R1AB_CVHNL
ID R1AB_CVHNL Reviewed; 6729 AA.
AC P0C6X5; Q6Q1S3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Replicase polyprotein 1ab;
DE Short=pp1ab;
DE AltName: Full=ORF1ab polyprotein;
DE Contains:
DE RecName: Full=Non-structural protein 1;
DE Short=nsp1;
DE AltName: Full=p9;
DE Contains:
DE RecName: Full=Non-structural protein 2;
DE Short=nsp2;
DE AltName: Full=p87;
DE Contains:
DE RecName: Full=Non-structural protein 3;
DE Short=nsp3;
DE EC=3.4.19.12;
DE EC=3.4.22.-;
DE AltName: Full=PL1-PRO/PL2-PRO;
DE AltName: Full=PLP1/PLP2;
DE AltName: Full=Papain-like proteinases 1/2;
DE AltName: Full=p195;
DE Contains:
DE RecName: Full=Non-structural protein 4;
DE Short=nsp4;
DE AltName: Full=Peptide HD2;
DE Contains:
DE RecName: Full=3C-like proteinase;
DE Short=3CL-PRO;
DE Short=3CLp;
DE EC=3.4.22.-;
DE AltName: Full=M-PRO;
DE AltName: Full=nsp5;
DE AltName: Full=p34;
DE Contains:
DE RecName: Full=Non-structural protein 6;
DE Short=nsp6;
DE Contains:
DE RecName: Full=Non-structural protein 7;
DE Short=nsp7;
DE AltName: Full=p5;
DE Contains:
DE RecName: Full=Non-structural protein 8;
DE Short=nsp8;
DE AltName: Full=p23;
DE Contains:
DE RecName: Full=Non-structural protein 9;
DE Short=nsp9;
DE AltName: Full=p12;
DE Contains:
DE RecName: Full=Non-structural protein 10;
DE Short=nsp10;
DE AltName: Full=Growth factor-like peptide;
DE Short=GFL;
DE AltName: Full=p14;
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 AltName: Full=p100;
DE Contains:
DE RecName: Full=Helicase;
DE Short=Hel;
DE EC=3.6.4.12;
DE EC=3.6.4.13;
DE AltName: Full=nsp13;
DE AltName: Full=p66;
DE AltName: Full=p66-HEL;
DE Contains:
DE RecName: Full=Exoribonuclease;
DE Short=ExoN;
DE EC=3.1.13.-;
DE AltName: Full=nsp14;
DE Contains:
DE RecName: Full=Uridylate-specific endoribonuclease;
DE EC=4.6.1.-;
DE AltName: Full=NendoU;
DE AltName: Full=nsp15;
DE AltName: Full=p41;
DE Contains:
DE RecName: Full=Putative 2'-O-methyl transferase;
DE EC=2.1.1.57;
DE AltName: Full=nsp16;
GN Name=rep; ORFNames=1a-1b;
OS Human coronavirus NL63 (HCoV-NL63).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Setracovirus.
OX NCBI_TaxID=277944;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Amsterdam I;
RX PubMed=15034574; DOI=10.1038/nm1024;
RA Van Der Hoek L., Pyrc K., Jebbink M.F., Vermeulen-Oost W., Berkhout R.J.,
RA Wolthers K.C., Wertheim-Van Dillen P.M., Kaandorp J., Spaargaren J.,
RA Berkhout B.;
RT "Identification of a new human coronavirus.";
RL Nat. Med. 10:368-373(2004).
RN [2]
RP FUNCTION.
RX PubMed=20181693; DOI=10.1128/jvi.02406-09;
RA Clementz M.A., Chen Z., Banach B.S., Wang Y., Sun L., Ratia K.,
RA Baez-Santos Y.M., Wang J., Takayama J., Ghosh A.K., Li K., Mesecar A.D.,
RA Baker S.C.;
RT "Deubiquitinating and interferon antagonism activities of coronavirus
RT papain-like proteases.";
RL J. Virol. 84:4619-4629(2010).
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:0000269|PubMed:20181693}.
