R1A_MERS1
ID R1A_MERS1 Reviewed; 4391 AA.
AC K9N638;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Replicase polyprotein 1a;
DE Short=pp1a;
DE AltName: Full=ORF1a polyprotein;
DE Contains:
DE RecName: Full=Host translation inhibitor nsp1;
DE Short=nsp1;
DE AltName: Full=Leader protein;
DE Contains:
DE RecName: Full=Non-structural protein 2;
DE Short=nsp2;
DE AltName: Full=p65 homolog;
DE Contains:
DE RecName: Full=Papain-like proteinase;
DE Short=PL-PRO;
DE EC=3.4.19.12;
DE EC=3.4.22.69;
DE AltName: Full=Non-structural protein 3;
DE Short=nsp3;
DE Contains:
DE RecName: Full=Non-structural protein 4;
DE Short=nsp4;
DE Contains:
DE RecName: Full=3C-like proteinase;
DE Short=3CL-PRO;
DE Short=3CLp;
DE EC=3.4.22.-;
DE AltName: Full=nsp5;
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 Contains:
DE RecName: Full=Non-structural protein 8;
DE Short=nsp8;
DE Contains:
DE RecName: Full=Non-structural protein 9;
DE Short=nsp9;
DE Contains:
DE RecName: Full=Non-structural protein 10;
DE Short=nsp10;
DE AltName: Full=Growth factor-like peptide;
DE Short=GFL;
DE Contains:
DE RecName: Full=Non-structural protein 11;
DE Short=nsp11;
GN ORFNames=1a;
OS Middle East respiratory syndrome-related coronavirus (isolate United
OS Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Merbecovirus.
OX NCBI_TaxID=1263720;
OH NCBI_TaxID=9838; Camelus dromedarius (Dromedary) (Arabian camel).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Nishi O., Iiyama K., Yasunaga-Aoki C., Shimizu S.;
RT "The phylogenetic status and pathogenicity of a new isolate of Metarhizium
RT sp. from a fruit beetle larvae in Japan.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION (PAPAIN-LIKE PROTEINASE).
RX PubMed=25142582; DOI=10.1128/jvi.01294-14;
RA Baez-Santos Y.M., Mielech A.M., Deng X., Baker S., Mesecar A.D.;
RT "Catalytic function and substrate specificity of the papain-like protease
RT domain of nsp3 from the Middle East respiratory syndrome coronavirus.";
RL J. Virol. 88:12511-12527(2014).
RN [3]
RP FUNCTION (NSP1).
RX PubMed=26311885; DOI=10.1128/jvi.01352-15;
RA Lokugamage K.G., Narayanan K., Nakagawa K., Terasaki K., Ramirez S.I.,
RA Tseng C.T., Makino S.;
RT "Middle east respiratory syndrome coronavirus nsp1 inhibits host gene
RT expression by selectively targeting mRNAs transcribed in the nucleus while
RT sparing mRNAs of cytoplasmic origin.";
RL J. Virol. 89:10970-10981(2015).
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 {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Host translation inhibitor nsp1]: Promotes the degradation
CC of host mRNAs by inducing an endonucleolytic RNA cleavage in template
CC mRNAs, and inhibits of host mRNA translation, a function that is
CC separable from its RNA cleavage activity. By suppressing host gene
CC expression, nsp1 facilitates efficient viral gene expression in
CC infected cells and evasion from host immune response.
CC {ECO:0000269|PubMed:26311885}.
CC -!- FUNCTION: [Non-structural protein 2]: May play a role in the modulation
CC of host cell survival signaling pathway by interacting with host PHB
CC and PHB2. Indeed, these two proteins play a role in maintaining the
CC functional integrity of the mitochondria and protecting cells from
CC various stresses. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Papain-like proteinase]: Responsible for the cleavages
CC located at the N-terminus of the replicase polyprotein. In addition,
CC PL-PRO possesses a deubiquitinating/deISGylating activity and processes
CC both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular
CC substrates. Participates, together with nsp4, in the assembly of
CC virally induced cytoplasmic double-membrane vesicles necessary for
CC viral replication. Antagonizes innate immune induction of type I
CC interferon by blocking the phosphorylation, dimerization and subsequent
CC nuclear translocation of host IRF3. Prevents also host NF-kappa-B.
