R1AB_BC279
ID R1AB_BC279 Reviewed; 7079 AA.
AC P0C6V9; Q0Q476;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Replicase polyprotein 1ab;
DE Short=pp1ab;
DE AltName: Full=ORF1ab 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.-;
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=RNA-directed RNA polymerase;
DE Short=Pol;
DE Short=RdRp;
DE EC=2.7.7.48;
DE AltName: Full=nsp12;
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 Contains:
DE RecName: Full=Guanine-N7 methyltransferase;
DE Short=ExoN;
DE EC=2.1.1.-;
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 Contains:
DE RecName: Full=2'-O-methyltransferase;
DE EC=2.1.1.57;
DE AltName: Full=nsp16;
GN Name=rep; ORFNames=1a-1b;
OS Bat coronavirus 279/2005 (BtCoV) (BtCoV/279/2005).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Sarbecovirus.
OX NCBI_TaxID=389167;
OH NCBI_TaxID=196889; Rhinolophus macrotis (Big-eared horseshoe bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16840328; DOI=10.1128/jvi.00697-06;
RA Tang X.C., Zhang J.X., Zhang S.Y., Wang P., Fan X.H., Li L.F., Li G.,
RA Dong B.Q., Liu W., Cheung C.L., Xu K.M., Song W.J., Vijaykrishna D.,
RA Poon L.L.M., Peiris J.S.M., Smith G.J., Chen H., Guan Y.;
RT "Prevalence and genetic diversity of coronaviruses in bats from China.";
RL J. Virol. 80:7481-7490(2006).
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]: Inhibits host translation
CC by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome
CC complex further induces an endonucleolytic cleavage near the 5'UTR of
CC host mRNAs, targeting them for degradation. Viral mRNAs are not
CC susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the
CC presence of a 5'-end leader sequence and are therefore protected from
CC degradation. By suppressing host gene expression, nsp1 facilitates
CC efficient viral gene expression in infected cells and evasion from host
CC immune response. {ECO:0000250|UniProtKB:P0C6X7}.
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 virally-
CC induced cytoplasmic double-membrane vesicles necessary for viral
CC replication. Antagonizes innate immune induction of type I interferon
CC by blocking the phosphorylation, dimerization and subsequent nuclear
CC translocation of host IRF3. Prevents also host NF-kappa-B signaling.
CC {ECO:0000250|UniProtKB:P0C6X7}.
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 -!- FUNCTION: [RNA-directed RNA polymerase]: Responsible for replication
CC and transcription of the viral RNA genome.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Helicase]: Multi-functional protein with a zinc-binding
CC domain in N-terminus displaying RNA and DNA duplex-unwinding activities
CC with 5' to 3' polarity. Activity of helicase is dependent on magnesium.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Guanine-N7 methyltransferase]: Enzyme possessing two
CC different activities: an exoribonuclease activity acting on both ssRNA
CC and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase
CC activity. {ECO:0000250|UniProtKB:P0C6X7}.
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 -!- FUNCTION: [2'-O-methyltransferase]: Methyltransferase that mediates
CC mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral
CC mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16.
CC Therefore plays an essential role in viral mRNAs cap methylation which
CC is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY: [Helicase]:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- CATALYTIC ACTIVITY: [Helicase]:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- CATALYTIC ACTIVITY: [Papain-like proteinase]:
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: [2'-O-methyltransferase]:
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: 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. Nsp10 forms a dodecamer and interacts
CC with nsp14 and nsp16; these interactions enhance nsp14 and nsp16
CC enzymatic activities. Nsp14 interacts (via N-terminus) with DDX1.
CC {ECO:0000250|UniProtKB:P0C6X7}.
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 -!- 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=P0C6V9-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6F5-1; 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. {ECO:0000250}.
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: Bat coronavirus 279/2005 is highly similar to SARS-CoV
CC (SARS-like).
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 -!- SEQUENCE CAUTION:
CC Sequence=ABG47068.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ648857; ABG47068.1; ALT_INIT; Genomic_RNA.
DR BMRB; P0C6V9; -.
DR SMR; P0C6V9; -.
DR Proteomes; UP000006573; Genome.
DR GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004532; F:exoribonuclease activity; IEA:InterPro.
DR GO; GO:0002151; F:G-quadruplex RNA binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProt.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003727; F:single-stranded RNA binding; 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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO: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:0039644; P:suppression by virus of host NF-kappaB cascade; 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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd21409; 1B_cv_Nsp13-like; 1.
