R1AB_CVHOC
ID R1AB_CVHOC Reviewed; 7095 AA.
AC P0C6X6; Q4VID8; Q4VIE7; Q696Q1; Q6TNG2; Q9WAC3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=p28;
DE Contains:
DE RecName: Full=Non-structural protein 2;
DE Short=nsp2;
DE AltName: Full=p65;
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 AltName: Full=p210;
DE Contains:
DE RecName: Full=Non-structural protein 4;
DE Short=nsp4;
DE AltName: Full=Peptide HD2;
DE AltName: Full=p44;
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=p27;
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=p10;
DE Contains:
DE RecName: Full=Non-structural protein 8;
DE Short=nsp8;
DE AltName: Full=p22;
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=p15;
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=p67;
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 AltName: Full=p35;
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 Human coronavirus OC43 (HCoV-OC43).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=31631;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate 19572 Belgium 2004, and Isolate 87309 Belgium 2003;
RX PubMed=15914223; DOI=10.1016/j.virol.2005.04.010;
RA Vijgen L., Keyaerts E., Lemey P., Moes E., Li S., Vandamme A.M.,
RA Van Ranst M.;
RT "Circulation of genetically distinct contemporary human coronavirus OC43
RT strains.";
RL Virology 337:85-92(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate ATCC VR-759, and Isolate clinical OC43-Paris;
RX PubMed=15280490; DOI=10.1128/jvi.78.16.8824-8834.2004;
RA St Jean J.R., Jacomy H., Desforges M., Vabret A., Freymuth F., Talbot P.J.;
RT "Human respiratory coronavirus OC43: genetic stability and neuroinvasion.";
RL J. Virol. 78:8824-8834(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate ATCC VR-759;
RX PubMed=15650185; DOI=10.1128/jvi.79.3.1595-1604.2005;
RA Vijgen L., Keyaerts E., Moes E., Thoelen I., Wollants E., Lemey P.,
RA Vandamme A.M., Van Ranst M.;
RT "Complete genomic sequence of human coronavirus OC43: molecular clock
RT analysis suggests a relatively recent zoonotic coronavirus transmission
RT event.";
RL J. Virol. 79:1595-1604(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 4871-5177.
RC STRAIN=Isolate Tulsa 1999;
RX PubMed=10392726; DOI=10.1016/s0168-1702(99)00017-9;
RA Stephensen C.B., Casebolt D.B., Gangopadhyay N.N.;
RT "Phylogenetic analysis of a highly conserved region of the polymerase gene
RT from 11 coronaviruses and development of a consensus polymerase chain
RT reaction assay.";
RL Virus Res. 60:181-189(1999).
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
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=P0C6X6-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6U7-1; Sequence=External;
CC -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC association of the replication complex and thereby alter the
CC architecture of the host cell membrane.
CC -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically
CC processed (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: The sequence shown is that of isolate 19572 Belgium
CC 2004.
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; AY903459; AAX85666.1; -; Genomic_RNA.
DR EMBL; AY903460; AAX85675.1; -; Genomic_RNA.
DR EMBL; AY585228; AAT84351.1; -; Genomic_RNA.
DR EMBL; AY585229; AAT84359.1; -; Genomic_RNA.
DR EMBL; AY391777; AAR01012.1; -; Genomic_RNA.
DR EMBL; AF124989; AAD32993.1; -; Genomic_RNA.
DR PDB; 7NH7; X-ray; 2.20 A; A=6797-7095.
DR PDBsum; 7NH7; -.
DR SMR; P0C6X6; -.
DR IntAct; P0C6X6; 59.
DR BindingDB; P0C6X6; -.
DR MEROPS; C16.006; -.
DR PRIDE; P0C6X6; -.
DR Proteomes; UP000007552; Genome.
DR Proteomes; UP000100580; Genome.
DR Proteomes; UP000159995; Genome.
DR Proteomes; UP000161137; Genome.
DR Proteomes; UP000180344; 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: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; cd21519; cv_beta_Nsp2_MHV-like; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21524; DPUP_MHV_Nsp3; 1.
DR CDD; cd21593; HCoV_HKU1-like_RdRp; 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; 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; -; 2.
