ID A0A859GSJ7_SARS2 Unreviewed; 7096 AA. AC A0A859GSJ7; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 27-MAR-2024, entry version 13. DE RecName: Full=ORF1ab polyprotein {ECO:0000256|PROSITE-ProRule:PRU01344}; GN Name=ORF1ab {ECO:0000313|EMBL:QKV25199.1}; OS Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae; OC Betacoronavirus; Sarbecovirus; OC Severe acute respiratory syndrome coronavirus. OX NCBI_TaxID=2697049 {ECO:0000313|EMBL:QKV25199.1}; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:QKV25199.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SARS-CoV-2/human/USA/CT-Yale-014/2020 RC {ECO:0000313|EMBL:QKV25199.1}; RX PubMed=32511630; RA Fauver J.R., Petrone M.E., Hodcroft E.B., Shioda K., Ehrlich H.Y., RA Watts A.G., Vogels C.B.F., Brito A.F., Alpert T., Muyombwe A., Razeq J., RA Downing R., Cheemarla N.R., Wyllie A.L., Kalinich C.C., Ott I., Quick J., RA Loman N.J., Neugebauer K.M., Greninger A.L., Jerome K.R., Roychoundhury P., RA Xie H., Shrestha L., Huang M.L., Pitzer V.E., Iwasaki A., Omer S.B., RA Khan K., Bogoch I., Martinello R.A., Foxman E.F., Landry M.L., Neher R.A., RA Ko A.I., Grubaugh N.D.; RT "Coast-to-coast spread of SARS-CoV-2 in the United States revealed by RT genomic epidemiology."; RL medRxiv 0:0-0(2020). 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 (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=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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC Endoplasmic reticulum-Golgi intermediate compartment CC {ECO:0000256|ARBA:ARBA00004399}. Host cytoplasm, host perinuclear CC region {ECO:0000256|ARBA:ARBA00004407}. Host endoplasmic reticulum- CC Golgi intermediate compartment {ECO:0000256|ARBA:ARBA00004452}. CC Membrane {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}. 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; MT635212; QKV25199.1; -; Genomic_RNA. 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-KW. 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:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0002151; F:G-quadruplex RNA binding; IEA:InterPro. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. 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: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; cd21516; betaCoV_Nsp2_SARS-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; cd21167; M_alpha_beta_cv_Nsp15-like; 1. DR CDD; cd21563; Macro_cv_SUD-M_Nsp3-like; 1. DR CDD; cd21557; Macro_X_Nsp3-like; 1. DR CDD; cd21161; NendoU_cv_Nsp15-like; 1. DR CDD; cd21171; NTD_alpha_betaCoV_Nsp15-like; 1. DR CDD; cd22662; SARS-CoV-like_Nsp1_C; 1. DR CDD; cd21796; SARS-CoV-like_Nsp1_N; 1. DR CDD; cd21814; SARS-CoV-like_Nsp3_betaSM; 1. DR CDD; cd21822; SARS-CoV-like_Nsp3_NAB; 1. DR CDD; cd21591; SARS-CoV-like_RdRp; 1. DR