ID A3EXI1_BCHK9 Unreviewed; 6923 AA.
AC A3EXI1;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=ORF1ab polyprotein {ECO:0000256|PROSITE-ProRule:PRU01344};
GN Name=orf1ab {ECO:0000313|EMBL:ABN10926.1};
OS Bat coronavirus HKU9-3.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Nobecovirus; Bat coronavirus HKU9.
OX NCBI_TaxID=424369 {ECO:0000313|EMBL:ABN10926.1, ECO:0000313|Proteomes:UP000115362};
RN [1] {ECO:0000313|EMBL:ABN10926.1, ECO:0000313|Proteomes:UP000115362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BF_493I {ECO:0000313|EMBL:ABN10926.1};
RX PubMed=17121802; DOI=10.1128/JVI.02182-06;
RA Woo P.C.Y., Wang M., Lau S.K.P., Xu H.F., Poon R.W.S., Guo R., Wong B.H.L.,
RA Gao K., Tsoi H.-W., Huang Y., Li K.S.M., Lam C.S.F., Chan K.-H.,
RA Zheng B.-J., Yuen K.-Y.;
RT "Comparative analysis of twelve genomes of three novel group 2c and group
RT 2d coronaviruses reveals unique group and subgroup features.";
RL J. Virol. 81:1574-1585(2007).
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}.
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DR EMBL; EF065515; ABN10926.1; -; Genomic_RNA.
DR Proteomes; UP000115362; 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-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: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: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-KW.
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-KW.
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; cd21596; batCoV-HKU9-like_RdRp; 1.
DR CDD; cd21560; betaCoV-Nsp6; 1.
DR CDD; cd21722; betaCoV_Nsp13-helicase; 1.
DR CDD; cd21659; betaCoV_Nsp14; 1.
DR CDD; cd21518; betaCoV_Nsp2_HKU9-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; cd21877; HKU9-like_Nsp1; 1.
DR CDD; cd21813; HKU9-like_Nsp3_betaSM; 1.
DR CDD; cd21825; HKU9-like_Nsp3_NAB; 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; cd21689; stalk_CoV_Nsp13-like; 1.
DR CDD; cd21537; SUD_C_HKU9_CoV_Nsp3; 1.
DR CDD; cd21715; TM_Y_HKU9-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; 3.40.220.10; 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; 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; 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; 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; 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; IPR021590; NSP1_glob_bCoV.
DR InterPro; IPR044386; NSP2_HKU9-like.
DR InterPro; IPR043615; NSP2_N_CoV.
DR InterPro; IPR024375; NSP3_bCoV.
DR InterPro; IPR047567; NSP3_G2M_bCoV.
DR InterPro; IPR032592; NSP3_NAB_bCoV.
DR InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
DR InterPro; IPR044352; Nsp3_SUD_C_HKU9_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; IPR044349; RdRp_batCoV_HKU9-like.
DR InterPro; IPR046441; RdRp_CoV.
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; 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; PF13604; AAA_30; 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; 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; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 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.