DR CDD; cd21560; betaCoV-Nsp6; 1.
DR CDD; cd21659; betaCoV_Nsp14; 1.
DR CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
DR CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR CDD; cd21516; cv_beta_Nsp2_SARS-like; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21167; M_alpha_beta_cv_Nsp15-like; 1.
DR CDD; cd21562; Macro_cv_SUD-N_Nsp3-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR CDD; cd21171; NTD_alpha_beta_cv_Nsp15-like; 1.
DR CDD; cd21591; SARS-CoV-like_RdRp; 1.
DR CDD; cd21525; SUD_C_SARS-CoV_Nsp3; 1.
DR CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1.
DR CDD; cd21466; Ubl2_cv_PLpro_N_Nsp3-like; 1.
DR CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR Gene3D; 1.10.150.420; -; 1.
DR Gene3D; 1.10.1840.10; -; 1.
DR Gene3D; 1.10.8.1190; -; 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; 3.30.160.820; -; 1.
DR Gene3D; 3.30.70.3540; -; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.220.20; -; 1.
DR Gene3D; 3.40.220.30; -; 1.
DR Gene3D; 3.40.30.150; -; 1.
DR Gene3D; 3.40.50.11020; -; 1.
DR Gene3D; 3.40.50.11580; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR043608; CoV_NSP15_M.
DR InterPro; IPR043606; CoV_NSP15_N.
DR InterPro; IPR043613; CoV_NSP2_C.
DR InterPro; IPR043611; CoV_NSP3_C.
DR InterPro; IPR032505; CoV_NSP4_C.
DR InterPro; IPR043612; CoV_NSP4_N.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR022733; DPUP_SUD_C_bCoV.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR044371; Macro_X_NSP3-like.
DR InterPro; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR036333; NSP10_sf_CoV.
DR InterPro; IPR044343; NSP13_1B_dom_CoV.
DR InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR InterPro; IPR044315; NSP14_betaCoV.
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; IPR021590; NSP1_bCoV.
DR InterPro; IPR038030; NSP1_sf_bCoV.
DR InterPro; IPR043615; NSP2_N_CoV.
DR InterPro; IPR044389; NSP2_SARS-CoV-like.
DR InterPro; IPR024375; NSP3_bCoV.
DR InterPro; IPR024358; NSP3_N_bCoV.
DR InterPro; IPR032592; NSP3_NAB_bCoV.
DR InterPro; IPR042570; NSP3_NAB_bCoV_sf.
DR InterPro; IPR038166; NSP3_PL2pro_sf_bCoV.
DR InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
DR InterPro; IPR044864; NSP3_SUD-N_bCoV.
DR InterPro; IPR044374; NSP3_SUD-N_SARS-CoV.
DR InterPro; IPR043478; NSP3_SUD-N_sf_bCoV.
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; 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; IPR043177; PLpro_N_sf_CoV.
DR InterPro; IPR043503; PLpro_palm_finger_dom_CoV.
DR InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR InterPro; IPR044351; RdRp_SARS-CoV-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR009469; RNA_pol_N_CoV.
DR InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF16251; bCoV_NAR; 1.
DR Pfam; PF11501; bCoV_NSP1; 1.
DR Pfam; PF12379; bCoV_NSP3_N; 1.
DR Pfam; PF12124; bCoV_SUD_C; 1.
DR Pfam; PF11633; bCoV_SUD_M; 1.
DR Pfam; PF06471; CoV_ExoN; 1.
DR Pfam; PF06460; CoV_Methyltr_2; 1.
DR Pfam; PF09401; CoV_NSP10; 1.
DR Pfam; PF19215; CoV_NSP15_C; 1.
DR Pfam; PF19216; CoV_NSP15_M; 1.
DR Pfam; PF19219; CoV_NSP15_N; 1.
DR Pfam; PF19212; CoV_NSP2_C; 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; PF06478; CoV_RPol_N; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF101816; SSF101816; 1.
DR SUPFAM; SSF140367; SSF140367; 1.
DR SUPFAM; SSF142877; SSF142877; 1.
DR SUPFAM; SSF143076; SSF143076; 1.
DR SUPFAM; SSF144246; SSF144246; 1.
DR SUPFAM; SSF159936; SSF159936; 1.
