R1AB_IBVM
ID R1AB_IBVM Reviewed; 6631 AA.
AC P0C6Y3; Q0GNB9; Q0GNC0; Q5I5Y0; Q5I5Y1;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Replicase polyprotein 1ab;
DE Short=pp1ab;
DE AltName: Full=ORF1ab polyprotein;
DE Contains:
DE RecName: Full=Non-structural protein 2;
DE Short=nsp2;
DE AltName: Full=p87;
DE Contains:
DE RecName: Full=Papain-like protease;
DE Short=PL-PRO;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:P0C6X7};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:P0C6X7};
DE AltName: Full=Non-structural protein 3;
DE Short=nsp3;
DE AltName: Full=p195;
DE Contains:
DE RecName: Full=Non-structural protein 4;
DE Short=nsp4;
DE AltName: Full=Peptide HD2;
DE AltName: Full=p41;
DE Contains:
DE RecName: Full=3C-like proteinase;
DE Short=3CL-PRO;
DE Short=3CLp;
DE EC=3.4.22.- {ECO:0000250|UniProtKB:P0C6X7};
DE AltName: Full=Main protease;
DE Short=Mpro;
DE AltName: Full=Non-structural protein 5;
DE Short=nsp5;
DE AltName: Full=p33;
DE Contains:
DE RecName: Full=Non-structural protein 6;
DE Short=nsp6;
DE AltName: Full=p34;
DE Contains:
DE RecName: Full=Non-structural protein 7;
DE Short=nsp7;
DE AltName: Full=p9;
DE Contains:
DE RecName: Full=Non-structural protein 8;
DE Short=nsp8;
DE AltName: Full=p24;
DE Contains:
DE RecName: Full=Non-structural protein 9;
DE Short=nsp9;
DE AltName: Full=p10;
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=p16;
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 {ECO:0000250|UniProtKB:P0C6X7};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P0C6X7};
DE AltName: Full=nsp13;
DE AltName: Full=p68;
DE Contains:
DE RecName: Full=Proofreading exoribonuclease {ECO:0000250|UniProtKB:P0C6X7};
DE Short=ExoN;
DE EC=2.1.1.-;
DE EC=3.1.13.-;
DE AltName: Full=Guanine-N7 methyltransferase {ECO:0000250|UniProtKB:P0C6X7};
DE AltName: Full=Non-structural protein 14;
DE Short=nsp14;
DE AltName: Full=p58;
DE Contains:
DE RecName: Full=Uridylate-specific endoribonuclease;
DE EC=4.6.1.- {ECO:0000250|UniProtKB:P0C6X7};
DE AltName: Full=NendoU;
DE AltName: Full=Non-structural protein 15;
DE Short=nsp15;
DE AltName: Full=p39;
DE Contains:
DE RecName: Full=2'-O-methyl transferase;
DE EC=2.1.1.57;
DE AltName: Full=Non-structural protein 16;
DE Short=nsp16;
DE AltName: Full=p35;
GN Name=rep; ORFNames=1a-1b;
OS Avian infectious bronchitis virus (strain M41) (IBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Gammacoronavirus; Igacovirus.
OX NCBI_TaxID=11127;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Mondal S.P., Buckles E.L.;
RT "Avian infectious bronchitis virus strain M41.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16934878; DOI=10.1016/j.jviromet.2006.07.018;
RA Callison S.A., Hilt D.A., Boynton T.O., Sample B.F., Robison R.,
RA Swayne D.E., Jackwood M.W.;
RT "Development and evaluation of a real-time Taqman RT-PCR assay for the
RT detection of infectious bronchitis virus from infected chickens.";
RL J. Virol. Methods 138:60-65(2006).
RN [3]
RP SUBCELLULAR LOCATION (PAPAIN-LIKE PROTEASE), SUBCELLULAR LOCATION
RP (NON-STRUCTURAL PROTEIN 4), AND SUBCELLULAR LOCATION (NON-STRUCTURAL
RP PROTEIN 6).
RX PubMed=30200673; DOI=10.3390/v10090477;
RA Doyle N., Neuman B.W., Simpson J., Hawes P.C., Mantell J., Verkade P.,
RA Alrashedi H., Maier H.J.;
RT "Infectious Bronchitis Virus Nonstructural Protein 4 Alone Induces Membrane
RT Pairing.";
RL Viruses 10:0-0(2018).
RN [4] {ECO:0007744|PDB:2Q6D}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 2782-3088, AND SUBUNIT (3C-LIKE
RP PROTEINASE).
RX PubMed=18094151; DOI=10.1128/jvi.02114-07;
RA Xue X., Yu H., Yang H., Xue F., Wu Z., Shen W., Li J., Zhou Z., Ding Y.,
RA Zhao Q., Zhang X.C., Liao M., Bartlam M., Rao Z.;
RT "Structures of two coronavirus main proteases: implications for substrate
RT binding and antiviral drug design.";
RL J. Virol. 82:2515-2527(2008).
RN [5] {ECO:0007744|PDB:5C94}
RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 3675-3785, SUBUNIT
RP (NON-STRUCTURAL PROTEIN 9), MUTAGENESIS OF PHE-3747; ILE-3769 AND GLY-3772,
RP AND FUNCTION (NON-STRUCTURAL PROTEIN 9).