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};
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 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};
KW Inhibition of host interferon signaling pathway by virus
KW {ECO:0000256|ARBA:ARBA00022830};
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};
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 2076..2094
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2158..2174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2181..2200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2615..2636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2884..2902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2914..2935
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2966..2991
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3413..3433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3445..3464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3471..3490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3510..3531
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3580..3600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3612..3635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..131
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000259|PROSITE:PS51962"
FT DOMAIN 177..431
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51989"
FT DOMAIN 432..644
FT /note="CoV Nsp2 middle"
FT /evidence="ECO:0000259|PROSITE:PS51990"
FT DOMAIN 646..772
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51991"
FT DOMAIN 775..885
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS51943"
FT DOMAIN 948..1110
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1212..1336
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51941"
FT DOMAIN 1341..1413
FT /note="DPUP"
FT /evidence="ECO:0000259|PROSITE:PS51942"
FT DOMAIN 1419..1474
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS51944"
FT DOMAIN 1488..1753
FT /note="Peptidase C16"
FT /evidence="ECO:0000259|PROSITE:PS51124"
FT DOMAIN 1766..1866
FT /note="Nucleic acid-binding"
FT /evidence="ECO:0000259|PROSITE:PS51945"
FT DOMAIN 1874..2007
FT /note="G2M"
FT /evidence="ECO:0000259|PROSITE:PS51994"
FT DOMAIN 2502..2605
FT /note="CoV Nsp3 Y"
FT /evidence="ECO:0000259|PROSITE:PS51992"
FT DOMAIN 3002..3098
FT /note="Nsp4C"
FT /evidence="ECO:0000259|PROSITE:PS51946"
FT DOMAIN 3099..3404
FT /note="Peptidase C30"
FT /evidence="ECO:0000259|PROSITE:PS51442"
FT DOMAIN 3695..3777