CC signaling. {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:25142582}.
CC -!- FUNCTION: [Non-structural protein 4]: Participates in the assembly of
CC virally-induced cytoplasmic double-membrane vesicles necessary for
CC viral replication. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [3C-like proteinase]: Cleaves the C-terminus of replicase
CC polyprotein at 11 sites. Recognizes substrates containing the core
CC sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-
CC phosphate (ADRP). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000255|PROSITE-
CC ProRule:PRU00772}.
CC -!- FUNCTION: [Non-structural protein 6]: Plays a role in the initial
CC induction of autophagosomes from host reticulum endoplasmic. Later,
CC limits the expansion of these phagosomes that are no longer able to
CC deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8
CC subunits of each) that may participate in viral replication by acting
CC as a primase. Alternatively, may synthesize substantially longer
CC products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8
CC subunits of each) that may participate in viral replication by acting
CC as a primase. Alternatively, may synthesize substantially longer
CC products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 9]: May participate in viral
CC replication by acting as a ssRNA-binding protein.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 10]: Plays a pivotal role in viral
CC transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16
CC 2'-O-methyltransferase activities. Therefore plays an essential role in
CC viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- CATALYTIC ACTIVITY:
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;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides
CC corresponding to the two self-cleavage sites of the SARS 3C-like
CC proteinase are the two most reactive peptide substrates. The enzyme
CC exhibits a strong preference for substrates containing Gln at P1
CC position and Leu at P2 position.; EC=3.4.22.69;
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: Nsp2 interacts with host PHB and PHB2. 3CL-PRO exists as
CC monomer and homodimer. Nsp4 interacts with PL-PRO and nsp6. Only the
CC homodimer shows catalytic activity. Eight copies of nsp7 and eight
CC copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling
CC ring structure. Nsp9 is a dimer. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- INTERACTION:
CC K9N638; PRO_0000037312 [P0C6X7]: rep; Xeno; NbExp=2; IntAct=EBI-25618448, EBI-25487250;
CC PRO_0000422456; Q64339: Isg15; Xeno; NbExp=2; IntAct=EBI-25635184, EBI-8345781;
CC PRO_0000422456; Q9GKP4: ISG17; Xeno; NbExp=2; IntAct=EBI-25635184, EBI-25821151;
CC PRO_0000422461; PRO_0000422460 [K9N638]: 1a; NbExp=2; IntAct=EBI-26366276, EBI-26366263;
CC -!- SUBCELLULAR LOCATION: [Papain-like proteinase]: Host membrane; Multi-
CC pass membrane protein. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane; Multi-
CC pass membrane protein. Host cytoplasm. Note=Localizes in virally-
CC induced cytoplasmic double-membrane vesicles.
CC {ECO:0000250|UniProtKB:P0C6X7}.
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=K9N638-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=K9N7C7-1; 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 (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1a]: Produced by
CC conventional translation.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000305}.
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DR EMBL; KC164505; AFY13305.1; -; Genomic_RNA.
DR PDB; 4R3D; X-ray; 2.82 A; A/B=1481-1811.
DR PDB; 5DUS; X-ray; 1.43 A; A=1110-1273.
DR PDB; 5HIH; X-ray; 1.66 A; A=1109-1275.
DR PDB; 5WKJ; X-ray; 2.05 A; A=3248-3553.
DR PDB; 5WKK; X-ray; 1.55 A; A=3248-3553.
DR PDB; 5WKL; X-ray; 1.85 A; A=3248-3553.
DR PDB; 5WKM; X-ray; 2.25 A; A=3248-3553.
DR PDB; 7T3Y; X-ray; 1.90 A; A/B=3248-3553.
DR PDB; 7T3Z; X-ray; 1.95 A; A/B=3248-3553.
DR PDB; 7T40; X-ray; 1.70 A; A=3248-3553.