RX PubMed=28257598; DOI=10.1002/pro.3150;
RA Hu T., Chen C., Li H., Dou Y., Zhou M., Lu D., Zong Q., Li Y., Yang C.,
RA Zhong Z., Singh N., Hu H., Zhang R., Yang H., Su D.;
RT "Structural basis for dimerization and RNA binding of avian infectious
RT bronchitis virus nsp9.";
RL Protein Sci. 26:1037-1048(2017).
CC -!- FUNCTION: [Isoform Replicase polyprotein 1ab]: Multifunctional protein
CC involved in the transcription and replication of viral RNAs. Contains
CC the proteinases responsible for the cleavages of the polyprotein.
CC {ECO:0000305}.
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 (By similarity). Indeed, these two proteins play a role in
CC maintaining the functional integrity of the mitochondria and protecting
CC cells from various stresses (By similarity).
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Papain-like protease]: Responsible for the cleavages located
CC at the N-terminus of the replicase polyprotein (By similarity). In
CC addition, PL-PRO possesses a deubiquitinating/deISGylating activity and
CC processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from
CC cellular substrates (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 4]: Plays a role in host membrane
CC rearrangement that leads to creation of cytoplasmic double-membrane
CC vesicles (DMV) necessary for viral replication (PubMed:30200673). Alone
CC is able to induce paired membranes (PubMed:30200673). Coexpression of
CC nsp3 and nsp4 does not result in the formation of DMVs
CC (PubMed:30200673). {ECO:0000269|PubMed:30200673}.
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. {ECO:0000255|PROSITE-ProRule:PRU00772}.
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]: Plays an essential role in viral
CC replication by forming a homodimer that binds single-stranded RNA.
CC {ECO:0000269|PubMed:28257598}.
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 (By similarity). Therefore plays an
CC essential role in viral mRNAs cap methylation (By similarity).
CC {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: [Proofreading exoribonuclease]: 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 (By similarity). Acts as a proofreading exoribonuclease for
CC RNA replication, thereby lowering The sensitivity of the virus to RNA
CC mutagens (By similarity). {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 (By similarity). Catalyzes a two-step reaction in which a 2'3'-cyclic
CC phosphate (2'3'-cP) is first generated by 2'-O transesterification,
CC which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If
CC not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and
CC activate host dsRNA sensors (By similarity).
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [2'-O-methyl transferase]: 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: [Papain-like protease]:
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; Evidence={ECO:0000250|UniProtKB:P0C6Y1};
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 Evidence={ECO:0000250|UniProtKB:P0C6X7};
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 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 -!- CATALYTIC ACTIVITY: [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 -!- 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 -!- COFACTOR: [Papain-like protease]:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC -!- SUBUNIT: [Non-structural protein 2]: Interacts with host PHB and PHB2.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [Non-structural protein 4]: Interacts with papain-like
CC protease and non-structural protein 6. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [3C-like proteinase]: Monomer (PubMed:18094151). Homodimer
CC (PubMed:18094151). Only the homodimer shows catalytic activity (By
CC similarity). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:18094151}.
CC -!- SUBUNIT: [Non-structural protein 7]: Eight copies of nsp7 and eight
CC copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling
CC ring structure. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [Non-structural protein 8]: Eight copies of nsp7 and eight
CC copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling
CC ring structure (By similarity). Interacts with ORF6 protein (By
CC similarity). {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [Non-structural protein 9]: Homodimer.
CC {ECO:0000269|PubMed:28257598}.
CC -!- SUBUNIT: [Non-structural protein 10]: Homododecamer (By similarity).
CC Interacts with proofreading exoribonuclease nsp14 and 2'-O-
CC methyltransferase nsp16; these interactions enhance nsp14 and nsp16
CC enzymatic activities (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [Proofreading exoribonuclease]: Interacts with host DDX1 (via
CC C-terminus) (By similarity). Interacts with non-structural protein 10
CC (By similarity). {ECO:0000250|UniProtKB:P0C6Y1}.
CC -!- SUBUNIT: [Uridylate-specific endoribonuclease]: Homohexamer.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [2'-O-methyl transferase]: Interacts with non-structural
CC protein 10. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBCELLULAR LOCATION: [Papain-like protease]: Host endoplasmic
CC reticulum membrane {ECO:0000305|PubMed:30200673}; Multi-pass membrane
CC protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}.
CC Note=Gammacoronaviruses induce membrane zippering to form zippered
CC endoplasmic reticulum (zER). {ECO:0000305|PubMed:30200673}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host endoplasmic
CC reticulum membrane {ECO:0000305|PubMed:30200673}; Multi-pass membrane
CC protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}.
CC Note=Gammacoronaviruses induce membrane zippering to form zippered
CC endoplasmic reticulum (zER). {ECO:0000305|PubMed:30200673}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 6]: Host endoplasmic
CC reticulum membrane {ECO:0000305|PubMed:30200673}; Multi-pass membrane
CC protein {ECO:0000305}. Note=Gammacoronaviruses induce membrane
CC zippering to form zippered endoplasmic reticulum (zER).
CC {ECO:0000305|PubMed:30200673}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host
CC perinuclear region {ECO:0000250|UniProtKB:P0C6X7}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 9]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes.
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.
CC -!- SUBCELLULAR LOCATION: [Proofreading exoribonuclease]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}.
CC -!- SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease]: Host
CC cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=Isoform Replicase polyprotein 1ab is produced by -1 ribosomal
CC frameshifting at the 1a-1b genes boundary. Isoform Replicase
CC polyprotein 1a is produced by conventional translation.