CDD; cd21689; stalk_CoV_Nsp13-like; 1. DR CDD; cd21525; SUD_C_SARS-CoV_Nsp3; 1. DR CDD; cd21717; TM_Y_SARS-CoV-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; -; 1. DR Gene3D; 2.60.120.1680; -; 1. DR Gene3D; 3.10.20.350; -; 1. DR Gene3D; 3.10.20.540; -; 1. DR Gene3D; 3.40.50.11580; -; 1. DR Gene3D; 6.10.140.2090; -; 1. DR Gene3D; 1.10.150.420; Coronavirus nonstructural protein 4 C-terminus; 1. DR Gene3D; 3.40.30.150; Coronavirus polyprotein cleavage domain; 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; 3.40.220.20; Nsp3, SUD-M subdomain; 1. DR Gene3D; 3.40.220.30; Nsp3, SUD-N subdomain; 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; 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; 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; 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; IPR009466; NSP14_CoV. DR InterPro; IPR044330; NSP15_alpha_betaCoV_N. DR InterPro; IPR044322; NSP15_M_alpha_beta_CoV. DR InterPro; IPR043174; NSP15_middle_sf. DR InterPro; IPR042515; NSP15_N_CoV. DR InterPro; IPR044401; NSP15_NendoU_CoV. DR InterPro; IPR009461; NSP16_CoV-like. DR InterPro; IPR021590; NSP1_glob_bCoV. DR InterPro; IPR038030; NSP1_glob_sf_bCoV. DR InterPro; IPR043615; NSP2_N_CoV. DR InterPro; IPR044389; NSP2_SARS-CoV-like. DR InterPro; IPR024375; NSP3_bCoV. DR InterPro; IPR047567; NSP3_G2M_bCoV. DR InterPro; IPR024358; NSP3_N_bCoV. DR InterPro; IPR032592; NSP3_NAB_bCoV. DR InterPro; IPR042570; NSP3_NAB_bCoV_sf. DR InterPro; IPR038166; NSP3_PL2pro_sf_bCoV. DR InterPro; IPR038400; NSP3_SUD-M_sf_bCoV. DR InterPro; IPR044864; NSP3_SUD-N_bCoV. DR InterPro; IPR043478; NSP3_SUD-N_sf_bCoV. DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV. DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV. DR InterPro; IPR038083; NSP3A-like. DR InterPro; IPR038123; NSP4_C_sf_CoV. DR InterPro; IPR044367; NSP6_betaCoV. DR InterPro; IPR043610; NSP6_CoV. DR InterPro; IPR014828; NSP7_CoV. DR InterPro; IPR037204; NSP7_sf_CoV. DR InterPro; IPR014829; NSP8_CoV. DR InterPro; IPR037230; NSP8_sf_CoV. DR InterPro; IPR014822; NSP9_CoV. DR InterPro; IPR036499; NSP9_sf_CoV. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR013016; Peptidase_C16_CoV. DR InterPro; IPR008740; Peptidase_C30_CoV. DR InterPro; IPR043477; Peptidase_C30_dom3_CoV. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR043177; PLpro_N_sf_CoV. DR InterPro; IPR043503; PLpro_palm_finger_dom_CoV. DR InterPro; IPR043178; PLpro_thumb_sf_CoV. DR InterPro; IPR046441; RdRp_CoV. DR InterPro; IPR009469; RdRp_N_CoV. DR InterPro; IPR044351; RdRp_SARS-CoV-like. 