ID C6GHR8_9BETC Unreviewed; 7172 AA.
AC C6GHR8;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=ORF1ab polyprotein {ECO:0000256|PROSITE-ProRule:PRU01344};
OS Rat coronavirus Parker.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus; Murine coronavirus.
OX NCBI_TaxID=502102 {ECO:0000313|EMBL:ACT11039.1, ECO:0000313|Proteomes:UP000173347};
RN [1] {ECO:0000313|EMBL:ACT11039.1, ECO:0000313|Proteomes:UP000173347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Parker {ECO:0000313|EMBL:ACT11039.1};
RA Spiro D., Halpin R., Wang S., Hostetler J., Overton L., Tsitrin T.,
RA Katzel D., Sarmiento M., Sitz J., Amedeo P., Caler E., Lorenzi H.,
RA Schobel S., Sundaram J., Weiss S.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cleaves the C-terminus of replicase polyprotein at 11 sites.
CC Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN].
CC Also able to bind an ADP-ribose-1''-phosphate (ADRP).
CC {ECO:0000256|ARBA:ARBA00002223}.
CC -!- FUNCTION: Forms a hexadecamer with nsp7 (8 subunits of each) that may
CC participate in viral replication by acting as a primase. Alternatively,
CC may synthesize substantially longer products than oligonucleotide
CC primers. {ECO:0000256|ARBA:ARBA00002182}.
CC -!- FUNCTION: Forms a hexadecamer with nsp8 (8 subunits of each) that may
CC participate in viral replication by acting as a primase. Alternatively,
CC may synthesize substantially longer products than oligonucleotide
CC primers. {ECO:0000256|ARBA:ARBA00003443}.
CC -!- FUNCTION: Forms a primer, NSP9-pU, which is utilized by the polymerase
CC for the initiation of RNA chains. Interacts with ribosome signal
CC recognition particle RNA (SRP). Together with NSP8, suppress protein
CC integration into the cell membrane, thereby disrupting host immune
CC defenses. {ECO:0000256|ARBA:ARBA00043928}.
CC -!- FUNCTION: Inhibits host translation by interacting with the 40S
CC ribosomal subunit. The nsp1-40S ribosome complex further induces an
CC endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them
CC for degradation. Viral mRNAs are not susceptible to nsp1-mediated
CC endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader
CC sequence and are therefore protected from degradation. By suppressing
CC host gene expression, nsp1 facilitates efficient viral gene expression
CC in infected cells and evasion from host immune response.
CC {ECO:0000256|ARBA:ARBA00002872}.
CC -!- FUNCTION: May play a role in the modulation of host cell survival
CC signaling pathway by interacting with host PHB and PHB2. Indeed, these
CC two proteins play a role in maintaining the functional integrity of the
CC mitochondria and protecting cells from various stresses.
CC {ECO:0000256|ARBA:ARBA00003115}.
CC -!- FUNCTION: Methyltransferase that mediates mRNA cap 2'-O-ribose
CC methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine
CC cap is a prerequisite for binding of nsp16. Therefore plays an
CC essential role in viral mRNAs cap methylation which is essential to
CC evade immune system. {ECO:0000256|ARBA:ARBA00002840}.
CC -!- FUNCTION: Multi-functional protein with a zinc-binding domain in N-
CC terminus displaying RNA and DNA duplex-unwinding activities with 5' to
CC 3' polarity. Activity of helicase is dependent on magnesium.
CC {ECO:0000256|ARBA:ARBA00002960}.
CC -!- FUNCTION: Participates in the assembly of virally-induced cytoplasmic
CC double-membrane vesicles necessary for viral replication.
CC {ECO:0000256|ARBA:ARBA00003070}.
CC -!- FUNCTION: Plays a pivotal role in viral transcription by stimulating
CC both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase
CC activities. Therefore plays an essential role in viral mRNAs cap
CC methylation. {ECO:0000256|ARBA:ARBA00002697}.
CC -!- FUNCTION: Plays a role in the initial induction of autophagosomes from
CC host reticulum endoplasmic. Later, limits the expansion of these
CC phagosomes that are no longer able to deliver viral components to
CC lysosomes. {ECO:0000256|ARBA:ARBA00003748}.
CC -!- FUNCTION: Plays a role in viral RNA synthesis through two distinct
CC activities. The N7-guanine methyltransferase activity plays a role in
CC the formation of the cap structure GpppA-RNA. The proofreading
CC exoribonuclease reduces the sensitivity of the virus to RNA mutagens
CC during replication. This activity acts on both ssRNA and dsRNA in a 3'-
CC 5' direction. {ECO:0000256|ARBA:ARBA00034456}.
