R1AB_BCHK4
ID R1AB_BCHK4 Reviewed; 7119 AA.
AC P0C6W3; A3EX93;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 108.
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 HKU4 (BtCoV) (BtCoV/HKU4/2004).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Merbecovirus.
OX NCBI_TaxID=694007;
OH NCBI_TaxID=258959; Tylonycteris pachypus (Lesser bamboo bat) (Vespertilio pachypus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HKU4-1;
RX PubMed=17121802; DOI=10.1128/jvi.02182-06;
RA Woo P.C.Y., Wang M., Lau S.K.P., Xu H.F., Poon R.W.S., Guo R., Wong B.H.L.,
RA Gao K., Tsoi H.-W., Huang Y., Li K.S.M., Lam C.S.F., Chan K.-H.,
RA Zheng B.-J., Yuen K.-Y.;
RT "Comparative analysis of twelve genomes of three novel group 2c and group
RT 2d coronaviruses reveals unique group and subgroup features.";
RL J. Virol. 81:1574-1585(2007).
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=P0C6W3-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6T4-1; 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: [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}.
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DR EMBL; EF065505; ABN10838.1; -; Genomic_RNA.
DR RefSeq; YP_001039952.1; NC_009019.1. [P0C6W3-1]
DR PDB; 4YO9; X-ray; 2.30 A; A/B=3292-3597.
DR PDB; 4YOG; X-ray; 2.00 A; A/B=3292-3597.
DR PDB; 4YOI; X-ray; 1.82 A; A/B=3292-3597.
DR PDB; 4YOJ; X-ray; 1.90 A; A/B=3292-3597.
DR PDB; 6MEA; X-ray; 1.35 A; A/B=1154-1324.
DR PDB; 6MEB; X-ray; 1.80 A; A/B=1154-1324.
DR PDB; 6MEN; X-ray; 1.50 A; A/B=1154-1324.
DR PDB; 6MWM; NMR; -; A=1445-1522.
DR PDBsum; 4YO9; -.
DR PDBsum; 4YOG; -.
DR PDBsum; 4YOI; -.
DR PDBsum; 4YOJ; -.
DR PDBsum; 6MEA; -.
DR PDBsum; 6MEB; -.
DR PDBsum; 6MEN; -.
DR PDBsum; 6MWM; -.
DR SMR; P0C6W3; -.
DR BindingDB; P0C6W3; -.
DR MEROPS; C16.011; -.
DR GeneID; 4835998; -.
DR KEGG; vg:4835998; -.
DR SABIO-RK; P0C6W3; -.
DR Proteomes; UP000006574; 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; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21167; M_alpha_beta_cv_Nsp15-like; 1.
DR CDD; cd21563; Macro_cv_SUD-M_Nsp3-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21592; MERS-CoV-like_RdRp; 1.
DR CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR CDD; cd21171; NTD_alpha_beta_cv_Nsp15-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 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; 3.40.50.11020; -; 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; IPR041679; DNA2/NAM7-like_C.
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; 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; 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; IPR044350; RdRp_MERS-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; PF13087; AAA_12; 1.
DR Pfam; PF16251; bCoV_NAR; 1.
DR Pfam; PF11501; bCoV_NSP1; 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 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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; 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; Reference proteome;
KW Repeat; Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
KW Thiol protease; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Viral immunoevasion; Viral RNA replication; Zinc;
KW Zinc-finger.