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; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1. DR PANTHER; PTHR43788:SF8; HELICASE WITH ZINC FINGER 2; 1. DR Pfam; PF13087; AAA_12; 1. DR Pfam; PF16251; bCoV_NAB; 1. DR Pfam; PF11501; bCoV_NSP1; 1. DR Pfam; PF12379; bCoV_NSP3_N; 1. DR Pfam; PF12124; bCoV_SUD_C; 1. DR Pfam; PF11633; bCoV_SUD_M; 1. DR Pfam; PF06471; CoV_ExoN; 1. DR Pfam; PF06460; CoV_Methyltr_2; 1. DR Pfam; PF09401; CoV_NSP10; 1. DR Pfam; 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; PF19212; CoV_NSP2_C; 1. DR Pfam; PF19211; CoV_NSP2_N; 1. DR Pfam; PF19218; CoV_NSP3_C; 1. DR Pfam; PF16348; CoV_NSP4_C; 1. DR Pfam; PF19217; CoV_NSP4_N; 1. DR Pfam; PF19213; CoV_NSP6; 1. DR Pfam; PF08716; CoV_NSP7; 1. DR Pfam; PF08717; CoV_NSP8; 1. DR Pfam; PF08710; CoV_NSP9; 1. DR Pfam; PF08715; CoV_peptidase; 1. DR Pfam; PF06478; CoV_RPol_N; 1. DR Pfam; PF01661; Macro; 1. DR Pfam; PF05409; Peptidase_C30; 1. DR Pfam; PF00680; RdRP_1; 1. DR SMART; SM00506; A1pp; 1. DR SUPFAM; 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; 1. DR SUPFAM; SSF160099; SARS Nsp1-like; 1. 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; PS51941; BCOV_NSP3C_M; 1. DR PROSITE; PS51994; BCOV_NSP3E_G2M; 1. DR PROSITE; PS51945; BCOV_NSP3E_NAB; 1. DR PROSITE; PS51952; COV_EXON_MTASE_COACT; 1. DR PROSITE; PS51954; COV_N7_MTASE; 1. DR PROSITE; PS51962; COV_NSP1; 1. DR PROSITE; 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; 1. DR PROSITE; PS51657; PSRV_HELICASE; 1. DR PROSITE; PS50507; RDRP_SSRNA_POS; 1. DR PROSITE; PS51940; SARS_NSP3C_N; 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 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 2229..2253 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2328..2351 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2363..2387 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2773..2790 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3043..3065 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3077..3098 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3104..3124 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3136..3154 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3582..3605 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3611..3629 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3636..3657 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3683..3701 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3731..3755 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3767..3789 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 12..127 FT /note="CoV Nsp1 globular" FT /evidence="ECO:0000259|PROSITE:PS51962" FT DOMAIN 148..179 FT /note="BetaCoV Nsp1 C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51963" FT DOMAIN 183..456 FT /note="CoV Nsp2 N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51989" FT DOMAIN 458..688 FT /note="CoV Nsp2 middle" FT /evidence="ECO:0000259|PROSITE:PS51990" FT DOMAIN 690..818 FT /note="CoV Nsp2 C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51991" FT DOMAIN 821..929 FT /note="Ubiquitin-like" FT /evidence="ECO:0000259|PROSITE:PS51943" FT DOMAIN 1025..1194 FT /note="Macro" FT /evidence="ECO:0000259|PROSITE:PS51154" FT DOMAIN 1231..1359 FT /note="Macro" FT /evidence="ECO:0000259|PROSITE:PS51940" FT DOMAIN 1367..1494 FT /note="Macro" FT /evidence="ECO:0000259|PROSITE:PS51941" FT DOMAIN 1496..1561 FT /note="DPUP" FT /evidence="ECO:0000259|PROSITE:PS51942" FT DOMAIN 1565..1620 FT /note="Ubiquitin-like" FT /evidence="ECO:0000259|PROSITE:PS51944" FT DOMAIN 1634..1898 FT /note="Peptidase C16" FT /evidence="ECO:0000259|PROSITE:PS51124" FT DOMAIN 1911..2021 FT /note="Nucleic acid-binding" FT /evidence="ECO:0000259|PROSITE:PS51945" FT DOMAIN 2046..2155 FT /note="G2M" FT /evidence="ECO:0000259|PROSITE:PS51994" FT DOMAIN 2660..2763 FT /note="CoV Nsp3 Y" FT /evidence="ECO:0000259|PROSITE:PS51992" FT DOMAIN 3165..3263 FT /note="Nsp4C" FT /evidence="ECO:0000259|PROSITE:PS51946" FT DOMAIN 3264..3569 FT /note="Peptidase C30" FT /evidence="ECO:0000259|PROSITE:PS51442" FT DOMAIN 3860..3942 FT /note="RdRp Nsp7 cofactor" FT /evidence="ECO:0000259|PROSITE:PS51949" FT DOMAIN 3943..4140 FT /note="RdRp Nsp8 cofactor" FT /evidence="ECO:0000259|PROSITE:PS51950" FT DOMAIN 4141..4253 FT /note="Nsp9 ssRNA-binding" FT /evidence="ECO:0000259|PROSITE:PS51951" FT DOMAIN 4254..4392 FT /note="ExoN/MTase coactivator" FT /evidence="ECO:0000259|PROSITE:PS51952" FT DOMAIN 4399..4653 FT /note="NiRAN" FT /evidence="ECO:0000259|PROSITE:PS51947" FT DOMAIN 4658..4756 FT /note="Nsp12 Interface" FT /evidence="ECO:0000259|PROSITE:PS52000" FT DOMAIN 4757..5324 FT /note="Nsp12 RNA-dependent RNA polymerase" FT /evidence="ECO:0000259|PROSITE:PS51948" FT DOMAIN 5004..5166 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT DOMAIN 5325..5408 FT /note="CV ZBD" FT /evidence="ECO:0000259|PROSITE:PS51653" FT DOMAIN 5581..5932 FT /note="(+)RNA virus helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51657" FT DOMAIN 5997..6212 FT /note="ExoN" FT /evidence="ECO:0000259|PROSITE:PS51953" FT DOMAIN 6221..6452 FT /note="N7-MTase" FT /evidence="ECO:0000259|PROSITE:PS51954" FT DOMAIN 6453..6513 FT /note="Nsp15 N-terminal oligomerization" FT /evidence="ECO:0000259|PROSITE:PS51960" FT DOMAIN 6514..6639 FT /note="AV-Nsp11N/CoV-Nsp15M" FT /evidence="ECO:0000259|PROSITE:PS51961" FT DOMAIN 6656..6795 FT /note="NendoU" FT /evidence="ECO:0000259|PROSITE:PS51958" FT DOMAIN 6800..7094 FT /note="Nidovirus-type SAM-dependent 2'-O-MTase" FT /evidence="ECO:0000259|PROSITE:PS51955" FT REGION 926..1000 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 6339..6353 FT /note="GpppA-binding" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299" FT COMPBIAS 927..947 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 984..1000 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 6015 