ID A0A168DJQ5_MERS Unreviewed; 7078 AA. AC A0A168DJQ5; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 22-FEB-2023, entry version 41. DE RecName: Full=Replicase polyprotein 1ab {ECO:0000256|ARBA:ARBA00022087}; DE AltName: Full=ORF1ab polyprotein {ECO:0000256|ARBA:ARBA00029611}; GN Name=orf1ab {ECO:0000313|EMBL:ANC28632.1}; OS Middle East respiratory syndrome-related coronavirus (MERS-CoV). OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae; OC Betacoronavirus; Merbecovirus. OX NCBI_TaxID=1335626 {ECO:0000313|EMBL:ANC28632.1}; RN [1] {ECO:0000313|EMBL:ANC28632.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MERS-CoV/KOR/Seoul/014-2015 {ECO:0000313|EMBL:ANC28632.1}; RA Park D., Huh H.J., Kim Y.J., Son D.-S., Jeon H.-J., Im E.-H., Kim J.-W., RA Lee N.Y., Kang E.-S., Chung D.R., Choi S.S., Ahn J.-H., Peck K.R., RA Ki C.-S., Park W.-Y.; RT "Intra-patient heterogeneity of Middle East respiratory syndrome RT coronavirus."; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalytic subunit of viral RNA capping enzyme which catalyzes CC the RNA guanylyltransferase reaction for genomic and sub-genomic RNAs. CC The kinase-like NiRAN domain of NSP12 transfers RNA to the amino CC terminus of NSP9, forming a covalent RNA-protein intermediate. CC Subsequently, the NiRAN domain transfers RNA to GDP, forming the core CC cap structure GpppA-RNA. The NSP14 and NSP16 methyltransferases then CC add methyl groups to form functional cap structures. CC {ECO:0000256|ARBA:ARBA00034461}. 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: 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: 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 transcription/replication and prevents CC the simultaneous activation of host cell dsRNA sensors, such as CC MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'- CC polyuridines generated during replication of the poly(A) region of CC viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in CC which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O CC transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) CC (By similarity). If not degraded, poly(U) RNA would hybridize with CC poly(A) RNA tails and activate host dsRNA sensors. CC {ECO:0000256|ARBA:ARBA00025521}. 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 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. The kinase-like NiRAN domain CC of NSP12 transfers RNA to the amino terminus of NSP9, forming a CC covalent RNA-protein intermediate. Subsequently, the NiRAN domain CC transfers RNA to GDP, and forms the core cap structure GpppA-RNA. CC {ECO:0000256|ARBA:ARBA00034462}. 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=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 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 -!