FT CHAIN 1..195
FT /note="Host translation inhibitor nsp1"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000290288"
FT CHAIN 196..847
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000290289"
FT CHAIN 848..2784
FT /note="Papain-like proteinase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000290290"
FT CHAIN 2785..3291
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000290291"
FT CHAIN 3292..3597
FT /note="3C-like proteinase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000290292"
FT CHAIN 3598..3889
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000290293"
FT CHAIN 3890..3972
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000290294"
FT CHAIN 3973..4171
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000290295"
FT CHAIN 4172..4281
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000290296"
FT CHAIN 4282..4420
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000290297"
FT CHAIN 4421..5354
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000290298"
FT CHAIN 5355..5952
FT /note="Helicase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000290299"
FT CHAIN 5953..6475
FT /note="Guanine-N7 methyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000290300"
FT CHAIN 6476..6817
FT /note="Uridylate-specific endoribonuclease"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000290301"
FT CHAIN 6818..7119
FT /note="2'-O-methyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000290302"
FT TRANSMEM 2112..2132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2145..2165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2222..2242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2326..2346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2350..2370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2375..2395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2800..2820
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3072..3092
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3105..3125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3149..3169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3603..3623
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3637..3657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3662..3682
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3707..3727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3735..3755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3784..3804
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3808..3828
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 25..151
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT DOMAIN 167..195
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT DOMAIN 197..472
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 478..712
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 714..847
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 851..960
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1152..1321
FT /note="Macro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1322..1446
FT /note="Macro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1446..1519
