN 1054
FT /note="C->A,G,S: Complete loss of PL1-PRO activity."
FT /evidence="ECO:0000269|PubMed:11431476"
FT MUTAGEN 1099
FT /note="G->A: Complete loss of PL1-PRO activity."
FT /evidence="ECO:0000269|PubMed:10329692"
FT MUTAGEN 1099
FT /note="G->P: No effect."
FT /evidence="ECO:0000269|PubMed:10329692"
FT MUTAGEN 1102
FT /note="G->A,S: No effect."
FT /evidence="ECO:0000269|PubMed:10329692"
FT MUTAGEN 1126
FT /note="C->D,H: Complete loss of PL1-PRO activity."
FT /evidence="ECO:0000269|PubMed:10329692"
FT MUTAGEN 1128
FT /note="C->A,D,P: Complete loss of PL1-PRO activity."
FT /evidence="ECO:0000269|PubMed:10329692"
FT MUTAGEN 1154
FT /note="C->A,H,D: Complete loss of PL1-PRO activity."
FT /evidence="ECO:0000269|PubMed:10329692"
FT MUTAGEN 1155
FT /note="Missing: Complete loss of PL1-PRO activity."
FT /evidence="ECO:0000269|PubMed:10329692"
FT MUTAGEN 1157
FT /note="C->A,D,H,P: Complete loss of PL1-PRO activity."
FT /evidence="ECO:0000269|PubMed:10329692"
FT MUTAGEN 1163
FT /note="C->A,D: No effect."
FT /evidence="ECO:0000269|PubMed:10329692"
FT MUTAGEN 1175
FT /note="V->H,P: Complete loss of PL1-PRO activity."
FT /evidence="ECO:0000269|PubMed:10329692"
FT MUTAGEN 1175
FT /note="V->N,T: No effect."
FT /evidence="ECO:0000269|PubMed:10329692"
FT MUTAGEN 1203
FT /note="C->A: Complete loss of PL1-PRO activity."
FT /evidence="ECO:0000269|PubMed:10329692"
FT MUTAGEN 1203
FT /note="C->D: No effect."
FT /evidence="ECO:0000269|PubMed:10329692"
FT MUTAGEN 1218
FT /note="D->A,E,H,K,N,Q: No effect."
FT /evidence="ECO:0000269|PubMed:10329692"
FT MUTAGEN 1702
FT /note="W->L: Complete loss of PL2-PRO activity."
FT /evidence="ECO:0000269|PubMed:11431476"
FT MUTAGEN 3006
FT /note="H->G,S,T,Y: Complete loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:9094676"
FT MUTAGEN 3028
FT /note="H->G,T: No loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:9094676"
FT MUTAGEN 3029
FT /note="N->A,D,E,Q: Increase of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:11842253,
FT ECO:0000269|PubMed:9094676"
FT MUTAGEN 3029
FT /note="N->G: No loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:11842253,
FT ECO:0000269|PubMed:9094676"
FT MUTAGEN 3029
FT /note="N->P: 95% loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:11842253,
FT ECO:0000269|PubMed:9094676"
FT MUTAGEN 3074
FT /note="E->H: No loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:9094676"
FT MUTAGEN 3099
FT /note="T->D: Complete loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:9094676"
FT MUTAGEN 3109
FT /note="C->P,S,V: Complete loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:9094676"
FT MUTAGEN 3127
FT /note="H->S: Complete loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:9094676"
FT MUTAGEN 3136
FT /note="H->A: 67% loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:9094676"
FT MUTAGEN 3136
FT /note="H->S: 77% loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:9094676"
FT MUTAGEN 3136
FT /note="H->T: 93% loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:9094676"
FT MUTAGEN 3267
FT /note="Q->A: No loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:9094676"
FT MUTAGEN 5284
FT /note="K->A: Almost complete loss of helicase activity."