CC -!- FUNCTION: The papain-like proteinase 1 (PLP1) and papain-like
CC proteinase 2 (PLP2) are responsible for the cleavages located at the N-
CC terminus of the replicase polyprotein. In addition, PLP2 possesses a
CC deubiquitinating/deISGylating activity and processes both 'Lys-48'- and
CC 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2
CC also antagonizes innate immune induction of type I interferon by
CC blocking the nuclear translocation of host IRF-3 (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: [3C-like proteinase]: Responsible for the majority of
CC cleavages as it cleaves the C-terminus of replicase polyprotein at 11
CC sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-
CC [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-
CC CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function
CC (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}.
CC -!- FUNCTION: The helicase which contains a zinc finger structure displays
CC RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Its
CC ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C),
CC poly(dA), but not by poly(G). {ECO:0000269|PubMed:20181693}.
CC -!- FUNCTION: The exoribonuclease acts on both ssRNA and dsRNA in a 3' to
CC 5' direction. {ECO:0000250}.
CC -!- FUNCTION: Nsp7-nsp8 hexadecamer may possibly confer processivity to the
CC polymerase, maybe by binding to dsRNA or by producing primers utilized
CC by the latter. {ECO:0000250}.
CC -!- FUNCTION: Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
CC -!- FUNCTION: [Uridylate-specific endoribonuclease]: Plays a role in viral
CC transcription/replication and prevents the simultaneous activation of
CC host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By
CC similarity). Acts by degrading the 5'-polyuridines generated during
CC replication of the poly(A) region of viral genomic and subgenomic RNAs.
CC Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-
CC cP) is first generated by 2'-O transesterification, which is then
CC hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded,
CC poly(U) RNA would hybridize with poly(A) RNA tails and activate host
CC dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- CATALYTIC ACTIVITY: [Non-structural protein 3]:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12;
CC -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
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: [Putative 2'-O-methyl transferase]:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC EC=2.1.1.57; Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC -!- CATALYTIC ACTIVITY: [Uridylate-specific endoribonuclease]:
CC Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-
CC 2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-
CC RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-
CC COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173079, ChEBI:CHEBI:173080;
CC Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC -!- COFACTOR: [Uridylate-specific endoribonuclease]:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC Note=Likely affects Nsp15 binding to RNA.
CC {ECO:0000250|UniProtKB:P0C6X7};
CC -!- SUBUNIT: 3CL-PRO exists as monomer and homodimer. Eight copies of nsp7
CC and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is
CC a dimer. Nsp10 forms a dodecamer (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC PRO_0000283876; Q14457: BECN1; Xeno; NbExp=3; IntAct=EBI-25622115, EBI-949378;
CC PRO_0000283876; Q00987: MDM2; Xeno; NbExp=3; IntAct=EBI-25622115, EBI-389668;
CC PRO_0000283876; Q96PM5: RCHY1; Xeno; NbExp=2; IntAct=EBI-25622115, EBI-947779;
CC PRO_0000283876; Q86WV6: STING1; Xeno; NbExp=4; IntAct=EBI-25622115, EBI-2800345;
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 9]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes (By similarity). {ECO:0000250}.
CC -!- 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=P0C6X5-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6U6-1; Sequence=External;
CC -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC association of the replication complex and thereby alter the
CC architecture of the host cell membrane.
CC -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically
CC processed.
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; AY567487; AAS58176.2; -; Genomic_RNA.
DR RefSeq; YP_003766.2; NC_005831.2. [P0C6X5-1]
DR PDB; 5NH0; X-ray; 2.35 A; A/C=2940-3238, B=2940-3239.
DR PDB; 6FV1; X-ray; 2.30 A; A/B/C=2940-3240.
DR PDB; 6FV2; X-ray; 2.95 A; A/B/C=2940-3240.
DR PDBsum; 5NH0; -.
DR PDBsum; 6FV1; -.
DR PDBsum; 6FV2; -.
DR SMR; P0C6X5; -.
DR IntAct; P0C6X5; 75.
DR BindingDB; P0C6X5; -.
DR MEROPS; C30.003; -.
DR PRIDE; P0C6X5; -.
DR DNASU; 2943501; -.
DR GeneID; 2943501; -.
DR KEGG; vg:2943501; -.
DR SABIO-RK; P0C6X5; -.
DR Proteomes; UP000008573; 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: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:0003723; F:RNA binding; IEA:UniProtKB-KW.
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:0008270; F:zinc ion binding; IEA:InterPro.
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:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
DR GO; GO: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; cd21558; alphaCoV-Nsp6; 1.
DR CDD; cd21660; alphaCoV_Nsp14; 1.
