ID B6VDV9_9NIDO Unreviewed; 6264 AA.
AC B6VDV9;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=ORF1ab polyprotein {ECO:0000256|PROSITE-ProRule:PRU01344};
GN Name=orf1ab {ECO:0000313|EMBL:ACJ12034.1};
OS Bulbul coronavirus HKU11-934.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Deltacoronavirus; Buldecovirus; Bulbul coronavirus HKU11.
OX NCBI_TaxID=572288 {ECO:0000313|EMBL:ACJ12034.1, ECO:0000313|Proteomes:UP000161619};
RN [1] {ECO:0000313|EMBL:ACJ12034.1, ECO:0000313|Proteomes:UP000161619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18971277; DOI=10.1128/JVI.01977-08;
RA Woo P.C., Lau S.K., Lam C.S., Lai K.K., Huang Y., Lee P., Luk G.S.,
RA Dyrting K.C., Chan K.H., Yuen K.Y.;
RT "Comparative analysis of complete genome sequences of three avian
RT coronaviruses reveals a novel group 3c coronavirus.";
RL J. Virol. 83:908-917(2009).
CC -!- FUNCTION: Inhibits host translation by interacting with the 40S
CC ribosomal subunit. The nsp1-40S ribosome complex further induces an
CC endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them
CC for degradation. Viral mRNAs are not susceptible to nsp1-mediated
CC endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader
CC sequence and are therefore protected from degradation. By suppressing
CC host gene expression, nsp1 facilitates efficient viral gene expression
CC in infected cells and evasion from host immune response.
CC {ECO:0000256|ARBA:ARBA00002872}.
CC -!- FUNCTION: Methyltransferase that mediates mRNA cap 2'-O-ribose
CC methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine
CC cap is a prerequisite for binding of nsp16. Therefore plays an
CC essential role in viral mRNAs cap methylation which is essential to
CC evade immune system. {ECO:0000256|ARBA:ARBA00002840}.
CC -!- 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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment {ECO:0000256|ARBA:ARBA00004399}. Host cytoplasm, host
CC perinuclear region {ECO:0000256|ARBA:ARBA00004407}. Host endoplasmic
CC reticulum-Golgi intermediate compartment
CC {ECO:0000256|ARBA:ARBA00004452}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000256|ARBA:ARBA00008087, ECO:0000256|PROSITE-ProRule:PRU01294}.
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; FJ376619; ACJ12034.1; -; Genomic_RNA.
DR Proteomes; UP000161619; 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:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; 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; cd20762; capping_2-OMTase_Nidovirales; 1.
DR CDD; cd21512; cv_gamma-delta_Nsp2_IBV-like; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21561; deltaCoV-Nsp6; 1.
DR CDD; cd21903; deltaCoV_Nsp10; 1.
DR CDD; cd21721; deltaCoV_Nsp13-helicase; 1.
DR CDD; cd21657; deltaCoV_Nsp14; 1.
DR CDD; cd21668; deltaCoV_Nsp5_Mpro; 1.
DR CDD; cd21829; deltaCoV_Nsp7; 1.
DR CDD; cd21833; deltaCoV_Nsp8; 1.
DR CDD; cd21900; deltaCoV_Nsp9; 1.
DR CDD; cd21734; deltaCoV_PLPro; 1.
DR CDD; cd21590; deltaCoV_RdRp; 1.
DR CDD; cd21169; M_dcv_Nsp15-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR CDD; cd21172; NTD_deltaCoV_Nsp15-like; 1.
DR CDD; cd21689; stalk_CoV_Nsp13-like; 1.
DR CDD; cd21711; TM_Y_deltaCoV_Nsp3_C; 1.
DR CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR Gene3D; 1.10.8.1190; -; 1.
DR Gene3D; 3.40.50.11580; -; 1.
DR Gene3D; 6.10.140.2090; -; 1.
DR Gene3D; 1.10.150.420; Coronavirus nonstructural protein 4 C-terminus; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 1.10.1840.10; main proteinase (3clpro) structure, domain 3; 1.
DR Gene3D; 3.30.160.820; Nsp15 N-terminal domain-like; 1.