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; 3.40.50.11020; -; 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; IPR022570; B-CoV_A_NSP1.
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; IPR044384; NSP2_MHV-like.
DR InterPro; IPR044381; NSP3_DPUP_MHV.
DR InterPro; IPR032592; NSP3_NAB_bCoV.
DR InterPro; IPR042570; NSP3_NAB_bCoV_sf.
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; IPR002705; Pept_C30/C16_B_coronavir.
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; IPR044347; RdRp_HCoV_HKU1-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; 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; 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; PF11963; DUF3477; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF01831; Peptidase_C16; 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; 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; 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 Decay of host mRNAs by virus; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Exonuclease; Helicase;
KW Host cytoplasm; Host gene expression shutoff by virus; Host membrane;
KW Host mRNA suppression by virus; Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host ISG15 by virus; Inhibition of host NF-kappa-B by virus;
KW Lyase; Membrane; Metal-binding; Methyltransferase;
KW Modulation of host ubiquitin pathway by viral deubiquitinase;
KW Modulation of host ubiquitin pathway by virus; Nuclease;
KW Nucleotide-binding; Nucleotidyltransferase; Protease; Repeat;
KW Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
KW Thiol protease; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Viral immunoevasion; Viral RNA replication; Zinc;
KW Zinc-finger.
FT CHAIN 1..246
FT /note="Host translation inhibitor nsp1"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000283826"
FT CHAIN 247..851
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000283827"
FT CHAIN 852..2750
FT /note="Papain-like proteinase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000283828"
FT CHAIN 2751..3246
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000283829"
FT CHAIN 3247..3549
FT /note="3C-like proteinase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000283830"
FT CHAIN 3550..3836
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000283831"
FT CHAIN 3837..3925
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000283832"
FT CHAIN 3926..4122
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000283833"
FT CHAIN 4123..4232
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000283834"
FT CHAIN 4233..4369
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000283835"
FT CHAIN 4370..5297
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000037308"
FT CHAIN 5298..5900
FT /note="Helicase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000283836"
FT CHAIN 5901..6421
FT /note="Guanine-N7 methyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000283837"
FT CHAIN 6422..6796
FT /note="Uridylate-specific endoribonuclease"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000283838"
FT CHAIN 6797..7095
FT /note="2'-O-methyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT /id="PRO_0000283839"