DR CDD; cd21665; alphaCoV_Nsp5_Mpro; 1.
DR CDD; cd21588; alphaCoV_RdRp; 1.
DR CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR CDD; cd21514; cv_alpha_Nsp2_HCoV-229E-like; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21167; M_alpha_beta_cv_Nsp15-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR CDD; cd21171; NTD_alpha_beta_cv_Nsp15-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; -; 2.
DR Gene3D; 1.10.8.370; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.40.10.250; -; 1.
DR Gene3D; 3.30.160.820; -; 1.
DR Gene3D; 3.30.70.3540; -; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.50.11580; -; 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; 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; IPR044313; NSP14_alphaCoV.
DR InterPro; IPR009466; NSP14_CoV.
DR InterPro; IPR044330; NSP15_alpha_betaCoV_N.
DR InterPro; IPR044322; NSP15_M_alpha_beta_CoV.
DR InterPro; IPR043174; NSP15_middle_sf.
DR InterPro; IPR042515; NSP15_N_CoV.
DR InterPro; IPR044401; NSP15_NendoU_CoV.
DR InterPro; IPR009461; NSP16_CoV-like.
DR InterPro; IPR044385; NSP2_HCoV-229E-like.
DR InterPro; IPR043615; NSP2_N_CoV.
DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR044309; NSP5_Mpro_alphaCoV.
DR InterPro; IPR044369; NSP6_alphaCoV.
DR InterPro; IPR043610; NSP6_CoV.
DR InterPro; IPR014828; NSP7_CoV.
DR InterPro; IPR037204; NSP7_sf_CoV.
DR InterPro; IPR014829; NSP8_CoV.
DR InterPro; IPR037230; NSP8_sf_CoV.
DR InterPro; IPR014822; NSP9_CoV.
DR InterPro; IPR036499; NSP9_sf_CoV.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR013016; Peptidase_C16_CoV.
DR InterPro; IPR008740; Peptidase_C30_CoV.
DR InterPro; IPR043477; Peptidase_C30_dom3_CoV.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR InterPro; IPR044356; RdRp_alphaCoV.
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; 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; 2.
DR Pfam; PF19211; CoV_NSP2_N; 1.
DR Pfam; PF19218; CoV_NSP3_C; 1.
DR Pfam; PF16348; CoV_NSP4_C; 1.
DR Pfam; PF19217; CoV_NSP4_N; 1.
DR Pfam; PF19213; CoV_NSP6; 1.
DR Pfam; PF08716; CoV_NSP7; 1.
DR Pfam; PF08717; CoV_NSP8; 1.
DR Pfam; PF08710; CoV_NSP9; 1.
DR Pfam; PF08715; CoV_peptidase; 2.
DR Pfam; PF06478; CoV_RPol_N; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; 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; SSF50494; SSF50494; 1.
DR SUPFAM; SSF51126; SSF51126; 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; 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; 2.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Endonuclease; Exonuclease; Helicase; Host cytoplasm; Host membrane;
KW Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host IRF3 by virus; Inhibition of host RLR pathway by virus;
KW Lyase; Membrane; Metal-binding; Methyltransferase;
KW Modulation of host ubiquitin pathway by viral deubiquitinase;
KW Modulation of host ubiquitin pathway by virus; Nuclease;
KW Nucleotide-binding; Nucleotidyltransferase; Protease; 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..110
FT /note="Non-structural protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000283874"
FT CHAIN 111..898
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000283875"
FT CHAIN 899..2462
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000283876"
FT CHAIN 2463..2939
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000283877"
FT CHAIN 2940..3242
FT /note="3C-like proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000283878"
FT CHAIN 3243..3521