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1524..1579
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1593..1864
FT /note="Peptidase C16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1878..1995
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 2012..2133
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2679..2782
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3195..3291
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3292..3597
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3890..3972
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3973..4171
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 4172..4281
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4282..4420
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT DOMAIN 4426..4683
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 4787..5354
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT DOMAIN 5034..5196
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 5355..5438
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT DOMAIN 5611..5792
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 5793..5967
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 6024..6239
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 6248..6475
FT /note="N7-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT DOMAIN 6476..6536
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT DOMAIN 6537..6658
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 6675..6814
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6819..7113
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ZN_FING 1714..1751
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4355..4371
FT /evidence="ECO:0000250"
FT ZN_FING 4397..4410
FT /evidence="ECO:0000250"
FT REGION 339..360
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 2112..2395
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2800..3169
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3603..3828
FT /note="HD3"
FT /evidence="ECO:0000250"
FT REGION 6361..6375
FT /note="GpppA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT ACT_SITE 1634
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1800
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3332
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3439
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 5181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 6042
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6044
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6705
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6720
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6760
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6863
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6947
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6987
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 7020
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 4355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 5359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5636..5643
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 6159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6283..6289
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6421
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT SITE 195..196
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 847..848
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000255"
FT SITE 2784..2785
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3291..3292
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3597..3598
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3889..3890
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 3972..3973
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4171..4172
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4281..4282
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 4420..4421
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 5354..5355
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 5952..5953
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 6475..6476
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT SITE 6817..6818
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000255"
FT STRAND 1158..1160
FT /evidence="ECO:0007829|PDB:6MEA"
FT STRAND 1162..1170
FT /evidence="ECO:0007829|PDB:6MEA"
FT HELIX 1172..1178
FT /evidence="ECO:0007829|PDB:6MEA"
FT STRAND 1179..1181
FT /evidence="ECO:0007829|PDB:6MEA"
FT STRAND 1183..1188
FT /evidence="ECO:0007829|PDB:6MEA"
FT HELIX 1198..1205
FT /evidence="ECO:0007829|PDB:6MEA"
FT TURN 1206..1208
FT /evidence="ECO:0007829|PDB:6MEA"
FT HELIX 1209..1221
FT /evidence="ECO:0007829|PDB:6MEA"
FT STRAND 1229..1233
FT /evidence="ECO:0007829|PDB:6MEA"
FT STRAND 1237..1245
FT /evidence="ECO:0007829|PDB:6MEA"
FT HELIX 1249..1251
FT /evidence="ECO:0007829|PDB:6MEA"
FT HELIX 1255..1257
FT /evidence="ECO:0007829|PDB:6MEA"
FT HELIX 1258..1263
FT /evidence="ECO:0007829|PDB:6MEA"
FT TURN 1264..1267
FT /evidence="ECO:0007829|PDB:6MEA"
FT STRAND 1268..1273
FT /evidence="ECO:0007829|PDB:6MEA"
FT HELIX 1285..1295
FT /evidence="ECO:0007829|PDB:6MEA"
FT STRAND 1298..1305
FT /evidence="ECO:0007829|PDB:6MEA"
FT HELIX 1307..1314
FT /evidence="ECO:0007829|PDB:6MEA"
FT HELIX 1450..1456
FT /evidence="ECO:0007829|PDB:6MWM"
FT TURN 1457..1459
FT /evidence="ECO:0007829|PDB:6MWM"
FT STRAND 1460..1466
FT /evidence="ECO:0007829|PDB:6MWM"
FT STRAND 1471..1473
FT /evidence="ECO:0007829|PDB:6MWM"
FT STRAND 1476..1484
FT /evidence="ECO:0007829|PDB:6MWM"
FT STRAND 1487..1491
FT /evidence="ECO:0007829|PDB:6MWM"
FT STRAND 1496..1499
FT /evidence="ECO:0007829|PDB:6MWM"
FT HELIX 1510..1514
FT /evidence="ECO:0007829|PDB:6MWM"
FT TURN 1515..1517
FT /evidence="ECO:0007829|PDB:6MWM"
FT STRAND 1518..1520
FT /evidence="ECO:0007829|PDB:6MWM"
FT HELIX 3302..3305
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3308..3313
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3316..3323
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3326..3330
FT /evidence="ECO:0007829|PDB:4YOI"
FT HELIX 3331..3334
FT /evidence="ECO:0007829|PDB:4YOI"
FT HELIX 3337..3339
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3340..3342