FT TRANSMEM 2138..2158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2199..2219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2221..2241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2313..2333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2343..2363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2365..2385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2752..2772
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2824..2844
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3009..3029
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3031..3051
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3063..3083
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3090..3110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3115..3135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3558..3578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3588..3608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3615..3635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3657..3677
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3684..3704
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3711..3731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 3755..3775
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 54..196
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01307"
FT DOMAIN 216..246
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01308"
FT DOMAIN 250..514
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT DOMAIN 524..713
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01334"
FT DOMAIN 733..851
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01335"
FT DOMAIN 853..966
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1036..1274
FT /note="Peptidase C16 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1275..1435
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1491..1563
FT /note="DPUP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01289"
FT DOMAIN 1562..1617
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1631..1892
FT /note="Peptidase C16 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 1906..2007
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01290"
FT DOMAIN 2020..2169
FT /note="G2M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01338"
FT DOMAIN 2647..2750
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 3149..3246
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 3247..3549
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3837..3925
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3926..4122
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 4123..4232
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 4233..4370
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT DOMAIN 4375..4630
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 4730..5297
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT DOMAIN 4977..5139
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 5298..5381
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT DOMAIN 5553..5734
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 5735..5904
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 5971..6186
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 6195..6421
FT /note="N7-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT DOMAIN 6422..6482
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT DOMAIN 6483..6603
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 6654..6793
