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   27-MAR-2024, entry version 113.
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=Viral protein genome-linked nsp9;
DE     AltName: Full=Non-structural protein 9;
DE              Short=nsp9;
DE     AltName: Full=RNA-capping enzyme subunit nsp9;
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 nsp12;
DE              Short=Pol;
DE              Short=RdRp;
DE              EC=2.7.7.48;
DE              EC=2.7.7.50;
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: [Viral protein genome-linked nsp9]: Forms a primer, NSP9-pU,
CC       which is utilized by the polymerase for the initiation of RNA chains.
CC       Interacts with ribosome signal recognition particle RNA (SRP). Together
CC       with NSP8, suppress protein integration into the cell membrane, thereby
CC       disrupting host immune defenses. {ECO:0000250|UniProtKB:P0DTD1}.
CC   -!- FUNCTION: [RNA-directed RNA polymerase nsp12]: RNA-directed RNA
CC       polymerase that catalyzes the transcription of viral genomic and
CC       subgenomic RNAs. Acts in complex with nsp7 and nsp8 to transcribe both
CC       the minus and positive strands of genomic RNA. The kinase-like NiRAN
CC       domain of NSP12 attaches one or more nucleotides to the amino terminus
CC       of NSP9, forming a covalent RNA-protein intermediate that serves as
CC       transcription/replication primer. Subgenomic RNAs (sgRNAs) are formed
CC       by discontinuous transcription: The polymerase has the ability to pause
CC       at transcription-regulating sequences (TRS) and jump to the leader TRS,
CC       resulting in a major deletion. This creates a series of subgenomic RNAs
CC       that are replicated, transcribed and translated. In addition, Nsp12 is
CC       a subunit of the viral RNA capping enzyme that catalyzes the RNA
CC       guanylyltransferase reaction for genomic and sub-genomic RNAs.
CC       Subsequently, the NiRAN domain transfers RNA to GDP, and forms the core
CC       cap structure GpppA-RNA. {ECO:0000250|UniProtKB:P0DTD1}.
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 nsp12]:
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: [RNA-directed RNA polymerase nsp12]:
CC       Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC         end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC         Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC         Evidence={ECO:0000250|UniProtKB:P0DTD1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013;
CC         Evidence={ECO:0000250|UniProtKB:P0DTD1};
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_0000037299; PRO_0000037300 [P0C6X1]: rep; NbExp=4; IntAct=EBI-26366570, EBI-26366585;
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: [Viral protein genome-linked nsp9]: Host
CC       cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9
CC       and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
CC       in infection, they merge into confluent complexes (By similarity).
CC       {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";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   PDB; 7YRZ; X-ray; 1.79 A; A/B=2966-3267.
DR   PDBsum; 1P9S; -.
DR   PDBsum; 2J97; -.
DR   PDBsum; 2J98; -.
DR   PDBsum; 3EJG; -.
DR   PDBsum; 4RS4; -.
DR   PDBsum; 4S1T; -.
DR   PDBsum; 7YRZ; -.
DR   SMR; P0C6X1; -.
DR   IntAct; P0C6X1; 43.
DR   BindingDB; P0C6X1; -.
DR   ChEMBL; CHEMBL4888440; -.
DR   MEROPS; C30.003; -.
DR   DNASU; 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:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro.
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-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0039648; P:modulation by symbiont 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: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; cd21901; alpha_betaCoV_Nsp10; 1.
DR   CDD; cd21558; alphaCoV-Nsp6; 1.
DR   CDD; cd21723; alphaCoV_Nsp13-helicase; 1.
DR   CDD; cd21660; alphaCoV_Nsp14; 1.
DR   CDD; cd21514; alphaCoV_Nsp2_HCoV-229E-like; 1.
DR   CDD; cd21665; alphaCoV_Nsp5_Mpro; 1.
DR   CDD; cd21826; alphaCoV_Nsp7; 1.
DR   CDD; cd21830; alphaCoV_Nsp8; 1.
DR   CDD; cd21897; alphaCoV_Nsp9; 1.
DR   CDD; cd21731; alphaCoV_PLPro; 1.
DR   CDD; cd21588; alphaCoV_RdRp; 1.
DR   CDD; cd21473; cv_Nsp4_TM; 1.
DR   CDD; cd21167; M_alpha_beta_cv_Nsp15-like; 1.
DR   CDD; cd21557; Macro_X_Nsp3-like; 1.
DR   CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR   CDD; cd21171; NTD_alpha_betaCoV_Nsp15-like; 1.
DR   CDD; cd21875; PEDV-like_alphaCoV_Nsp1; 1.
DR   CDD; cd21689; stalk_CoV_Nsp13-like; 1.
DR   CDD; cd21712; TM_Y_alphaCoV_Nsp3_C; 1.
DR   CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR   Gene3D; 1.10.8.1190; -; 2.
DR   Gene3D; 3.40.50.11580; -; 1.
DR   Gene3D; 6.10.140.2090; -; 1.
