R1A_CVH22
ID R1A_CVH22 Reviewed; 4085 AA.
AC P0C6U2; Q05002;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Replicase polyprotein 1a;
DE Short=pp1a;
DE AltName: Full=ORF1a 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=Non-structural protein 11;
DE Short=nsp11;
GN ORFNames=1a;
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].
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 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 [5]
RP ERRATUM OF PUBMED:10329692.
RA Herold J., Siddell S.G., Gorbalenya A.E.;
RL J. Biol. Chem. 274:21490-21490(1999).
RN [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 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: 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 -!- CATALYTIC ACTIVITY:
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 -!- 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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6U2-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=P0C6X1-1; 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 1a]: Produced by
CC conventional translation.
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; AAG48590.1; -; Genomic_RNA.
DR EMBL; X69721; CAA49377.1; -; Genomic_RNA.
DR PIR; S28600; S28600.
DR RefSeq; NP_073550.1; NC_002645.1. [P0C6U2-1]
DR PDB; 1P9S; X-ray; 2.54 A; A/B=2966-3265.
DR PDB; 2ZU2; X-ray; 1.80 A; A/B=2966-3267.
DR PDB; 3EWQ; X-ray; 2.10 A; A=1269-1436.
DR PDB; 3EWR; X-ray; 2.01 A; A=1269-1436.
DR PDBsum; 1P9S; -.
DR PDBsum; 2ZU2; -.
DR PDBsum; 3EWQ; -.
DR PDBsum; 3EWR; -.
DR SASBDB; P0C6U2; -.
DR SMR; P0C6U2; -.
DR MEROPS; C30.003; -.
DR PRIDE; P0C6U2; -.
DR DNASU; 918764; -.
DR GeneID; 918764; -.
DR SABIO-RK; P0C6U2; -.
DR EvolutionaryTrace; P0C6U2; -.
DR Proteomes; UP000006716; Genome.
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:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase 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:0016740; F:transferase activity; IEA:InterPro.
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: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:0019079; P:viral genome replication; IEA:InterPro.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR CDD; cd21558; alphaCoV-Nsp6; 1.
DR CDD; cd21665; alphaCoV_Nsp5_Mpro; 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; cd21466; Ubl2_cv_PLpro_N_Nsp3-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; 2.30.30.1000; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.40.10.250; -; 1.
DR Gene3D; 3.30.70.3540; -; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR InterPro; IPR038634; A-CoV_nsp1_sf.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
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; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR044371; Macro_X_NSP3-like.
DR InterPro; IPR036333; NSP10_sf_CoV.
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; IPR011050; Pectin_lyase_fold/virulence.
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; IPR018995; RNA_synth_NSP10_CoV.
DR Pfam; PF09401; CoV_NSP10; 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; PF01661; Macro; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF101816; SSF101816; 1.
DR SUPFAM; SSF140367; SSF140367; 1.
DR SUPFAM; SSF143076; SSF143076; 1.
DR SUPFAM; SSF144246; SSF144246; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
DR PROSITE; PS51962; COV_NSP1; 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; PS51442; M_PRO; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51124; PEPTIDASE_C16; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; 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 Membrane; Metal-binding;
KW Modulation of host ubiquitin pathway by viral deubiquitinase;
KW Modulation of host ubiquitin pathway by virus; Protease;
KW Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
KW Thiol protease; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Viral immunoevasion; Zinc; Zinc-finger.