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250"
FT /id="PRO_0000283879"
FT CHAIN 3522..3604
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000283880"
FT CHAIN 3605..3799
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000283881"
FT CHAIN 3800..3908
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250"
FT /id="PRO_0000283882"
FT CHAIN 3909..4043
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250"
FT /id="PRO_0000283883"
FT CHAIN 4044..4970
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000283884"
FT CHAIN 4971..5567
FT /note="Helicase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000283885"
FT CHAIN 5568..6085
FT /note="Exoribonuclease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000283886"
FT CHAIN 6086..6429
FT /note="Uridylate-specific endoribonuclease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000283887"
FT CHAIN 6430..6729
FT /note="Putative 2'-O-methyl transferase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000283888"
FT TRANSMEM 1903..1923
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1968..1988
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2050..2070
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2073..2093
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2111..2131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2468..2488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2727..2747
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2752..2769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2772..2792
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2800..2820
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3254..3274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3279..3299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3303..3323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3342..3362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3376..3396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3397..3417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3442..3462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 2..109
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT DOMAIN 112..358
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 388..778
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 776..898
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 899..994
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1021..1262
FT /note="Peptidase C16 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1263..1421
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1579..1633
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1640..1886
FT /note="Peptidase C16 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 2357..2461
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 2844..2939
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 2940..3242
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3522..3604
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3605..3799
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 3800..3908
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 3909..4047
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT DOMAIN 4049..4298
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 4403..4970
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT DOMAIN 4650..4812
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 4971..5054
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT DOMAIN 5228..5409