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51949"
FT DOMAIN 3778..3977
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51950"
FT DOMAIN 3978..4089
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS51951"
FT DOMAIN 4090..4228
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000259|PROSITE:PS51952"
FT DOMAIN 4234..4489
FT /note="NiRAN"
FT /evidence="ECO:0000259|PROSITE:PS51947"
FT DOMAIN 4494..4592
FT /note="Nsp12 Interface"
FT /evidence="ECO:0000259|PROSITE:PS52000"
FT DOMAIN 4593..5160
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000259|PROSITE:PS51948"
FT DOMAIN 4840..5002
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT DOMAIN 5161..5244
FT /note="CV ZBD"
FT /evidence="ECO:0000259|PROSITE:PS51653"
FT DOMAIN 5407..5773
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51657"
FT DOMAIN 5833..6051
FT /note="ExoN"
FT /evidence="ECO:0000259|PROSITE:PS51953"
FT DOMAIN 6060..6291
FT /note="N7-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51954"
FT DOMAIN 6292..6352
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000259|PROSITE:PS51960"
FT DOMAIN 6353..6471
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000259|PROSITE:PS51961"
FT DOMAIN 6488..6625
FT /note="NendoU"
FT /evidence="ECO:0000259|PROSITE:PS51958"
FT DOMAIN 6630..6923
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51955"
FT REGION 894..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 6175..6189
FT /note="GpppA-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
FT COMPBIAS 894..929
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 5851
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5853
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5952
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6032
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6037
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6518
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6532
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6571
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT BINDING 6095..6101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
SQ SEQUENCE 6923 AA; 769750 MW; BE243295E56A33D1 CRC64;
MEGVPGPSKL RSMVTITLKW IDPNIMPSVT GWDMPMCEAL EIVKDELRKP EPDLVFVPKY
LCHTPLIGRN RVVITDATYR TTVLGWIPIR ELAYDESETR YGRSGTYGVL LPMQDSKYIM
GSIDIDMRKY GAGAGSDRPE PMLWDGFVDL PRSQKQYLDY PDNCRPTKPK AKRGGNVYMS
DQYGFDNNGN LVKPVLELLG GIKPDLTLEK LTLALSEYRN SDGYDLPGGF VRVAVSVIRK