CC -!- FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription
CC of viral genomic and subgenomic RNAs. Acts in complex with nsp7 and
CC nsp8 to transcribe both the minus and positive strands of genomic RNA.
CC The kinase-like NiRAN domain of NSP12 attaches one or more nucleotides
CC to the amino terminus of NSP9, forming a covalent RNA-protein
CC intermediate that serves as transcription/replication primer.
CC Subgenomic RNAs (sgRNAs) are formed by discontinuous transcription: The
CC polymerase has the ability to pause at transcription-regulating
CC sequences (TRS) and jump to the leader TRS, resulting in a major
CC deletion. This creates a series of subgenomic RNAs that are replicated,
CC transcribed and translated. In addition, Nsp12 is a subunit of the
CC viral RNA capping enzyme that catalyzes the RNA guanylyltransferase
CC reaction for genomic and sub-genomic RNAs. Subsequently, the NiRAN
CC domain transfers RNA to GDP, and forms the core cap structure GpppA-
CC RNA. {ECO:0000256|ARBA:ARBA00043918}.
CC -!- FUNCTION: Responsible for the cleavages located at the N-terminus of
CC the replicase polyprotein. In addition, PL-PRO possesses a
CC deubiquitinating/deISGylating activity and processes both 'Lys-48'- and
CC 'Lys-63'-linked polyubiquitin chains from cellular substrates.
CC Participates together with nsp4 in the assembly of virally-induced
CC cytoplasmic double-membrane vesicles necessary for viral replication.
CC Antagonizes innate immune induction of type I interferon by blocking
CC the phosphorylation, dimerization and subsequent nuclear translocation
CC of host IRF3. Prevents also host NF-kappa-B signaling.
CC {ECO:0000256|ARBA:ARBA00003569}.
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:0000256|ARBA:ARBA00003368}.
CC -!- CATALYTIC ACTIVITY:
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:0000256|ARBA:ARBA00001665};
CC -!- CATALYTIC ACTIVITY:
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:0000256|ARBA:ARBA00001556};
CC -!- CATALYTIC ACTIVITY:
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:0000256|ARBA:ARBA00000707};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC ChEBI:CHEBI:167617; EC=2.1.1.56;
CC Evidence={ECO:0000256|ARBA:ARBA00034403};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67009;
CC Evidence={ECO:0000256|ARBA:ARBA00034403};
CC -!- CATALYTIC ACTIVITY:
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:0000256|ARBA:ARBA00024256};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC Evidence={ECO:0000256|ARBA:ARBA00024520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013;
CC Evidence={ECO:0000256|ARBA:ARBA00024520};
CC -!- CATALYTIC ACTIVITY:
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:0000256|ARBA:ARBA00024600};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Interacts with host PHB and PHB2.
CC {ECO:0000256|ARBA:ARBA00025984}.
CC -!- SUBUNIT: Interacts with nsp12. {ECO:0000256|ARBA:ARBA00034503}.
CC -!- SUBUNIT: Interacts with nsp7 and nsp8 to form the replication-
CC transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up
CC to two subunits of nsp13. Interacts with nsp9.
CC {ECO:0000256|ARBA:ARBA00034511}.
CC -!- SUBUNIT: Interacts with nsp7, nsp13 and nsp12 to form the replication-
CC transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up
CC to two subunits of nsp13. {ECO:0000256|ARBA:ARBA00034514}.
CC -!- SUBUNIT: Interacts with nsp8 and nsp12 to form the replication-
CC transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up
CC to two subunits of nsp13. {ECO:0000256|ARBA:ARBA00034507}.
CC -!- SUBUNIT: Interacts with nsp8 to form the replication-transcription
CC complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two
CC subunits of nsp13. {ECO:0000256|ARBA:ARBA00034500}.
CC -!- SUBUNIT: Interacts with papain-like protease nsp3 and non-structural
CC protein 6. {ECO:0000256|ARBA:ARBA00034512}.
CC -!- SUBUNIT: Interacts with proofreading exoribonuclease nsp14 and 2'-O-
CC methyltransferase nsp16; these interactions enhance nsp14 and nsp16
CC enzymatic activities. {ECO:0000256|ARBA:ARBA00034506}.
CC -!- SUBUNIT: Monomer. Homodimer. Only the homodimer shows catalytic
CC activity. {ECO:0000256|ARBA:ARBA00034508}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment {ECO:0000256|ARBA:ARBA00004399}. Host cytoplasm, host
CC perinuclear region {ECO:0000256|ARBA:ARBA00004407}. Host endoplasmic
CC reticulum-Golgi intermediate compartment
CC {ECO:0000256|ARBA:ARBA00004452}. Host membrane
CC {ECO:0000256|ARBA:ARBA00004301}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004301}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000256|ARBA:ARBA00008087, ECO:0000256|PROSITE-ProRule:PRU01294}.