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 5410..5579
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 5639..5853
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 5862..6083
FT /note="N7-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT DOMAIN 6086..6146
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT DOMAIN 6147..6269
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 6286..6426
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6430..6726
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ZN_FING 1134..1165
FT /note="C4-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 1757..1788
FT /note="C4-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 3982..3998
FT /evidence="ECO:0000250"
FT ZN_FING 4024..4037
FT /evidence="ECO:0000250"
FT REGION 245..265
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 1903..2131
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2468..2820
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3254..3462
FT /note="HD3"
FT /evidence="ECO:0000250"
FT REGION 5974..5988
FT /note="GpppA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT ACT_SITE 1062
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1212
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1678
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1836
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 2980
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3083
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 4797
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 4798
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 4799
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5657
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5659
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5758
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5834
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5839
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6558
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6598
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6631
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 3982
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3985
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3991
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3998
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4024
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4027
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4035
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4037
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4975
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4978
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4986
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4989
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4996
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4999
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5003
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5009
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5020
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5025
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5042
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5045
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5253..5260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 5774
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5776
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5792
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5795
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5823
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5827
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5830
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5845
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5897..5903
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6012
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6029
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6040
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6043
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT SITE 110..111
FT /note="Cleavage; by PL1-PRO"
FT /evidence="ECO:0000250"
FT SITE 898..899
FT /note="Cleavage; by PL1-PRO"
FT /evidence="ECO:0000250"
FT SITE 2462..2463
FT /note="Cleavage; by PL2-PRO"
FT /evidence="ECO:0000250"
FT SITE 2939..2940
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3242..3243
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3521..3522
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3604..3605
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3799..3800
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3908..3909
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4043..4044
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4970..4971
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 6085..6086
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 6429..6430
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT HELIX 2950..2953
FT /evidence="ECO:0007829|PDB:6FV1"
FT STRAND 2956..2961
FT /evidence="ECO:0007829|PDB:6FV1"
FT STRAND 2964..2971
FT /evidence="ECO:0007829|PDB:6FV1"
FT STRAND 2974..2978
FT /evidence="ECO:0007829|PDB:6FV1"
FT HELIX 2979..2982
FT /evidence="ECO:0007829|PDB:6FV1"
FT STRAND 2986..2988
FT /evidence="ECO:0007829|PDB:6FV1"
FT HELIX 2992..2997
FT /evidence="ECO:0007829|PDB:6FV1"
FT HELIX 3001..3003
FT /evidence="ECO:0007829|PDB:6FV1"
FT STRAND 3004..3008
FT /evidence="ECO:0007829|PDB:6FV1"
FT STRAND 3011..3013
FT /evidence="ECO:0007829|PDB:6FV1"
FT STRAND 3015..3021
FT /evidence="ECO:0007829|PDB:6FV1"
FT STRAND 3024..3031
FT /evidence="ECO:0007829|PDB:6FV1"
FT STRAND 3038..3041
FT /evidence="ECO:0007829|PDB:6FV1"
FT STRAND 3049..3056
FT /evidence="ECO:0007829|PDB:6FV1"
FT STRAND 3059..3067
FT /evidence="ECO:0007829|PDB:6FV1"
FT STRAND 3086..3090
FT /evidence="ECO:0007829|PDB:6FV1"
FT STRAND 3096..3105
FT /evidence="ECO:0007829|PDB:6FV1"
FT STRAND 3111..3114
FT /evidence="ECO:0007829|PDB:6FV1"
FT HELIX 3121..3123
FT /evidence="ECO:0007829|PDB:6FV1"
FT STRAND 3126..3129
FT /evidence="ECO:0007829|PDB:6FV1"
FT HELIX 3140..3152
FT /evidence="ECO:0007829|PDB:6FV1"
FT HELIX 3166..3175
FT /evidence="ECO:0007829|PDB:6FV1"
FT HELIX 3184..3187
FT /evidence="ECO:0007829|PDB:6FV1"
FT HELIX 3188..3194
FT /evidence="ECO:0007829|PDB:6FV1"
FT HELIX 3198..3208
FT /evidence="ECO:0007829|PDB:6FV1"
FT STRAND 3220..3222
FT /evidence="ECO:0007829|PDB:6FV1"
FT HELIX 3229..3237
FT /evidence="ECO:0007829|PDB:6FV1"
SQ SEQUENCE 6729 AA; 752702 MW; 86F9F04C687A65FA CRC64;
MFYNQVTLAV ASDSEISGFG FAIPSVAVRT YSEAAAQGFQ ACRFVAFGLQ DCVTGINDDD
YVIALTGTNQ LCAKILPFSD RPLNLRGWLI FSNSNYVLQD FDVVFGHGAG SVVFVDKYMC
GFDGKPVLPK NMWEFRDYFN NNTDSIVIGG VTYQLAWDVI RKDLSYEQQN VLAIESIHYL
GTTGHTLKSG CKLTNAKPPK YSSKVVLSGE WNAVYRAFGS PFITNGMSLL DIIVKPVFFN
AFVKCNCGSE SWSVGAWDGY LSSCCGTPAK KLCVVPGNVV PGDVIITSTS AGCGVKYYAG
LVVKHITNIT GVSLWRVTAV HSDGMFVASS SYDALLHRNS LDPFCFDVNT LLSNQLRLAF