- 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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host CC cytoplasm, host perinuclear region {ECO:0000256|ARBA:ARBA00004407}. 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; KX034093; ANC28632.1; -; Genomic_RNA. 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'-exoribonuclease 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:0002151; F:G-quadruplex RNA binding; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IEA:UniProt. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro. DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-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:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0010506; P:regulation of autophagy; IEA:InterPro. DR GO; GO:0039657; P:suppression by virus of host gene expression; 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; cd21560; betaCoV-Nsp6; 1. DR CDD; cd21659; betaCoV_Nsp14; 1. DR CDD; cd21666; betaCoV_Nsp5_Mpro; 1. DR CDD; cd20762; capping_2-OMTase_Nidovirales; 1. DR CDD; cd21517; cv_beta_Nsp2_MERS-like; 1. DR CDD; cd21473; cv_Nsp4_TM; 1. DR CDD; cd17934; DEXXQc_Upf1-like; 1. DR CDD; cd21165; M_cv-Nsp15-like; 1. DR CDD; cd21563; Macro_cv_SUD-M_Nsp3-like; 1. DR CDD; cd21592; MERS-CoV-like_RdRp; 1. DR CDD; cd21161; NendoU_cv_Nsp15-like; 1. DR CDD; cd21171; NTD_alpha_beta_cv_Nsp15-like; 1. DR CDD; cd21523; SUD_C_MERS-CoV_Nsp3; 1. DR CDD; cd21467; Ubl1_cv_Nsp3_N-like; 1. DR CDD; cd21466; Ubl2_cv_PLpro_N_Nsp3-like; 1. DR CDD; cd21401; ZBD_cv_Nsp13-like; 1. DR Gene3D; 1.10.8.1190; -; 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; 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; 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; IPR046435; COV_N7_MTASE. DR InterPro; IPR046441; CoV_NSP12_RDRP. DR InterPro; IPR043608; CoV_NSP15_M. DR InterPro; IPR043606; CoV_NSP15_N. DR InterPro; IPR043613; CoV_NSP2_C. DR InterPro; IPR043611; CoV_NSP3_C. DR InterPro; IPR032505; CoV_NSP4_C. DR InterPro; IPR043612; CoV_NSP4_N. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR041679; DNA2/NAM7-like_C. DR InterPro; IPR022733; DPUP_SUD_C_bCoV. DR InterPro; IPR037227; EndoU-like. DR InterPro; 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; IPR044343; NSP13_1B_dom_CoV. DR InterPro; IPR027352; NSP13_ZBD_CoV-like. DR InterPro; IPR044315; NSP14_betaCoV. DR InterPro; IPR009466; NSP14_CoV. DR InterPro; IPR044330; NSP15_alpha_betaCoV_N. DR InterPro; IPR044327; NSP15_M_MERS. 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; IPR044388; NSP2_MERS-like. DR InterPro; IPR043615; NSP2_N_CoV. DR InterPro; IPR024375; NSP3_bCoV. DR InterPro; IPR032592; NSP3_NAB_bCoV. DR InterPro; IPR042570; NSP3_NAB_bCoV_sf. DR InterPro; IPR038400; NSP3_SUD-M_sf_bCoV. DR InterPro; IPR044382; NSP3_SUD_C_MERS-CoV. 