FT CHAIN 1..4085
FT /note="Replicase polyprotein 1a"
FT /id="PRO_0000338182"
FT CHAIN 1..111
FT /note="Non-structural protein 1"
FT /id="PRO_0000338183"
FT CHAIN 112..897
FT /note="Non-structural protein 2"
FT /id="PRO_0000338184"
FT CHAIN 898..2484
FT /note="Non-structural protein 3"
FT /id="PRO_0000338185"
FT CHAIN 2485..2965
FT /note="Non-structural protein 4"
FT /id="PRO_0000338186"
FT CHAIN 2966..3267
FT /note="3C-like proteinase"
FT /id="PRO_0000338187"
FT CHAIN 3268..3546
FT /note="Non-structural protein 6"
FT /id="PRO_0000338188"
FT CHAIN 3547..3629
FT /note="Non-structural protein 7"
FT /id="PRO_0000338189"
FT CHAIN 3630..3824
FT /note="Non-structural protein 8"
FT /id="PRO_0000338190"
FT CHAIN 3825..3933
FT /note="Non-structural protein 9"
FT /id="PRO_0000338191"
FT CHAIN 3934..4068
FT /note="Non-structural protein 10"
FT /id="PRO_0000338192"
FT CHAIN 4069..4085
FT /note="Non-structural protein 11"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338193"
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 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 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 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 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 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 CONFLICT 1982
FT /note="A -> Q (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 4042
FT /note="F -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 1275..1278
FT /evidence="ECO:0007829|PDB:3EWR"
FT STRAND 1281..1285
FT /evidence="ECO:0007829|PDB:3EWR"
FT HELIX 1288..1294
FT /evidence="ECO:0007829|PDB:3EWR"
FT STRAND 1298..1304
FT /evidence="ECO:0007829|PDB:3EWR"
FT HELIX 1313..1321
FT /evidence="ECO:0007829|PDB:3EWR"
FT TURN 1322..1324
FT /evidence="ECO:0007829|PDB:3EWR"
FT HELIX 1325..1333
FT /evidence="ECO:0007829|PDB:3EWR"
FT STRAND 1345..1350
FT /evidence="ECO:0007829|PDB:3EWR"
FT STRAND 1353..1359
FT /evidence="ECO:0007829|PDB:3EWR"
FT HELIX 1367..1380
FT /evidence="ECO:0007829|PDB:3EWR"
FT STRAND 1381..1383
FT /evidence="ECO:0007829|PDB:3EWR"
FT STRAND 1385..1387
FT /evidence="ECO:0007829|PDB:3EWR"
FT HELIX 1399..1409
FT /evidence="ECO:0007829|PDB:3EWR"
FT STRAND 1415..1419
FT /evidence="ECO:0007829|PDB:3EWR"
FT HELIX 1422..1433
FT /evidence="ECO:0007829|PDB:3EWR"
FT HELIX 2976..2979
FT /evidence="ECO:0007829|PDB:2ZU2"
FT STRAND 2982..2987
FT /evidence="ECO:0007829|PDB:2ZU2"
FT STRAND 2990..2997
FT /evidence="ECO:0007829|PDB:2ZU2"
FT STRAND 3000..3004
FT /evidence="ECO:0007829|PDB:2ZU2"
FT HELIX 3005..3008
FT /evidence="ECO:0007829|PDB:2ZU2"
FT HELIX 3018..3024
FT /evidence="ECO:0007829|PDB:2ZU2"
FT HELIX 3027..3029
FT /evidence="ECO:0007829|PDB:2ZU2"
FT STRAND 3030..3034
FT /evidence="ECO:0007829|PDB:2ZU2"
FT STRAND 3037..3039