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298" FT ACT_SITE 6017 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298" FT ACT_SITE 6116 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298" FT ACT_SITE 6193 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298" FT ACT_SITE 6198 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298" FT ACT_SITE 6686 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303" FT ACT_SITE 6701 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303" FT ACT_SITE 6741 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303" FT BINDING 6256..6262 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299" SQ SEQUENCE 7096 AA; 794070 MW; 25A7FB5E451164C5 CRC64; MESLVPGFNE KTHVQLSLPV LQVRDVLVRG FGDSVEEVLS EARQHLKDGT CGLVEVEKGV LPQLEQPYVF IKRSDARTAP HGHVMVELVA ELEGIQYGRS GETLGVLVPH VGEIPVAYRK VLLRKNGNKG AGGHSYGADL KSFDLGDELG TDPYEDFQEN WNTKHSSGVT RELMRELNGG AYTRYVDNNF CGPDGYPLEC IKDLLARAGK ASCTLSEQLD FIDTKRGVYC CREHEHEIAW YTERSEKSYE LQTPFEIKLA KKFDIFNGEC PNFVFPLNSI IKTIQPRVEK KKLDGFMGRI RSVYPVASPN ECNQMCLSTL MKCDHCGETS WQTGDFVKAT CEFCGTENLT KEGATTCGYL PQNAVVKIYC PACHNSEVGP EHSLAEYHNE SGLKTILRKG GRTIAFGGCV FSYVGCHNKC AYWVPRASAN IGCNHTGVVG EGSEGLNDNL LEILQKEKVN INIVGDFKLN EEIAIILASF SASTSAFVET VKGLDYKAFK QIVESCGNFK VTKGKAKKGA WNIGEQKSIL SPLYAFASEA ARVVRSIFSR TLETAQNSVR VLQKAAITIL DGISQYSLRL IDAMMFTSDL ATNNLVVMAY ITGGVVQLTS QWLTNIFGTV YEKLKPVLDW LEEKFKEGVE FLRDGWEIVK FISTCACEIV GGQIVTCAKE IKESVQTFFK LVNKFLALCA DSIIIGGAKL KALNLGETFV THSKGLYRKC VKSREETGLL MPLKAPKEII FLEGETLPTE VLTEEVVLKT GDLQPLEQPT SEAVEAPLVG TPVCINGLML LEIKDTEKYC ALAPNMMVTN NTFTLKGGAP TKVTFGDDTV IEVQGYKSVN ITFELDERID KVLNEKCSAY TVELGTEVNE FACVVADAVI KTLQPVSELL TPLGIDLDEW SMATYYLFDE SGEFKLASHM YCSFYPPDED EEEGDCEEEE FEPSTQYEYG TEDDYQGKPL EFGATSAALQ PEEEQEEDWL DDDSQQTVGQ QDGSEDNQTT TIQTIVEVQP QLEMELTPVV QTIEVNSFSG YLKLTDNVYI KNADIVEEAK KVKPTVVVNA ANVYLKHGGG VAGALNKATN NAMQVESDDY IATNGPLKVG GSCVLSGHNL AKHCLHVVGP NVNKGEDIQL LKSAYENFNQ HEVLLAPLLS AGIFGADPIH SLRVCVDTVR TNVYLAVFDK NLYDKLVSSF LEMKSEKQVE QKIAEIPKEE VKPFITESKP SVEQRKQDDK KIKACVEEVT TTLEETKFLT ENLLLYIDIN GNLHPDSATL VSDIDITFLK KDAPYIVGDV VQEGVLTAVV IPTKKAGGTT EMLAKALRKV PTDNYITTYP GQGLNGYTVE EAKTVLKKCK SAFYILPSII SNEKQEILGT VSWNLREMLA HAEETRKLMP VCVETKAIVS TIQRKYKGIK IQEGVVDYGA RFYFYTSKTT VASLINTLND LNETLVTMPL GYVTHGLNLE EAARYMRSLK VPATVSVSSP DAVTAYNGYL TSSSKTPEEH FIETISLAGS YKDWSYSGQS TQLGIEFLKR GDKSVYYTSN PTTFHLDGEV ITFDNLKTLL SLREVRTIKV FTTVDNINLH TQVVDMSMTY GQQFGPTYLD GADVTKIKPH NSHEGKTFYV LPNDDTLRVE AFEYYHTTDP SFLGRYMSAL NHTKKWKYPQ VNGLTSIKWA DNNCYLATAL LTLQQIELKF NPPALQDAYY RARAGEAANF CALILAYCNK TVGELGDVRE TMSYLFQHAN LDSCKRVLNV VCKTCGQQQT TLKGVEAVMY MGTLSYEQFK KGVQIPCTCG KQATKYLVQQ ESPFVMMSAP PAQYELKHGT FTCASEYTGN YQCGHYKHIT SKETLYCIDG ALLTKSSEYK GPITDVFYKE NSYTTTIKPV TYKLDGVVCT EIDPKLDNYY KKDNSYFTEQ PIDLVPNQPY PNASFDNFKF