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DR EMBL; FJ938068; ACT11039.1; -; Genomic_RNA.
DR RefSeq; YP_003029844.1; NC_012936.1.
DR MEROPS; C16.006; -.
DR GeneID; 11273175; -.
DR KEGG; vg:11273175; -.
DR Proteomes; UP000173347; Genome.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
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:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro.
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-dependent 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:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-UniRule.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0039648; P:modulation by symbiont 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-UniRule.
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; cd21901; alpha_betaCoV_Nsp10; 1.
DR CDD; cd21560; betaCoV-Nsp6; 1.
DR CDD; cd21722; betaCoV_Nsp13-helicase; 1.
DR CDD; cd21659; betaCoV_Nsp14; 1.
DR CDD; cd21519; betaCoV_Nsp2_MHV-like; 1.
DR CDD; cd21666; betaCoV_Nsp5_Mpro; 1.
DR CDD; cd21827; betaCoV_Nsp7; 1.
DR CDD; cd21831; betaCoV_Nsp8; 1.
DR CDD; cd21898; betaCoV_Nsp9; 1.
DR CDD; cd21732; betaCoV_PLPro; 1.
DR CDD; cd20762; capping_2-OMTase_Nidovirales; 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; cd21879; MHV-like_Nsp1; 1.
DR CDD; cd21812; MHV-like_Nsp3_betaSM; 1.
DR CDD; cd21824; MHV-like_Nsp3_NAB; 1.
DR CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR CDD; cd21171; NTD_alpha_betaCoV_Nsp15-like; 1.
DR CDD; cd21689; stalk_CoV_Nsp13-like; 1.
DR CDD; cd21714; TM_Y_MHV-like_Nsp3_C; 1.
DR CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1.
DR CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR Gene3D; 1.10.8.1190; -; 2.
DR Gene3D; 2.60.120.1680; -; 1.
DR Gene3D; 3.10.20.350; -; 1.
DR Gene3D; 3.10.20.540; -; 1.
DR Gene3D; 3.40.50.11580; -; 1.
DR Gene3D; 6.10.140.2090; -; 1.
DR Gene3D; 1.10.150.420; Coronavirus nonstructural protein 4 C-terminus; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 1.10.1840.10; main proteinase (3clpro) structure, domain 3; 1.
DR Gene3D; 3.30.160.820; Nsp15 N-terminal domain-like; 1.
DR Gene3D; 1.10.8.370; nsp7 replicase; 1.
DR Gene3D; 3.30.70.3540; Nsp8 replicase, head domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.40.10.250; Replicase NSP9; 1.
DR Gene3D; 3.40.50.11020; Replicase polyprotein, nucleic acid-binding domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR046443; a/bCoV_NSP1_glob.
DR InterPro; IPR046440; AV_NSP11N_COV_NSP15M.
DR InterPro; IPR022570; B-CoV_A_NSP1.
DR InterPro; IPR046442; bCoV_NSP1_C.
DR InterPro; IPR043608; CoV_NSP15_M.
DR InterPro; IPR043606; CoV_NSP15_N.
DR InterPro; IPR043613; CoV_NSP2_C.
DR InterPro; IPR047573; CoV_NSP2_M.
DR InterPro; IPR043611; CoV_NSP3_C.
DR InterPro; IPR047566; CoV_NSP3_Y3.
DR InterPro; IPR032505; CoV_NSP4_C.
DR InterPro; IPR043612; CoV_NSP4_N.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR045055; DNA2/NAM7-like.
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; IPR046435; N7_MTase_CoV.
DR InterPro; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR046438; NIV_2_O_MTASE.
DR InterPro; IPR046436; NIV_EXON.
DR InterPro; IPR036333; NSP10_sf_CoV.
DR InterPro; IPR047570; NSP12_IF_CoV.
DR InterPro; IPR044343; NSP13_1B_dom_CoV.
DR InterPro; IPR048673; NSP13_stalk_CoV.
DR InterPro; IPR048672; NSP13_ZBD_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; IPR043615; NSP2_N_CoV.
DR InterPro; IPR044381; NSP3_DPUP_MHV.
DR InterPro; IPR047567; NSP3_G2M_bCoV.
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; IPR046441; RdRp_CoV.
DR InterPro; IPR044347; RdRp_HCoV_HKU1-like.
DR InterPro; IPR009469; RdRp_N_CoV.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF530; HELICASE MAGATAMA 3-RELATED; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF13604; AAA_30; 1.
DR Pfam; PF11963; B-CoV_A_NSP1; 2.
DR Pfam; PF16251; bCoV_NAB; 1.