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; IPR044350; RdRp_MERS-CoV-like. DR InterPro; IPR001205; RNA-dir_pol_C. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR InterPro; IPR009469; RNA_pol_N_CoV. DR InterPro; IPR018995; RNA_synth_NSP10_CoV. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR43788:SF8; DNA-BINDING PROTEIN SMUBP-2; 1. DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1. DR Pfam; PF13087; AAA_12; 1. DR Pfam; PF13604; AAA_30; 1. DR Pfam; PF16251; bCoV_NAB; 1. DR Pfam; PF11501; bCoV_NSP1; 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; 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; PF05409; Peptidase_C30; 1. DR Pfam; PF00680; RdRP_1; 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; 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; 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; PS51945; BCOV_NSP3E_NAB; 1. DR PROSITE; PS51952; COV_EXON_MTASE_COACT; 1. DR PROSITE; PS51954; COV_N7_MTASE; 1. DR PROSITE; PS51962; COV_NSP1; 1. DR PROSITE; PS51948; COV_NSP12_RDRP; 1. DR PROSITE; PS51960; COV_NSP15_NTD; 1. DR PROSITE; 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; 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Decay of host mRNAs by virus {ECO:0000256|ARBA:ARBA00022616}; 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|PROSITE-ProRule:PRU01298}; KW Host gene expression shutoff by virus {ECO:0000256|ARBA:ARBA00022995}; 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 {ECO:0000256|PROSITE- KW ProRule:PRU01308}; KW Inhibition of host interferon signaling pathway by virus KW {ECO:0000256|PROSITE-ProRule:PRU01308}; KW Lyase {ECO:0000256|ARBA:ARBA00023239}; KW Manganese {ECO:0000256|ARBA:ARBA00023211}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE- KW ProRule:PRU01299}; 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 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}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Viral immunoevasion {ECO:0000256|PROSITE-ProRule:PRU01308}; KW 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 2175..2195 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2307..2325 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2337..2362 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2756..2777 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3024..3049 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3061..3092 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3112..3138 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3564..3582 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3594..3613 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3620..3638 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3669..3687 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3694..3710 