LGASVTEDVK FAASTGVIDI SAGMFGLYDD ILTNNKPWFV RKASGLFDAI WDAFVAAIKL
VPTTTGVLVR FVKSIASTVL TVSNGVIIMC ADVPDAFQSV YRTFTQAICA AFDFSLDVFK
IGDVKFKRLG DYVLTENALV RLTTEVVRGV RDARIKKAMF TKVVVGPTTE VKFSVIELAT
VNLRLVDCAP VVCPKGKIVV IAGQAFFYSG GFYRFMVDPT TVLNDPVFTG DLFYTIKFSG
FKLDGFNHQF VTASSATDAI IAVELLLLDF KTAVFVYTCV VDGCSVIVRR DATFATHVCF
KDCYNVWEQF CIDNCGEPWF LTDYNAILQS NNPQCAIVQA SESKVLLERF LPKCPEILLS
IDDGHLWNLF VEKFNFVTDW LKTLKLTLTS NGLLGNCAKR FRRVLVKLLD VYNGFLETVC
SVAYTAGVCI KYYAVNVPYV VISGFVSRVI RRERCDMTFP CVSCVTFFYE FLDTCFGVSK
PNAIDVEHLE LKETVFVEPK DGGQFFVSGD YLWYVVDDIY YPASCNGVLP VAFTKLAGGK
ISFSDDVIVH DVEPTHKVKL IFEFEDDVVT SLCKKSFGKS IIYTGDWEGL HEVLTSAMNV
IGQHIKLPQF YIYDEEGGYD VSKPVMISQW PISNDSNGCV VEASTDFHQL ECIVDDSVRE
EVDIIEQPFE EVEHVLSIKQ PFSFSFRDEL GVRVLDQSDN NCWISTTLVQ LQLTKLLDDS
IEMQLFKVGK VDSIVQKCYE LSHLISGSLG DSGKLLSELL KEKYTCSITF EMSCDCGKKF
DDQVGCLFWI MPYTKLFQKG ECCICHKMQT YKLVSMKGTG VFVQDPAPID IDAFPVKPIC
SSVYLGVKGS GHYQTNLYSF NKAIDGFGVF DIKNSSVNTV CFVDVDFHSV EIEAGEVKPF
AVYKNVKFYL GDISHLVNCV SFDFVVNAAN ENLLHGGGVA RAIDILTEGQ LQSLSKDYIS
SNGPLKVGAG VMLECEKFNV FNVVGPRTGK HEHSLLVEAY NSILFENGIP LMPLLSCGIF
GVRIENSLKA LFSCDINKPL QVFVYSSNEE QAVLKFLDGL DLTPVIDDVD VVKPFRVEGN
FSFFDCGVNA LDGDIYLLFT NSILMLDKQG QLLDTKLNGI LQQAALDYLA TVKTVPAGNL
VKLFVESCTI YMCVVPSIND LSFDKNLGRC VRKLNRLKTC VIANVPAIDV LKKLLSSLTL
TVKFVVESNV MDVNDCFKND NVVLKITEDG INVKDVVVES SKSLGKQLGV VSDGVDSFEG
VLPINTDTVL SVAPEVDWVA FYGFEKAALF ASLDVKPYGY PNDFVGGFRV LGTTDNNCWV
NATCIILQYL KPTFKSKGLN VLWNKFVTGD VGPFVSFIYF ITMSSKGQKG DAEEALSKLS
EYLISDSIVT LEQYSTCDIC KSTVVEVKSA IVCASVLKDG CDVGFCPHRH KLRSRVKFVN
GRVVITNVGE PIISQPSKLL NGIAYTTFSG SFDNGHYVVY DAANNAVYDG ARLFSSDLST
LAVTAIVVVG GCVTSNVPTI VSEKISVMDK LDTGAQKFFQ FGDFVMNNIV LFLTWLLSMF
SLLRTSIMKH DIKVIAKAPK RTGVILTRSF KYNIRSALFV IKQKWCVIVT LFKFLLLLYA
IYALVFMIVQ FSPFNSLLCG DIVSGYEKST FNKDIYCGNS MVCKMCLFSY QEFNDLDHTS
LVWKHIRDPI LISLQPFVIL VILLIFGNMY LRFGLLYFVA QFISTFGSFL GFHQKQWFLH
FVPFDVLCNE FLATFIVCKI VLFVRHIIVG CNNADCVACS KSARLKRVPL QTIINGMHKS
FYVNANGGTC FCNKHNFFCV NCDSFGPGNT FINGDIAREL GNVVKTAVQP TAPAYVIIDK
VDFVNGFYRL YSGDTFWRYD FDITESKYSC KEVLKNCNVL ENFIVYNNSG SNITQIKNAC
VYFSQLLCEP IKLVNSELLS TLSVDFNGVL HKAYVDVLCN SFFKELTANM SMAECKATLG
LTVSDDDFVS AVANAHRYDV LLSDLSFNNF FISYAKPEDK LSVYDIACCM RAGSKVVNHN
VLIKESIPIV WGVKDFNTLS QEGKKYLVKT TKAKGLTFLL TFNDNQAITQ VPATSIVAKQ
GAGFKRTYNF LWYVCLFVVA LFIGVSFIDY TTTVTSFHGY DFKYIENGQL KVFEAPLHCV
RNVFDNFNQW HEAKFGVVTT NSDKCPIVVG VSERINVVPG VPTNVYLVGK TLVFTLQAAF
GNTGVCYDFD GVTTSDKCIF NSACTRLEGL GGDNVYCYNT DLIEGSKPYS TLQPNAYYKY
DAKNYVRFPE ILARGFGLRT IRTLATRYCR VGECRDSHKG VCFGFDKWYV NDGRVDDGYI
CGDGLIDLLV NVLSIFSSSF SVVAMSGHML FNFLFAAFIT FLCFLVTKFK RVFGDLSYGV
FTVVCATLIN NISYVVTQNL FFMLLYAILY FVFTRTVRYA WIWHIAYIVA YFLLIPWWLL
TWFSFAAFLE LLPNVFKLKI STQLFEGDKF IGTFESAAAG TFVLDMRSYE RLINTISPEK
LKNYAASYNK YKYYSGSASE ADYRCACYAH LAKAMLDYAK DHNDMLYSPP TISYNSTLQS
GLKKMAQPSG CVERCVVRVC YGSTVLNGVW LGDTVTCPRH VIAPSTTVLI DYDHAYSTMR
LHNFSVSHNG VFLGVVGVTM HGSVLRIKVS QSNVHTPKHV FKTLKPGDSF NILACYEGIA
SGVFGVNLRT NFTIKGSFIN GACGSPGYNV RNDGTVEFCY LHQIELGSGA HVGSDFTGSV
YGNFDDQPSL QVESANLMLS DNVVAFLYAA LLNGCRWWLC STRVNVDGFN EWAMANGYTS
VSSVECYSIL AAKTGVSVEQ LLASIQHLHE GFGGKNILGY SSLCDEFTLA EVVKQMYGVN
LQSGKVIFGL KTMFLFSVFF TMFWAELFIY TNTIWINPVI LTPIFCLLLF LSLVLTMFLK
HKFLFLQVFL LPTVIATALY NCVLDYYIVK FLADHFNYNV SVLQMDVQGL VNVLVCLFVV
FLHTWRFSKE RFTHWFTYVC SLIAVAYTYF YSGDFLSLLV MFLCAISSDW YIGAIVFRLS
RLIVFFSPES VFSVFGDVKL TLVVYLICGY LVCTYWGILY WFNRFFKCTM GVYDFKVSAA
EFKYMVANGL HAPHGPFDAL WLSFKLLGIG GDRCIKISTV QSKLTDLKCT NVVLLGCLSS