FT /evidence="ECO:0007829|PDB:4YOI"
FT HELIX 3345..3351
FT /evidence="ECO:0007829|PDB:4YOI"
FT HELIX 3354..3356
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3357..3361
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3363..3365
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3367..3369
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3371..3377
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3380..3387
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3394..3397
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3405..3412
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3415..3423
FT /evidence="ECO:0007829|PDB:4YOI"
FT HELIX 3436..3438
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3442..3447
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3450..3462
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3465..3469
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3475..3478
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3481..3484
FT /evidence="ECO:0007829|PDB:4YOI"
FT HELIX 3495..3507
FT /evidence="ECO:0007829|PDB:4YOI"
FT HELIX 3521..3530
FT /evidence="ECO:0007829|PDB:4YOI"
FT HELIX 3540..3549
FT /evidence="ECO:0007829|PDB:4YOI"
FT HELIX 3553..3565
FT /evidence="ECO:0007829|PDB:4YOI"
FT STRAND 3575..3577
FT /evidence="ECO:0007829|PDB:4YOI"
FT HELIX 3584..3590
FT /evidence="ECO:0007829|PDB:4YOI"
FT TURN 3591..3593
FT /evidence="ECO:0007829|PDB:4YOG"
SQ SEQUENCE 7119 AA; 795200 MW; E85475854586DD79 CRC64;
MLSKASVTTQ GARGKYRAEL YNEKRSDHVA CTVPLCDTDD MACKLTPWFE DGETAFNQVS
SILKEKGKIL FVPMHMQRAM KFLPGPRVYL VERLTGGMLS KHFLVNQLAY KDQVGAAMMR
TTLNAKPLGM FFPYDSSLET GEYTFLLRKN GLGGQLFRER PWDRKETPYV EILDDLEADP
TGKYSQNLLK KLIGGDCIPI DQYMCGKNGK PIADYAKIVA KEGLTTLADI EVDVKSRMDS
DRFIVLNKKL YRVVWNVTRR NVPYPKQTAF TIVSVVQCDD KDSVPEHTFT IGSQILMVSP
LKATNNKNFN LKQRLLYTFY GKDAVQQPGY IYHSAYVDCN ACGRGTWCTG NAIQGFACDC
GANYSANDVD LQSSGLVPRN ALFLANCPCA NNGACSHSAA QVYNILDGKA CVEVGGKSFT
LTFGGVVYAY MGCCDGTMYF VPRAKSCVSR IGDAIFTGCT GTWDKVVETA NLFLEKAQRS
LNFCQQFALT EVVLAILSGT TSTFEELRDL CHNASYEKVR DHLVNHGFVV TIGDYIRDAI
NIGANGVCNA TINAPFIAFT GLGESFKKVS AIPWKICSNL KSALDYYSSN IMFRVFPYDI
PCDVSNFVEL LLDCGKLTVA TSYFVLRYLD EKFDTVLGTV SSACQTALSS FLNACVAASR
ATAGFINDMF KLFKVLMHKL YVYTSCGYVA VAEHSSKIVQ QVLDIMSKAM KLLHTNVSWA
GTKLSAIIYE GREALLFNSG TYFCLSTKAK TLQGQMNLVL PGDYNKKTLG ILDPVPNADT
IDVNANSTVV DVVHGQLEPT NEHGPSMIVG NYVLVSDKLF VRTEDEEFYP LCTNGKVVST
LFRLKGGMPS KKVTFGDVNT VEVTAYRSVS ITYDIHPVLD ALLSSSKLAT FTVEKDLLVE
DFVDVIKDEV LTLLTPLLRG YDIDGFDVED FIDVPCYVYN QDGDCAWSSN MTFSINPVED
VEEVEEFIED DYLSDELPIA DDEEAWARAV EEVMPLDDIL VAEIELEEDP PLETALESVE
AEVVETAEAQ EPSVESIDST PSTSTVVGEN DLSVKPMSRV AETDDVLELE TAVVGGPVSD
VTAIVTNDIV SVEQAQQCGV SSLPIQDEAS ENQVHQVSDL QGNELLCSET KVEIVQPRQD
LKPRRSRKSK VDLSKYKHTV INNSVTLVLG DAIQIASLLP KCILVNAANR HLKHGGGIAG
VINKASGGDV QEESDEYISN NGPLHVGDSV LLKGHGLADA ILHVVGPDAR NNEDAALLKR
CYKAFNKHTI VVTPLISAGI FSVDPKVSFE YLLANVTTTT YVVVNNEDIY NTLATPSKPD
GLVYSFEGWR GTVRTAKNYG FTCFICTEYS ANVKFLRTKG VDTTKKIQTV DGVSYYLYSA
RDALTDVIAA ANGCSGICAM PFGYVTHGLD LAQSGNYVRQ VKVPYVCLLA SKEQIPIMNS
DVAIQTPETA FINNVTSNGG YHSWHLVSGD LIVKDVCYKK LLHWSGQTIC YADNKFYVVK