DR Gene3D; 1.10.8.370; nsp7 replicase; 1.
DR Gene3D; 3.30.70.3540; Nsp8 replicase, head domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.40.10.250; Replicase NSP9; 1.
DR Gene3D; 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; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR046440; AV_NSP11N_COV_NSP15M.
DR InterPro; IPR043608; CoV_NSP15_M.
DR InterPro; IPR043606; CoV_NSP15_N.
DR InterPro; IPR043611; CoV_NSP3_C.
DR InterPro; IPR047566; CoV_NSP3_Y3.
DR InterPro; IPR032505; CoV_NSP4_C.
DR InterPro; IPR043612; CoV_NSP4_N.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; 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; IPR044317; NSP14_deltaCoV.
DR InterPro; IPR044324; NSP15_M_deltaCoV.
DR InterPro; IPR043174; NSP15_middle_sf.
DR InterPro; IPR042515; NSP15_N_CoV.
DR InterPro; IPR044331; NSP15_N_deltaCoV.
DR InterPro; IPR044401; NSP15_NendoU_CoV.
DR InterPro; IPR009461; NSP16_CoV-like.
DR InterPro; IPR044383; NSP2_IBV-like.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR044307; NSP5_Mpro_deltaCoV.
DR InterPro; IPR043610; NSP6_CoV.
DR InterPro; IPR044365; NSP6_deltaCoV.
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; IPR043178; PLpro_thumb_sf_CoV.
DR InterPro; IPR046441; RdRp_CoV.
DR InterPro; IPR044354; RdRp_deltaCoV.
DR InterPro; IPR009469; RdRp_N_CoV.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF525; HELICASE SENATAXIN-RELATED; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF06471; CoV_ExoN; 1.
DR Pfam; PF06460; CoV_Methyltr_2; 1.
DR Pfam; PF09401; CoV_NSP10; 1.
DR Pfam; PF20631; CoV_NSP13_1B; 1.
DR Pfam; PF20633; CoV_NSP13_stalk; 1.
DR Pfam; PF20632; CoV_NSP13_ZBD; 1.
DR Pfam; PF19215; CoV_NSP15_C; 1.
DR Pfam; PF19216; CoV_NSP15_M; 1.
DR Pfam; PF19219; CoV_NSP15_N; 1.
DR Pfam; PF19218; CoV_NSP3_C; 1.
DR Pfam; PF16348; CoV_NSP4_C; 1.
DR Pfam; PF19217; CoV_NSP4_N; 1.
DR Pfam; PF19213; CoV_NSP6; 1.
DR Pfam; 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; 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; 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; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
DR PROSITE; PS51954; COV_N7_MTASE; 1.
DR PROSITE; PS52000; COV_NSP12_IF; 1.
DR PROSITE; PS51948; COV_NSP12_RDRP; 1.
DR PROSITE; PS51960; COV_NSP15_NTD; 1.
DR PROSITE; PS51992; COV_NSP3_Y3; 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; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE-
KW ProRule:PRU01303};
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 membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01303}; 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 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:PRU01296};
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 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:PRU00986}.