PVPVVKQTIF TVQGVVEQHV EGFYYPYSTM SVVKHTKPRS DKPLGKTVES IMLSLYGTSG
YSPATPVVRL RCSYCDFYGW VPPRDMGTVV CSCGAEFQLT SACVDAESAG AIKPGCVMLL
DRSPGMRLIP GNRIYVAFGG AIWSPIGTVN GVSVWVPRSY SVVAGDHSGA VGSCDVTTMN
KEIMAFIIEG FKIDEDTLEK PSCATFIANM QCDEKTPVVH TVETIVQLCL DNKVVLGNHP
LPDDEFHPVI VGLNYYTQRT LWYAALNSKT FAAMRDYVCR EEERLRAFCG RAFIPVGAGL
HMAYQTGKVT LTSAYHVLEA ALTKTKDAFG GAAAVVVDLL KPVMDWVLNK MSLAKGIWLR
YAEAILALFR AQFTFIEGKF HFVRDTLNSS CGALRDLLSA LLSKLLTSAR WAGCKVEAVY
TGTYHYFAKF GVVSELQIRA KALGVLLTPR QQKMEVEVLE GKADAPVELT SLELEELHGT
LEEVFGYSDL GLVKGSLVTM ASKVFVRTDD GVLYRYVKSG GVLLKAFRLR GGGPPKVTFG
DEEVRTIPNT VTVNFSYDIC EGLNEILGKV MAPFQVEEGT DLADLACVVQ QAVHEKLSEL
LSECPAELRP INLEEFSEAE CYVYSRDYEK VLESEMYFSL EDVTPVEDDV SEADIIEEDE
VDQTTDSDDQ WLGDESPSED VEQIAADEQE SSDDPGLPLE SVVVSNQLEG PAGYKQLTEC
VYIKCADIVQ EARAYKYAVL VNAANVNLHH GGGVAGALNR ATGNAMQKES NDYTRANGPL
QPGGHVLLGA HGLANTGILH VVGPDKRLGQ DIKLLDSVYQ AYAGFDTVLT PLVSAGIFGF
TVEESLLSLV NNVSCKTYIV VYDRQLYERA LAVDVKPAPA PDTSTAALDW AAAVELQESD
APVVTQQACD VVSDTDVTED VTACMRDLLR RVVRQVKRDT RSLALPVAAT EVERPKEVPA
SDSAILKETT PLVDVVCLSF SAMLQRGKAQ GLLTPVVIDY PAFNKVLKRY EPKEGFYTFD
GQDFYGYSRD TPIEDVSKAL NALGRSLLMI PFGFIVNGQS LAVSAVSMRK LTVPHTVVLP
SESCVPLYRA YFNGSFNGDT TAVQDFVVDI LVNGVQTWDV IQTTCTVDRR VYKTVCKRGD
TFMCYDDTNL YAITGNVVLK FATVLKARAY LSTQPKVPET LIKVLTTVDG INYNTVLVSR
EQTYRAQIGT VFCDGRDYSD RRPTIADEGV HLFKQDNFSM EELQSMREYY GVEDPNIVAR
AMSVRKIVQQ WPYAVIDGRV LLAQRDSNCY VNVALSLLQD VDVTFTTPWV ARAYSALKGG
NPLPMAEVLI ALSKATPGEC DDAHMVLSTV LNHGTVDARR VMQTVCEVCG VSQFVFTGTD
ACTFYGSVML DDLYEPVSIV CACGRSAIRY VLEQRSPWLL MSHTPTQVPL DTSGNWQAAI
VFRGPVTAGH YMYAVNGTLI SVFDANTRKR TSDLKLPATD ILYGPTSFTS ASKVETYYLD
GVKRTTIDPD LSKYVKRGDY YFTAAPLDVV AAPKLVTPYD GFYLSSCQNA KLADEFNKAI
NATKQGPMKL LTVYPNTAGD VIAVVDDNVA VHPYGSLHMG KPVLFVNKPN TWKKLVPLLS
SLVVETTNKY TVLPVDPLPK GESTTKAVSV KATVPLYGLK SSMVLDGTTY VPGKKGDLLC
LRELTLTDLQ TFYVEGVQPF VILKASHLSK VLGLRVSDTK LHVNRLSAGL VYAYAATRCT
ARVTKTVLGD VVTRVVRKTA DFVRGTNPGA KCVGLLCLFY QLLVRCWLVV TKPPIFKVSG
IVAYNTGCGV TSCVLNYLRQ RCGNISWTRL IKWLRYVLYV WFVWTCLTIC GVWLSEPYAP
DWLNRVRSFI GLVMPCDYVL VNETGTGWLH HLCMAGMDNL DYPALRMQQH RYGSPYDYTY
ILMLLEAFLA YLLYTPALPI VGVLAVLHLV VLYLPIPLGN SWLVVFLYYL IRLVPFTSML
RMYIVMAFLW LCYKGFLHVR YGCNNVACLM CYKKNVARRI ECSTVVNGVK RMFYVNANGG
THFCTKHNWN CVSCDTYTVD STFISRQVAL DLSAQFKRPI LPTDEAYYEV TSVEVRNGYV
YCYFDSDGQR SYERFPMDAF TNVSKLHYAE LKGAAPAFNV LVFDATNRIE ENAVKAAAIY
FAQLACKPIL LVDKRMVGVV GDDATIAKAM FEAYAQNYLL KYNIAMDKVK HLYSTALQQI