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6798..7092
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ZN_FING 1151..1179
FT /note="C4-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 1749..1785
FT /note="C4-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 4306..4322
FT /evidence="ECO:0000250"
FT ZN_FING 4348..4361
FT /evidence="ECO:0000250"
FT REGION 392..416
FT /note="C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT REGION 995..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2138..2385
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 2752..3135
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 3319..3775
FT /note="HD3"
FT /evidence="ECO:0000250"
FT REGION 6308..6322
FT /note="GpppA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT COMPBIAS 1003..1025
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1074
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1225
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1671
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1828
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3287
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 3391
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 5124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5989
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5991
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6090
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6684
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6699
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6739
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6842
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6926
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6966
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6999
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01333"
FT BINDING 4306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 5302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5578..5585
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 6106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 6230..6236
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 6381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT SITE 246..247
FT /note="Cleavage; by PL1-PRO"
FT /evidence="ECO:0000250"
FT SITE 851..852
FT /note="Cleavage; by PL1-PRO"
FT /evidence="ECO:0000250"
FT SITE 2750..2751
FT /note="Cleavage; by PL2-PRO"
FT /evidence="ECO:0000250"
FT SITE 3246..3247
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3549..3550
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3836..3837
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 3925..3926
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4122..4123
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4232..4233
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 4369..4370
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 5297..5298
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 5900..5901
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 6421..6422
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT SITE 6796..6797
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250"
FT VARIANT 88
FT /note="H -> D (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 207