CC {ECO:0000305};
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=P0C6Y3-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6V5-1; Sequence=External;
CC -!- DOMAIN: [Papain-like protease]: The hydrophobic region HD1 probably
CC mediates the membrane association of the replication complex.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- DOMAIN: [Non-structural protein 4]: The hydrophobic region HD2 probably
CC mediates the membrane association of the replication complex.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- DOMAIN: [Non-structural protein 6]: The hydrophobic region HD3 probably
CC mediates the membrane association of the replication complex.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- PTM: [Isoform Replicase polyprotein 1ab]: Specific enzymatic cleavages
CC in vivo by its own proteases yield mature proteins (By similarity). 3C-
CC like proteinase nsp5 liberates nsps 6-16 from the polyprotein (By
CC similarity). Papain-like and 3C-like proteinases are autocatalytically
CC processed. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- PTM: [Non-structural protein 4]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P0C6Y1}.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW33784.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAW33785.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABI26421.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABI26422.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ834384; ABI26421.1; ALT_SEQ; Genomic_RNA.
DR EMBL; DQ834384; ABI26422.1; ALT_SEQ; Genomic_RNA.
DR EMBL; AY851295; AAW33784.1; ALT_SEQ; Genomic_RNA.
DR EMBL; AY851295; AAW33785.1; ALT_SEQ; Genomic_RNA.
DR PDB; 2Q6D; X-ray; 2.35 A; A/B/C=2783-3088.
DR PDB; 2Q6F; X-ray; 2.00 A; A/B=2783-3088.
DR PDB; 5C94; X-ray; 2.44 A; A=3675-3785.
DR PDB; 7F52; X-ray; 2.56 A; A/B=1-673.
DR PDBsum; 2Q6D; -.
DR PDBsum; 2Q6F; -.
DR PDBsum; 5C94; -.
DR PDBsum; 7F52; -.
DR SMR; P0C6Y3; -.
DR MEROPS; C30.002; -.
DR SABIO-RK; P0C6Y3; -.
DR EvolutionaryTrace; P0C6Y3; -.
DR Proteomes; UP000007642; Genome.
DR Proteomes; UP000096468; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; 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: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: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:0006508; P:proteolysis; 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; cd20762; capping_2-OMTase_Nidovirales; 1.
DR CDD; cd21512; cv_gamma-delta_Nsp2_IBV-like; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21559; gammaCoV-Nsp6; 1.
DR CDD; cd21658; gammaCoV_Nsp14; 1.
DR CDD; cd21667; gammaCoV_Nsp5_Mpro; 1.
DR CDD; cd21587; gammaCoV_RdRp; 1.
DR CDD; cd21168; M_gcv_Nsp15-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR CDD; cd21170; NTD_cv_Nsp15-like; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1.
DR CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR Gene3D; 1.10.150.420; -; 1.
DR Gene3D; 1.10.1840.10; -; 1.
DR Gene3D; 1.10.8.1190; -; 1.
DR Gene3D; 1.10.8.370; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.40.10.250; -; 1.
DR Gene3D; 2.60.120.1680; -; 1.
DR Gene3D; 3.30.160.820; -; 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; 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; IPR009466; NSP14_CoV.
DR InterPro; IPR044316; NSP14_gammaCoV.
DR InterPro; IPR044328; NSP15_gammaCoV_N.
DR InterPro; IPR044325; NSP15_M_gammaCoV.
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; IPR040795; NSP2_gammaCoV.
DR InterPro; IPR044383; NSP2_IBV-like.
DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR044308; NSP5_Mpro_GammaCoV.
DR InterPro; IPR043610; NSP6_CoV.
DR InterPro; IPR044368; NSP6_gammaCoV.
DR InterPro; IPR014828; NSP7_CoV.
DR InterPro; IPR037204; NSP7_sf_CoV.
DR InterPro; IPR014829; NSP8_CoV.
DR InterPro; IPR037230; NSP8_sf_CoV.
DR InterPro; IPR014822; NSP9_CoV.
DR InterPro; IPR036499; NSP9_sf_CoV.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013016; Peptidase_C16_CoV.
DR InterPro; IPR008740; Peptidase_C30_CoV.
DR InterPro; IPR043477; Peptidase_C30_dom3_CoV.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043503; PLpro_palm_finger_dom_CoV.
DR InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR InterPro; IPR044358; RdRp_gammaCoV.
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; 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; PF19218; CoV_NSP3_C; 1.
DR Pfam; PF16348; CoV_NSP4_C; 1.
DR Pfam; PF19217; CoV_NSP4_N; 1.
DR Pfam; PF19213; CoV_NSP6; 1.
DR Pfam; PF08716; CoV_NSP7; 1.
DR Pfam; PF08717; CoV_NSP8; 1.
DR Pfam; PF08710; CoV_NSP9; 1.
DR Pfam; PF08715; CoV_peptidase; 1.
DR Pfam; PF06478; CoV_RPol_N; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF17896; NSP2_gammaCoV; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF101816; SSF101816; 1.
DR SUPFAM; SSF140367; SSF140367; 1.
DR SUPFAM; SSF142877; SSF142877; 1.
DR SUPFAM; SSF143076; SSF143076; 1.
DR SUPFAM; SSF144246; SSF144246; 1.