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3730..3752 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 3764..3786 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 25..149 FT /note="CoV Nsp1 globular" FT /evidence="ECO:0000259|PROSITE:PS51962" FT DOMAIN 165..193 FT /note="BetaCoV Nsp1 C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51963" FT DOMAIN 856..966 FT /note="Ubiquitin-like" FT /evidence="ECO:0000259|PROSITE:PS51943" FT DOMAIN 1278..1404 FT /note="Macro" FT /evidence="ECO:0000259|PROSITE:PS51941" FT DOMAIN 1404..1477 FT /note="DPUP" FT /evidence="ECO:0000259|PROSITE:PS51942" FT DOMAIN 1482..1537 FT /note="Ubiquitin-like" FT /evidence="ECO:0000259|PROSITE:PS51944" FT DOMAIN 1552..1823 FT /note="Peptidase C16" FT /evidence="ECO:0000259|PROSITE:PS51124" FT DOMAIN 1837..1954 FT /note="Nucleic acid-binding" FT /evidence="ECO:0000259|PROSITE:PS51945" FT DOMAIN 3151..3247 FT /note="Nsp4C" FT /evidence="ECO:0000259|PROSITE:PS51946" FT DOMAIN 3248..3553 FT /note="Peptidase C30" FT /evidence="ECO:0000259|PROSITE:PS51442" FT DOMAIN 3846..3928 FT /note="RdRp Nsp7 cofactor" FT /evidence="ECO:0000259|PROSITE:PS51949" FT DOMAIN 3929..4127 FT /note="RdRp Nsp8 cofactor" FT /evidence="ECO:0000259|PROSITE:PS51950" FT DOMAIN 4128..4237 FT /note="Nsp9 ssRNA-binding" FT /evidence="ECO:0000259|PROSITE:PS51951" FT DOMAIN 4238..4377 FT /note="ExoN/MTase coactivator" FT /evidence="ECO:0000259|PROSITE:PS51952" FT DOMAIN 4383..4639 FT /note="NiRAN" FT /evidence="ECO:0000259|PROSITE:PS51947" FT DOMAIN 4743..5310 FT /note="Nsp12 RNA-dependent RNA polymerase" FT /evidence="ECO:0000259|PROSITE:PS51948" FT DOMAIN 4990..5152 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT DOMAIN 5311..5394 FT /note="CV ZBD" FT /evidence="ECO:0000259|PROSITE:PS51653" FT DOMAIN 5567..5923 FT /note="(+)RNA virus helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51657" FT DOMAIN 5980..6195 FT /note="ExoN" FT /evidence="ECO:0000259|PROSITE:PS51953" FT DOMAIN 6204..6432 FT /note="N7-MTase" FT /evidence="ECO:0000259|PROSITE:PS51954" FT DOMAIN 6433..6493 FT /note="Nsp15 N-terminal oligomerization" FT /evidence="ECO:0000259|PROSITE:PS51960" FT DOMAIN 6494..6616 FT /note="AV-Nsp11N/CoV-Nsp15M" FT /evidence="ECO:0000259|PROSITE:PS51961" FT DOMAIN 6633..6772 FT /note="NendoU" FT /evidence="ECO:0000259|PROSITE:PS51958" FT DOMAIN 6777..7071 FT /note="Nidovirus-type SAM-dependent 2'-O-MTase" FT /evidence="ECO:0000259|PROSITE:PS51955" FT REGION 6318..6332 FT /note="GpppA-binding" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299" FT ACT_SITE 5998 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298" FT ACT_SITE 6000 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298" FT ACT_SITE 6099 