SSGMTVEAVL KVFVGSTRSE AKDLESDVDT NDLVSCMRLC HQEGWDWTTD SWNNLVPTYI
KQDTLSTLEV GQFMTANARY VNANVAKGAA VNLVWRYADF VKLSESVRRQ LRVAARKTGL
NLLVTTSSLK ADVPCMVTPF KIIGGHRRLV PWKRVLLHVF MLIVVLNPQW FTPWYIMRPI
NYNVVDFRVI DNAVIRDITP ADQCFANKFS TFDAWYSNRY GSYVNSRSCP MVVGVVSDVV
GNLVPGLPAR FLRVGATLLP LVNYGLGAVG SVCYTPHHSI SYDVFETSAC VLAATCTLFS
SANGELMPYC ADSALIQNAS RYDTLNPHVM YPFYEQFGYI RFPEVISAGV HIVKTMAMEY
CKVGRCDVSE AGLCMSLQPR WVVNNAYFRQ QPGVYCGTGT LDLFLNMLLP IFTPVGAVDI
TTSILMGALL AVVVSMSLYY LLRFRRAFGD YSGVIFTNIL AFVLNVIVLC LEGPYPMLPS
IYAMAFLYAT CYFGSDIACM MHVSFLIMFV GVVPLWVTAL YIVVVLSRHI LWFTSLCTKR
TVQVGDLAFH SFQDAALQTF MLDKEVFLRL KREISSDAYA KYLAMYNKYK YYSGPMDTAA
YREAACSHLV MALEKYSNGG GDTIYQPPRC SVASAALQAG LARMAHPSGL VEPCIVKVSY
GSMTLNGIWL DNFVICPRHV MCSRDELTNP DYARLSMRAA NYDFHVAQNG HNIRVVGHVM
EGSLLKLTVD VNNPKTPSYS FIRVSTGQAM SLLACYDGVP TGVYTCTLRS SGTLRASFLC
GSCGSPGFVM NGKEVQFCYL HQLELPNGTH TGTDFSGVFY GPFEDKQVPQ LAAPDNTITV
NVLAWLYAAV LSGENWFLTK SSISPAEFNN CAIKYMCQSV TSESLQVLQP LAAKTGVSVE
RMLSALKVLL SAGFCGRTIM GSCALEDEHT PYDIGRQMLG VKLQGKFQSA CKWTLQWFSI
VFILTVLILL QLAQWTFVGA LPLSLLLPLI GFLACCVGAV SLLVKHKHAY LTVYLLPVAM
VTAYYNFQYT PEGVQGYLLS VYNYVNPGRI DVVGTDIVTM LIISVACTLL SVRMVRTDAY
SRVWYVCTAI GWLYNCWTGS PDTVAISYLT FMVSVFTNYT GVACVSLYAA QLMTWVLIYL
DPAILLLYGK FRCVLVCYLI VGYFCTCYFG VFNLINRLFR CTLGNYEYVV SSQELRYMNS
HGLLPPTTSW QALMLNMKLA GIGGIPIYKV STIQSNMTDL KCTSVVLLSV LQQLRVESSS
KLWALCVKLH NEILASSSPT EAFEAFVSLL SVLLSLPGAI NLDELCGSIL ENNSVLQAVA
SEFSNLSSYV DYENAQKAYD TAVATGAPAS TVNALKKAMN IAKSVLDKDV ATTRKLERMS
ELAMTAMYKQ ARAEDRRSKV TAAMQTMLFN MIRRLDSDAL SNILNNARNG VVPLGVIPRT
SANKLLLVVP DFSVYTATIT MPTLTYAGSA WDVMQVADAD GKPVNATDIT RENSVNLAWP
LVVTAQRQQA TSPVKLQNNE LMPQSVKRMN VVAGVSQTAC VTDVVAYYNA TKEGRHVMAI
LADTDGLAYA KVEKSTGDGF VILELEPPCK FMVDTPKGPA LKYLYFTKGL KNLCRGTVLG
TLACTVRLHA GSATEVSSNS SILSLCAFSV DPEATYKDYL DNGGSPIGNC VKMLTPHTGT
GLAITAKPDA NIDQESFGGA SCCLYCRCHI EHPGASGVCK YKGKFVQIPI VGVNDPIGFC
IRNIVCAVCN MWQGYGCPCA SLREINLQAR DDCFLNRVRG TSGVARLVPL GSGVEPDIVL
RAFDICNTKV AGFGLHLKNN CCRYQELDVD GVQLDSYFVV KRHTESNYLL EQRCYEKLKD
CGVVARHDFF KFNIEGVMTP HVSRERLTKY TMADLVYSLR HFDNNNCDTL KEILVLRGCC
TSDYFDRADW YDPVENPDII RVYHKLGETV RNAVLSATKL ADAMVEQGLI GVLTLDNQDL
NGQWYDFGDF IEGPAGAGVA IMDTYYSLAM PVYTMTNMLA AESHIDGDLS KPKRVWDICT
YDYTQFKYSL FSKYFKHWDM QYHPNCVACA DDRCILHCAN FNILFSMVLP NTSFGPLVQK
IYVDGVPFVV STGYHYRELG VVMNQDVRQH AQRLSLRELL VYAADPAMHV AASNALADKR
TVCMSVAAMT TGVTFQTVKP GQFNEDFYNF ALKCGFFKEG STISFKHFFY AQDGNAAISD