DR SUPFAM; SSF160099; SSF160099; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; 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; PS51954; COV_N7_MTASE; 1.
DR PROSITE; PS51962; COV_NSP1; 1.
DR PROSITE; PS51948; COV_NSP12_RDRP; 1.
DR PROSITE; PS51960; COV_NSP15_NTD; 1.
DR PROSITE; PS51991; COV_NSP2_C; 1.
DR PROSITE; PS51990; COV_NSP2_M; 1.
DR PROSITE; PS51989; COV_NSP2_N; 1.
DR PROSITE; PS51992; COV_NSP3_Y3; 1.
DR PROSITE; PS51943; COV_NSP3A_UBL; 1.
DR PROSITE; PS51944; COV_NSP3D_UBL; 1.
DR PROSITE; PS51946; COV_NSP4C; 1.
DR PROSITE; PS51949; COV_NSP7; 1.
DR PROSITE; PS51950; COV_NSP8; 1.
DR PROSITE; PS51951; COV_NSP9_SSRNA_BD; 1.
DR PROSITE; PS51653; CV_ZBD; 1.
DR PROSITE; PS51442; M_PRO; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51958; NENDOU; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS51955; NIV_2_O_MTASE; 1.
DR PROSITE; PS51953; NIV_EXON; 1.
DR PROSITE; PS51124; PEPTIDASE_C16; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51940; SARS_NSP3C_N; 1.
PE 3: Inferred from homology;
KW Activation of host autophagy by virus; ATP-binding;
KW Decay of host mRNAs by virus; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Exonuclease; Helicase;
KW Host cytoplasm; 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 ISG15 by virus; Inhibition of host NF-kappa-B 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; Repeat;
KW 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..179
FT /note="Host translation inhibitor nsp1"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000289896"
FT CHAIN 180..818
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000289897"
FT CHAIN 819..2746
FT /note="Papain-like proteinase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000289898"
FT CHAIN 2747..3246
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000289899"
FT CHAIN 3247..3552
FT /note="3C-like proteinase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000289900"
FT CHAIN 3553..3842
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000289901"
FT CHAIN 3843..3925
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000289902"
FT CHAIN 3926..4123
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000289903"
FT CHAIN 4124..4236
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000289904"
FT CHAIN 4237..4375
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000289905"
FT CHAIN 4376..5307
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000289906"
FT CHAIN 5308..5908
FT /note="Helicase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000289907"
FT CHAIN 5909..6435
FT /note="Guanine-N7 methyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000289908"
FT CHAIN 6436..6781
FT /note="Uridylate-specific endoribonuclease"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000289909"
FT CHAIN 6782..7079
FT /note="2'-O-methyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000289910"
FT TRANSMEM 2209..2229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2310..2330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2357..2377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2761..2781
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2998..3018
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3028..3048
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3060..3080