DR SUPFAM; 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; PS51952; COV_EXON_MTASE_COACT; 1.
DR PROSITE; PS51954; COV_N7_MTASE; 1.
DR PROSITE; PS51948; COV_NSP12_RDRP; 1.
DR PROSITE; PS51960; COV_NSP15_NTD; 1.
DR PROSITE; PS51992; COV_NSP3_Y3; 1.
DR PROSITE; PS51943; COV_NSP3A_UBL; 1.
DR PROSITE; PS51944; COV_NSP3D_UBL; 1.
DR PROSITE; PS51946; COV_NSP4C; 1.
DR PROSITE; PS51949; COV_NSP7; 1.
DR PROSITE; PS51950; COV_NSP8; 1.
DR PROSITE; PS51951; COV_NSP9_SSRNA_BD; 1.
DR PROSITE; PS51653; CV_ZBD; 1.
DR PROSITE; PS51442; M_PRO; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51958; NENDOU; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS51955; NIV_2_O_MTASE; 1.
DR PROSITE; PS51953; NIV_EXON; 1.
DR PROSITE; PS51124; PEPTIDASE_C16; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Endonuclease; Exonuclease; Helicase; Host cytoplasm;
KW Host endoplasmic reticulum; Host membrane; Host-virus interaction;
KW Hydrolase; Lyase; Membrane; Metal-binding; Methyltransferase; Nuclease;
KW Nucleotide-binding; Nucleotidyltransferase; Protease; Repeat;
KW Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
KW Thiol protease; Transferase; Transmembrane; Transmembrane helix;
KW Viral RNA replication; Zinc; Zinc-finger.
FT CHAIN 1..673
FT /note="Non-structural protein 2"
FT /id="PRO_0000283889"
FT CHAIN 674..2267
FT /note="Papain-like protease"
FT /id="PRO_0000283890"
FT CHAIN 2268..2781
FT /note="Non-structural protein 4"
FT /id="PRO_0000283891"
FT CHAIN 2782..3088
FT /note="3C-like proteinase"
FT /id="PRO_0000283892"
FT CHAIN 3089..3381
FT /note="Non-structural protein 6"
FT /id="PRO_0000283893"
FT CHAIN 3382..3464
FT /note="Non-structural protein 7"
FT /id="PRO_0000283894"
FT CHAIN 3465..3674
FT /note="Non-structural protein 8"
FT /id="PRO_0000283895"
FT CHAIN 3675..3785
FT /note="Non-structural protein 9"
FT /id="PRO_0000283896"
FT CHAIN 3786..3930
FT /note="Non-structural protein 10"
FT /id="PRO_0000283897"
FT CHAIN 3931..4870
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000283898"
FT CHAIN 4871..5470
FT /note="Helicase"
FT /id="PRO_0000283899"
FT CHAIN 5471..5991
FT /note="Proofreading exoribonuclease"
FT /id="PRO_0000283900"
FT CHAIN 5992..6329
FT /note="Uridylate-specific endoribonuclease"
FT /id="PRO_0000283901"
FT CHAIN 6330..6631
FT /note="2'-O-methyl transferase"
FT /id="PRO_0000283902"
FT TOPO_DOM 1..1752
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 1753..1773
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1774..1845
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 1846..1866
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1867..2282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 2283..2303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2304..2561
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 2562..2582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2583..2613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 2614..2634
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2635..2645
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 2646..2666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2667..3098
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 3099..3119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3120..3123
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 3124..3144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3145..3153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 3154..3174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3175..3190
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 3191..3211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3212..3259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 3260..3280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3281..3298
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 3299..3319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3320..6631
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT DOMAIN 675..780
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1005..1181
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1177..1229
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1238..1499
FT /note="Peptidase C16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 2163..2265
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 2686..2781
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 2782..3088
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3382..3464
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3465..3674
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 3675..3785
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 3787..3928
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT DOMAIN 3942..4200
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 4304..4870
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT DOMAIN 4550..4712
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 4871..4954
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT DOMAIN 5127..5307
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 5308..5479
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 5541..5755
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 5764..5991
FT /note="N7-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT DOMAIN 5992..6052
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT DOMAIN 6053..6168
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 6185..6326
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6329..6628
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ZN_FING 1355..1392
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 3860..3880
FT /evidence="ECO:0000250"
FT ZN_FING 3906..3919
FT /evidence="ECO:0000250"
FT REGION 1753..1866
FT /note="HD1"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT REGION 2283..2666
FT /note="HD2"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT REGION 3099..3319
FT /note="HD3"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT REGION 5879..5893
FT /note="GpppA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT ACT_SITE 1276
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1439
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1450
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000250|UniProtKB:P0C6Y1"
FT ACT_SITE 2822
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 2924
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 4697
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 4698
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 4699
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5559
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5561
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5660
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5736
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5741
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6457
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6534
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 3860
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3863
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3869
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3880
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3906
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3909
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3917
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3919
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 4875
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4878
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4886
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4889
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4899
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4903
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4909
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4920
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4925
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4942
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4945
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5152..5159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 5676
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5678
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5694
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5697
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5725
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5729
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5732
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5747
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5799..5805
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 5917
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 5937
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 5948
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 5951
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT SITE 673..674
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 2267..2268
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 2781..2782
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 3088..3089
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 3381..3382
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 3464..3465
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 3674..3675
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 3785..3786
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 3930..3931
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 4870..4871
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 5470..5471
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 5991..5992
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 6329..6330
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT VARIANT 807
FT /note="L -> S"
FT VARIANT 1618
FT /note="S -> F"
FT VARIANT 1739
FT /note="S -> A"
FT VARIANT 2631
FT /note="M -> L"
FT VARIANT 2774
FT /note="S -> P"
FT VARIANT 4230
FT /note="D -> G"
FT VARIANT 4692
FT /note="S -> P"
FT VARIANT 4859
FT /note="Y -> C"
FT VARIANT 5104
FT /note="S -> P"
FT VARIANT 6033
FT /note="V -> A"
FT VARIANT 6080
FT /note="T -> M"
FT VARIANT 6314
FT /note="A -> T"
FT MUTAGEN 3747
FT /note="F->G: Loss of dimerization for Non-structural
FT protein 9."