MNIAANSSEW AYCVDLHNKI NLCDDPEKAQ SMLLALLAFF LSKHSDFGLD GLIDSYFDNS
STLQSVASSF VSMPSYIAYE NARQAYEDAI ANGSSSQLIK QLKRAMNIAK SEFDHEISVQ
KKINRMAEQA ATQMYKEARS VNRKSKVISA MHSLLFGMLR RLDMSSVETV LNLARDGVVP
LSVIPATSAS KLTIVSPDLE SYSKIVCDGS VHYAGVVWTL NDVKDNDGRP VHVKEITKEN
VETLTWPLIL NCERVVKLQN NEIMPGKLKQ KPMKAEGDGG VLGDGNALYN TEGGKTFMYA
YISNKADLKF VKWEYEGGCN TIELDSPCRF MVETPNGPQV KYLYFVKNLN TLRRGAVLGF
IGATIRLQAG KQTELAVNSG LLTACAFSVD PATTYLEAVK HGAKPVSNCI KMLSNGAGNG
QAITTSVDAN TNQDSYGGAS ICLYCRAHVP HPSMDGYCKF KGKCVQVPIG CLDPIRFCLE
NNVCNVCGCW LGHGCACDRT TIQSVDISYL NRARGSSAAR LEPCNGTDID KCVRAFDIYN
KNVSFLGKCL KMNCVRFKNA DLKDGYFVIK RCTKSVMEHE QSMYNLLNFS GALAEHDFFT
WKDGRVIYGN VSRHNLTKYT MMDLVYAMRN FDEQNCDVLK EVLVLTGCCD NSYFDSKGWY
DPVENEDIHR VYASLGKIVA RAMLKCVALC DAMVAKGVVG VLTLDNQDLN GNFYDFGDFV
VSLPNMGVPC CTSYYSYMMP IMGLTNCLAS ECFVKSDIFG SDFKTFDLLK YDFTEHKENL
FNKYFKHWSF DYHPNCSDCY DDMCVIHCAN FNTLFATTIP GTAFGPLCRK VFIDGVPLVT
TAGYHFKQLG LVWNKDVNTH SVRLTITELL QFVTDPSLII ASSPALVDQR TICFSVAALS
TGLTNQVVKP GHFNEEFYNF LRLRGFFDEG SELTLKHFFF AQNGDAAVKD FDFYRYNKPT
ILDICQARVT YKIVSRYFDI YEGGCIKACE VVVTNLNKSA GWPLNKFGKA SLYYESISYE
EQDALFALTK RNVLPTMTQL NLKYAISGKE RARTVGGVSL LSTMTTRQYH QKHLKSIVNT
RNATVVIGTT KFYGGWNNML RTLIDGVENP MLMGWDYPKC DRALPNMIRM ISAMVLGSKH
VNCCTATDRF YRLGNELAQV LTEVVYSNGG FYFKPGGTTS GDASTAYANS IFNIFQAVSS
NINRLLSVPS DSCNNVNVRD LQRRLYDNCY RLTSVEESFI DDYYGYLRKH FSMMILSDDG
VVCYNKDYAE LGYIADISAF KATLYYQNNV FMSTSKCWVE EDLTKGPHEF CSQHTMQIVD
KDGTYYLPYP DPSRILSAGV FVDDVVKTDA VVLLERYVSL AIDAYPLSKH PNSEYRKVFY
VLLDWVKHLN KNLNEGVLES FSVTLLDNQE DKFWCEDFYA SMYENSTILQ AAGLCVVCGS
QTVLRCGDCL RKPMLCTKCA YDHVFGTDHK FILAITPYVC NASGCGVSDV KKLYLGGLNY
YCTNHKPQLS FPLCSAGNIF GLYKNSATGS LDVEVFNRLA TSDWTDVRDY KLANDVKDTL
RLFAAETIKA KEESVKSSYA FATLKEVVGP KELLLSWESG KVKPPLNRNS VFTCFQISKD
SKFQIGEFIF EKVEYGSDTV TYKSTVTTKL VPGMIFVLTS HNVQPLRAPT IANQEKYSSI
YKLHPAFNVS DAYANLVPYY QLIGKQKITT IQGPPGSGKS HCSIGLGLYY PGARIVFVAC
AHAAVDSLCA KAMTVYSIDK CTRIIPARAR VECYSGFKPN NTSAQYIFST VNALPECNAD
IVVVDEVSMC TNYDLSVINQ RLSYKHIVYV GDPQQLPAPR VMITKGVMEP VDYNVVTQRM
CAIGPDVFLH KCYRCPAEIV NTVSELVYEN KFVPVKPASK QCFKVFFKGN VQVDNGSSIN
RKQLEIVKLF LVKNPSWSKA VFISPYNSQN YVASRFLGLQ IQTVDSSQGS EYDYVIYAQT
SDTAHACNVN RFNVAITRAK KGIFCVMCDK TLFDSLKFFE IKHADLHSSQ VCGLFKNCTR
TPLNLPPTHA HTFLSLSDQF KTTGDLAVQI GSNNVCTYEH VISFMGFRFD ISIPGSHSLF
CTRDFAIRNV RGWLGMDVES AHVCGDNIGT NVPLQVGFSN GVNFVVQTEG CVSTNFGDVI
KPVCAKSPPG EQFRHLIPLL RKGQPWLIVR RRIVQMISDY LSNLSDILVF VLWAGSLELT
TMRYFVKIGP IKYCYCGNSA TCYNSVSNEY CCFKHALGCD YVYNPYAFDI QQWGYVGSLS
QNHHTFCNIH RNEHDASGDA VMTRCLAVHD CFVKNVDWTV TYPFIANEKF INGCGRNVQG
HVVRAALKLY KPSVIHDIGN PKGVRCAVTD AKWYCYDKQP VNSNVKLLDY DYATHGQLDG
LCLFWNCNVD MYPEFSIVCR FDTRTRSVFN LEGVNGGSLY VNKHAFHTPA YDKRAFVKLK
PMPFFYFDDS DCDVVQEQVN YVPLRASSCV TRCNIGGAVC SKHANLYQKY VEAYNTFTQA
GFNIWVPHSF DVYNLWQIFI ETNLQSLENI AFNVVKKGCF TGVDGELPVA VVNDKVFVRY
GDVDNLVFTN KTTLPTNVAF ELFAKRKMGL TPPLSILKNL GVVATYKFVL WDYEAERPFT
SYTKSVCKYT DFNEDVCVCF DNSIQGSYER FTLTTNAVLF STVVIKNLTP IKLNFGMLNG
MPVSSIKGDK GVEKLVNWYI YVRKNGQFQD HYDGFYTQGR NLSDFTPRSD MEYDFLNMDM
GVFINKYGLE DFNFEHVVYG DVSKTTLGGL HLLISQFRLS KMGVLKADDF VTASDTTLRC
CTVTYLNELS SKVVCTYMDL LLDDFVTILK SLDLGVISKV HEVIIDNKPY RWMLWCKDNH
LSTFYPQLQS AEWKCGYAMP QIYKLQRMCL EPCNLYNYGA GIKLPSGIML NVVKYTQLCQ
YLNSTTMCVP HNMRVLHYGA GSDKGVAPGT TVLKRWLPPD AIIIDNDIND YVSDADFSIT
GDCATVYLED KFDLLISDMY DGRIKFCDGE NVSKDGFFTY LNGVIREKLA IGGSVAIKIT
EYSWNKYLYE LIQRFAFWTL FCTSVNTSSS EAFLIGINYL GDFIQGPFIA GNTVHANYIF
WRNSTIMSLS YNSVLDLSKF ECKHKATVVV TLKDSDVNDM VLSLIKSGRL LLRNNGRFGG
FSNHLVSTK