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298" FT ACT_SITE 6176 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298" FT ACT_SITE 6181 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298" FT ACT_SITE 6663 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303" FT ACT_SITE 6678 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303" FT ACT_SITE 6718 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303" FT BINDING 6239..6245 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299" SQ SEQUENCE 7078 AA; 790280 MW; 1953E5C22387197F CRC64; MSFVAGVIAQ GARGTYRAAL NSEKHQDHVS LTVPLCGSGN LVEKLSPWFM DGENAYEVVK AMLLKKEPLL YVPIRLAGHT RHLPGPRVYL VERLIACENP FMVNQLAYSS SANGSLVGTT LQGKPIGMFF PYDIELVTGK QNILLRKYGR GGYHYTPVHY ERDNTSCPEW MDDFEADPKG KYAQNLLKKL IGGDVTPVDQ YMCGVDGKPI SAYAFLMAKD GITKLADVEA DVAARADDEG FITLKNNLYR LVWHVERKDV PYPKQSIFTI NSVVQKDGVE NTPPHYFTLG CKILTLTPRN KWSGVSDLSL KQKLLYTFYG KESLENPTYI YHSAFIECGS CGNDSWLTGN AIQGFACGCG ASYTANDVEV QSSGMIKPNA LLCATCPFAK GDSCSSNCKH SVAQLVSYLS ERCNVIADSK SFTLIFGGVA YAYFGCEEGT MYFVPRAKSV VSRIGDSIFT GCTGSWNKVT QIANMFLEQT QHSLNFVGEF VVNDVVLAIL SGTTTNVDKI RQLLKGVTID KLRDYLADYD VAVTAGPFMD NAINVGGTGL QYAAITAPYV VLTGLGESFK KVATIPYKVC NSVKDTLTYY AHSVLYRVFP YDMDSGVSSF SELLFDCVDL SVASTYFLVR LLQDKTGDFM STIITSCQTA VSKLLDTCFE ATEATFNFLL DLAGLFRIFL RNAYVYTSQG FVVVNGKVST LVKQVLDLLN KGMQLLHTKV SWAGSNISAV IYSGRESLIF PSGTYYCVTT KAKSVQQDLD VILPGEFSKK QLGLLQPTDN STTVSVTVSS NMVETVVGQL EQTNMHSPDV IVGDYVIISE KLFVRSKEED GFAFYPACTN GHAVPTLFRL KGGAPVKKVA FGGDQVHEVA AVRSVTVEYN IHAVLDTLLA SSSLRTFVVD KSLSIEEFAD VVKEQVSDLL VKLLRGMPIP DFDLDDFIDA PCYCFNAEGD ASWSSTMIFS LHPVXXXXXX XXXEASGLEE GESECISETS TEQVDVSHEV SDDEWAAAVD EAFPLDEAED VTEXXXXXXX XXXXPVEDIA QVVIADTLQE TPVVSDTVEV PPQVVKLPSE PQTIQPEVKE VAPVYEADTE QTQSVTVKPK RLRKKRNVDP LSNFEHKVIT ECVTXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXG PLQVGDXXXX XXXXXXXNIL HVVGXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XREAKTRVLV VVNSQDVYKS LTIVDIPQSL TFSYDGLRGA IRKAKDYGFT VXXXXDNSAN TKVLRNKGVD YTKKFLTVDG VQYYCYTSKD TLDDILQQAN KSVGIISMPL GYVSHGLDLI QAGSVVRRVN VPYVCLLANK EQEAILMSED VKLNPSEDFI KHVRTNGGYN SWHLVEGELL VQDLRLNKLL HWSDQTICYK DSVFYVVKNS TAFPFETLSA CRAYLDSRTT QQLTIEVLVT VDGVNFRTVV LNNKNTYRSQ LGCVFFNGAD ISDTIPDEKQ NGHSLYLADN LTADETKALK ELYGPVDPTF LHRFYSLKAA VHKWKMVVCD KVRSLKLSDN NCYLNAVIMT LDLLKDIKFV IPALQHAFMK HKGGDSTDFI ALIMAYGNCT FGAPDDASRL LHTVLAKAEL CCSARMVWRE WCNVCGIKDV VLQGLKACCY VGVQTVEDLR ARMTYVCQCG GERHRQIVEH TTPWLLLSGT PNEKLVTTST APDFVAFNVF QGIETAVGHY VHACLKGGLI LKFDSGTVSK TSDWKCKVTD VLFPGQKYSS DCNVVRYSLD GNFRTEVDPD LSAFYVKDGK YFTSEPPVTY SPATILAGSV YTNSCLVSSD GQPGGDAISL SFNNLLGFDS SKPVTKKYTY SFLPKEDGDV LLAEFDTYDP IYKNGAMYKG KPILWVNKAS YDTNLNKFNR ASLRQIFDVA PIELENKFTP LSVASTPVEP PTVDVVALQQ EMTIVKCKGL NKPFVKDNVS FVVDDSGTPV VEYLSKEDLH TLYVDPKYQV