DR Pfam; PF06471; CoV_ExoN; 1.
DR Pfam; PF06460; CoV_Methyltr_2; 1.
DR Pfam; PF09401; CoV_NSP10; 1.
DR Pfam; PF20631; CoV_NSP13_1B; 1.
DR Pfam; PF20633; CoV_NSP13_stalk; 1.
DR Pfam; PF20632; CoV_NSP13_ZBD; 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; PF01831; Peptidase_C16; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF144246; Coronavirus NSP10-like; 1.
DR SUPFAM; SSF140367; Coronavirus NSP7-like; 1.
DR SUPFAM; SSF143076; Coronavirus NSP8-like; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF142877; EndoU-like; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF159936; NSP3A-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF101816; Replicase NSP9; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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; PS52000; COV_NSP12_IF; 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 3: Inferred from homology;
KW Activation of host autophagy by virus {ECO:0000256|ARBA:ARBA00023050};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Decay of host mRNAs by virus {ECO:0000256|ARBA:ARBA00022616};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE-
KW ProRule:PRU01303};
KW Eukaryotic host gene expression shutoff by virus
KW {ECO:0000256|ARBA:ARBA00023247};
KW Eukaryotic host translation shutoff by virus
KW {ECO:0000256|ARBA:ARBA00022809, ECO:0000256|PROSITE-ProRule:PRU01308};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PROSITE-
KW ProRule:PRU01298}; Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host gene expression shutoff by virus {ECO:0000256|ARBA:ARBA00022995};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host mRNA suppression by virus {ECO:0000256|ARBA:ARBA00022557,
KW ECO:0000256|PROSITE-ProRule:PRU01308};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01303};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022632, ECO:0000256|PROSITE-ProRule:PRU01308};
KW Inhibition of host interferon signaling pathway by virus
KW {ECO:0000256|ARBA:ARBA00022830, ECO:0000256|PROSITE-ProRule:PRU01308};
KW Inhibition of host ISG15 by virus {ECO:0000256|ARBA:ARBA00023208};
KW Inhibition of host NF-kappa-B by virus {ECO:0000256|ARBA:ARBA00022863};
KW Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00023208};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01299};
KW Modulation of host ubiquitin pathway by viral deubiquitinase
KW {ECO:0000256|ARBA:ARBA00022876};
KW Modulation of host ubiquitin pathway by virus
KW {ECO:0000256|ARBA:ARBA00022662};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PROSITE-
KW ProRule:PRU01298}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01289};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01299};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280, ECO:0000256|PROSITE-
KW ProRule:PRU01308}; Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00444}.
FT TRANSMEM 2279..2300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2387..2412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2432..2454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2837..2856