DR PDB; 7T41; X-ray; 2.10 A; A=3248-3553.
DR PDBsum; 4R3D; -.
DR PDBsum; 5DUS; -.
DR PDBsum; 5HIH; -.
DR PDBsum; 5WKJ; -.
DR PDBsum; 5WKK; -.
DR PDBsum; 5WKL; -.
DR PDBsum; 5WKM; -.
DR PDBsum; 7T3Y; -.
DR PDBsum; 7T3Z; -.
DR PDBsum; 7T40; -.
DR PDBsum; 7T41; -.
DR SMR; K9N638; -.
DR BioGRID; 4383912; 1.
DR IntAct; K9N638; 10.
DR DrugBank; DB15797; GC-373.
DR DrugBank; DB15796; GC-376 free acid.
DR PRIDE; K9N638; -.
DR SABIO-RK; K9N638; -.
DR Proteomes; UP000139997; 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: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:0002151; F:G-quadruplex RNA binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
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:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0039579; P:suppression by virus of host ISG15-protein conjugation; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; 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; cd21560; betaCoV-Nsp6; 1.
DR CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
DR CDD; cd21517; cv_beta_Nsp2_MERS-like; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21563; Macro_cv_SUD-M_Nsp3-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21523; SUD_C_MERS-CoV_Nsp3; 1.
DR CDD; cd21467; Ubl1_cv_Nsp3_N-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; -; 1.
DR Gene3D; 1.10.8.370; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.40.10.250; -; 1.
DR Gene3D; 2.60.120.1680; -; 1.
DR Gene3D; 3.10.20.350; -; 1.
DR Gene3D; 3.10.20.540; -; 1.
DR Gene3D; 3.30.70.3540; -; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.220.20; -; 1.
DR Gene3D; 3.40.50.11020; -; 1.
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; IPR022733; DPUP_SUD_C_bCoV.
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; IPR021590; NSP1_bCoV.
DR InterPro; IPR044388; NSP2_MERS-like.
DR InterPro; IPR043615; NSP2_N_CoV.
DR InterPro; IPR024375; NSP3_bCoV.
DR InterPro; IPR032592; NSP3_NAB_bCoV.
DR InterPro; IPR042570; NSP3_NAB_bCoV_sf.
DR InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
DR InterPro; IPR044382; NSP3_SUD_C_MERS-CoV.
DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR InterPro; IPR038083; NSP3A-like.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR044367; NSP6_betaCoV.
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; 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; IPR043177; PLpro_N_sf_CoV.
DR InterPro; IPR043503; PLpro_palm_finger_dom_CoV.
DR InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR Pfam; PF16251; bCoV_NAR; 1.
DR Pfam; PF11501; bCoV_NSP1; 1.
DR Pfam; PF11633; bCoV_SUD_M; 1.
DR Pfam; PF09401; CoV_NSP10; 1.
DR Pfam; PF19212; CoV_NSP2_C; 1.
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; 1.
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; SSF159936; SSF159936; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS51963; BCOV_NSP1_C; 1.
DR PROSITE; PS51942; BCOV_NSP3C_C; 1.
DR PROSITE; PS51941; BCOV_NSP3C_M; 1.
DR PROSITE; PS51994; BCOV_NSP3E_G2M; 1.
DR PROSITE; PS51945; BCOV_NSP3E_NAB; 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; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus;
KW Decay of host mRNAs by virus;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Host cytoplasm;
KW Host gene expression shutoff by virus; Host membrane;
KW Host mRNA suppression by virus; Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host IRF3 by virus; Inhibition of host ISG15 by virus;
KW Inhibition of host RLR pathway by virus; Membrane; Metal-binding;
KW Modulation of host ubiquitin pathway by viral deubiquitinase;
KW Modulation of host ubiquitin pathway by virus; Protease; Repeat;
KW Ribosomal frameshifting; RNA-binding; Thiol protease; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Viral immunoevasion; Zinc;
KW Zinc-finger.