FT /evidence="ECO:0007829|PDB:2ZU2"
FT STRAND 3041..3047
FT /evidence="ECO:0007829|PDB:2ZU2"
FT STRAND 3050..3057
FT /evidence="ECO:0007829|PDB:2ZU2"
FT STRAND 3064..3067
FT /evidence="ECO:0007829|PDB:2ZU2"
FT STRAND 3075..3093
FT /evidence="ECO:0007829|PDB:2ZU2"
FT STRAND 3112..3117
FT /evidence="ECO:0007829|PDB:2ZU2"
FT STRAND 3120..3130
FT /evidence="ECO:0007829|PDB:2ZU2"
FT STRAND 3136..3139
FT /evidence="ECO:0007829|PDB:2ZU2"
FT HELIX 3146..3148
FT /evidence="ECO:0007829|PDB:2ZU2"
FT STRAND 3151..3154
FT /evidence="ECO:0007829|PDB:2ZU2"
FT HELIX 3165..3177
FT /evidence="ECO:0007829|PDB:2ZU2"
FT HELIX 3191..3199
FT /evidence="ECO:0007829|PDB:2ZU2"
FT TURN 3200..3202
FT /evidence="ECO:0007829|PDB:2ZU2"
FT HELIX 3209..3212
FT /evidence="ECO:0007829|PDB:2ZU2"
FT HELIX 3213..3219
FT /evidence="ECO:0007829|PDB:2ZU2"
FT HELIX 3223..3233
FT /evidence="ECO:0007829|PDB:2ZU2"
FT STRAND 3245..3247
FT /evidence="ECO:0007829|PDB:2ZU2"
FT HELIX 3254..3262
FT /evidence="ECO:0007829|PDB:2ZU2"
SQ SEQUENCE 4085 AA; 454215 MW; EAB38E3D375F36B5 CRC64;
MACNRVTLAV ASDSEISANG CSTIAQAVRR YSEAASNGFR ACRFVSLDLQ DCIVGIADDT
YVMGLHGNQT LFCNIMKFSD RPFMLHGWLV FSNSNYLLEE FDVVFGKRGG GNVTYTDQYL
CGADGKPVMS EDLWQFVDHF GENEEIIING HTYVCAWLTK RKPLDYKRQN NLAIEEIEYV
HGDALHTLRN GSVLEMAKEV KTSSKVVLSD ALDKLYKVFG SPVMTNGSNI LEAFTKPVFI
SALVQCTCGT KSWSVGDWTG FKSSCCNVIS NKLCVVPGNV KPGDAVITTQ QAGAGIKYFC
GMTLKFVANI EGVSVWRVIA LQSVDCFVAS STFVEEEHVN RMDTFCFNVR NSVTDECRLA
MLGAEMTSNV RRQVASGVID ISTGWFDVYD DIFAESKPWF VRKAEDIFGP CWSALASALK
QLKVTTGELV RFVKSICNSA VAVVGGTIQI LASVPEKFLN AFDVFVTAIQ TVFDCAVETC
TIAGKAFDKV FDYVLLDNAL VKLVTTKLKG VRERGLNKVK YATVVVGSTE EVKSSRVERS
TAVLTIANNY SKLFDEGYTV VIGDVAYFVS DGYFRLMASP NSVLTTAVYK PLFAFNVNVM
GTRPEKFPTT VTCENLESAV LFVNDKITEF QLDYSIDVID NEIIVKPNIS LCVPLYVRDY
VDKWDDFCRQ YSNESWFEDD YRAFISVLDI TDAAVKAAES KAFVDTIVPP CPSILKVIDG
GKIWNGVIKN VNSVRDWLKS LKLNLTQQGL LGTCAKRFKR WLGILLEAYN AFLDTVVSTV
KIGGLTFKTY AFDKPYIVIR DIVCKVENKT EAEWIELFPH NDRIKSFSTF ESAYMPIADP
THFDIEEVEL LDAEFVEPGC GGILAVIDEH VFYKKDGVYY PSNGTNILPV AFTKAAGGKV
SFSDDVEVKD IEPVYRVKLC FEFEDEKLVD VCEKAIGKKI KHEGDWDSFC KTIQSALSVV
SCYVNLPTYY IYDEEGGNDL SLPVMISEWP LSVQQAQQEA TLPDIAEDVV DQVEEVNSIF
DIETVDVKHD VSPFEMPFEE LNGLKILKQL DNNCWVNSVM LQIQLTGILD GDYAMQFFKM
GRVAKMIERC YTAEQCIRGA MGDVGLCMYR LLKDLHTGFM VMDYKCSCTS GRLEESGAVL
FCTPTKKAFP YGTCLNCNAP RMCTIRQLQG TIIFVQQKPE PVNPVSFVVK PVCSSIFRGA
VSCGHYQTNI YSQNLCVDGF GVNKIQPWTN DALNTICIKD ADYNAKVEIS VTPIKNTVDT
TPKEEFVVKE KLNAFLVHDN VAFYQGDVDT VVNGVDFDFI VNAANENLAH GGGLAKALDV
YTKGKLQRLS KEHIGLAGKV KVGTGVMVEC DSLRIFNVVG PRKGKHERDL LIKAYNTINN
EQGTPLTPIL SCGIFGIKLE TSLEVLLDVC NTKEVKVFVY TDTEVCKVKD FVSGLVNVQK
VEQPKIEPKP VSVIKVAPKP YRVDGKFSYF TEDLLCVADD KPIVLFTDSM LTLDDRGLAL
DNALSGVLSA AIKDCVDINK AIPSGNLIKF DIGSVVVYMC VVPSEKDKHL DNNVQRCTRK