VCDNIKFADD LNQLTGYKKP ASRELKVTFF PDLNGDVVAI DYKHYTPSFK KGAKLLHKPI VWHVNNATNK ATYKPNTWCI RCLWSTKPVE TSNSFDVLKS EDAQGMENLA CEDLKPVSEE VVENPTIQKD VLECNVKTTE VVGDIILKPA NNSLKITEEV GHTDLMAAYV DNSSLTIKKP NELSRVLGLK TLATHGLAAV NSVPWDTIAN YAKPFLNKVV STTTNIVTRC LNRVCTNYMP YFFTLLLQLC TFTRSTNSRI KASMPTTIAK NTVKSVGKFC LEASFNYLKS PNFSKLINII IWFLLLSVCL GSLIYSTAAL GVLMSNLGMP SYCTGYREGY LNSTNVTIAT YCTGSIPCSV CLSGLDSLDT YPSLETIQIT ISSFKWDLTA FGLVAEWFLA YILFTRFFYV LGLAAIMQLF FSYFAVHFIS NSWLMWLIIN LVQMAPISAM VRMYIFFASF YYVWKSYVHV VDGCNSSTCM MCYKRNRATR VECTTIVNGV RRSFYVYANG GKGFCKLHNW NCVNCDTFCA GSTFISDEVA RDLSLQFKRP INPTDQSSYI VDSVTVKNGS IHLYFDKAGQ KTYERHSLSH FVNLDNLRAN NTKGSLPINV IVFDGKSKCE ESSAKSASVY YSQLMCQPIL LLDQALVSDV GDSAEVAVKM FDAYVNTFSS TFNVPMEKLK TLVATAEAEL AKNVSLDNVL STFISAARQG FVDSDVETKD VVECLKLSHQ SDIEVTGDSC NNYMLTYNKV ENMTPRDLGA CIDCSARHIN AQVAKSHNIA LIWNVKDFMS LSEQLRKQIR SAAKKNNLPF KLTCATTRQV VNVVTTKIAL KGGKIVNNWL KQLIKVTLVF LFVAAIFYLI TPVHVMSKHT DFSSEIIGYK AIDGGVTRDI ASTDTCFANK HADFDTWFSQ RGGSYTNDKA CPLIAAVITR EVGFVVPGLP GTILRTTNGD FLHFLPRVFS AVGNICYTPS KLIEYTDFAT SACVLAAECT IFKDASGKPV PYCYDTNVLE GSVAYESLRP DTRYVLMDGS IIQFPNTYLE GSVRVVTTFD SEYCRHGTCE RSEAGVCVST SGRWVLNNDY YRSLPGVFCG VDAVNLLTNM FTPLIQPIGA LDISASIVAG GIVAIVVTCL AYYFMRFRRA FGEYSHVVAF NTLLFLMSFT VLCLTPVYSF LPGVYSVIYL YLTFYLTNDV SFLAHIQWMV MFTPLVPFWI TIAYIICIST KHFYWFFSNY LKRRVVFNGV SFSTFEEAAL CTFLLNKEMY LKLRSDVLLP LTQYNRYLAL YNKYKYFSGA MDTTSYREAA CCHLAKALND FSNSGSDVLY QPPQTSITSA VLQSGFRKMA FPSGKVEGCM VQVTCGTTTL NGLWLDDVVY CPRHVICTSE DMLNPNYEDL LIRKSNHNFL VQAGNVQLRV IGHSMQNCVL KLKVDTANPK TPKYKFVRIQ PGQTFSVLAC YNGSPSGVYQ CAMRPNFTIK GSFLNGSCGS VGFNIDYDCV SFCYMHHMEL PTGVHAGTDL EGNFYGPFVD RQTAQAAGTD TTITVNVLAW LYAAVINGDR WFLNRFTTTL NDFNLVAMKY NYEPLTQDHV DILGPLSAQT GIAVLDMCAS LKELLQNGMN GRTILGSALL EDEFTPFDVV RQCSGVTFQS AVKRTIKGTH HWLLLTILTS LLVLVQSTQW SLFFFLYENA FLPFAMGIIA MSAFAMMFVK HKHAFLCLFL LPSLATVAYF NMVYMPASWV MRIMTWLDMV DTSLSGFKLK DCVMYASAVV LLILMTARTV YDDGARRVWT LMNVLTLVYK VYYGNALDQA ISMWALIISV TSNYSGVVTT VMFLARGIVF MCVEYCPIFF ITGNTLQCIM LVYCFLGYFC TCYFGLFCLL NRYFRLTLGV YDYLVSTQEF RYMNSQGLLP PKNSIDAFKL NIKLLGVGGK PCIKVATVQS KMSDVKCTSV VLLSVLQQLR VESSSKLWAQ CVQLHNDILL AKDTTEAFEK MVSLLSVLLS MQGAVDINKL CEEMLDNRAT LQAIASEFSS LPSYAAFATA QEAYEQAVAN GDSEVVLKKL KKSLNVAKSE FDRDAAMQRK LEKMADQAMT QMYKQARSED KRAKVTSAMQ TMLFTMLRKL DNDALNNIIN NARDGCVPLN IIPLTTAAKL MVVIPDYNTY KNTCDGTTFT YASALWEIQQ VVDADSKIVQ LSEISMDNSP NLAWPLIVTA LRANSAVKLQ NNELSPVALR QMSCAAGTTQ TACTDDNALA YYNTTKGGRF VLALLSDLQD LKWARFPKSD GTGTIYTELE PPCRFVTDTP KGPKVKYLYF IKGLNNLNRG MVLGSLAATV RLQAGNATEV PANSTVLSFC AFAVDAAKAY KDYLASGGQP ITNCVKMLCT HTGTGQAITV TPEANMDQES FGGASCCLYC RCHIDHPNPK GFCDLKGKYV QIPTTCANDP VGFTLKNTVC TVCGMWKGYG CSCDQLREPM LQSADAQSFL NRVCGVSAAR LTPCGTGTST DVVYRAFDIY NDKVAGFAKF LKTNCCRFQE KDEDDNLIDS YFVVKRHTFS NYQHEETIYN LLKDCPAVAK