FT /evidence="ECO:0000269|PubMed:28257598"
FT MUTAGEN 3769
FT /note="I->D: Loss of dimerization and nucleic acid binding
FT for Non-structural protein 9."
FT /evidence="ECO:0000269|PubMed:28257598"
FT MUTAGEN 3772
FT /note="G->D: Loss of dimerization and nucleic acid binding
FT for Non-structural protein 9."
FT /evidence="ECO:0000269|PubMed:28257598"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 42..57
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:7F52"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 162..174
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 182..197
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 337..344
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 347..354
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 363..371
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 377..390
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 394..403
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 412..415
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 432..439
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 455..467
FT /evidence="ECO:0007829|PDB:7F52"
FT TURN 469..474
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 478..491
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 497..505
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 511..519
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 526..530
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 553..561
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 562..565
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:7F52"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:7F52"
FT HELIX 2792..2795
FT /evidence="ECO:0007829|PDB:2Q6D"
FT STRAND 2798..2802
FT /evidence="ECO:0007829|PDB:2Q6D"
FT STRAND 2807..2813
FT /evidence="ECO:0007829|PDB:2Q6D"
FT STRAND 2816..2820
FT /evidence="ECO:0007829|PDB:2Q6D"
FT HELIX 2821..2824
FT /evidence="ECO:0007829|PDB:2Q6D"
FT TURN 2829..2831
FT /evidence="ECO:0007829|PDB:2Q6D"
FT HELIX 2832..2838
FT /evidence="ECO:0007829|PDB:2Q6D"
FT HELIX 2841..2843
FT /evidence="ECO:0007829|PDB:2Q6D"
FT STRAND 2845..2847
FT /evidence="ECO:0007829|PDB:2Q6D"
FT STRAND 2856..2862
FT /evidence="ECO:0007829|PDB:2Q6D"
FT STRAND 2865..2872
FT /evidence="ECO:0007829|PDB:2Q6D"
FT STRAND 2879..2882
FT /evidence="ECO:0007829|PDB:2Q6D"
FT STRAND 2890..2897
FT /evidence="ECO:0007829|PDB:2Q6D"
FT STRAND 2900..2908
FT /evidence="ECO:0007829|PDB:2Q6D"
FT STRAND 2927..2932
FT /evidence="ECO:0007829|PDB:2Q6D"
FT STRAND 2935..2945
FT /evidence="ECO:0007829|PDB:2Q6D"
FT STRAND 2950..2954
FT /evidence="ECO:0007829|PDB:2Q6D"
FT HELIX 2961..2963
FT /evidence="ECO:0007829|PDB:2Q6D"
FT STRAND 2966..2969
FT /evidence="ECO:0007829|PDB:2Q6D"
FT HELIX 2980..2993
FT /evidence="ECO:0007829|PDB:2Q6D"