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3107..3132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3144..3165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3193..3216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3636..3658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3664..3689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3696..3717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3737..3758
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3765..3785
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3805..3829
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3836..3858
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..196
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000259|PROSITE:PS51962"
FT DOMAIN 216..246
FT /note="BetaCoV Nsp1 C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51963"
FT DOMAIN 250..510
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51989"
FT DOMAIN 517..705
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000259|PROSITE:PS51990"
FT DOMAIN 725..831
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51991"
FT DOMAIN 833..945
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS51943"
FT DOMAIN 1082..1331
FT /note="Peptidase C16"
FT /evidence="ECO:0000259|PROSITE:PS51124"
FT DOMAIN 1309..1480
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1535..1607
FT /note="DPUP"
FT /evidence="ECO:0000259|PROSITE:PS51942"
FT DOMAIN 1606..1661
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS51944"
FT DOMAIN 1676..1935
FT /note="Peptidase C16"
FT /evidence="ECO:0000259|PROSITE:PS51124"
FT DOMAIN 1949..2050
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000259|PROSITE:PS51945"
FT DOMAIN 2105..2250
FT /note="G2M"
FT /evidence="ECO:0000259|PROSITE:PS51994"
FT DOMAIN 2728..2831
FT /note="CoV Nsp3 Y"
FT /evidence="ECO:0000259|PROSITE:PS51992"
FT DOMAIN 3230..3327
FT /note="Nsp4C"
FT /evidence="ECO:0000259|PROSITE:PS51946"
FT DOMAIN 3328..3630
FT /note="Peptidase C30"
FT /evidence="ECO:0000259|PROSITE:PS51442"
FT DOMAIN 3918..4006
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51949"
FT DOMAIN 4007..4203
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51950"
FT DOMAIN 4204..4313
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS51951"
FT DOMAIN 4314..4451
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000259|PROSITE:PS51952"
FT DOMAIN 4456..4711
FT /note="NiRAN"
FT /evidence="ECO:0000259|PROSITE:PS51947"
FT DOMAIN 4712..4810
FT /note="Nsp12 Interface"
FT /evidence="ECO:0000259|PROSITE:PS52000"
FT DOMAIN 4811..5378
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000259|PROSITE:PS51948"
FT DOMAIN 5058..5220
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT DOMAIN 5379..5462
FT /note="CV ZBD"
FT /evidence="ECO:0000259|PROSITE:PS51653"
FT DOMAIN 5634..5985
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51657"
FT DOMAIN 6049..6264
FT /note="ExoN"