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3083..3103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3111..3131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3148..3168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3570..3590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3592..3612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3618..3638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3665..3684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3691..3710
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3734..3754
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3762..3782
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 12..127
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT DOMAIN 148..179
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT DOMAIN 183..456
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 458..688
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 690..818
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 822..930
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1001..1167
FT /note="Macro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1213..1341
FT /note="Macro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1349..1476
FT /note="Macro 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1478..1544
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1548..1603
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1617..1881
FT /note="Peptidase C16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1894..2004
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 2029..2138
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2643..2746
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3148..3246
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3247..3552
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3843..3925
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3926..4123
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 4124..4236
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4237..4375
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT DOMAIN 4382..4636
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 4740..5307
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT DOMAIN 4987..5149
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 5308..5391
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT DOMAIN 5564..5745
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 5746..5915
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 5980..6195
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 6204..6435
FT /note="N7-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT DOMAIN 6436..6496
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT DOMAIN 6497..6622
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 6639..6778
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6783..7077
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ZN_FING 1735..1772
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4310..4326
FT /evidence="ECO:0000250"
FT ZN_FING 4353..4366
FT /evidence="ECO:0000250"
FT REGION 200..236
FT /note="C2H2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 323..344
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 370..416
FT /note="C2HC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 2098..2377
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2761..3168