FT HELIX 3012..3019
FT /evidence="ECO:0007829|PDB:2Q6D"
FT TURN 3020..3023
FT /evidence="ECO:0007829|PDB:2Q6D"
FT HELIX 3031..3039
FT /evidence="ECO:0007829|PDB:2Q6D"
FT HELIX 3044..3056
FT /evidence="ECO:0007829|PDB:2Q6D"
FT STRAND 3066..3068
FT /evidence="ECO:0007829|PDB:2Q6D"
FT HELIX 3075..3080
FT /evidence="ECO:0007829|PDB:2Q6D"
FT STRAND 3681..3693
FT /evidence="ECO:0007829|PDB:5C94"
FT HELIX 3694..3696
FT /evidence="ECO:0007829|PDB:5C94"
FT STRAND 3699..3708
FT /evidence="ECO:0007829|PDB:5C94"
FT STRAND 3711..3720
FT /evidence="ECO:0007829|PDB:5C94"
FT STRAND 3726..3730
FT /evidence="ECO:0007829|PDB:5C94"
FT STRAND 3736..3741
FT /evidence="ECO:0007829|PDB:5C94"
FT STRAND 3745..3751
FT /evidence="ECO:0007829|PDB:5C94"
FT STRAND 3754..3763
FT /evidence="ECO:0007829|PDB:5C94"
FT HELIX 3768..3778
FT /evidence="ECO:0007829|PDB:5C94"
FT HELIX 3779..3781
FT /evidence="ECO:0007829|PDB:5C94"
FT STRAND 3782..3784
FT /evidence="ECO:0007829|PDB:5C94"
SQ SEQUENCE 6631 AA; 744412 MW; CB222611D8C1B9E2 CRC64;
MASSLKQGVS PKLRDVILVS KDIPEQLCDA LFFYTSHNPK DYADAFAVRQ KFDRNLQTGK
QFKFETVCGL FLLKGVDKIT PGVPAKVLKA TSKLADLEDI FGVSPFARKY RELLKTACQW
SLTVETLDAR AQTLDEIFDP TEILWLQVAA KIQVSAMAMR RLVGEVTAKV MDALGSNMSA
LFQIFKQQIV RIFQKALAIF ENVSELPQRI AALKMAFAKC AKSITVVVME RTLVVREFAG
TCLASINGAV AKFFEELPNG FMGAKIFTTL AFFREAAVKI VDNIPNAPRG TKGFEVVGNA
KGTQVVVRGM RNDLTLLDQK AEIPVESEGW SAILGGHLCY VFKSGDRFYA APLSGNFALH
DVHCCERVVC LSDGVTPEIN DGLILAAIYS SFSVAELVAA IKRGEPFKFL GHKFVYAKDA
AVSFTLAKAA TIADVLKLFQ SARVKVEDVW SSLTEKSFEF WRLAYGKVRN LEEFVKTCFC
KAQMAIVILA TVLGEGIWHL VSQVIYKVGG LFTKVVDFCE KYWKGFCAQL KRAKLIVTET
LCVLKGVAQH CFQLLLDAIQ FMYKSFKKCA LGRIHGDLLF WKGGVHKIIQ EGDEIWFDAI
DSIDVEDLGV VQEKLIDFDV CDNVTLPENQ PGHMVQIEDD GKNYMFFRFK KDENIYYTPM
SQLGAINVVC KAGGKTVTFG ETTVQEIPPP DVVFIKVSIE CCGEPWNTIF KKAYKEPIEV
ETDLTVEQLL SVVYEKMCDD LKLFPEAPEP PPFENVTLVD KNGKDLDCIK SCHLIYRDYE
SDDDIEEEDA EECDTDSGDA EECDTNLECE EEDEDTKVLA LIQDPASNKY PLPLDDDYSV
YNGCIVHKDA LDVVNLPSGE ETFVVNNCFE GAVKALPQKV IDVLGDWGEA VDAQEQLCQQ
ESTRVISEKS VEGFTGSCDA MAEQAIVEEQ EIVPVVEQSQ DVVVFTPADL EVVKETAEEV
DEFILISAVP KEEVVSQEKE EPQVEQEPTL VVKAQREKKA KKFKVKPATC EKPKFLEYKT
CVGDLAVVIA KALDEFKEFC IVNAANEHMS HGGGVAKAIA DFCGPDFVEY CADYVKKHGP
QQKLVTPSFV KGIQCVNNVV GPRHGDSNLR EKLVAAYKSV LVGGVVNYVV PVLSSGIFGV
DFKISIDAMR EAFKGCAIRV LLFSLSQEHI DYFDATCKQK TIYLTEDGVK YRSVVLKPGD
SLGQFGQVFA RNKVVFSADD VEDKEILFIP TTDKTILEYY GLDAQKYVTY LQTLAQKWDV
QYRDNFVILE WRDGNCWISS AIVLLQAAKI RFKGFLAEAW AKLLGGDPTD FVAWCYASCN
AKVGDFSDAN WLLANLAEHF DADYTNALLK KCVSCNCGVK SYELRGLEAC IQPVRAPNLL
HFKTQYSNCP TCGASSTDEV IEASLPYLLL FATDGPATVD CDENAVGTVV FIGSTNSGHC
YTQADGKAFD NLAKDRKFGR KSPYITAMYT RFSLRSENPL LVVEHSKGKA KVVKEDVSNL
ATSSKASFDD LTDFEQWYDS NIYESLKVQE TPDNLDEYVS FTTKEDSKLP LTLKVRGIKS