FT CHAIN 1..193
FT /note="Host translation inhibitor nsp1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000422454"
FT CHAIN 194..853
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000422455"
FT CHAIN 854..2740
FT /note="Papain-like proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000422456"
FT CHAIN 2741..3247
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000422457"
FT CHAIN 3248..3553
FT /note="3C-like proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000422458"
FT CHAIN 3554..3845
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250"
FT /id="PRO_0000422459"
FT CHAIN 3846..3928
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000422460"
FT CHAIN 3929..4127
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000422461"
FT CHAIN 4128..4237
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250"
FT /id="PRO_0000422462"
FT CHAIN 4238..4377
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250"
FT /id="PRO_0000422463"
FT CHAIN 4378..4391
FT /note="Non-structural protein 11"
FT /evidence="ECO:0000250"
FT /id="PRO_0000422464"
FT TRANSMEM 2105..2125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2177..2197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2281..2301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2305..2325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2330..2350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2757..2777
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3028..3048
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3062..3082
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3104..3124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3125..3145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3559..3579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3593..3613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3618..3638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3664..3684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3691..3711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3740..3760
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3765..3785
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 25..149
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT DOMAIN 165..193
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT DOMAIN 195..475
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 481..715
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 717..853
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 857..966
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1110..1276
FT /note="Macro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1278..1404
FT /note="Macro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1404..1477
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1482..1537
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1552..1823