DR   Gene3D; 1.10.150.420; Coronavirus nonstructural protein 4 C-terminus; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR   Gene3D; 1.10.1840.10; main proteinase (3clpro) structure, domain 3; 1.
DR   Gene3D; 3.30.160.820; Nsp15 N-terminal domain-like; 1.
DR   Gene3D; 1.10.8.370; nsp7 replicase; 1.
DR   Gene3D; 3.30.70.3540; Nsp8 replicase, head domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 2.40.10.250; Replicase NSP9; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR046443; a/bCoV_NSP1_glob.
DR   InterPro; IPR046440; AV_NSP11N_COV_NSP15M.
DR   InterPro; IPR043608; CoV_NSP15_M.
DR   InterPro; IPR043606; CoV_NSP15_N.
DR   InterPro; IPR043613; CoV_NSP2_C.
DR   InterPro; IPR047573; CoV_NSP2_M.
DR   InterPro; IPR043611; CoV_NSP3_C.
DR   InterPro; IPR047566; CoV_NSP3_Y3.
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; IPR046435; N7_MTase_CoV.
DR   InterPro; IPR043609; NendoU_nidovirus.
DR   InterPro; IPR044863; NIRAN.
DR   InterPro; IPR046438; NIV_2_O_MTASE.
DR   InterPro; IPR046436; NIV_EXON.
DR   InterPro; IPR036333; NSP10_sf_CoV.
DR   InterPro; IPR047570; NSP12_IF_CoV.
DR   InterPro; IPR044343; NSP13_1B_dom_CoV.
DR   InterPro; IPR047912; Nsp13_helicase_alphaCoV.
DR   InterPro; IPR048673; NSP13_stalk_CoV.
DR   InterPro; IPR048672; NSP13_ZBD_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; IPR044322; NSP15_M_alpha_beta_CoV.
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; IPR046441; RdRp_CoV.
DR   InterPro; IPR009469; RdRp_N_CoV.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR43788:SF8; HELICASE WITH ZINC FINGER 2; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF13604; AAA_30; 1.
DR   Pfam; PF06471; CoV_ExoN; 1.
DR   Pfam; PF06460; CoV_Methyltr_2; 1.
DR   Pfam; PF09401; CoV_NSP10; 1.
DR   Pfam; PF20631; CoV_NSP13_1B; 1.
DR   Pfam; PF20633; CoV_NSP13_stalk; 1.
DR   Pfam; PF20632; CoV_NSP13_ZBD; 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; SSF144246; Coronavirus NSP10-like; 1.
DR   SUPFAM; SSF140367; Coronavirus NSP7-like; 1.
DR   SUPFAM; SSF143076; Coronavirus NSP8-like; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF142877; EndoU-like; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF101816; Replicase NSP9; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR   PROSITE; PS51993; COV_3ECTO; 1.
DR   PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
DR   PROSITE; PS51954; COV_N7_MTASE; 1.
DR   PROSITE; PS51962; COV_NSP1; 1.
DR   PROSITE; PS52000; COV_NSP12_IF; 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_Y; 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   Disulfide bond; Endonuclease; Exonuclease; Helicase; Host cytoplasm;
KW   Host membrane; 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="Viral protein genome-linked nsp9"
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 nsp12"
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          2005..2070
FT                   /note="3Ecto"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DOMAIN          2144..2483
FT                   /note="CoV Nsp3 Y"
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          4329..4427
FT                   /note="Nsp12 Interface"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
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..5108
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; degenerate"
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          2144..2234
FT                   /note="Y1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2148..2161
FT                   /note="ZF1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2194..2204
FT                   /note="ZF2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2235..2483
FT                   /note="CoV-Y"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2235..2324
FT                   /note="Y2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2325..2381
FT                   /note="Y3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2382..2483
FT                   /note="Y4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   REGION          2491..2854
FT                   /note="HD2"
FT   REGION          3281..3487
FT                   /note="HD3"
FT   REGION          4430..4644
FT                   /note="RdRp Fingers N-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          4645..4683
FT                   /note="RdRp Palm N-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          4684..4742
FT                   /note="RdRp Fingers C-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          4743..4878
FT                   /note="RdRp Palm C-ter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   REGION          4879..4995
FT                   /note="RdRp Thumb"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
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        1218
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        1868
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                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         248
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT   BINDING         1780
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1783
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1813
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         1815
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT   BINDING         2148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2201
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         2204
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT   BINDING         4007
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4010
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4016
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4023
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4049
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4052
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4060
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4062
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT   BINDING         4358
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4364
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4369
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4373
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01344"
FT   BINDING         4550
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         4705
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         4708
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         4709
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT   BINDING         5000
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5003
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5011
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5014
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5021
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5024
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5028
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5034
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5045
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5050
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5067
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT   BINDING         5070
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="11"
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="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5801
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5817
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5820
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5848
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5852
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5855
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT   BINDING         5870
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="13"
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="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6054
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6065
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT   BINDING         6068
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="14"
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   DISULFID        2021..2048
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
FT   DISULFID        2039..2045
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01337"
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
//