NDVALPFSDL EACRAYLTSR AAQQVNIEVL VTIDGVNFRT VILNDTTTFR KQLGATFYKG
VDISDAFPTV KMGGESLFVA DNLSESEKVV LKEYYGTSDV TFLQRYYSLQ PLVQQWKFVV
HDGVKSLKLS NYNCYINATI MMIDMLHDIK FVVPALQNAY LRYKGGDPYD FLALIMAYGD
CTFDNPDDEA KLLHTLLAKA ELTVSAKMVW REWCTVCGIR DIEYTGMRAC VYAGVNSMEE
LQSVFNETCV CGSVKHRQLV EHSAPWLLVS GLNEVKVSTS TDPIYRAFNV FQGVETSVGH
YVHIRVKDGL FYKYDSGSLT KTSDMKCKMT SVWYPTVRYT ADCNVVVYDL DGVTKVEVNP
DLSNYYMKDG KYYTSKPTIK YSPATILPGS VYSNSCLVGV DGTPGSDTIS KFFNDLLGFD
ETKPISKKLT YSLLPNEDGD VLLSEFSNYN PVYKKGVMLK GKPILWVNNG VCDSALNKPN
RASLRQLYDV APIVLDNKYT VLQDNTSQLV EHNVPVVDDV PITTRKLIEV KCKGLNKPFV
KGNFSFVNDP NGVTVVDTLG LTELRALYVD INTRYIVLRD NNWSSLFKLH TVESGDLQIV
AAGGSVTRRA RVLLGASSLF ASFAKITVTA TTAACKTAGR GFCKFVVNYG VLQNMFVFLK
MLFFLPFNYL WPKKQPTVDI GVSGLRTAGI VTTNIVKQCG TAAYYMLLGK FKRVDWKATL
RLFLLLCTTI LLLSSIYHLV LFNQVLSSDV MLEDATGILA IYKEVRSYLG IRTLCDGLVV
EYRNTSFDVM EFCSNRSVLC QWCLIGQDSL TRYSALQMLQ THITSYVLNI DWIWFALEFF
LAYVLYTSSF NVLLLVVTAQ YFFAYTSAFV NWRAYNYIVS GLFFLVTHIP LHGLVRVYNF
LACLWFLRKF YSHVINGCKD TACLLCYKRN RLTRVEASTI VCGTKRTFYI AANGGTSYCC
KHNWNCVECD TAGVGNTFIC TEVANDLTTT LRRLIKPTDQ SHYYVDSVVV KDAVVELHYN
RDGSSCYERY PLCYFTNLEK LKFKEVCKTP TGIPEHNFLI YDTNDRGQEN LARSACVYYS
QVLCKPMLLV DVNLVTTVGD SREIAIKMLD SFINSFISLF SVSRDKLEKL INTARDCVRR
GDDFQNVLKT FTDAARGHAG VESDVETTMV VDALQYAHKN DIQLTTECYN NYVPGYIKPD
SINTLDLGCL IDLKAASVNQ TSMRNANGAC VWNSGDYMKL SDSFKRQIRI ACRKCNIPFR
LTTSKLRAAD NILSVKFSAT KIVGGAPSWL LRVRDLTVKG YCILTLFVFT VAVLSWFCLP
SYSIATVNFN DDRILTYKVI ENGIVRDIAP NDVCFANKYG HFSKWFNENH GGVYRNSMDC
PITIAVIAGV AGARVANVPA NLAWVGKQIV LFVSRVFANT NVCFTPINEI PYDTFSDSGC
VLSSECTLFR DAEGNLNPFC YDPTVLPGAS SYADMKPHVR YDMYDSDMYI KFPEVIVEST
LRITKTLATQ YCRFGSCEES AAGVCISTNG SWALYNQNYS TRPGIYCGDD YFDIVRRLAI
SLFQPVTYFQ LSTSLAMGLV LCVFLTAAFY YINKVKRALA DYTQCAVVAV VAALLNSLCL
CFIVANPLLV APYTAMYYYA TFYLTGEPAF IMHISWYVMF GAVVPIWMLA SYTVGVMLRH
LFWVLAYFSK KHVDVFTDGK LNCSFQDAAS NIFVIGKDTY VALRNAITQD SFVRYLSLFN
KYKYYSGAMD TASYREACAA HLCKALQTYS ETGSDILYQP PNCSVTSSVL QSGLVKMSAP
SGAVENCIVQ VTCGSMTLNG LWLDNTVWCP RHIMCPADQL TDPNYDALLI SKTNHSFIVQ
KHIGAQANLR VVAHSMVGVL LKLTVDVANP STPAYTFSTV KPGASFSVLA CYNGKPTGVF
TVNLRHNSTI KGSFLCGSCG SVGYTENGGV INFVYMHQME LSNGTHTGSS FDGVMYGAFE
DKQTHQLQLT DKYCTINVVA WLYAAVLNGC KWFVKPTRVG IVTYNEWALS NQFTEFVGTQ
SIDMLAHRTG VSVEQMLAAI QSLHAGFQGK TILGQSTLED EFTPDDVNMQ VMGVVMQSGV
KRISYGFIHW LISTFVLAYV SVMQLTKFTM WTYLFETIPT QMTPLLLGFM ACVMFTVKHK
HTFMSLFLLP VALCLTYANI VYEPQTLISS TLIAVANWLT PTSVYMRTTH FDFGLYISLS
FVLAIIVRRL YRPSMSNLAL ALCSGVMWFY TYVIGDHSSP ITYLMFITTL TSDYTITVFA
TVNLAKFISG LVFFYAPHLG FILPEVKLVL LIYLGLGYMC TMYFGVFSLL NLKLRVPLGV
YDYSVSTQEF RFLTGNGLHA PRNSWEALIL NFKLLGIGGT PCIKVATVQS KLTDLKCTSV
VLLTVLQQLH LESNSKAWSY CVKLHNEILA AVDPTEAFER FVCLFATLMS FSANVDLDAL
ANDLFENSSV LQATLTEFSH LATYAELETA QSSYQKALNS GDASPQVLKA LQKAVNVAKN
AYEKDKAVAR KLERMAEQAM TSMYKQARAE DKKAKIVSAM QTMLFGMIKK LDNDVLNGVI
ANARNGCVPL SIVPLCASNK LRVVIPDISV WNKVVNWPSV SYAGSLWDIT VINNVDNEVV
KPTDVVETNE SLTWPLVIEC SRSSSSAVKL QNNEIHPKGL KTMVITAGVD QVNCNSSAVA
YYEPVQGHRM VMGLLSENAH LKWAKVEGKD GFINIELQPP CKFLIAGPKG PEIRYLYFVK
NLNNLHRGQL LGHIAATVRL QAGANTEFAS NSTVLTLVAF AVDPAKAYLD YVGSGGTPLS