FT /note="C -> R (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 291
FT /note="P -> L (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 317
FT /note="C -> R (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 356
FT /note="F -> V (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 545
FT /note="I -> L (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 762
FT /note="D -> N (in strain: Isolate 87309 Belgium 2003)"
FT VARIANT 953
FT /note="F -> L (in strain: ATCC VR-759, Isolate clinical
FT OC43-Paris and Isolate 87309 Belgium 2003)"
FT VARIANT 989
FT /note="I -> V (in strain: ATCC VR-759, Isolate clinical
FT OC43-Paris and Isolate 87309 Belgium 2003)"
FT VARIANT 1305
FT /note="V -> A (in strain: ATCC VR-759, Isolate clinical
FT OC43-Paris and Isolate 87309 Belgium 2003)"
FT VARIANT 1328
FT /note="N -> D (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 1379
FT /note="F -> L (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 1504
FT /note="L -> V (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 1740
FT /note="G -> E (in strain: Isolate 87309 Belgium 2003)"
FT VARIANT 1825
FT /note="N -> K (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 1936
FT /note="S -> A (in strain: ATCC VR-759, Isolate clinical
FT OC43-Paris and Isolate 87309 Belgium 2003)"
FT VARIANT 1965
FT /note="N -> T (in strain: ATCC VR-759, Isolate clinical
FT OC43-Paris)"
FT VARIANT 2004
FT /note="L -> S (in strain: ATCC VR-759, Isolate clinical
FT OC43-Paris and Isolate 87309 Belgium 2003)"
FT VARIANT 2022
FT /note="S -> G (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 2138..2140
FT /note="TSA -> ISV (in strain: ATCC VR-759 and Isolate
FT clinical OC43-Paris)"
FT VARIANT 2256
FT /note="I -> M (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 2257
FT /note="Q -> H (in strain: Isolate 87309 Belgium 2003)"
FT VARIANT 2386
FT /note="K -> R (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 2500
FT /note="I -> T (in strain: ATCC VR-759, Isolate clinical
FT OC43-Paris and Isolate 87309 Belgium 2003)"
FT VARIANT 2921
FT /note="D -> E (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 2961
FT /note="V -> I (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 3086
FT /note="T -> I (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 3440
FT /note="P -> L (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 3451
FT /note="L -> V (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 3466
FT /note="I -> V (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 4067
FT /note="I -> V (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 4071
FT /note="I -> V (in strain: ATCC VR-759, Isolate clinical
FT OC43-Paris and Isolate 87309 Belgium 2003)"
FT VARIANT 4382
FT /note="A -> T (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 4994
FT /note="I -> L (in strain: ATCC VR-759, Isolate clinical
FT OC43-Paris and Isolate Tulsa 1999 and Isolate 87309 Belgium
FT 2003)"
FT VARIANT 5014..5015
FT /note="SD -> RT (in strain: Isolate Tulsa 1999)"
FT VARIANT 5765
FT /note="L -> S (in strain: ATCC VR-759, Isolate clinical
FT OC43-Paris and Isolate 87309 Belgium 2003)"
FT VARIANT 5997
FT /note="L -> R (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 6236
FT /note="G -> A (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 6454
FT /note="T -> A (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT VARIANT 6546