FT /note="Peptidase C16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1837..1954
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 1967..2088
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2634..2737
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3151..3247
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3248..3553
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3846..3928
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3929..4127
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 4128..4237
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4238..4377
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT ZN_FING 1672..1709
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4311..4327
FT ZN_FING 4354..4367
FT REGION 338..359
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 383..436
FT /note="C2HC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 2040..2363
FT /note="HD1"
FT REGION 2761..3171
FT /note="HD2"
FT REGION 3571..3785
FT /note="HD3"
FT ACT_SITE 1592
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1759
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3288
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3395
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 4311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 4314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 4320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 4327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 4354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 4357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 4365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 4367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT SITE 193..194
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 853..854
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250"
FT SITE 2740..2741
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3247..3248
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3553..3554
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3845..3846
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3928..3929
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4127..4128
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4237..4238
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4377..4378
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT HELIX 1110..1113
FT /evidence="ECO:0007829|PDB:5DUS"
FT STRAND 1116..1118
FT /evidence="ECO:0007829|PDB:5DUS"
FT STRAND 1120..1128
FT /evidence="ECO:0007829|PDB:5DUS"
FT HELIX 1130..1134
FT /evidence="ECO:0007829|PDB:5DUS"
FT STRAND 1141..1146
FT /evidence="ECO:0007829|PDB:5DUS"
FT HELIX 1156..1163
FT /evidence="ECO:0007829|PDB:5DUS"
FT TURN 1164..1166
FT /evidence="ECO:0007829|PDB:5DUS"
FT HELIX 1167..1179
FT /evidence="ECO:0007829|PDB:5DUS"
FT STRAND 1187..1191
FT /evidence="ECO:0007829|PDB:5DUS"
FT STRAND 1195..1203
FT /evidence="ECO:0007829|PDB:5DUS"