IVLKDNVLSS MLRLHTVESG DINVVAASGS LTRKVKLLFR ASFYFKEFAT RTFTATTAVG SCIKSVVRHL GVTKGILTGC FSFVKMLFIL PLAYFSDSKL GTTEVKVSAL KTAGVVTGNV VKQCCTAAVD LSMDKLRRVD WKSTLRLLLM LCTTMVLLSS VYHLYVFNQV LSSDVMFEDA QGLKKFYKEV RAYLGISSAC DGLASAYRAN SFDVPTFCAN RSAMCNWCLI SQDSITHYPA LKMVQTHLSH YVLNIDWLWF AFETGLAYML YTSAFNWLLL AGTLHYFFAQ TSIFVDWRSY NYAVSSAFWL FTHIPMAGLV RMYNLLACLW LLRKFYQHVI NGCKDTACLL CYKRNRLTRV EASTVVCGGK RTFYITANGG ISFCRRHNWN CVDCDIAGVG NTFICEEVAN DLTTALRRPI NATDRSHYYV DSVTVKETVV QFNYRRDGQP FYERFPLCAF TNLDKLKFKE VCKTTTGIPE YNFIIYDSSD RGQESLARSA CVYYSQVLCK SILLVDSSLV TSVGDSSEIA TKMFDSFVNS FVSLYNVTRD KLEKLISTAR DGVRRGDNFH SVLTTFIDAA RGPAGVESDV ETNEIVDSVQ YAHKHDIQIT NESYNNYVPS YVKPDSVSTS DLGSLIDCNA ASVNQIVLRN SNGACIWNAA AYMKLSDALK RQIRIACRKC NLAFRLTTSK LRANDNILSV RFTANKIVGG APTWFNVLRD FTLKGYVLAT IIVFLCAVLM YLCLPTFSMV PVEFYEDRIL DFKVLDNGII RDVNPDDKCF ANKHRSFTQW YHEHVGGVYD NSITCPLTVA VIAGVAGARI PDVPTTLAWV NNQIIFFVSR VFANTGSVCY TPIDEIPYKS FSDSGCILPS ECTMFRDAEG RMTPYCHDPT VLPGAFAYSQ MRPHVRYDLY DGNMFIKFPE VVFESTLRIT RTLSTQYCRF GSCEYAQEGV CITTNGSWAI FNDHHLNRPG VYCGSDFIDI VRRLAVSLFQ PITYFQLTTS LVLGIGLCAF LTLLFYYINK VKRAFADYTQ CAVIAVVAAV LNSLCICFVA SIPLCIVPYT ALYYYATFYF TNEPAFIMHV SWYIMFGPIV PIWMTCVYTV AMCFRHFFWV LAYFSKKHVE VFTDGKLNCS FQDAASNIFV INKDTYAALR NSLTNDAYSR FLGLFNKYKY FSGAMETAAY REAAACHLAK ALQTYSETGS DLLYQPPNCS ITSGVLQSGL VKMSHPSGDV EACMVQVTCG SMTLNGLWLD NTVWCPRHVM CPADQLSDPN YDALLISMTN HSFSVQKHIG APANLRVVGH AMQGTLLKLT VDVANPSTPA YTFTTVKPGA AFSVLACYNG RPTGTFTVVM RPNYTIKGSF LCGSCGSVGY TKEGSVINFC YMHQMELANG THTGSAFDGT MYGAFMDKQV HQVQLTDKYC SVNVVAWLYA AILNGCAWFV KPNRTSVVSF NEWALANQFT EFVGTQSVDM LAVKTGVAIE QLLYAIQQLY TGFQGKQILG STMLEDEFTP EDVNMQIMGV VMQSGVRKVT YGTAHWLFAT LVSTYVIILQ ATKFTLWNYL FETIPTQLFP LLFVTMAFVM LLVKHKHTFL TLFLLPVAIC LTYANIVYEP TTPISSALIA VANWLAPTNA YMRTTHTDIG VYISMSLVLV IVVKRLYNPS LSNFALALCS GVMWLYTYSI GEASSPIAYL VFVTTLTSDY TITVFVTVNL AKVCTYAIFA YSPQLTLVFP EVKMILLLYT CLGFMCTCYF GVFSFLNLKL RAPMGVYDFK VSTQEFRFMT ANNLTAPRNS WEAMALNFKL IGIGGTPCIK VAAMQSKLTD LKCTSVVLLS VLQQLHLEAN SRAWAFCVKC HNDILAATDP SEAFEKFVSL FATLMTFSGN VDLDALASDI FDTPSVLQAT LSEFSHLATF AELEAAQKAY QEAMDSGDTS PQVLKALQKA VNIAKNAYEK DKAVARKLER MADQAMTSMY KQARAEDKKA KIVSAMQTML FGMIKKLDND VLNGIISNAR NGCIPLSVIP LCASNKLRVV IPDFTVWNQV VTYPSLNYAG ALWDITVINN VDNEIVKSSD VVDSNENLTW PLVLECTRAS TSAVKLQNNE IKPSGLKTMV VSAGQEQTNC NTSSLAYYEP VQGRKMLMAL LSDNAYLKWA RVEGKDGFVS VELQPPCKFL IAGPKGPEIR YLYFVKNLNN LHRGQVLGHI AATVRLQAGS NTEFASNSSV LSLVNFTVDP QKAYLDFVNA GGAPLTNCVK MLTPKTGTGI AISVKPESTA DQETYGGASV CLYCRAHIEH PDVSGVCKYK GKFVQIPAQC VRDPVGFCLS NTPCNVCQYW IGYGCNCDSL RQVALPQSKD SNFLNRVRGS IVNARIEPCS SGLSTDVVFR AFDICNYKAK VAGIGKYYKT NTCRFVELDD QGHHLDSYFV VKRHTMENYE LEKHCYDLLR DCDAVAPHDF FIFDVDKVKT PHIVRQRLTE YTMMDLVYAL RHFDQNSEVL KAILVKYGCC DVTYFENKLW FDFVENPSVI