FT /evidence="ECO:0000259|PROSITE:PS51953"
FT DOMAIN 6273..6499
FT /note="N7-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51954"
FT DOMAIN 6500..6560
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000259|PROSITE:PS51960"
FT DOMAIN 6561..6681
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000259|PROSITE:PS51961"
FT DOMAIN 6731..6870
FT /note="NendoU"
FT /evidence="ECO:0000259|PROSITE:PS51958"
FT DOMAIN 6875..7169
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51955"
FT REGION 6386..6400
FT /note="GpppA-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
FT ACT_SITE 6067
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6069
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6761
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6776
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6816
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT BINDING 6308..6314
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
SQ SEQUENCE 7172 AA; 802717 MW; 141CB9BBD44D9142 CRC64;
MAKMGKYGLG FKWAPEFPWM LPNASEKLGN PERSEEDGFC PSAAQEPKVK GRTLVNHVRV
DCSRLPALEC CVQSAIIRDI FVDKDPQKVE ASTMMALQFG SAVLIMPSKR LSIQAWANLG
VLPRTPAMGL FKRVCLCNTR GCSCDVHVAF QLFTVQPDGV CLGNGRFIGW FVPVTAIPEY
AKQWLQPWSI LLRKGGNKGS VTSGHRRAVT MPVYDFNVED ACEEVHLNPK GKYSRKAYTL
LKGYRGVKPI LFVDQYGCDY TGCLAKGLED YGDLTLSEMK ELFPVWRESL DNEVVVAWHV
DRDPRAVMRL QTLATLRSID YVGQPTEDVV DGDVVVREPA HLLAADALVK RLPRLVETML
YTDSSVTEFC YKTKLCDCGF ITQFGYVDCC GDTCDFRGWV PGNMLDGFPC PGCSKSYMPW
ELEAQSSGVI PEGGVLFTQS TDTVNREAFK LYGHAVVPFG SAVYWSPYPG MWLPVVWSSV
KSYSGLTYTG VVGCKAIVQE TDAICRSLYM DYVQHKCGNL DQRATLGLDD VYHRQLLVNR
GDYSLLLENV DLFVKRRAEF ACKFATCGDG FVPLLLDGLV PRSYYLIKSG QAYTSMMVNF
SHEVIDMCMD MALLFMHDVK VATKYVKKFT GKLAVRFKAL GVAVVRKITE WFDLAVDIAA
SAAGWLCYQL VNGLFAVANG VITFVQEAPE LVKNFVAKFR AFFKVLIDSM SVSILSGLTV
VKTASNRVCL AGSKVYEVVQ KSLSAYVLPV GCSEATCLVG ESEPAVFEDD VVGVVKTPLT
YQGCCKPPTS FEKICIVDKL YMAKCGDQFY PVVVDNDTVG VLDQCWRFPC AGKKVVFNDK
PKVKEVPSTR KIKIIFALDA TFDSVLSKAC SEFEVDKDVT LDELLDVVLD AVESTLSPCK
EHDVIGTKVC ALLDRLAEDY VYLFDEGGDE VIAPRMYCSF SAPDDEDCVA ADVVDADENQ
DDDADDSVVL VADAQEDGVA KEQVEVDSEI CVAHTGGQDE LTEPDAVGSQ TPIASAEKTE
VGEASDREGI AEAKATVCAD DLDACPDQVE AFEIEEVEDS ILDELQTELN APADRTYEDV
LAFDAIYSKA LSAVYAVPSD ETHFKVCGFY SPAIERTNCW LRSTLIVMQS LPLEFKDLEM
QKLWLSYKAG YDQCFVDKLV KSVPRSIILP QGGYVADFAY YFLSQCSFKA HANWRCLKCD
MASKLQGLDA MFFYGDVVSH MCKCGSGMTL LSADIPYTLH FGVRDDKFCA FYTPRKVFRA
ACAVDVNDCH SMAVVDGKLI DGKNVTKFTG DKFDFMVGHG MTFSMSPFET AQLYGSCITP
NVCFVKGDVI KVARLVEAEV IVNPANGRMA HGAGVAGAIA KAAGKFFIKE TADMVKNQGV
CLVGECYESA GGKLCKKVLN IVGPDARGQG RQCYSLLERA YQHINKCDNV VTTLISAGIF
SVPTDVSLTY LLGVVTKNVI LVSNNKDDFD VIEKCQVTSV AGTKALSLQL AKNLCRDVKF
ETNACDTLFG ASCFVASYDV LQEVELLRHD IQLDDDARVF VQANMDCLPT DWRLVNKLDV
VDGVRTIKYF ECPGEIFVSS QGKKFGYVQN GLFKVASVSQ IRALLANKVD VLCTVDGVNF
RSCCVTEGEV FGKTLGSVFC DGINVTKVRC SAIHKGKVFF QYSGLSEADL VAVKDAFGFD
EPQLLKYYNM LGMCKWPVVV CGNYFAFKQS NNNCYINVAC LMLQHLNLKF PKWQWQEAWN
EFRSGKPLRF VSLVLAKGSF KFNEPSDSTD FIRVVLREAD LSGATCDLEF ICKCGVKQDQ