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3570..3782
FT /note="HD3"
FT /evidence="ECO:0000250"
FT REGION 6322..6336
FT /note="GpppA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT ACT_SITE 1657
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1818
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3287
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3391
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 5134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5998
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6000
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6099
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6669
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6684
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6724
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6827
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6911
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6951
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6984
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 4310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 5312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5589..5596
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 6115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6239..6245
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT SITE 179..180
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 818..819
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3246..3247
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3552..3553
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3842..3843
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3925..3926
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4123..4124
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4236..4237
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4375..4376
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 5307..5308
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 5908..5909
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 6435..6436
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 6781..6782
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
SQ SEQUENCE 7079 AA; 791654 MW; CE92AE7AE019B902 CRC64;
MESLALGVSE KTHVQLSLPV LQVRDVLVRG FGDSVEEALA EAREHLKNGT CGLVELEKGV
LPQLEQPYVF IKRSDAQGTN HGYKVVELVA ELDGIQYGRS GTTLGVLVPH VGETPVAYRN
VLLRKNGNKG AGGHSYGIDL KSYDLGVELG TDPIEDYEQN WNTKHGGGVL RELIRELNGG
AFTRYVDNNF CGPDGYPLEC IKDLLARAGK SMCTLSEQLD YIESKRGVYC CREHEHEIVW
FTERSEKSYE RQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
RSVYPVATPQ ECNDMHLSTL MKCNHCDEVS WQTCDFLKAT CEQCGTENLV CEGPTTCGYL
PANAVVKMPC PACQDPEVGP EHSVADYHNH SNIETRLRKG GRTKCFGGCV FAYVGCYNKR
AYWVPRASAN IGASHTGITG DNVETLNEDL MEILNRDRVN INIVGDFHLN EEVAIILASF
SASTCAFVDT VKGLDYKTFK DIVESCGNFK VTRGRAKKGA WNIGQEKSIL TPLYGFPSQA
AGVIRSIFTR ALDTANHSIP DLQRAAITIL DGISEQSLRL IDAMVYTSDL LTNSVIVMAY
VTGGLVQQIT QWLSNMLGTT VDKLKPVFTW VEAKLSAGIE FLRDAWEILK FLVTGVFDIV
KGQIQVASDN LKECVKAFLD VLNKALEMCI DQVIIAGAKL RTLNLGEVFI AQSKGLYRQC
IRGKEQLQLL MPLRAPKEVT FFEGDSHDTV FTSEEVVLKN GELEALETPV DSFTNGAVIG
TPVCVNGLML LELKDKEQYC ALSPGLLATN NVFSLKGGAP VKGVTFGEDT VLEVQGYKNV
KITFELDERV DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTNMGIDLDE
WSVATFYLFD DAGEEKLSSR MYCSFYPPDE EEDCEEYEDE EEIPEETCEH EYGTEDDYKG