FT /note="F -> L (in strain: ATCC VR-759, Isolate clinical
FT OC43-Paris and Isolate 87309 Belgium 2003)"
FT VARIANT 6636
FT /note="D -> E (in strain: Isolate 87309 Belgium 2003)"
FT VARIANT 6665
FT /note="A -> T (in strain: Isolate 87309 Belgium 2003)"
FT VARIANT 6754
FT /note="T -> A (in strain: ATCC VR-759 and Isolate clinical
FT OC43-Paris)"
FT CONFLICT 426
FT /note="I -> M (in Ref. 3; AAT84359/AAT84351)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="D -> A (in Ref. 3; AAT84359/AAT84351)"
FT /evidence="ECO:0000305"
FT CONFLICT 4376..4377
FT /note="LN -> FK (in Ref. 2; AAR01012)"
FT /evidence="ECO:0000305"
FT HELIX 6798..6801
FT /evidence="ECO:0007829|PDB:7NH7"
FT STRAND 6802..6806
FT /evidence="ECO:0007829|PDB:7NH7"
FT HELIX 6809..6812
FT /evidence="ECO:0007829|PDB:7NH7"
FT HELIX 6838..6850
FT /evidence="ECO:0007829|PDB:7NH7"
FT STRAND 6862..6867
FT /evidence="ECO:0007829|PDB:7NH7"
FT HELIX 6876..6884
FT /evidence="ECO:0007829|PDB:7NH7"
FT STRAND 6890..6897
FT /evidence="ECO:0007829|PDB:7NH7"
FT STRAND 6902..6909
FT /evidence="ECO:0007829|PDB:7NH7"
FT HELIX 6911..6913
FT /evidence="ECO:0007829|PDB:7NH7"
FT STRAND 6920..6925
FT /evidence="ECO:0007829|PDB:7NH7"
FT STRAND 6936..6938
FT /evidence="ECO:0007829|PDB:7NH7"
FT HELIX 6945..6956
FT /evidence="ECO:0007829|PDB:7NH7"
FT STRAND 6957..6967
FT /evidence="ECO:0007829|PDB:7NH7"
FT STRAND 6969..6971
FT /evidence="ECO:0007829|PDB:7NH7"
FT HELIX 6974..6979
FT /evidence="ECO:0007829|PDB:7NH7"
FT HELIX 6980..6982
FT /evidence="ECO:0007829|PDB:7NH7"
FT STRAND 6983..6992
FT /evidence="ECO:0007829|PDB:7NH7"
FT TURN 6993..6996
FT /evidence="ECO:0007829|PDB:7NH7"
FT STRAND 7000..7007
FT /evidence="ECO:0007829|PDB:7NH7"
FT HELIX 7017..7029
FT /evidence="ECO:0007829|PDB:7NH7"
FT HELIX 7038..7041
FT /evidence="ECO:0007829|PDB:7NH7"
FT STRAND 7054..7056
FT /evidence="ECO:0007829|PDB:7NH7"
FT HELIX 7060..7062
FT /evidence="ECO:0007829|PDB:7NH7"
FT HELIX 7065..7071
FT /evidence="ECO:0007829|PDB:7NH7"
FT TURN 7072..7074
FT /evidence="ECO:0007829|PDB:7NH7"
FT STRAND 7076..7079
FT /evidence="ECO:0007829|PDB:7NH7"
SQ SEQUENCE 7095 AA; 797914 MW; 157CDEBD4CE45D4A CRC64;
MSKINKYGLE LHWAPEFPWM FEDAEEKLDN PSSSEVDMIC STTAQKLETD GICPENHVMV
DCRRLLKQEC CVQSSLIREI VMNASPYHLE VLLQDALQSR EAVLVTTPLG MSLEACYVRG
CNPKGWTMGL FRRRSVCNTG RCTVNKHVAY QLYMIDPAGV CLGAGQFVGW VIPLAFMPVQ
SRKFIVPWVM YLRKRGEKGA YNKDHGCGGF GHVYDFKVED AYDQVHDEPK GKFSKKAYAL
IRGYRGVKPL LYVDQYGCDY TGSLADGLEA YADKTLQEMK ALFPTWSQEL PFDVIVAWHV
VRDPRYVMRL QSAATICSVA YVANPTEDLC DGSVVIKEPV HVYADDSIIL RQYNLFDIMS
HFYMEADTVV NAFYGVALKD CGFVMQFGYI DCEQDSCDFK GWIPGNMIDG FACTTCGHVY
EVGDLIAQSS GVLPVNPVLH TKSAAGYGGF GCKDSFTLYG QTVVYFGGCV YWSPARNIWI
PILKSSVKSY DSLVYTGVLG CKAIVKETNL ICKALYLDYV QHKCGNLHQR ELLGVSDVWH
KQLLINRGVY KPLLENIDYF NMRRAKFSLE TFTVCADGFM PFLLDDLVPR AYYLAVSGQA
FCDYADKLCH AVVSKSKELL DVSLDSLGAA IHYLNSKIVD LAQHFSDFGT SFVSKIVHFF
KTFTTSTALA FAWVLFHVLH GAYIVVESDI YFVKNIPRYA SAVAQAFQSV AKVVLDSLRV
TFIDGLSCFK IGRRRICLSG RKIYEVERGL LHSSQLPLDV YDLTMPSQVQ KAKQKPIYLK
GSGSDFSLAD SVVEVVTTSL TPCGYSEPPK VADKICIVDN VYMAKAGDKY YPVVVDDHVG
LLDQAWRVPC AGRRVTFKEQ PTVKEIISMP KIIKVFYELD NDFNTILNTA CGVFEVDDTV
DMEEFYAVVI DAIEEKLSPC KELEGVGAKV SAFLQKLEDN PLFLFDEAGE EVFAPKLYCA
FTAPEDDDFL EESDVEEDDV EGEETDLTIT SAGQPCVASE QEESSEVLED TLDDGPSVET