FT HELIX 1207..1209
FT /evidence="ECO:0007829|PDB:5DUS"
FT HELIX 1213..1215
FT /evidence="ECO:0007829|PDB:5DUS"
FT HELIX 1216..1221
FT /evidence="ECO:0007829|PDB:5DUS"
FT HELIX 1222..1225
FT /evidence="ECO:0007829|PDB:5DUS"
FT STRAND 1226..1231
FT /evidence="ECO:0007829|PDB:5DUS"
FT HELIX 1243..1253
FT /evidence="ECO:0007829|PDB:5DUS"
FT STRAND 1256..1263
FT /evidence="ECO:0007829|PDB:5DUS"
FT HELIX 1265..1272
FT /evidence="ECO:0007829|PDB:5DUS"
FT STRAND 1484..1494
FT /evidence="ECO:0007829|PDB:4R3D"
FT STRAND 1496..1505
FT /evidence="ECO:0007829|PDB:4R3D"
FT HELIX 1507..1510
FT /evidence="ECO:0007829|PDB:4R3D"
FT STRAND 1513..1516
FT /evidence="ECO:0007829|PDB:4R3D"
FT HELIX 1528..1530
FT /evidence="ECO:0007829|PDB:4R3D"
FT STRAND 1534..1537
FT /evidence="ECO:0007829|PDB:4R3D"
FT HELIX 1543..1553
FT /evidence="ECO:0007829|PDB:4R3D"
FT HELIX 1560..1570
FT /evidence="ECO:0007829|PDB:4R3D"
FT TURN 1571..1573
FT /evidence="ECO:0007829|PDB:4R3D"
FT STRAND 1576..1579
FT /evidence="ECO:0007829|PDB:4R3D"
FT STRAND 1582..1585
FT /evidence="ECO:0007829|PDB:4R3D"
FT TURN 1589..1591
FT /evidence="ECO:0007829|PDB:4R3D"
FT HELIX 1592..1603
FT /evidence="ECO:0007829|PDB:4R3D"
FT STRAND 1607..1611
FT /evidence="ECO:0007829|PDB:4R3D"
FT HELIX 1612..1622
FT /evidence="ECO:0007829|PDB:4R3D"
FT HELIX 1627..1636
FT /evidence="ECO:0007829|PDB:4R3D"
FT HELIX 1647..1655
FT /evidence="ECO:0007829|PDB:4R3D"
FT STRAND 1658..1662
FT /evidence="ECO:0007829|PDB:4R3D"
FT STRAND 1665..1672
FT /evidence="ECO:0007829|PDB:4R3D"
FT TURN 1673..1675
FT /evidence="ECO:0007829|PDB:4R3D"
FT STRAND 1676..1683
FT /evidence="ECO:0007829|PDB:4R3D"
FT HELIX 1684..1687
FT /evidence="ECO:0007829|PDB:4R3D"
FT STRAND 1689..1692
FT /evidence="ECO:0007829|PDB:4R3D"
FT HELIX 1696..1699
FT /evidence="ECO:0007829|PDB:4R3D"
FT STRAND 1703..1706
FT /evidence="ECO:0007829|PDB:4R3D"
FT STRAND 1710..1740
FT /evidence="ECO:0007829|PDB:4R3D"
FT STRAND 1745..1751
FT /evidence="ECO:0007829|PDB:4R3D"
FT STRAND 1759..1766
FT /evidence="ECO:0007829|PDB:4R3D"
FT STRAND 1769..1773
FT /evidence="ECO:0007829|PDB:4R3D"
FT STRAND 1780..1799
FT /evidence="ECO:0007829|PDB:4R3D"
FT HELIX 3258..3261
FT /evidence="ECO:0007829|PDB:5WKK"
FT STRAND 3264..3269
FT /evidence="ECO:0007829|PDB:5WKK"
FT STRAND 3273..3279
FT /evidence="ECO:0007829|PDB:5WKK"
FT STRAND 3282..3286
FT /evidence="ECO:0007829|PDB:5WKK"
FT HELIX 3287..3290
FT /evidence="ECO:0007829|PDB:5WKK"
FT HELIX 3293..3295
FT /evidence="ECO:0007829|PDB:5WKK"
FT STRAND 3296..3298
FT /evidence="ECO:0007829|PDB:5WKL"
FT HELIX 3301..3307
FT /evidence="ECO:0007829|PDB:5WKK"
FT HELIX 3310..3312
FT /evidence="ECO:0007829|PDB:5WKK"
FT STRAND 3313..3316
FT /evidence="ECO:0007829|PDB:5WKK"
FT STRAND 3319..3321
FT /evidence="ECO:0007829|PDB:7T3Z"
FT STRAND 3323..3325
FT /evidence="ECO:0007829|PDB:7T3Z"
FT STRAND 3327..3333
FT /evidence="ECO:0007829|PDB:5WKK"