RKGVDAVMHF GTLDKSDLVK GYNIACTCGS KLVHCTQFNV PFLICSYTPE GRKLPDDVVA
ANIFTGGSLG HYTHVKCKPK YQLYDACNVS KVSEAKGNFT DCLYLKNLKQ TFSSVLTTYY
LDDVKCVEYK PDLSQYYCES GKYYTKPIIK AQFRTFEKVD GVYTNFKLVG HSIAEKLNAK
LGFDCDSPFV EYKITEWPTA TGDVVLASDD LYVSRYLSGC ITFGKPVVWL GHEEASLKSL
TYFNRPSVVC ENKFNVLPVD VSEPTDKEPV PAAVLVTGVP SADASADAGT AKEQKACASD
NVEEQVVTEV HQEPSVSAVD VKEVKLNGVK KPVKVEDSVV VNDPTSDTKV VKSLSIVDDM
FLTGCKYVVW TANELSRLVN SPTVREYVKW GKIVIPTKLL LLRDERQEFV APKVVKAKAI
ACYGAVKWFF FYCFSWIKFN TDNKVIYTTE LASKLTFKLC CLAFKNALQT FNWSVVSRGF
FLVATVFLLW FNFLYANVIL SDFYLPNIGS LPTFVGQIVA WFKTTFGVST ICDFYQVTDL
GYRSSFCNGS MVCELCFSGF DMLDSYDAIN VVQHVVDRRV SFDYISILKL VVELIIGYSL
YTVCFYPLFV LIGMQLLTTW LPEFFMLETM HWSARLFVFV ANMLPAFTLL RFYIVVTAMY
KVYCLCRHVM YGCSNPGCLF CYKRNRSVRV KCSTVVGGSL RYYDVMANGG TGFCTKHQWN
CLNCDSWKPG NTFITLEAAA DLSKELKRPV NPTDSAYYSV TEVKQVGCSM RLFYERDGQR
VYDDVSASLF VDMNGLLHSK VKGVPETHVV VVENEADKAG FLGAAVFYAQ SLYRPMLMVE
KKLITTANTG LSVSQTMFDL YVDSLLNVLD VDRKSLTSFV NAAHNSLKEG VQLEQVMDTF
VGCARRKCAI DSDVETRSIT KSVMSAVNAG VDFTDESCNN LVPTYVKSDT IVAADLGVLI
QNNAKHVQSN VAKAANVACI WSVDAFNQLS ADLQHRLRKA CSKTGLKIKL TYNKQEANVP
ILTTPFSLKG GAVFSKFLQW LFVANLICFI VLWALIPTYA VHKSDMQLPL YASFKVIENG
VLRDVSVTDA CFANKFNQFD QWYESTFGLA YYRNSKACPV VVAVIDQDIG HTLFNVPTKV
LRHGFHVLHF ITHAFATDSV QCYTPHMQIP YDNFYASGCV LSSLCTMLAH ADGTPHPYCY
TEGVMHNASL YSSLVPHVRY NLASSNGYIR FPEVVSEGIV RVVRTRSMTY CRVGLCEEAE
EGICFNFNSS WVLNNPYYRA MPGTFCGRNA FDLIHQVLGG LVQPIDFFAL TASSVAGAIL
AIIVVLAFYY LIKLKRAFGD YTSVVVINVI VWCINFMMLF VFQVYPTLSC LYACFYFYTT
LYFPSEISVV MHLQWLVMYG AIMPLWFCII YVAVVVSNHA LWLFSYCRKI GTEVRSDGTF
EEMALTTFMI TKESYCKLKN SVSDVAFNRY LSLYNKYRYF SGKMDTAAYR EAACSQLAKA
METFNHNNGN DVLYQPPTAS VTTSFLQSGI VKMVSPTSKV EPCVVSVTYG NMTLNGLWLD
DKVYCPRHVI CSSDDMTDPD YPNLLCRVTS SDFCVMSDRM SLTVMSYQMQ GSLLVLTVTL
QNPNTPKYSF GVVKPGETFT VLAAYNGRPQ GAFHVVMRSS HTIKGSFLCG SCGSVGYVLT
GDSVRFVYMH QLELSTGCHT GTDLSGNFYG PYRDAQVVQL PVQDYTQTVN VVAWLYAAIL
NRCNWFVQSD SCSLEEFNVW AMTNGFSSIK ADLVLDALAS MTGVTVEQVL AAIKRLYSGF
QGKQILGSCV LEDELTPSDV YQQLSGVKLQ SKRTRVIKGT CCWILASTFL FCSIIAAFVK
WTMFMYVTTH MLGVTLCALC FVSFAMLLIK HKHLYLTMYI MPVLCTLFYT NYLVVYKQSF
RGLAYAWLSH FVPAVDYTYM DEVLYGVVLL IAMVFVTMRS INHDVFSIMF LVGRLVSLVS
MWYFGANLEE EVLLFLTSLF GTYTWTTMLS LATAKVIAKW LAVNVLYFTD VPQIKLVLLS
YLCIGYVCCC YWGVLSLLNS IFRMPLGVYN YKISVQELRY MNANGLRPPK NSFEALVLNF
KLLGIGGVPV IEVSQIQSRL TDVKCANVVL LNCLQHLHIA SNSKLWQYCS TLHNEILATS
DLSVAFDKLA QLLVVLFANP AAVDSKCLAS IEEVSDDYVR DNTVLHALQS EFVNMASFVE
YELAKKNLDE AKASGSANQQ QIKQLEKACN IAKSAYERDR AVARKLERMA DLALTNMYKE
ARINDKKSKV VSALQTMLFS MVRKLDNQAL NSILDNAVKG CVPLNAIPSL TSNTLTIIVP
DKQVFDQVVD NVYVTYAGNV WHIQSIQDAD GAVKQLNEID VNSIWPLVIA ANRHNEVSTV
VLQNNELMPQ KLRTQVVNSG SDMNCNTPTQ CYYNTTGTGK IVYAILSDCD GLKYTKIVKE
DGNCVVLELD PPCKFSVQDV KGLKIKYLYF VKGCNTLARG WVVGTLSSTV RLQAGTATEY
ASNSAILSLC AFSVDPKKTY LDYIQQGGVP VTNCVKMLCD HAGTGMAITI KPEATTNQDS
YGGASVCIYC RSRVEHPDVD GLCKLRGKFV QVPLGIKDPV LYVLTHDVCQ VCGFWRDGSC
SCVGTGSQFQ SKDTNFLNRV RGTSVNARLV PCASGLDTDV QLRAFDICNA NRAGIGLYYK