FT TRANSMEM 1465..1490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1559..1584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1591..1613
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1964..1986
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2255..2278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2284..2303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2346..2364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2781..2799
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2805..2822
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2834..2852
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2872..2891
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2933..2954
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2966..2990
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 898..1067
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1852..1953
FT /note="CoV Nsp3 Y"
FT /evidence="ECO:0000259|PROSITE:PS51992"
FT DOMAIN 2367..2465
FT /note="Nsp4C"
FT /evidence="ECO:0000259|PROSITE:PS51946"
FT DOMAIN 2466..2773
FT /note="Peptidase C30"
FT /evidence="ECO:0000259|PROSITE:PS51442"
FT DOMAIN 3050..3145
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51949"
FT DOMAIN 3146..3347
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51950"
FT DOMAIN 3335..3443
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS51951"
FT DOMAIN 3445..3580
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000259|PROSITE:PS51952"
FT DOMAIN 3580..3840
FT /note="NiRAN"
FT /evidence="ECO:0000259|PROSITE:PS51947"
FT DOMAIN 3843..3941
FT /note="Nsp12 Interface"
FT /evidence="ECO:0000259|PROSITE:PS52000"
FT DOMAIN 3942..4505
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000259|PROSITE:PS51948"
FT DOMAIN 4187..4348
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT DOMAIN 4506..4589
FT /note="CV ZBD"
FT /evidence="ECO:0000259|PROSITE:PS51653"
FT DOMAIN 4756..5114
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51657"
FT DOMAIN 5218..5433
FT /note="ExoN"
FT /evidence="ECO:0000259|PROSITE:PS51953"
FT DOMAIN 5441..5658
FT /note="N7-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51954"
FT DOMAIN 5595..5625
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 5659..5719
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000259|PROSITE:PS51960"
FT DOMAIN 5720..5831
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000259|PROSITE:PS51961"
FT DOMAIN 5847..5982
FT /note="NendoU"
FT /evidence="ECO:0000259|PROSITE:PS51958"
FT DOMAIN 5984..6264
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51955"
FT REGION 752..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5119..5138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5553..5567
FT /note="GpppA-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
FT COMPBIAS 818..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 5236
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5238
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5414
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5419
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5877
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 5892
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 5927