FT STRAND 3336..3343
FT /evidence="ECO:0007829|PDB:5WKK"
FT STRAND 3350..3353
FT /evidence="ECO:0007829|PDB:5WKK"
FT STRAND 3361..3368
FT /evidence="ECO:0007829|PDB:5WKK"
FT STRAND 3371..3379
FT /evidence="ECO:0007829|PDB:5WKK"
FT STRAND 3398..3403
FT /evidence="ECO:0007829|PDB:5WKK"
FT STRAND 3406..3416
FT /evidence="ECO:0007829|PDB:5WKK"
FT STRAND 3422..3425
FT /evidence="ECO:0007829|PDB:5WKK"
FT HELIX 3432..3434
FT /evidence="ECO:0007829|PDB:7T3Y"
FT STRAND 3437..3440
FT /evidence="ECO:0007829|PDB:5WKK"
FT HELIX 3451..3463
FT /evidence="ECO:0007829|PDB:5WKK"
FT HELIX 3477..3485
FT /evidence="ECO:0007829|PDB:5WKK"
FT TURN 3486..3488
FT /evidence="ECO:0007829|PDB:5WKK"
FT HELIX 3496..3505
FT /evidence="ECO:0007829|PDB:5WKK"
FT HELIX 3509..3520
FT /evidence="ECO:0007829|PDB:5WKK"
FT STRAND 3531..3533
FT /evidence="ECO:0007829|PDB:5WKK"
FT HELIX 3540..3546
FT /evidence="ECO:0007829|PDB:5WKK"
SQ SEQUENCE 4391 AA; 486059 MW; D0A87AE59773BBB8 CRC64;
MSFVAGVTAQ GARGTYRAAL NSEKHQDHVS LTVPLCGSGN LVEKLSPWFM DGENAYEVVK
AMLLKKEPLL YVPIRLAGHT RHLPGPRVYL VERLIACENP FMVNQLAYSS SANGSLVGTT
LQGKPIGMFF PYDIELVTGK QNILLRKYGR GGYHYTPFHY ERDNTSCPEW MDDFEADPKG
KYAQNLLKKL IGGDVTPVDQ YMCGVDGKPI SAYAFLMAKD GITKLADVEA DVAARADDEG
FITLKNNLYR LVWHVERKDV PYPKQSIFTI NSVVQKDGVE NTPPHYFTLG CKILTLTPRN
KWSGVSDLSL KQKLLYTFYG KESLENPTYI YHSAFIECGS CGNDSWLTGN AIQGFACGCG
ASYTANDVEV QSSGMIKPNA LLCATCPFAK GDSCSSNCKH SVAQLVSYLS ERCNVIADSK
SFTLIFGGVA YAYFGCEEGT MYFVPRAKSV VSRIGDSIFT GCTGSWNKVT QIANMFLEQT
QHSLNFVGEF VVNDVVLAIL SGTTTNVDKI RQLLKGVTLD KLRDYLADYD VAVTAGPFMD
NAINVGGTGL QYAAITAPYV VLTGLGESFK KVATIPYKVC NSVKDTLTYY AHSVLYRVFP
YDMDSGVSSF SELLFDCVDL SVASTYFLVR LLQDKTGDFM STIITSCQTA VSKLLDTCFE
ATEATFNFLL DLAGLFRIFL RNAYVYTSQG FVVVNGKVST LVKQVLDLLN KGMQLLHTKV
SWAGSNISAV IYSGRESLIF PSGTYYCVTT KAKSVQQDLD VILPGEFSKK QLGLLQPTDN
STTVSVTVSS NMVETVVGQL EQTNMHSPDV IVGDYVIISE KLFVRSKEED GFAFYPACTN
GHAVPTLFRL KGGAPVKKVA FGGDQVHEVA AVRSVTVEYN IHAVLDTLLA SSSLRTFVVD
KSLSIEEFAD VVKEQVSDLL VKLLRGMPIP DFDLDDFIDA PCYCFNAEGD ASWSSTMIFS
LHPVECDEEC SEVEASDLEE GESECISETS TEQVDVSHEI SDDEWAAAVD EAFPLDEAED
VTESVQEEAQ PVEVPVEDIA QVVIADTLQE TPVVSDTVEV PPQVVKLPSE PQTIQPEVKE
VAPVYEADTE QTQSVTVKPK RLRKKRNVDP LSNFEHKVIT ECVTIVLGDA IQVAKCYGES
VLVNAANTHL KHGGGIAGAI NAASKGAVQK ESDEYILAKG PLQVGDSVLL QGHSLAKNIL
HVVGPDARAK QDVSLLSKCY KAMNAYPLVV TPLVSAGIFG VKPAVSFDYL IREAKTRVLV
VVNSQDVYKS LTIVDIPQSL TFSYDGLRGA IRKAKDYGFT VFVCTDNSAN TKVLRNKGVD
YTKKFLTVDG VQYYCYTSKD TLDDILQQAN KSVGIISMPL GYVSHGLDLI QAGSVVRRVN
VPYVCLLANK EQEAILMSED VKLNPSEDFI KHVRTNGGYN SWHLVEGELL VQDLRLNKLL
HWSDQTICYK DSVFYVVKNS TAFPFETLSA CRAYLDSRTT QQLTIEVLVT VDGVNFRTVV
LNNKNTYRSQ LGCVFFNGAD ISDTIPDEKQ NGHSLYLADN LTADETKALK ELYGPVDPTF
LHRFYSLKAA VHKWKMVVCD KVRSLKLSDN NCYLNAVIMT LDLLKDIKFV IPALQHAFMK
HKGGDSTDFI ALIMAYGNCT FGAPDDASRL LHTVLAKAEL CCSARMVWRE WCNVCGIKDV
VLQGLKACCY VGVQTVEDLR ARMTYVCQCG GERHRQIVEH TTPWLLLSGT PNEKLVTTST