YDYYRYNLPT MCDIKQLLFS LEVVDKYFEC YDGGCLQASQ VVVANYDKSA GFPFNKFGKA
RLYYESLSYA DQDELFAYTK RNVLPTITQM NLKYAISAKN RARTVAGVSI ASTMTNRQFH
QKMLKSIAAA RGASVVIGTT KFYGGWNRML RTLCEGVESP HLMGWDYPKC DRAMPNLLRI
FASLILARKH STCCNASERF YRLANECAQV LSEMVLCGGG FYVKPGGTSS GDSTTAYANS
VFNICQAVSA NLNTFLSIDG NKIYTTYVQE LQRRLYMGIY RSNTVDNELV LDYYNYLRKH
FSMMILSDDG VVCYNSDYAQ KGYVADIQGF KELLYFQNNV FMSEAKCWVE PDITKGPHEF
CSQHTMLVDM KGEQVYLPYP DPSRILGAGC FVDDLLKTDG TLMMERYVSL AIDAYPLTKH
SDPEYQNVFW CYLQYIKKLH EELTGHLLDT YSVMLASDNA SKYWEVDFYE NMYMESATLQ
SVGTCVVCNS QTSLRCGGCI RRPFLCCKCC YDHVVSTTHK LVLSVTPYVC NHPSCDVADV
TQLYLGGMSY YCREHRPPIS FPLCANGQVF GLYKNICTGS PDVADFNSLA TCDWSNSKDY
VLANTATERL KLFAAETLRA TEENAKQAYA SAVVKEVLSD RELVLSWETG KMRPPLNRNY
VFTGFHITKN SKVQLGEYIF EKGDYGDVVN YRSSTTYKLQ VGDYFVLTSH SVQPLSSPTL
LPQERYTKLV GLYPAMNVPE SFVSNVVHYQ RVGMARYTTV QGPPGTGKSH LSIGLALYYP
SAKIVYTACS HAAVDALCEK AHKNLPINRC SRIVPAKARV ECFSKFKVND VSAQYVFSTI
NALPETTADI LVVDEVSMCT NYDLSMINAR VRAKHIVYVG DPAQLPAPRT LLTKGTLAPE
HFNSVCRLMV AVGPDIFLAT CYRCPKEIVD TVSALVYDKK LKANKPTTGE CYKCYYKGSV
THDSSSAINK PQLGLVKEFL VKNPKWHNAV FISPYNSQNS VARRMLGLQT QTVDSSQGSE
FDYVIYCQTS DTAHALNVNR FNVAITRAKK GILCVMSDSN LYESLEFTPL DVNDYVKPKM
QADVTVGLFK DCAKAEPLGP AYAPTFVSVN DKFKLNESLC VYFDTTELQM PYNRLISKMG
FKFDLSIPGY SKLFITREQA IKEVRGWIGF DVEGAHACGP NIGTNLPLQI GFSTGVNFVV
TPSGYVDTES GSRLAQVVSK APPGDQFKHL IPLMRRGEPW SLVRKRIVEM LCDTLDGVSD
TVTFVTWAHG FELTTLHYFA KVGPERNCFM CPKRATLFSS VYGAYSCWSH HRHIGGADFV
YNPFLVDVQQ WGYVGNLQVN HDNVCDVHKG AHVASCDAIM TRCLAIHDCF CGEVNWDVEY
PIIANELAIN KACRSVQRVV LRAAVKALHI DTIYDIGNPK AIKVYGVNVS NWKFYDTKPV
VEGVKQLHYV YDVYKDQFKD GLAMFWNCNV DCYPHNALVC RFDTRVLSKL NLAGCNGGSF
YVNQHAFHTD AFNKNAFINL KPLPFFYYSD TACENATGLS TNYVSEVDYV PLKSNVCITR
CNLGGAVCKK HADEYRIFLE SYNTMVSAGF TLWVDKTFDI FNLWSTFVKL QSLENVAYNV
LKSGHFTPVA GELPVAIFND RLYIREDGVD KLLFTNNTCL PTNVAFELWA KRSVNVVPEV
KLLRNLGVTC TYNLVIWDYE HNAPLVPNTV GVCTYTDLIN LDDQVVLVDG RQLDAYSKFC
QLKNAVYFSP TKPKCISARG PMHASINGVV VEAPDKGTAF WYAVRKDGAF VQPADGYFTQ
SRTLDNFQPR TQLELDFLDL DESCFLDRYD LHDLGLEHIA YGQFEGTIGG LHLLLGAVRR
RRTANLVMET VLGTDTVTSY AVIDQPTAAN KQVCSVFDMV LDDFVALIKS QDRTVVSKVV
QCCLDFKMFR FMLWCKDGKI ATFYPQLQAK QDWKPGYSMP ALYKVQNAVL EPCLLHNYGQ
AVRLPTGTLM NVAKYTQLCQ YLNTCTLATP AKMRVIHFGA GSDKGVCPGT AVLKQWLPSD
ALLVDNDLDH CASDANFTFV GNCELFNTTY KWDLIISDMY DARTKQVSGV NTSKEGFFTY
LTGFIRGKLA LGGSVAIKLT EHSWSADLYA LMGHFNWWTC FCTSVNSSSS ETFLVGVNYL
ATGTLIDGDQ AHANYVFWRN STLMQLSSYS LYDLQRFQLR TKGTPVMALK EDQLNELVLN
LIRAGRLLVR DVGDIANIAF STC
//