VVDFRSKDGF TYKLTPDTDE NSKTPVYYPV LDSISLRAIW VEGSANFVVG HPNYYSKSLR
IPTFWENAES FVKMGYKIDG VTMGLWRAEH LNKPNLERIF NIAKKAIVGS SVVTTQCGKI
LVKAATYVAD KVGDGVVRNI TDRIKGLCGF TRGHFEKKMS LQFLKTLVFF FFYFLKASSK
SLVSSYKIVL CKVVFATLLI VWFIYTSNPV VFTGIRVLDF LFEGSLCGPY NDYGKDSFDV
LRYCAGDFTC RVCLHDRDSL HLYKHAYSVE QIYKDAASGI NFNWNWLYLV FLILFVKPVA
GFVIICYCVK YLVLSSTVLQ TGVGFLDWFV KTVFTHFNFM GAGFYFWLFY KIYVQVHHIL
YCKDVTCEVC KRVARSNRQE VSVVVGGRKQ IVHVYTNSGY NFCKRHNWYC RNCDDYGHQN
TFMSPEVAGE LSEKLKRHVK PTAYAYHVVY EACVVDDFVN LKYKAAIPGK DNASSAVKCF
SVTDFLKKAV FLKEALKCEQ ISNDGFIVCN TQSAHALEEA KNAAVYYAQY LCKPILILDQ
ALYEQLIVEP VSKSVIDKVC SILSNIISVD TAALNYKAGT LRDALLSITK DEEAVDMAIF
CHNHEVEYTG DGFTNVIPSY GMDTDKLTPR DRGFLINADA SIANLRVKNA PPVVWKFSDL
IKLSDSCLKY LISATVKSGG RFFITKSGAK QVISCHTQKL LVEKKAGGVI NNTFKWFMSC
FKWLFVFYIL FTACCLGYYY MEMNKSFVHP MYDVNSTLHV EGFKVIDKGV IREIVSEDNC
FSNKFVNFDA FWGKSYENNK NCPIVTVVID GDGTVAVGVP GFVSWVMDGV MFVHMTQTDR
RPWYIPTWFN REIVGYTQDS IITEGSFYTS IALFSARCLY LTASNTPQLY CFNGDNDAPG
ALPFGSIIPH RVYFQPNGVR LIVPQQILHT PYIVKFVSDS YCRGSVCEYT KPGYCVSLDS
QWVLFNDEYI SKPGVFCGST VRELMFNMVS TFFTGVNPNI YIQLATMFLI LVVIVLIFAM
VIKFQGVFKA YATIVFTIML VWVINAFVLC VHSYNSVLAV ILLVLYCYAS MVTSRNTAII
MHCWLVFTFG LIVPTWLACC YLGFILYMYT PLVFWCYGTT KNTRKLYDGN EFVGNYDLAA
KSTFVIRGTE FVKLTNEIGD KFEAYLSAYA RLKYYSGTGS EQDYLQACRA WLAYALDQYR
NSGVEVVYTP PRYSIGVSRL QAGFKKLVSP SSAVEKCIVS VSYRGNNLNG LWLGDSIYCP
RHVLGKFSGD QWGDVLNLAN NHEFEVVTQN GVTLNVVSRR LKGAVLILQT AVANAETPKY
KFVKANCGDS FTIACSYGGT VIGLYPVTMR SNGTIRASFL AGACGSVGFN IEKGVVNFFY
MHHLELPNAL HTGTDLMGEF YGGYVDEEVA QRVPPDNLVT NNIVAWLYAA IISVKESSFS
QPKWLESTTV SIEDYNRWAS DNGFTPFSTS TAITKLSAIT GVDVCKLLRT IMVKSAQWGS
DPILGQYNFE DELTPESVFN QVGGVRLQSS FVRKATSWFW SRCVLACFLF VLCAIVLFTA
VPLKFYVHAA VILLMAVLFI SFTVKHVMAY MDTFLLPTLI TVIIGVCAEV PFIYNTLISQ
VVIFLSQWYD PVVFDTMVPW MLLPLVLYTA FKCVQGCYMN SFNTSLLMLY QFMKLGFVIY
TSSNTLTAYT EGNWELFFEL VHTIVLANVS SNSLIGLIVF KCAKWMLYYC NATYFNNYVL
MAVMVNGIGW LCTCYFGLYW WVNKVFGLTL GKYNFKVSVD QYRYMCLHKV NPPKTVWEVF
TTNILIQGIG GDRVLPIATV QSKLSDVKCT TVVLMQLLTK LNVEANSKMH AYLVELHNKI
LASDDVGECM DNLLGMLITL FCIDSTIDLG EYCDDILKRS TVLQSVTQEF SHIPSYAEYE
RAKSIYEKVL ADSKNGGVTQ QELAAYRKAA NIAKSVFDRD LAVQKKLDSM AERAMTTMYK
EARVTDRRAK LVSSLHALLF SMLKKIDSEK LNVLFDQANS GVVPLATVPI VCSNKLTLVI
PDPETWVKCV EGVHVTYSTV VWNIDCVTDA DGTELHPTST GSGLTYCISG DNIAWPLKVN
LTRNGHNKVD VALQNNELMP HGVKTKACVA GVDQAHCSVE SKCYYTSISG SSVVAAITSS
NPNLKVASFL NEAGNQIYVD LDPPCKFGMK VGDKVEVVYL YFIKNTRSIV RGMVLGAISN
VVVLQSKGHE TEEVDAVGIL SLCSFAVDPA DTYCKYVAAG NQPLGNCVKM LTVHNGSGFA
ITSKPSPTPD QDSYGGASVC LYCRAHIAHP GGAGNLDGRC QFKGSFVQIP TTEKDPVGFC
LRNKVCTVCQ CWIGYGCQCD SLRQPKPSVQ SVAVASGFDK NYLNRVRGSS EARLIPLANG
CDPDVVKRAF DVCNKESAGM FQNLKRNCAR FQEVRDTEDG NLEYCDSYFV VKQTTPSNYE
HEKACYEDLK SEVTADHDFF VFNKNIYNIS RQRLTKYTMM DFCYALRHFD PKDCEVLKEI
LVTYGCIEDY HPKWFEENKD WYDPIENPKY YAMLAKMGPI VRRALLNAIE FGNLMVEKGY