GVYHKLGERV RQAILNTVKF CDHMVKAGLV GVLTLDNQDL NGKWYDFGDF VITQPGSGVA IVDSYYSYLM PVLSMTDCLA AETHRDCDFN KPLIEWPLTE YDFTDYKVQL FEKYFKYWDQ TYHANCVNCT DDRCVLHCAN FNVLFAMTMP KTCFGPIVRK IFVDGVPFVV SCGYHYKELG LVMNMDVSLH RHRLSLKELM MYAADPAMHI ASSNAFLDLR TSCFSVAALT TGLTFQTVRP GNFNQDFYDF VVSKGFFKEG SSVTLKHFFF AQDGNAAITD YNYYSYNLPT MCDIKQMLFC MEVVNKYFEI YDGGCLNASE VVVNNLDKSA GHPFNKFGKA RVYYESMSYQ EQDELFAMTK RNVIPTMTQM NLKYAISAKN RARTVAGVSI LSTMTNRQYH QKMLKSMAAT RGATCVIGTT KFYGGWDFML KTLYKDVDNP HLMGWDYPKC DRAMPNMCRI FASLILARKH GTCCTTRDRF YRLANECAQV LSEYVLCGGG YYVKPGGTSS GDATTAYANS VFNILQATTA NVSALMGANG NKIVDKEVKD MQFDLYVNVY RSTSPDPKFV DKYYAFLNKH FSMMILSDDG VVCYNSDYAA KGYIAGIQNF KETLYYQNNV FMSEAKCWVE TDLKKGPHEF CSQHTLYIKD GDDGYFLPYP DPSRILSAGC FVDDIVKTDG TLMVERFVSL AIDAYPLTKH EDIEYQNVFW VYLQYIEKLY KDLTGHMLDS YSVMLCGDNS AKFWEEAFYR DLYSSPTTLQ AVGSCVVCHS QTSLRCGTCI RRPFLCCKCC YDHVIATPHK MVLSVSPYVC NAPGCGVSDV TKLYLGGMSY FCVDHRPVCS FPLCANGLVF GLYKNMCTGS PSIVEFNRLA TCDWTESGDY TLANTTTEPL KLFAAETLRA TEEASKQSYA IATIKEIVGE RQLLLVWEAG KSKPPLNRNY VFTGYHITKN SKVQLGEYIF ERIDYSDAVS YKSSTTYKLT VGDIFVLTSH SVATLTAPTI VNQERYVKIT GLYPTITVPE EFASHVANFQ KSGYSKYVTV QGPPGTGKSH FAIGLAIYYP TARVVYTACS HAAVDALCEK AFKYLNIAKC SRIIPAKARV ECYDRFKVNE TNSQYLFSTI NALPETSADI LVVDEVSMCT NYDLSIINAR IKAKHIVYVG DPAQLPAPRT LLTRGTLEPE NFNSVTRLMC NLGPDIFLSM CYRCPKEIVS TVSALVYNNK LLAKKELSGQ CFKILYKGNV THDASSAINR PQLTFVKNFI TANPAWSKAV FISPYNSQNA VARSMLGLTT QTVDSSQGSE YQYVIFCQTA DTAHANNINR FNVAITRAQK GILCVMTSQA LFESLEFTEL SFTNYKLQSQ IVTGLFKDCS RETSGLSPAY APTYVSVDDK YKTSDELCVN LNLPANIPYS RVISRMGFKL DATVPGYPKL FITREEAVRQ VRSWIGFDVE GAHASRNACG TNVPLQLGFS TGVNFVVQPV GVVDTEWGNM LTGIAARPPP GEQFKHLVPL MHKGAAWPIV RRRIVQMLSD TLDKLSDYCT FVCWAHGFEL TSASYFCKIG KEQKCCMCNR RAAAYSSPLQ SYACWTHSCG YDYVYNPFFV DVQQWGYVGN LATNHDRYCS VHQGAHVASN DAIMTRCLAI HSCFIERVDW DIEYPYISHE KKLNSCCRIV ERNVVRAALL AGSFDKVYDI GNPKGIPIVD DPVVDWHYFD AQPLTRKVQQ LFYTEDMASR FADGLCLFWN CNVPKYPNNA IVCRFDTRVH SEFNLPGCDG GSLYVNKHAF HTPAYDVSAF RDLKPLPFFY YSTTPCEVHG NGSMIEDIDY VPLKSAVCIT ACNLGGAVCR KHATEYREYM EAYNLVSASG FRLWCYKTFD IYNLWSTFTK VQGLENIAFN VVKQGHFIGV EGELPVAVVN DKIFTKSGVN DICMFENKTT LPTNIAFELY AKRAVRSHPD FKLLHNLQAD ICYKFVLWDY ERSNIYGTAT IGVCKYTDID VNSALNICFD IRDNGSLEKF MSTPNAIFIS DRKIKKYPCI VGPDYAYFNG AIIRDSDVVK QPVKFYLYKK VNNEFIDPTE CIYTQSRSCS DFLPLSDMEK DFLSFDSDVF IKKYGLENYA FEHVVYGDFS HTTLGGLHLL IGLYKKQQEG HIIMEEMLKG SSTIHNYFIT ETNTAAFKAV CSVIDLKLDD FVMILKSQDL GVVSKVVKVP IDLTMIEFML WCKDGQVQTF YPRLQASADW KPGHAMPSLF KVQNVNLERC ELANYKQSIP MPRGVHMNIA KYMQLCQYLN TCTLAVPANM RVIHFGAGSD KGIAPGTSVL RQWLPTDAII IDNDLNEFVS DADITLFGDC VTVRVSQQVD LVISDMYDPT TKNVTGSNES KALFFTYLCN LINNNLALGG SVAIKITEHS WSVELYELMG KFAWWTVFCT NANASSSEGF LLGINYLGTI KENIDGGAMH ANYIFWRNST PMNLSTYSLF DLSKFQLKLK GTPVLQLKES QINELVISLL SQGKLLIRDN DTLSVSTDVL VNTYRKLR //