LNRLMCDIVC TIPADYILPL VLSSLTCNVS FVGELKAAEA KVITIKVTED GVNVHDVTVT
TDKSFEQQVG VIADKDKDLS GAVPSDLNTS ELLTKAIDVD WVEFYGFKDA VTFATVDHSA
FAYESAVVNG IRVLKTSDNN CWVNAVCIAL QYSKPHFISQ GLDAAWNKFV LGDVEIFVAF
VYYVARLMKG DKGDAEDTLT KLSKYLANEA QVQLEHYSSC VECDAKFKNS VASINSAIVC
ASVKRDGVQV GYCVHGIKYY SRVRSVRGRA IIVSVEQLEP CAQSRLLSGV AYTAFSGPVD
KGHYTVYDTA KKSMYDGDRF VKHDLSLLSV TSVVMVGGYV APVNTVKPKP VINQLDEKAQ
KFFDFGDFLI HNFVIFFTWL LSMFTLCKTA VTTGDVKIMA KAPQRTGVVL KRSLKYNLKA
SAAVLKSKWW LLAKFTKLLL LIYTLYSVVL LCVRFGPFNF CSETVNGYAK SNFVKDDYCD
GSLGCKMCLF GYQELSQFSH LDVVWKHITD PLFSNMQPFI VMVLLLIFGD NYLRCFLLYF
VAQMISTVGV FLGYKETNWF LHFIPFDVIC DELLVTVIVI KVISFVRHVL FGCENPDCIA
CSKSARLKRF PVNTIVNGVQ RSFYVNANGG SKFCKKHRFF CVDCDSYGYG STFITPEVSR
ELGNITKTNV QPTGPAYVMI DKVEFENGFY RLYSCETFWR YNFDITESKY SCKEVFKNCN
VLDDFIVFNN NGTNVTQVKN ASVYFSQLLC RPIKLVDSEL LSTLSVDFNG VLHKAYIDVL
RNSFGKDLNA NMSLAECKRA LGLSISDHEF TSAISNAHRC DVLLSDLSFN NFVSSYAKPE
EKLSAYDLAC CMRAGAKVVN ANVLTKDQTP IVWHAKDFNS LSAEGRKYIV KTSKAKGLTF
LLTINENQAV TQIPATSIVA KQGAGDAGHS LTWLWLLCGL VCLIQFYLCF FMPYFMYDIV
SSFEGYDFKY IENGQLKNFE APLKCVRNVF ENFEDWHYAK FGFTPLNKQS CPIVVGVSEI
VNTVAGIPSN VYLVGKTLIF TLQAAFGNAG VCYDIFGVTT PEKCIFTSAC TRLEGLGGNN
VYCYNTALME GSLPYSSIQA NAYYKYDNGN FIKLPEVIAQ GFGFRTVRTI ATKYCRVGEC
VESNAGVCFG FDKWFVNDGR VANGYVCGTG LWNLVFNILS MFSSSFSVAA MSGQILLNCA
LGAFAIFCCF LVTKFRRMFG DLSVGVCTVV VAVLLNNVSY IVTQNLVTMI AYAILYFFAT
RSLRYAWIWC AAYLIAYISF APWWLCAWYF LAMLTGLLPS LLKLKVSTNL FEGDKFVGTF
ESAAAGTFVI DMRSYEKLAN SISPEKLKSY AASYNRYKYY SGNANEADYR CACYAYLAKA
MLDFSRDHND ILYTPPTVSY GSTLQAGLRK MAQPSGFVEK CVVRVCYGNT VLNGLWLGDI
VYCPRHVIAS NTTSAIDYDH EYSIMRLHNF SIISGTAFLG VVGATMHGVT LKIKVSQTNM
HTPRHSFRTL KSGEGFNILA CYDGCAQGVF GVNMRTNWTI RGSFINGACG SPGYNLKNGE
VEFVYMHQIE LGSGSHVGSS FDGVMYGGFE DQPNLQVESA NQMLTVNVVA FLYAAILNGC
TWWLKGEKLF VEHYNEWAQA NGFTAMNGED AFSILAAKTG VCVERLLHAI QVLNNGFGGK
QILGYSSLND EFSINEVVKQ MFGVNLQSGK TTSMFKSISL FAGFFVMFWA ELFVYTTTIW
VNPGFLTPFM ILLVALSLCL TFVVKHKVLF LQVFLLPSII VAAIQNCAWD YHVTKVLAEK
FDYNVSVMQM DIQGFVNIFI CLFVALLHTW RFAKERCTHW CTYLFSLIAV LYTALYSYDY
VSLLVMLLCA ISNEWYIGAI IFRICRFGVA FLPVEYVSYF DGVKTVLLFY MLLGFVSCMY
YGLLYWINRF CKCTLGVYDF CVSPAEFKYM VANGLNAPNG PFDALFLSFK LMGIGGPRTI
KVSTVQSKLT DLKCTNVVLM GILSNMNIAS NSKEWAYCVE MHNKINLCDD PETAQELLLA
LLAFFLSKHS DFGLGDLVDS YFENDSILQS VASSFVGMPS FVAYETARQE YENAVANGSS
PQIIKQLKKA MNVAKAEFDR ESSVQKKINR MAEQAAAAMY KEARAVNRKS KVVSAMHSLL
FGMLRRLDMS SVDTILNMAR NGVVPLSVIP ATSAARLVVV VPDHDSFVKM MVDGFVHYAG
VVWTLQEVKD NDGKNVHLKD VTKENQEILV WPLILTCERV VKLQNNEIMP GKMKVKATKG
EGDGGITSEG NALYNNEGGR AFMYAYVTTK PGMKYVKWEH DSGVVTVELE PPCRFVIDTP
TGPQIKYLYF VKNLNNLRRG AVLGYIGATV RLQAGKQTEF VSNSHLLTHC SFAVDPAAAY
LDAVKQGAKP VGNCVKMLTN GSGSGQAITC TIDSNTTQDT YGGASVCIYC RAHVAHPTMD
GFCQYKGKWV QVPIGTNDPI RFCLENTVCK VCGCWLNHGC TCDRTAIQSF DNSYLNESGA
LVPLD