SDSQVEEDVE MSDFVDLESV IQDYENVCFE FYTTEPEFVK VLGLYVPKAT RNNCWLRSVL
AVMQKLPCQF KDKNLQDLWV LYKQQYSQLF VDTLVNKIPA NIVLPQGGYV ADFAYWFLTL
CDWQCVAYWK CIKCDLALKL KGLDAMFFYG DVVSHICKCG ESMVLIDVDV PFTAHFALKD
KLFCAFITKR IVYKAACVVD VNDSHSMAVV DGKQIDDHRI TSITSDKFDF IIGHGMSFSM
TTFEIAQLYG SCITPNVCFV KGDIIKVSKL VKAEVVVNPA NGHMVHGGGV AKAIAVAAGQ
QFVKETTNMV KSKGVCATGD CYVSTGGKLC KTVLNVVGPD ARTQGKQSYV LLERVYKHFN
NYDCVVTTLI SAGIFSVPSD VSLTYLLGTA KKQVVLVSNN QEDFDLISKC QITAVEGTKK
LAARLSFNVG RSIVYETDAN KLILINDVAF VSTFNVLQDV LSLRHDIALD DDARTFVQSN
VDVLPEGWRV VNKFYQINGV RTVKYFECTG GIDICSQDKV FGYVQQGIFN KATVAQIKAL
FLDKVDILLT VDGVNFTNRF VPVGESFGKS LGNVFCDGVN VTKHKCDINY KGKVFFQFDN
LSSEDLKAVR SSFNFDQKEL LAYYNMLVNC FKWQVVVNGK YFTFKQANNN CFVNVSCLML
QSLHLTFKIV QWQEAWLEFR SGRPARFVAL VLAKGGFKFG DPADSRDFLR VVFSQVDLTG
AICDFEIACK CGVKQEQRTG LDAVMHFGTL SREDLEIGYT VDCSCGKKLI HCVRFDVPFL
ICSNTPASVK LPKGVGSANI FIGDNVGHYV HVKCEQSYQL YDASNVKKVT DVTGKLSDCL
YLKNLKQTFK SVLTTYYLDD VKKIEYKPDL SQYYCDGGKY YTQRIIKAQF KTFEKVDGVY
TNFKLIGHTV CDSLNSKLGF DSSKEFVEYK ITEWPTATGD VVLANDDLYV KRYERGCITF
GKPVIWLSHE KASLNSLTYF NRPLLVDDNK FDVLKVDDVD DSGDSSESGA KETKEINIIK
LSGVKKPFKV EDSVIVNDDT SETKYVKSLS IVDVYDMWLT GCKYVVRTAN ALSRAVNVPT
IRKFIKFGMT LVSIPIDLLN LREIKPAVNV VKAVRNKTSA CFNFIKWLFV LLFGWIKISA
DNKVIYTTEI ASKLTCKLVA LAFKNAFLTF KWSMVARGAC IIATIFLLWF NFIYANVIFS
DFYLPKIGFL PTFVGKIAQW IKNTFSLVTI CDLYSIQDVG FKNQYCNGSI ACQFCLAGFD
MLDNYKAIDV VQYEADRRAF VDYTGVLKIV IELIVSYALY TAWFYPLFAL ISIQILTTWL
PELFMLSTLH WSFRLLVALA NMLPAHVFMR FYIIIASFIK LFSLFKHVAY GCSKSGCLFC
YKRNRSLRVK CSTIVGGMIR YYDVMANGGT GFCSKHQWNC IDCDSYKPGN TFITVEAALD
LSKELKRPIQ PTDVAYHTVT DVKQVGCSMR LFYDRDGQRI YDDVNASLFV DYSNLLHSKV
KSVPNMHVVV VENDADKANF LNAAVFYAQS LFRPILMVDK NLITTANTGT SVTETMFDVY
VDTFLSMFDV DKKSLNALIA TAHSSIKQGT QIYKVLDTFL SCARKSCSID SDVDTKCLAD
SVMSAVSAGL ELTDESCNNL VPTYLKSDNI VAADLGVLIQ NSAKHVQGNV AKIAGVSCIW
SVDAFNQFSS DFQHKLKKAC CKTGLKLKLT YNKQMANVSV LTTPFSLKGG AVFSYFVYVC
FVLSLVCFIG LWCLMPTYTV HKSDFQLPVY ASYKVLDNGV IRDVSVEDVC FANKFEQFDQ
WYESTFGLSY YSNSMACPIV VAVIDQDFGS TVFNVPTKVL RYGYHVLHFI THALSADGVQ
CYTPHSQISY SNFYASGCVL SSACTMFTMA DGSPQPYCYT DGLMQNASLY SSLVPHVRYN
LANAKGFIRF PEVLREGLVR VVRTRSMSYC RVGLCEEADE GICFNFNGSW VLNNDYYRSL
PGTFCGRDVF DLIYQLFKGL AQPVDFLALT ASSIAGAILA VIVVLVFYYL IKLKRAFGDY
TSVVFVNVIV WCVNFMMLFV FQVYPTLSCV YAICYFYATL YFPSEISVIM HLQWLVMYGT
IMPLWFCLLY IAVVVSNHAF WVFSYCRKLG TSVRSDGTFE EMALTTFMIT KDSYCKLKNS
LSDVAFNRYL SLYNKYRYYS GKMDTAAYRE AACSQLAKAM DTFTNNNGSD VLYQPPTASV
STSFLQSGIV KMVNPTSKVE PCVVSVTYGN MTLNGLWLDD KVYCPRHVIC SASDMTNPDY
TNLLCRVTSS DFTVLFDRLS LTVMSYQMRG CMLVLTVTLQ NSRTPKYTFG VVKPGETFTV
LAAYNGKPQG AFHVTMRSSY TIKGSFLCGS CGSVGYVIMG DCVKFVYMHQ LELSTGCHTG
TDFNGDFYGP YKDAQVVQLP IQDYIQSVNF LAWLYAAILN NCNWFIQSDK CSVEDFNVWA
LSNGFSQVKS DLVIDALASM TGVSLETLLA AIKRLKNGFQ GRQIMGSCSF EDELTPSDVY
QQLAGIKLQS KRTRLFKGTV CWIMASTFLF SCIITAFVKW TMFMYVTTNM FSITFCALCV
ISLAMLLVKH KHLYLTMYIT PVLFTLLYNN YLVVYKHTFR GYVYAWLSYY VPSVEYTYTD
EVIYGMLLLV GMVFVTLRSI NHDLFSFIMF VGRLISVFSL WYKGSNLEEE ILLMLASLFG
TYTWTTVLSM AVAKVIAKWV AVNVLYFTDI PQIKIVLLCY LFIGYIISCY WGLFSLMNSL
FRMPLGVYNY KISVQELRYM NANGLRPPKN SFEALMLNFK LLGIGGVPII EVSQFQSKLT
DVKCANVVLL NCLQHLHVAS NSKLWHYCST LHNEILATSD LSVAFEKLAQ LLIVLFANPA
AVDSKCLTSI EEVCDDYAKD NTVLQALQSE FVNMASFVEY EVAKKNLDEA RFSGSANQQQ
LKQLEKACNI AKSAYERDRA VAKKLERMAD LALTNMYKEA RINDKKSKVV SALQTMLFSM
VRKLDNQALN SILDNAVKGC VPLNAIPSLA ANTLNIIVPD KSVYDQIVDN IYVTYAGNVW