LPLEFGASTE IQQVDEEEEE DWLEEAIAAK PEPEPLPEEP VNQFTGYLKL TDNVAIKCVD
IVKEAQHAKP TVIVNAANVH LKHGGGVAGA LNKATNGAMQ QESDDYIKKN GPLTVGGSCL
LSGHNLAKKC MHVVGPNLNA GEDVQLLKAA YANFNSQDVL LAPLLSAGIF GAKPLQSLKM
CVETVRTQVY FAVNDQDLYD HVVLGYLDSL KPKVETPTQE NLELKEQPAV ETLTQENLEL
EELPVIEKPV DVKFKARIEE VNTSLEETKF LTSRLLLFAD INGKLYQDSQ NMLRGEDMFF
LEKDAPYIVG DVISSGDITC VIIPAKKAGG TTEMLAKALK KVPVSEYITT YPGQGCAGYT
LEEAKTALRK CKSVFYVLPS KTPNDKEEIL GTVSWNLREM LAHAEETRKL MLICMDVKAL
MSTIHRRYKG IKVQEGIVDY GVRFFFYTSK EPVASIITKL NLLNEPLVTM PIGYVTHGLN
LEEAARCMRS LKAPAVVSVS SPDAVTTYNG YLTSSSKTSE EHFIETVSLA GMYRDWSYSG
QRTELGVEFL KRGDKVVYHT VGSPIQFHLD GEVLLLDKLK SLLSLREVRT IKVFTTVDNT
NLHTQIVDMS MTYGQQFGPT YLDGADVTKI KPHAKHEGKT FFVLPSDDTL RSEAFEYYHT
LDESFLGRYM SALNHTKKWK FPQIGGLTSI KWADNNCYLS SVLLALQQIE VKFNAPALQE
AYYRARAGDA ANFCALILAY SNRTVGELGD VRETMTHLLQ HANLESAKRV LNVVCKTCGQ
KSTTLTGVEA VMYMGTLSYE ELKTGVTIPC ICGRDATQYL VQQESSFVMM SAPPSEYTLQ
QGAFLCANEY TGSYQCGHYT HVTVKETLYR IDGAYLTKMS EYKGPVTDVF YKEISYTTTI
KPVSYKLDGV IYTEIQPKLD EYYKKDNAYY TEQPIDLVPT QPLPNASFDN FKLTCSNTKF
ADDLNQMTGF KKPASRELSV TFFPDLNGDV VAIDYRHYSA SFKKGAKLLH KPIIWHINQT
TNKTTYKPNT WCLRCLWSTK PVETSNSFEV LEVEDTQGMD NLACESQTPT SEEVVENPTI
QKEVIECDVK TIEVVGNVIL KPSEEGVKVT QELGHEDLMA AYVEETSITI KKPNELSLAL
GLRTLATHGA AAINSVPWSK ILAYVKPFLG QAAVTTTNCI KRCVQRVFNN YMPYVITLLF
QLCTFTRSTN SRIRASLPTT IAKNSVKSVA KLCLDVCINY VKSPKFSKLF TIAMWLLLLS
ICLGSLIYVT AAFGVLLSNL GIPSYCDGVR ESYVNSSNVT TMDFCEGSFL CSVCLNGLDS
LDSYPALETI QVTISSYKLD LTSLGLAAEW FLAYMLFTKF FYLLGLSAIM QVFFGYFASH
FISNSWLMWF IISIVQMAPV SAMVRMYIFF AFCYYVWKSY VHIMDGCTSS TCMMCYKRNR
ATRVECTTIV NGMKRSFYVY ANGGRGFCKA HNWNCLNCDT FCAGSTFISD EVARDLSLQF
KRPINPTDQS SYVVDSVAVK NGALHLYFDK AGQKTYERHP LSHFVNLDNL RANNTKGSLP
INVIVFDGKS KCDESAAKSA SVYYSQLMCQ PILLLDQALV SDVGDSTEVS VKMFDAYVDT
FSATFSVPME KLKALVATAH SELAKGVALD GVLSTFVSAA RQGVVDTDVD TKDVIECLKL
SHHSDLEVTG DSCNNFMLTY NKVENMTPRD LGACIDCNAR HINAQVAKSH NVSLIWNVKD
YMSLSEQLRK QIRSAAKKNN IPFRLTCATT RQVVNAITTK ISLKGGKIVS TWFKLMLKAT
LLCVLAALFC YIIMPVHSLS VHDGYTNEII GYKAIQDGVT RDIMATDDCF ANKHAGFDSW
FSQRGGSYRN DKSCPVVAAI ITREIGFIVP GLPGTVLRAI NGDFLHFLPR VFSAVGNICY
TPSKLIEYSD FATSACVLAA ECTIFKDAMG KPVPYCYDTN LLEGSISYSE LRPDTRYVLM
DGSIIQFPNT YLEGSVRVVT TFDAEYCRHG TCERSEAGVC LSTSGRWVLN NEHYRALPGV
FCGVDAMNLI ANIFTPLVQP VGALDVSASV VAGGIIAILV TCAAYYFMKF RRAFGEYNHV
VAANALLFLM SFTILCLAPA YSFLPGVYSI FYLYLTFYFT NDVSFLAHLQ WFAMFSPIVP
FWITAIYVFC ISLKHCHWFF NNYLRKRVMF NGVTFSTFEE AALCTFLLNK EMYLKLRSET
LLPLTQYNRY LALYNKYKYF SGALDTTSYR EAACCHLAKA LNDFSNSGAD VLYQPPQTSI
TSAVLQSGFR KMAFPSGKVE GCMVQVTCGT TTLNGLWLDD TVYCPRHVIC TAEDMLNPNY
EDLLIRKSNH SFLVQAGNVQ LRVIGHSMQN CLLRLKVDTS NPKTPKYKFV RIQPGQTFSV
LACYNGSPSG VYQCAMRPNY TIKGSFLNGS CGSVGFNIDY DCVSFCYMHH MELPTGVHAG
TDLEGKFYGP FVDRQTAQAA GTDTTITLNV LAWLYAAVIN GDRWFLNRFT TTLNDFNLVA
MKYNYEPLTQ DHVDILGPLS AQTGIAVLDM CAALKELLQN GMNGRTILGS TILEDEFTPF
DVVRQCSGVT FQGKFKKIVK GTHHWMLLTF LTSLLILVQS TQWSLFFFVY ENAFLPFTLG
IMAIAACAML LVKHKHAFLC LFLLPSLATV AYFNMVYMPA SWVMRIMTWL ELADTSLSGY
RLKDCVMYAS ALVLLVLMTA RTVYDDAARR VWTLMNVITL VYKVYYGNSL DQAISMWALV
ISVTSNYSGV VTTIMFLARA IVFVCVEYYP LLFITGNTLQ CIMLVYCFLG YCCCCYFGLF
CLLNRYFRLT LGVYDYLVST QEFRYMNSQG LLPPKSSIDA FKLNIKLLGI GGKPCIKVAT
VQSKMSDVKC TSVVLLSVLQ QLRVESSSKL WAQCVQLHND ILLAKDTTEA FEKMVSLLSV
LLSMQGAVDI NKLCEEMLDN RATLQAIASE FSSLPSYAAY ATAQEAYEQA VANGDSEVVL
KKLKKSLNVA KSEFDRDAAM QRKLEKMADQ AMTQMYKQAR SEDKRAKVTS AMQTMLFTML