VNCCRFQRVD EDGNKLDKFF VVKRTNLEVY NKEKECYELT KECGVVAEHE FFTFDVEGSR
VPHIVRKDLS KFTMLDLCYA LRHFDRNDCS TLKEILLTYA ECGESYFQKK DWYDFVENPD
IINVYKKLGP IFNRALLNTA KFADALVEAG LVGVLTLDNQ DLYGQWYDFG DFVKTVPGCG
VAVADSYYSY MMPMLTMCHA LDSELYVNGT YREFDLVQYD FTDFKLELFN KYFKHWSMTY
HPNTCECEDD RCIIHCANFN ILFSMVLPKT CFGPLVRQIF VDGVPFVVSI GYHYKELGVV
MNMDVDTHRY RLSLKDLLLY AADPALHVAS ASALLDLRTC CFSVAAITSG VKFQTVKPGN
FNQDFYEFIL SKGLFKEGSS VDLKHFFFTQ DGNAAITDYN YYKYNLPTMV DIKQLLFVLE
VVNKYFEIYE GGCIPATQVI VNNYDKSAGY PFNKFGKARL YYEALSFEEQ DEIYAYTKRN
VLPTLTQMNL KYAISAKNRA RTVAGVSILS TMTGRMFHQK CLKSIAATRG VPVVIGTTKF
YGGWDDMLRR LIKDVDSPVL MGWDYPKCDR AMPNILRIVS SLVLARKHDS CCSHTDRFYR
LANECAQVLS EIVMCGGCYY VKPGGTSSGD ATTAFANSVF NICQAVSANV CSLMACNGHK
IEDLSIRELQ KRLYSNVYRA DHVDPAFVSE YYEFLNKHFS MMILSDDGVV CYNSEFASKG
YIANISAFQQ VLYYQNNVFM SEAKCWVETD IEKGPHEFCS QHTMLVKMDG DEVYLPYPDP
SRILGAGCFV DDLLKTDSVL LIERFVSLAI DAYPLVHHEN PEYQNVFRVY LEYIKKLYND
LGNQILDSYS VILSTCDGQK FTDETFYKNM YLRSAVMQSV GACVVCSSQT SLRCGSCIRK
PLLCCKCSYD HVMATDHKYV LSVSPYVCNS PGCDVNDVTK LYLGGMSYYC EDHKPQYSFK
LVMNGMVFGL YKQSCTGSPY IEDFNKIASC KWTEVDDYAL ANECTERLKL FAAETQKATE
EAFKQCYASA TIREIVSDRE LILSWEIGKV RPPLNKNYVF TGYHFTNNGK TVLGEYVFDK
SELTNGVYYR ATTTYKLSVG DVFILTSHAV SSLSAPTLVP QENYTSIRFA SVYSVPETFQ
NNVPNYQHIG MKRYCTVQGP PGTGKSHLAI GLAVYYCTAR VVYTAASHAA VDALCEKAHK
FLNINDCTRI VPAKVRVDCY DKFKVNDTTR KYVFTTINAL PELVTDIIVV DEVSMLTNYE
LSVINSRVRA KHYVYIGDPA QLPAPRVLLN KGTLEPRYFN SVTKLMCCLG PDIFLGTCYR
CPKEIVDTVS ALVYNNKLKA KNDNSSMCFK VYYKGQTTHE SSSAVNMQQI HLISKFLKAN
PSWSNAVFIS PYNSQNYVAK RVLGLQTQTV DSAQGSEYDF VIYSQTAETA HSVNVNRFNV
AITRAKKGIL CVMSSMQLFE SLNFTTLTLD KINNPRLQCT TNLFKDCSKS YDGYHPAHAP
SFLAVDDKYK VGGDLAVCLN VADSSVTYSR LISLMGFKLD LTLDGYCKLF ITRDEAIKRV
RAWVGFDAEG AHATRDSIGT NFPLQLGFST GIDFVVEATG MFAEREGYVF KKAAARAPPG
EQFKHLVPLM SRGQKWDVVR IRIVQMLSDH LVDLADSVVL VTWAASFELT CLRYFAKVGK
EVVCSVCNKR ATCFNSRTGY YGCWRHSYSC DYLYNPLIVD IQQWGYTGSL TSNHDPICSV
HKGAHVASSD AIMTRCLAVH DCFCKSVNWN LEYPIILNEV SVNTSCRLLQ RVMFRAAMLC
NRYDVCYDIG NPKGLACVKG YDFKFYDASP VVKSVKQFVY KYEAHKDQFL DGLCMFWNCN
VDKYPANAVV CRFDTRVLNK LNLPGCNGGS LYVNKHAFHT SPFTRAAFEN LKPMPFFYYS
DTPCVYMEGM ESKQVDYVPL RSATCITRCN LGGAVCLKHA EEYREYLESY NTATTAGFTF
WVYKTFDFYN LWNTFTRLQS LENVVYNLVN AGHFDGRAGE LPCAIIGEKV IAKIQNEDVV
VFKNNTPFPT NVAVELFAKR SIRPHPELKL FRNLNIDVCW SHVLWDYAKD SVFCSSTYKV
CKYTDLQCIE SLNVLFDGRD NGALEAFKKC RNGVYINTTK IKNLSMIKGP QRADLNGVVV
EKVGDSDVEF WFAMRSDGDD VIFSRTESLE PSHYRSPQGN PVGNRVGDLS GNEALARGTI
FTQSRFLSSF APRSEMEKDF MDLDEDVFVT KYSLQDYAFE HVVYGSFNQK IIGGLHLLIG
LARRQRKSNL VIQEFVSYDS SIHSYFITDE NSGSSKSVCT VIDLLLDDFV DILKSLNLNC
VSKVVNVNVD FKDFQFMLWC NEEKVMTFYP RLQAAADWKP GYVMPVLYKY LESPLERVNL
WNYGKPITLP TGCLMNVAKY TQLCQYLNTT TIAVPANMRV LHLGAGSDKG VAPGSAVLRQ
WLPAGSILVD NDVNPFVSDS VASYYGNCIT LPFDCQWDLI ISDMYDPLTK NIGEYNVSKD
GFFTYLCHLI CDKLALGGSV AIKITEFSWN AELYSLMGKF AFWTIFCTNV NASSSEGFLI
GINWLNRTRT EIDGKTMHAN YLFWRNSTMW NGGAYSLFDM SKFPLKAAGT AVVSLKPDQI
NDLVLSLIEK GRLLVRDTRK EVFVGDSLVN VK
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