FT /evidence="ECO:0000269|PubMed:10917600"
FT CONFLICT 1982
FT /note="A -> Q (in Ref. 1; Ref/1)"
FT /evidence="ECO:0000305"
FT CONFLICT 4042
FT /note="F -> S (in Ref. 1; Ref/1)"
FT /evidence="ECO:0000305"
FT STRAND 1275..1278
FT /evidence="ECO:0007829|PDB:3EJG"
FT STRAND 1281..1285
FT /evidence="ECO:0007829|PDB:3EJG"
FT HELIX 1288..1294
FT /evidence="ECO:0007829|PDB:3EJG"
FT STRAND 1298..1304
FT /evidence="ECO:0007829|PDB:3EJG"
FT HELIX 1313..1321
FT /evidence="ECO:0007829|PDB:3EJG"
FT TURN 1322..1324
FT /evidence="ECO:0007829|PDB:3EJG"
FT HELIX 1325..1337
FT /evidence="ECO:0007829|PDB:3EJG"
FT STRAND 1345..1350
FT /evidence="ECO:0007829|PDB:3EJG"
FT STRAND 1353..1359
FT /evidence="ECO:0007829|PDB:3EJG"
FT HELIX 1367..1380
FT /evidence="ECO:0007829|PDB:3EJG"
FT STRAND 1381..1383
FT /evidence="ECO:0007829|PDB:3EJG"
FT STRAND 1385..1387
FT /evidence="ECO:0007829|PDB:3EJG"
FT HELIX 1393..1395
FT /evidence="ECO:0007829|PDB:3EJG"
FT HELIX 1399..1409
FT /evidence="ECO:0007829|PDB:3EJG"
FT STRAND 1415..1419
FT /evidence="ECO:0007829|PDB:3EJG"
FT HELIX 1422..1433
FT /evidence="ECO:0007829|PDB:3EJG"
FT HELIX 3829..3831
FT /evidence="ECO:0007829|PDB:2J98"
FT STRAND 3834..3842
FT /evidence="ECO:0007829|PDB:2J97"
FT HELIX 3843..3845
FT /evidence="ECO:0007829|PDB:2J97"
FT STRAND 3847..3855
FT /evidence="ECO:0007829|PDB:2J97"
FT STRAND 3858..3860
FT /evidence="ECO:0007829|PDB:2J98"
FT STRAND 3862..3869
FT /evidence="ECO:0007829|PDB:2J97"
FT STRAND 3873..3878
FT /evidence="ECO:0007829|PDB:2J97"
FT STRAND 3881..3883
FT /evidence="ECO:0007829|PDB:2J97"
FT STRAND 3885..3889
FT /evidence="ECO:0007829|PDB:2J97"
FT STRAND 3893..3897
FT /evidence="ECO:0007829|PDB:2J97"
FT STRAND 3904..3911
FT /evidence="ECO:0007829|PDB:2J97"
FT HELIX 3916..3930
FT /evidence="ECO:0007829|PDB:2J97"
FT HELIX 6112..6122
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6134..6137
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6140..6144
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6149..6154
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6157..6159
FT /evidence="ECO:0007829|PDB:4S1T"
FT HELIX 6161..6169
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6174..6176
FT /evidence="ECO:0007829|PDB:4S1T"
FT HELIX 6180..6184
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6189..6194
FT /evidence="ECO:0007829|PDB:4S1T"
FT TURN 6198..6201
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6202..6211
FT /evidence="ECO:0007829|PDB:4S1T"
FT TURN 6213..6215
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6223..6226
FT /evidence="ECO:0007829|PDB:4S1T"
FT HELIX 6232..6238
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6240..6248
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6252..6254
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6262..6267
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6270..6273
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6287..6293
FT /evidence="ECO:0007829|PDB:4S1T"
FT TURN 6311..6313
FT /evidence="ECO:0007829|PDB:4S1T"
FT HELIX 6319..6326
FT /evidence="ECO:0007829|PDB:4S1T"
FT HELIX 6329..6336
FT /evidence="ECO:0007829|PDB:4S1T"
FT TURN 6339..6342
FT /evidence="ECO:0007829|PDB:4S1T"
FT HELIX 6343..6346
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6352..6355
FT /evidence="ECO:0007829|PDB:4S1T"
FT HELIX 6362..6371
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6374..6380
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6386..6394
FT /evidence="ECO:0007829|PDB:4S1T"
FT TURN 6395..6398
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6399..6407
FT /evidence="ECO:0007829|PDB:4S1T"
FT HELIX 6411..6418
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6423..6434
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6437..6446
FT /evidence="ECO:0007829|PDB:4S1T"
FT STRAND 6449..6455
FT /evidence="ECO:0007829|PDB:4S1T"
SQ 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