RKLDNDALNN IINNARDGCV PLNIIPLTTA AKLMVVVPDY GTYKNTCDGN TFTYASALWE
IQQVVDADSK IVQLSEINMD NSQNLAWPLI VTALRANSAV KLQNNELSPV ALRQMSCAAG
TTQTACTDDN ALAYYNNSKG GRFVLALLSD HQDLKWARFP KSDGTGTIYT ELEPPCRFVT
DTPRGPKVKY LYFIKGLNNL NRGMVLGSLA ATVRLQAGNA TEVPANSAVL SFCAFAVDPA
KAYKDYLASG GQPITNCVKM LCTHTGTGQA ITVTPEANMD QESFGGASCC LYCRCHIDHP
NPKGFCDLKG KYVQIPATCA NDPVGFTLKN TVCTVCGTWK GYGCSCDQLR EPMMQSADAS
TFLNRVCGVS AARLTPCGTG TSTDVVYRAF DIYNERVAGF AKFLKTNCCR FQEKDEEGNL
LDSYFVVKRH TMSNYQHEET IYNLVKECPA VAVHDFFKFR VDGDMVPHIS RQRLTKYTMA
DLVYALRHFD EGNCDTLKEI LVTYNCCDDD YFNKKDWYDF VENPDILRVY ANLGERVRQA
LLKTVQFCDA MRDAGIVGVL TLDNQDLNGN WYDFGDFVQV APGCGVPIVD SYYSLLMPIL
TLTKALAAES HMDADLAKPL IKWDLLKYDF TEERLCLFDR YFKYWDQTYH PNCINCLDDR
CILHCANFNV LFSTVFPPTS FGPLVRKIFV DGVPFVVSTG YHFRELGVVH NQDVNLHSSR
LSFKELLVYA ADPAMHAASG NLLLDKRTTC FSVAALTNNV AFQTVKPGNF NKDFYDFAVS
KGFFKEGSSV ELKHFFFAQD GNAAISDYDY YRYNLPTMCD IRQLLFVVEV VDKYFDCYDG
GCINANQVIV NNLDKSAGFP FNKWGKARLY YDSMSYEDQD VLFAYTKRNV IPTITQMNLK
YAISAKNRAR TVAGVSICST MTNRQFHQKL LKSIAATRGA TVVIGTSKFY GGWHNMLKTV
YSDVETPHLM GWDYPKCDRA MPNMLRIMAS LVLARKHSTC CNLSHRFYRL ANECAQVLSE
MVMCGGSLYV KPGGTSSGDA TTAYANSVFN ICQAVTANVN ALLSTDGNKI ADKYVRNLQH
RLYECLYRNR DVDHEFVDEF YAYLRKHFSM MILSDDAVVC YNSNYAAQGL VASIKNFKAV
HYYQNNVFMS EAKCWTETDL TKGPHEFCSQ HTMLVKQGDD YVYLPYPDPS RILGAGCFVD
DIVKTDGTLM IERFVSLAID AYPLTKHPNQ EYADVFHLYL QYIRKLHDEL TGHMLDMYSV
MLTNDNTSRY WEPEFYEAMY TPHTVLQAVG ACVLCNSQTS LRCGACIRRP FLCCKCCYDH
VISTSHKLVL SVNPYVCNAP GCDVTDVTQL YLGGMSYYCK LHKPPISFPL CANGQVFGLY
KNTCVGSDNV TDFNAIATCD WTNAGDYILA NTCTERLKLF AAETLKATEE TFKLSYGIAT
VREVLSDREL HLSWEVGKPR PPLNRNYVFT GYRVTKNSKV QIGEYTFEKG DYGDAVVYRG
TTTYKLNVGD YFVLTSHTVM PLSAPTLVPQ EHYVRITGLY PTLNISDEFS SNVANYQKVG
MQKYSTLQGP PGTGKSHFAI GLALYYPSAR IVYTACSHAA VDALCEKALK YLPIDKCSRI
IPARARVECF DKFKVNSTLE QYVFCTVNAL PETTADIVVF DEISMATNYD LSVVNARLRA
KHYVYIGDPA QLPAPRTLLT KGTLEPEYFN SVCRLMKTIG PDMFLGTCRR CPAEIVDTVS
ALVYDNKLKA HKEKSAQCFK MFYKGVITHD VSSAINRPQI GVVREFLTRN PAWRKAVFIS
PYNSQNAVAS KILGLPTQTV DSSQGSEYDY VIFTQTTETA HSCNVNRFNV AITRAKIGIL
CIMSDRDLYD KLQFTSLEVP RRNVATLQAE NVTGLFKDCS KIITGLHPTQ APTHLSVDTK
FKTEGLCVDI PGIPKDMTYR RLISMMGFKM NYQVNGYPNM FITREEAIRH VRAWIGFDVE
GCHATRDAVG TNLPLQLGFS TGVNLVAVPT GYVDTENNTE FTRVNAKPPP GDQFKHLIPL
MYKGLPWNVV RIKIVQMLSD TLKGLSDRVV FVLWAHGFEL TSMKYFVKIG PERTCCLCDR
RATCFSTSSD TYACWNHSVG FDYVYNPFMI DVQQWGFTGN LQSNHDQHCQ VHGNAHVASC
DAIMTRCLAV HECFVKRVDW SVEYPIIGDE LKINAACRKV QHMVVKSALL ADKFSVLHDI
GNPKAIKCVP QAEVDWKFYD AQPCSDKAYK IEELFYSYAT HHDKFTDGVC LFWNCNVDRY
PANAIVCRFD TRVLSNLNLP GCDGGSLYVN KHAFHTPAFD KSAFTYLKQL PFFYYSDSPC
ESHGKQVVSD IDYVPLKSAT CITRCNLGGA VCRRHANEYR QYLDAYNMMI SAGFSLWIYK
QFDTYNLWNT FTRLQSLENV AYNVVNKGHF DGQIGEAPVS IINNAVYTKV DGNDVEIFEN
KTTLPVNVAF ELWAKRNIKP VPEIKILNNL GVDIAANTVI WDYKREAPAH VSTIGVCTMT
DIAKKPTESA CSSLTVLFDG RVEGQVDLFR NARNGVLITE GSVKGLTPSK GPAQASVNGV
TLIGESVKTQ FNYFKKVDGI IQQLPETYFT QSRDLEDFKP RSKMETDFLE LAMDEFIQRY
KLEGYAFEHI VYGDFSHGQL GGLHLMIGLA KRSQDSPLKL EDFIPTDSTV KNYFITDAQT
GSSKCVCSVI DLLLDDFVEI IKSQDLSVIS KVVKVTIDYA EISFMLWCKD GHVETFYPKL
QASQAWQPGV AMPNLYKMQR MLLEKCDLQN YGENAVIPKG IMMNVAKYTQ LCQYLNTLTL
AVPYNMRVIH FGAGSDKGVA PGTAVLRQWL PTGALLVDSD LNDFVSDADS TLIGDCATVH
TANKWDLIIS DMYDPKTKHV TKENDSKEGF FTYLCGFIKQ KLALGGSVAV KITEHSWNAD
LYKLMGHFSW WTAFVTNVNA SSSEAFLIGV NYLGKLREQI DGYTMHANYI FWRNTNPIQL
SSYSLFDMSK FPLKLRGTAV MSLKENQIND MIYSLLENGR LIIRENNRVV VSSDILVNN