HDFFKFRIDG DMVPHISRQR LTKYTMADLV YALRHFDEGN CDTLKEILVT YNCCDDDYFN KKDWYDFVEN PDILRVYANL GERVRQALLK TVQFCDAMRN AGIVGVLTLD NQDLNGNWYD FGDFIQTTPG SGVPVVDSYY SLLMPILTLT RALTAESHVD TDLTKPYIKW DLLKYDFTEE RLKLFDRYFK YWDQTYHPNC VNCLDDRCIL HCANFNVLFS TVFPLTSFGP LVRKIFVDGV PFVVSTGYHF RELGVVHNQD VNLHSSRLSF KELLVYAADP AMHAASGNLL LDKRTTCFSV AALTNNVAFQ TVKPGNFNKD FYDFAVSKGF FKEGSSVELK HFFFAQDGNA AISDYDYYRY NLPTMCDIRQ LLFVVEVVDK YFDCYDGGCI NANQVIVNNL DKSAGFPFNK WGKARLYYDS MSYEDQDALF AYTKRNVIPT ITQMNLKYAI SAKNRARTVA GVSICSTMTN RQFHQKLLKS IAATRGATVV IGTSKFYGGW HNMLKTVYSD VENPHLMGWD YPKCDRAMPN MLRIMASLVL ARKHTTCCSL SHRFYRLANE CAQVLSEMVM CGGSLYVKPG GTSSGDATTA YANSVFNICQ AVTANVNALL STDGNKIADK YVRNLQHRLY ECLYRNRDVD TDFVNEFYAY LRKHFSMMIL SDDAVVCFNS TYASQGLVAS IKNFKSVLYY QNNVFMSEAK CWTETDLTKG PHEFCSQHTM LVKQGDDYVY LPYPDPSRIL GAGCFVDDIV KTDGTLMIER FVSLAIDAYP LTKHPNQEYA DVFHLYLQYI RKLHDELTGH MLDMYSVMLT NDNTSRYWEP EFYEAMYTPH TVLQAVGACV LCNSQTSLRC GACIRRPFLC CKCCYDHVIS TSHKLVLSVN PYVCNAPGCD VTDVTQLYLG GMSYYCKSHK PPISFPLCAN GQVFGLYKNT CVGSDNVTDF NAIATCDWTN AGDYILANTC TERLKLFAAE TLKATEETFK LSYGIATVRE VLSDRELHLS WEVGKPRPPL NRNYVFTGYR VTKNSKVQIG EYTFEKGDYG DAVVYRGTTT YKLNVGDYFV LTSHTVMPLS APTLVPQEHY VRITGLYPTL NISDEFSSNV ANYQKVGMQK YSTLQGPPGT GKSHFAIGLA LYYPSARIVY TACSHAAVDA LCEKALKYLP IDKCSRIIPA RARVECFDKF KVNSTLEQYV FCTVNALPET TADIVVFDEI SMATNYDLSV VNARLRAKHY VYIGDPAQLP APRTLLTKGT LEPEYFNSVC RLMKTIGPDM FLGTCRRCPA EIVDTVSALV YDNKLKAHKD KSAQCFKMFY KGVITHDVSS AINRPQIGVV REFLTRNPAW RKAVFISPYN SQNAVASKIL GLPTQTVDSS QGSEYDYVIF TQTTETAHSC NVNRFNVAIT RAKVGILCIM SDRDLYDKLQ FTSLEIPRRN VATLQAENVT GLFKDCSKVI TGLHPTQAPT HLSVDTKFKT EGLCVDIPGI PKDMTYRRLI SMMGFKMNYQ VNGYPNMFIT REEAIRHVRA WIGFDVEGCH ATREAVGTNL PLQLGFSTGV NLVAVPTGYV DTPNNTDFSR VSAKPPPGDQ FKHLIPLMYK GLPWNVVRIK IVQMLSDTLK NLSDRVVFVL WAHGFELTSM KYFVKIGPER TCCLCDRRAT CFSTASDTYA CWHHSIGFDY VYNPFMIDVQ QWGFTGNLQS NHDLYCQVHG NAHVASCDAI MTRCLAVHEC FVKRVDWTIE YPIIGDELKI NAACRKVQHM VVKAALLADK FPVLHDIGNP KAIKCVPQAD VEWKFYDAQP CSDKAYKIEE LFYSYATHSD KFTDGVCLFW NCNVDRYPAN SIVCRFDTRV LSNLNLPXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXKQFD TYNLWNTFTR LQSLENVAFN VVNKGHFDGQ QGEVPVSIIN NTVYTKVDGV DVELFENKTT LPVNVAFELW AKRNIKPVPE VKILNNLGVD IAANTVIWDY KRDAPAHIST IGVCSMTDIA KKPTETICAP LTVFFDGRVD GQVDLFRNAR NGVLITEGSV KGLQPSVGPK QASLNGVTLI GEAVKTQFNY YKKVDGVVQQ LPETYFTQSR NLQEFKPRSQ MEIDFLELAM DEFIERYKLE GYAFEHIVYG DFSHSQLGGL HLLIGLAKRF KESPFELEDF IPMDSTVKNY FITDAQTGSS KCVCSVIDLL LDDFVEIIKS QDLSVVSKVV KVTIDYTEIS FMLWCKDGHV ETFYPKLQSS QAWQPGVAMP NLYKMQRMLL EKCDLQNYGD SATLPKGIMM NVAKYTQLCQ YLNTLTLAVP YNMRVIHFGA GSDKGVAPGT AVLRQWLPTG TLLVDSDLND FVSDADSTLI GDCATVHTAN KWDLIISDMY DPKTKNVTKE NDSKEGFFTY ICGFIQQKLA LXGSVAIKIT EHSWNADLYK LMGHFAWWTA FVTNVNASSS EAFLIGCNYL GKPREQIDGY VMHANYIFWR NTNPIQLSSY SLFDMSKFPL KLRGTAVMSL KEGQINDMIL SLLSKGRLII RENNRVVISS DVLVNN //