QIQTIQDSDG TNKQLNEISD DCNWPLVIIA NRYNEVSATV LQNNELMPAK LKIQVVNSGP
DQTCNTPTQC YYNNSNNGKI VYAILSDVDG LKYTKILKDD GNFVVLELDP PCKFTVQDAK
GLKIKYLYFV KGCNTLARGW VVGTISSTVR LQAGTATEYA SNSSILSLCA FSVDPKKTYL
DFIQQGGTPI ANCVKMLCDH AGTGMAITVK PDATTSQDSY GGASVCIYCR ARVEHPDVDG
LCKLRGKFVQ VPVGIKDPVS YVLTHDVCRV CGFWRDGSCS CVSTDTTVQS KDTNFLNRVR
GASVDARLVP CASGLSTDVQ LRAFDIYNAS VAGIGLHLKV NCCRFQRVDE NGDKLDQFFV
VKRTDLTIYN REMKCYERVK DCKFVAEHDF FTFDVEGSRV PHIVRKDLTK YTMLDLCYAL
RHFDRNDCML LCDILSIYAG CEQSYFTKKD WYDFVENPDI INVYKKLGPI FNRALVSATE
FADKLVEVGL VGVLTLDNQD LNGKWYDFGD YVIAAPGCGV AIADSYYSYI MPMLTMCHAL
DCELYVNNAY RLFDLVQYDF TDYKLELFNK YFKHWSMPYH PNTVDCQDDR CIIHCANFNI
LFSMVLPNTC FGPLVRQIFV DGVPFVVSIG YHYKELGIVM NMDVDTHRYR LSLKDLLLYA
ADPALHVASA SALYDLRTCC FSVAAITSGV KFQTVKPGNF NQDFYDFVLS KGLLKEGSSV
DLKHFFFTQD GNAAITDYNY YKYNLPTMVD IKQLLFVLEV VYKYFEIYDG GCIPASQVIV
NNYDKSAGYP FNKFGKARLY YEALSFEEQD EIYAYTKRNV LPTLTQMNLK YAISAKNRAR
TVAGVSILST MTGRMFHQKC LKSIAATRGV PVVIGTTKFY GGWDDMLRRL IKDVDNPVLM
GWDYPKCDRA MPNILRIVSS LVLARKHETC CSQSDRFYRL ANECAQVLSE IVMCGGCYYV
KPGGTSSGDA TTAFANSVFN ICQAVSANVC ALMSCNGNKI EDLSIRALQK RLYSHVYRSD
KVDSTFVTEY YEFLNKHFSM MILSDDGVVC YNSDYASKGY IANISAFQQV LYYQNNVFMS
ESKCWVEHDI NNGPHEFCSQ HTMLVKMDGD DVYLPYPNPS RILGAGCFVD DLLKTDSVLL
IERFVSLAID AYPLVYHENE EYQKVFRVYL AYIKKLYNDL GNQILDSYSV ILSTCDGQKF
TDESFYKNMY LRSAVMQSVG ACVVCSSQTS LRCGSCIRKP LLCCKCCYDH VMATDHKYVL
SVSPYVCNAP GCDVNDVTKL YLGGMSYYCE DHKPQYSFKL VMNGLVFGLY KQSCTGSPYI
DDFNRIASCK WTDVDDYILA NECTERLKLF AAETQKATEE AFKQSYASAT IQEIVSEREL
ILSWEIGKVK PPLNKNYVFT GYHFTKNGKT VLGEYVFDKS ELTNGVYYRA TTTYKLSVGD
VFVLTSHSVA NLSAPTLVPQ ENYSSIRFAS VYSVLETFQN NVVNYQHIGM KRYCTVQGPP
GTGKSHLAIG LAVFYCTARV VYTAASHAAV DALCEKAYKF LNINDCTRIV PAKVRVECYD
KFKINDTTRK YVFTTINALP EMVTDIVVVD EVSMLTNYEL SVINARIRAK HYVYIGDPAQ
LPAPRVLLSK GTLEPKYFNT VTKLMCCLGP DIFLGTCYRC PKEIVDTVSA LVYENKLKAK
NESSLLCFKV YYKGVTTHES SSAVNMQQIY LINKFLKANP LWHKAVFISP YNSQNFAAKR
VLGLQTQTVD SAQGSEYDYV IYSQTAETAH SVNVNRFNVA ITRAKKGILC VMSNMQLFEA
LQFTTLTLDK VPQAVETKVQ CSTNLFKDCS KSYSGYHPAH APSFLAVDDK YKATGDLAVC
LGIGDSAVTY SRLISLMGFK LDVTLDGYCK LFITKEEAVK RVRAWVGFDA EGAHATLDSI
GTNFPLQLGF STGIDFVVEA TGLFADRDGY SFKKAVAKAP PGEQFKHLIP LMTRGHRWDV
VRPRIVQMFA DHLIDLSDCV VLVTWAANFE LTCLRYFAKV GREISCNVCT KRATVYNSRT
GYYGCWRHSV TCDYLYNPLI VDIQQWGYIG SLSSNHDLYC SVHKGAHVAS SDAIMTRCLA
VYDCFCNNIN WNVEYPIISN ELSINTSCRV LQRVILKAAM LCNRYTLCYD IGNPKGIACV
KDFDFKFYDA QPIVKSVKTL LYSFEAHKDS FKDGLCMFWN CNVDKYPPNA VVCRFDTRVL
NNLNLPGCNG GSLYVNKHAF HTKPFARAAF EHLKPMPFFY YSDTPCVYMD GMDAKQVDYV
PLKSATCITR CNLGGAVCLK HAEEYREYLE SYNTATTAGF TFWVYKTFDF YNLWNTFTKL
QSLENVVYNL VKTGHYTGQA GEMPCAIIND KVVTKIDKED VVIFINNTTY PTNVAVELFA
KRSVRHHPEL KLFRNLNIDV CWKHVIWDYA RESIFCSNTY GVCMYTDLKF IDKLNVLFDG
RDNGAFEAFK RSNNGVYIST TKVKSLSMIR GPPRAELNGV VVDKVGDTDC VFYFAVRKEG
QDVIFSQFDS LGVSSNQSPQ GNLGSNGKPG NVGGNDALSI STIFTQSRVI SSFTCRTDME
KDFIALDQDV FIQKYGLEDY AFEHIVYGNF NQKIIGGLHL LIGLYRRQQT SNLVVQEFVS
YDSSIHSYFI TDEKSGGSKS VCTVIDILLD DFVTLVKSLN LNCVSKVVNV NVDFKDFQFM
LWCNDEKVMT FYPRLQAASD WKPGYSMPVL YKYLNSPMER VSLWNYGKPV TLPTGCMMNV
AKYTQLCQYL NTTTLAVPVN MRVLHLGAGS EKGVAPGSAV LRQWLPAGTI LVDNDLYPFV
SDSVATYFGD CITLPFDCQW DLIISDMYDP ITKNIGEYNV SKDGFFTYIC HMIRDKLALG
GSVAIKITEF SWNAELYKLM GYFAFWTVFC TNANASSSEG FLIGINYLCK PKVEIDGNVM
HANYLFWRNS TVWNGGAYSL FDMAKFPLKL AGTAVINLRA DQINDMVYSL LEKGKLLIRD
TNKEVFVGDS LVNVI