VGVITLDNQD LNGKFYDFGD FQKTAPGAGV PVFDTYYSYM MPIIAMTDAL APERYFEYDV
HKGYKSYDLL KYDYTEEKQD LFQKYFKYWD QEYHPNCRDC SDDRCLIHCA NFNILFSTLV
PQTSFGNLCR KVFVDGVPFI ATCGYHSKEL GVIMNQDNTM SFSKMGLSQL MQFVGDPALL
VGTSNKLVDL RTSCFSVCAL ASGITHQTVK PGHFNKDFYD FAEKAGMFKE GSSIPLKHFF
YPQTGNAAIN DYDYYRYNRP TMFDIRQLLF CLEVTSKYFE CYEGGCIPAS QVVVNNLDKS
AGYPFNKFGK ARLYYEMSLE EQDQLFESTK KNVLPTITQM NLKYAISAKN RARTVAGVSI
LSTMTNRQFH QKILKSIVNT RNAPVVIGTT KFYGGWDNML RNLIQGVEDP ILMGWDYPKC
DRAMPNLLRI AASLVLARKH TNCCTWSERV YRLYNECAQV LSETVLATGG IYVKPGGTSS
GDATTAYANS VFNIIQATSA NVARLLSVIT RDIVYDDIKS LQYELYQQVY RRVNFDPAFV
EKFYSYLCKN FSLMILSDDG VVCYNNTLAK QGLVADISGF REVLYYQNNV FMADSKCWVE
PDLEKGPHEF CSQHTMLVEV DGEPRYLPYP DPSRILCACV FVDDLDKTES VAVMERYIAL
AIDAYPLVHH ENEEYKKVFF VLLSYIRKLY QELSQNMLMD YSFVMDIDKG SKFWEQEFYE
NMYRAPTTLQ SCGVCVVCNS QTILRCGNCI RKPFLCCKCC YDHVMHTDHK NVLSINPYIC
SQPGCGEADV TKLYLGGMSY FCGNHKPKLS IPLVSNGTVF GIYRANCAGS ENVDDFNQLA
TTNWSTVEPY ILANRCVDSL RRFAAETVKA TEELHKQQFA SAEVREVLSD RELILSWEPG
KTRPPLNRNY VFTGFHFTRT SKVQLGDFTF EKGEGKDVVY YRATSTAKLS VGDIFVLTSH
NVVSLIAPTL CPQQTFSRFV NLRPNVMVPA CFVNNIPLYH LVGKQKRTTV QGPPGSGKSH
FAIGLAAYFS NARVVFTACS HAAVDALCEK AFKFLKVDDC TRIVPQRTTI DCFSKFKAND
TGKKYIFSTI NALPEVSCDI LLVDEVSMLT NYELSFINGK INYQYVVYVG DPAQLPAPRT
LLNGSLSPKD YNVVTNLMVC VKPDIFLAKC YRCPKEIVDT VSTLVYDGKF IANNPESRQC
FKVIVNNGNS DVGHESGSAY NITQLEFVKD FVCRNKEWRE ATFISPYNAM NQRAYRMLGL
NVQTVDSSQG SEYDYVIFCV TADSQHALNI NRFNVALTRA KRGILVVMRQ RDELYSALKF
IELDSVASLQ GTGLFKICNK EFSGVHPAYA VTTKALAATY KVNDELAALV NVEAGSEITY
KHLISLLGFK MSVNVEGCHN MFITRDEAIR NVRGWVGFDV EATHACGTNI GTNLPFQVGF
STGADFVVTP EGLVDTSIGN NFEPVNSKAP PGEQFNHLRA LFKSAKPWHV VRPRIVQMLA
DNLCNVSDCV VFVTWCHGLE LTTLRYFVKI GKDQVCSCGS RATTFNSHTQ AYACWKHCLG
FDFVYNPLLV DIQQWGYSGN LQFNHDLHCN VHGHAHVASA DAIMTRCLAI NNAFCQDVNW
DLTYPHIANE DEVNSSCRYL QRMYLNACVD ALKVNVVYDI GNPKGIKCVR RGDLNFRFYD
KNPIVPNVKQ FEYDYNQHKD KFADGLCMFW NCNVDCYPDN SLVCRYDTRN LSVFNLPGCN
GGSLYVNKHA FHTPKFDRTS FRNLKAMPFF FYDSSPCETI QLDGVAQDLV SLATKDCITK
CNIGGAVCKK HAQMYADFVT SYNAAVTAGF TFWVTNNFNP YNLWKSFSAL QSIDNIAYNM
YKGGHYDAIA GEMPTIVTGD KVFVIDQGVE KAVFFNQTIL PTSVAFELYA KRNIRTLPNN
RILKGLGVDV TNGFVIWDYT NQTPLYRNTV KVCAYTDIEP NGLIVLYDDR YGDYQSFLAA
DNAVLVSTQC YKRYSYVEIP SNLLVQNGIP LKDGANLYVY KRVNGAFVTL PNTLNTQGRS
YETFEPRSDV ERDFLDMSEE SFVEKYGKEL GLQHILYGEV DKPQLGGLHT VIGMCRLLRA
NKLNAKSVTN SDSDVMQNYF VLADNGSYKQ VCTVVDLLLD DFLELLRNIL KEYGTNKSKV
VTVSIDYHSI NFMAWFEDGI IKTCYPQLQS AWTCGYNMPE LYKVQNCVME PCNIPNYGVG
IALPSGIMMN VAKYTQLCQY LSKTTMCVPH NMRVMHFGAG SDKGVAPGST VLKQWLPEGT
LLVDNDIVDY VSDAHVSVLS DCNKYKTEHK FDLVISDMYT DNDSKRKHEG VIANNGNDDV
FIYLSSFLRN NLALGGSFAV KVTETSWHEV LYDIAQDCAW WTMFCTAVNA SSSEAFLVGV
NYLGASEKVK VSGKTLHANY IFWRNCNYLQ TSAYSIFDVA KFDLRLKATP VVNLKTEQKT
DLVFNLIKCG KLLVRDVGNT SFTSDSFVCT M