NYVKMLAPKT GTGVAISVKP EATADQETYG GASVCLYCRA HIEHPDVSGV CKYKTRFVQI
PAHVRDPVGF LLKNVPCNVC QYWVGYGCNC DALRNNTVPQ SKDTNFLNRV RGSSVNARLE
PCSSGLTTDV VYRAFDICNF KARVAGIGKY YKTNTCRFVQ VDDEGHKLDS YFIVKRHTMS
NYELEKRCYD LLKDCDAVAI HDFFIFDVDK TKTPHIVRQS LTEYTMMDLV YALRHFDQNN
CEVLKSILVK YGCCEQSYFD NKLWFDFVEN PSVIGVYHKL GERIRQAMLN TVKMCDHMVK
SGLVGVLTLD NQDLNGKWYD FGDFVITQPG AGVAIVDSYY SYLMPVLSMT NCLAAETHKD
CDFNKPLIEW PLLEYDYTDY KIGLFNKYFK YWDQTYHPNC VNCSDDRCIL HCANFNVLFS
MVLPNTSFGP IVRKIFVDGV PFIVSCGYHY KELGLVMNMD FNIHRHRLAL KELMMYAADP
AMHIASASAL WDLRTPCFSV AALTTGLTFQ TVRPGNFNKD FYDFVVSRGF FKEGSSVTLK
HFFFAQDGHA AITDYSYYAY NLPTMVDIKQ MLFCMEVVDK YFDIYDGGCL NASEVIVNNL
DKSAGHPFNK FGKARVYYES MSYQEQDELF AVTKRNVLPT ITQMNLKYAI SAKNRARTVA
GVSILSTMTN RQYHQKMLKS MAATRGATCV IGTTKFYGGW DFMLKTLYKD VESPHLMGWD
YPKCDRAMPN MCRILASLIL ARKHSTCCTN SDRFYRLANE CAQVLSEYVL CGGGYYVKPG
GTSSGDATTA YANSVFNILQ ATTANVSALM SANGNTIIDR EIKDMQFDLY INVYRKVVPD
PKFVDKYYAF LNKHFSMMIL SDDGVVCYNS DYAAKGYVAS IQNFKETLYY QNNVFMSEAK
CWVETNLEKG PHEFCSQHTL YIKDGDDGYF LPYPDPSRIL SAGCFVDDIV KTDGTVMMER
YVSLAIDAYP LTKHDDTEYQ NVFWVYLQYI EKLYKDLTGH MLDSYSVMLC GDDSAKFWEE
GFYRDLYSSP TTLQAVGSCV VCHSQTSLRC GTCIRRPFLC CKCCYDHVIA TPHKMVLSVS
PYVCNAPGCD VSDVTKLYLG GMSYYCNDHR PVCSFPLCAN GLVFGLYKNM CTGSSSIMEF
NRLATCDWSD SGDYTLANTT TEPLKLFAAE TLRATEEASK QSYAIATIKE IVGERELILV
WEVGKSKPPL NRNYVFTGYH LTKNSKVQLG EYVFERIDYS DAVSYKSSTT YKLAVGDIFV
LTSHSVATLS APTIVNQERY LKITGIYPTI TVPEEFANHV VNFQKAGFSK YVTVQGPPGT
GKSHFAIGLA IYYPTARIVY TACSHAAVDA LCEKAFKYLN IAKCSRIIPA KARVECYDRF
KVNDTNSQYL FSTVNALPEI SVDILVVDEV SMCTNYDLSI INSRVKAKHI VYVGDPAQLP
APRTLLIRGT LEPENFNSVT RLMCNLGPDI FLSVCYRCPK EIVSTVSALV YNNKLSAKKD
ASGQCFKILF KGSVTHDASS AINRPQLNFV KTFIAANPNW SKAVFISPYN SQNAVARSML
GLTTQTVDSS QGSEYPYVIF CQTADTAHAN NLNRFNVAVT RAQKGILCVM TSQVLFDSLE
FAELSLNNYK LQSQIVTGLF KDCSREDTGL PPAYAPTYLS VDAKYKTTDE LCVNLNITPN
VTYSRVISRM GFKLDATIPG YPKLFITRDE AIRQVRSWVG FDVEGAHASR NACGTNVPLQ
LGFSTGVNFV VQPVGVVDTE WGSMLTTISA RPPPGEQFKH LVPLMNKGAT WPIVRRRIVQ
MLSDTLDKLS DYCTFVCWAH GFELTSASYF CKIGKEQRCS MCSRRASTFS SPLQSYACWS
HSSGYDYVYN PFFVDVQQWG YVGNLATNHD RYCGIHAGAH VASSDAIMTR CLAIYDCFIE
RVDWDVTYPY ISHEQKLNSC CRTVERNVVR SAVLSGKFEK IYDIGNPKGI AIISEPVEWH
FYDAQPLSNK VKKLFYTDDV SKQFEDGLCL FWNCNVSKYP SNAVVCRFDT RVHSEFNLPG
CNGGSLYVNK HAFHTPAYDI NAFRDLKPLP FFYYSTTPCE VHGSGNMLED IDYVPLKSAV
CITACNLGGA VCRKHAAEYR DYMEAYNIVS AAGFRLWVYK TFDIYNLWST FVKVQGLENI
AFNVIKQGHF TGVDGELPVA VVNDKIFTKN GTDDVCIFKN ETALPTNVAF ELYAKRAVRS
HPDLNLLRNL EVDVCYNFVL WDYDRNNIYG TTTIGVCKYT DIDVNPNLNM CFDIRDKGSL
ERFMSMPNGV LISDRKIKNY PCISGPKHAY FNGAILRNID AKQPVIFYLY KKVNNEFVSF
SDTFYTCGRT VGDFTVLTPM EEDFLVLDSD VFIKKYGLED YAFEHVVYGD FSHTTLGGLH
LLIGLYKKMR EGHILMEEML KDRATVHNYF ITDSNTASYK AVCSVIDLRL DDFVTIIKEM
DLDVVSKVVK VPIDLTMIEF MLWCRDGKVQ TFYPRLQATN DWKPGLTMPS LFKVQQMNLE
PCLLANYKQS IPMPNGVHMN VAKYMQLCQY LNTCTLAVPA NMRVIHFGAG CEKGVAPGTS
VLRQWLPLDA VLIDNDLNEF VSDADITIFG DCVTVHVGQQ VDLLISDMYD PCTKAVGEVN
QTKALFFVYL CNFIKNNLAL GGSVAIKITE HSWSADLYKI MGRFAYWTVF CTNANASSSE
GFLIGINFLG ELKEEIDGNV MHANYIFWRN STPMNLSTYS LFDLSRFPLK LKGTPVLQLK
ESQINELVIS LLSQGKLLIR DNDTLNVSTD VLVNFRKRL