APDFVAFNVF QGIETAVGHY VHARLKGGLI LKFDSGTVSK TSDWKCKVTD VLFPGQKYSS
DCNVVRYSLD GNFRTEVDPD LSAFYVKDGK YFTSEPPVTY SPATILAGSV YTNSCLVSSD
GQPGGDAISL SFNNLLGFDS SKPVTKKYTY SFLPKEDGDV LLAEFDTYDP IYKNGAMYKG
KPILWVNKAS YDTNLNKFNR ASLRQIFDVA PIELENKFTP LSVESTPVEP PTVDVVALQQ
EMTIVKCKGL NKPFVKDNVS FVADDSGTPV VEYLSKEDLH TLYVDPKYQV IVLKDNVLSS
MLRLHTVESG DINVVAASGS LTRKVKLLFR ASFYFKEFAT RTFTATTAVG SCIKSVVRHL
GVTKGILTGC FSFVKMLFML PLAYFSDSKL GTTEVKVSAL KTAGVVTGNV VKQCCTAAVD
LSMDKLRRVD WKSTLRLLLM LCTTMVLLSS VYHLYVFNQV LSSDVMFEDA QGLKKFYKEV
RAYLGISSAC DGLASAYRAN SFDVPTFCAN RSAMCNWCLI SQDSITHYPA LKMVQTHLSH
YVLNIDWLWF AFETGLAYML YTSAFNWLLL AGTLHYFFAQ TSIFVDWRSY NYAVSSAFWL
FTHIPMAGLV RMYNLLACLW LLRKFYQHVI NGCKDTACLL CYKRNRLTRV EASTVVCGGK
RTFYITANGG ISFCRRHNWN CVDCDTAGVG NTFICEEVAN DLTTALRRPI NATDRSHYYV
DSVTVKETVV QFNYRRDGQP FYERFPLCAF TNLDKLKFKE VCKTTTGIPE YNFIIYDSSD
RGQESLARSA CVYYSQVLCK SILLVDSSLV TSVGDSSEIA TKMFDSFVNS FVSLYNVTRD
KLEKLISTAR DGVRRGDNFH SVLTTFIDAA RGPAGVESDV ETNEIVDSVQ YAHKHDIQIT
NESYNNYVPS YVKPDSVSTS DLGSLIDCNA ASVNQIVLRN SNGACIWNAA AYMKLSDALK
RQIRIACRKC NLAFRLTTSK LRANDNILSV RFTANKIVGG APTWFNALRD FTLKGYVLAT
IIVFLCAVLM YLCLPTFSMV PVEFYEDRIL DFKVLDNGII RDVNPDDKCF ANKHRSFTQW
YHEHVGGVYD NSITCPLTVA VIAGVAGARI PDVPTTLAWV NNQIIFFVSR VFANTGSVCY
TPIDEIPYKS FSDSGCILPS ECTMFRDAEG RMTPYCHDPT VLPGAFAYSQ MRPHVRYDLY
DGNMFIKFPE VVFESTLRIT RTLSTQYCRF GSCEYAQEGV CITTNGSWAI FNDHHLNRPG
VYCGSDFIDI VRRLAVSLFQ PITYFQLTTS LVLGIGLCAF LTLLFYYINK VKRAFADYTQ
CAVIAVVAAV LNSLCICFVA SIPLCIVPYT ALYYYATFYF TNEPAFIMHV SWYIMFGPIV
PIWMTCVYTV AMCFRHFFWV LAYFSKKHVE VFTDGKLNCS FQDAASNIFV INKDTYAALR
NSLTNDAYSR FLGLFNKYKY FSGAMETAAY REAAACHLAK ALQTYSETGS DLLYQPPNCS
ITSGVLQSGL VKMSHPSGDV EACMVQVTCG SMTLNGLWLD NTVWCPRHVM CPADQLSDPN
YDALLISMTN HSFSVQKHIG APANLRVVGH AMQGTLLKLT VDVANPSTPA YTFTTVKPGA
AFSVLACYNG RPTGTFTVVM RPNYTIKGSF LCGSCGSVGY TKEGSVINFC YMHQMELANG
THTGSAFDGT MYGAFMDKQV HQVQLTDKYC SVNVVAWLYA AILNGCAWFV KPNRTSVVSF
NEWALANQFT EFVGTQSVDM LAVKTGVAIE QLLYAIQQLY TGFQGKQILG STMLEDEFTP
EDVNMQIMGV VMQSGVRKVT YGTAHWLFAT LVSTYVIILQ ATKFTLWNYL FETIPTQLFP
LLFVTMAFVM LLVKHKHTFL TLFLLPVAIC LTYANIVYEP TTPISSALIA VANWLAPTNA
YMRTTHTDIG VYISMSLVLV IVVKRLYNPS LSNFALALCS GVMWLYTYSI GEASSPIAYL
VFVTTLTSDY TITVFVTVNL AKVCTYAIFA YSPQLTLVFP EVKMILLLYT CLGFMCTCYF
GVFSLLNLKL RAPMGVYDFK VSTQEFRFMT ANNLTAPRNS WEAMALNFKL IGIGGTPCIK
VAAMQSKLTD LKCTSVVLLS VLQQLHLEAN SRAWAFCVKC HNDILAATDP SEAFEKFVSL
FATLMTFSGN VDLDALASDI FDTPSVLQAT LSEFSHLATF AELEAAQKAY QEAMDSGDTS
PQVLKALQKA VNIAKNAYEK DKAVARKLER MADQAMTSMY KQARAEDKKA KIVSAMQTML
FGMIKKLDND VLNGIISNAR NGCIPLSVIP LCASNKLRVV IPDFTVWNQV VTYPSLNYAG
ALWDITVINN VDNEIVKSSD VVDSNENLTW PLVLECTRAS TSAVKLQNNE IKPSGLKTMV
VSAGQEQTNC NTSSLAYYEP VQGRKMLMAL LSDNAYLKWA RVEGKDGFVS VELQPPCKFL
IAGPKGPEIR YLYFVKNLNN LHRGQVLGHI AATVRLQAGS NTEFASNSSV LSLVNFTVDP
QKAYLDFVNA GGAPLTNCVK MLTPKTGTGI AISVKPESTA DQETYGGASV CLYCRAHIEH
PDVSGVCKYK GKFVQIPAQC VRDPVGFCLS NTPCNVCQYW IGYGCNCDSL RQAALPQSKD
SNFLNESGVL L