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT BINDING 5476..5482
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
SQ SEQUENCE 6264 AA; 699007 MW; 058BA8D8AAB096B3 CRC64;
MVKNVSKRSP IVLPQIQPPP LQLFIAVAAA EEGHPKDLKY LGNYNLVTSK VIPGVQVLNP
KISLTEFEQL FGAQPVLRAL RNLVVETRNA AWNGSKQDFA AKAQSLTFTD HVLRAMIKYC
PPRVSALASL ALFYRIVKID AKDLCDVAID CAIEVAYSGK TEQHFADAKS VVLTHKDGYL
TLSADCVGIP FTSTLLAQAK PSNGAMIYSD YLLYPGATIR IVDGKPVALV TKPIVAIIQS
TPFVEEDVSL LPDYNQTPAI QVAGVDCVVN GVSYLKTHDN PPLYYPRVKG GVVNVPLKQQ
GTAAKKLSVV FHAKPDDVLM AFIQLQEFLN RTTGSVVDIA DQTTYDVAPN VTVTIGTSKP
GDIVVSNEDE YLKCFETPEV SALYKVFQTE SWAVVEQKFR RLRVRAADAL YDFISFLQSL
ADNFKPLFVA VEAVIAQLQN ITLDLAVSIN KMRITYTAGH LVVDASNFVV KLIQPLCDFI
TPFLRKIAGF ATYAYGKSML LFTSAGTFLL KQTTGVVNKA CYVFDVSPDY PVDLTTDKIY
HEDSLHPTDD KPTRALEVVS VVVGNAILQM ATDGVAYYPT DGKYASTPAF KAGSDELNIV
FTCDLFDDDT NAMINETLVG YELNNLVAPR NSTPRDIATL VVNTLVDAIT DHYPEKCLDL
PENYQVFSTH DDMPLTNEHI PGHLTLYVQA MEGSDDGDDI IIEEDEYSCE DDGADEGVIP
QCWDVPNLDT ILTKIKKDEP CVEVQQGVQN AESTNVEASS LVENTQQTTD DAQETELSTE
TSEHLLVIND DEFLAIPEFD RPLKDYIQEK QLDVIIEESE SSSVTSNSPE PVGDDVPSAL
DDSNIHTASE TPSDEEFQDA ECGNDDVSTI ITDSTENGEE DPLPETIVNQ PFIVDNNLPV
CAIKEPSSTK VELVVGDLAT IKFDNSVLVN PANPQLTNGG GAAKAIADLA GPEYQAHCNK
IAPITGVVVT EPYNARTVGV ACILHVVPPK GTDADVQEKL YEAYRSILTE PAHYVIPLLG
AGIYGCNPVH SLDAFKKACP PDIGRVTIVT KDVNHVQLWD ALNRTVVRTT KDFDQITTQA
LTPQGILDAN LFDGDTFVQE PVPDVVYLAV DDSVQEQAKE LGLTLSQYCK YLKACHHKWV
TVRTNGILHL KQKDNNCFVS AAINLFQATH YKLRPAIDQL YQEYLNGNPC RFVAWIYASI
DQTIGDMGCP QQVTSLLVNN SNSKFSGTVH CCKTYFTHDG VVSNVREFDL LQPKVFCMRC
DTWTTFSAEN VEGVIVLGNT PGKAPTHAIQ FGNSHCWYTN GKKSVNGYDI DSDVVAIYHK
FQTTPVRNIV VTQPISTSNT FSVLPVQDIP KESILNDDPS VVVVSSKKAQ NHEVLDNPNC
LDLLDVWIRK PKYVMVKSWD VVGKPLFKTG KVVLLSGKHL TRIYDYLCSI GAIDTTAKLS
ISLAYKCVKR VLPSSNTLIR TIKGLFYSFR TILFACAPFL LLPAVASILA SGYQLGVYVY
AKTGIPCYGN STDHYDYQSF CAGDLTCLAC FDGQDSLHLY KHLRVDQRTY GSNDYTTHAL
AIVLLLANTT LVLLTLVACF LFNFYKFTIP FYGVVSVDYQ TTLVVVFSVY YLLRVVKFLR
HIAKGCKTPT CTICSKLRIP PTITVDTIVQ GRKYPSVVQT NAGFKICKEH NFYCKNCSQQ
NPDTFIPTEA IESLSRATRL NVKSTAPAYV LARDVECQTD AILARASHDG QPMVCISKYS
DVRTVEALLK PTPLFSYTPD VIIAADFDNA GSLKTAKELA VVLSMDLKRT IFIIDQSYSR
PVDNYTEIVS RMEKYFTFQK ITPTGDIFTD VKTATNGQAS DTAINAAILA VQKGLDFTID
NPNHILPHYA FDFNTLSAED QSVLLEAGCA KGNLKGTNVG VVLAANLVMR LSQSAIRIIA
NAASRNGVTC AVTPSNITLR GNIATQPFQR VKAGSDNKHS VVKFLVVFLV LYATAFSLST
IASYAYNPSH PAVMSDIHTT GFYVIRDGVL DTIRSTDTCF SNKFVSFDGY IQAEYTNDPA
CPVVVGVADV TTKSIPGIPA GVLHRDGGIL HIYEQALYDR LQRQSMVQEA LNLKVRPLFN
LGQQTIVGYT RTEVVVGTSY LRSPALFNAK CTYLEHHGER NLYCYDVVNK DHKLYTDVVP
HVEYKAVDFN GNLVPFKIPE QLMFYPHIVR YTGNSYCRMG QCFKTNPGIC ISFTDQFPYS
ENVQPGVYCA DTGLQLATNF LVGTISGVHV FTSTAALIGS TCVILLCVVG ILIFQRLFKE
YTTFVLYTLA IAIVNVCGIV LIYKYTAISF VYYTIYLYFV LTFVPVKRNI ALFYFAVVVI
PHISNMQLLT IAVVCVLYLC YSYIRVVSKT TGKFSSFLEA SKSTFVIDND KYVILKDLAG
SDYDSYLASY NKYKYFSGTA SDKDYDKVCM AFLAKALSAF REGGGSQLYT PPKLAVVQSL
KAKLQAGIKI LLHPSGVVER CMVAVTYNGS ALNGVWLNNV VYCPRHVLGK YRGEQWQHMV
SIADCRDFAI TCPAQGIQLT VQSIKMVGAI LQLTVHTSNS GTPDYEFVRI TPGSSMTIAC
AYDGVVRNVY HVVLQTNNLI YASFLNGACG SVGYTLRGKT LLLHYMHHLE FNNQTHGGTD
LHGQFYGPYI DEEVAQQQTA FQYYTDNVVA QLYAHLLTID ASPRWLASAE ISESDFNSWA
SSNSFANFPC EQSNMAYILG LSQTAKVSVG RILNTIIQLT LNRSGALIMG KPDFECDWTP
EMVYNQAPIT LQSGVVKRAS MWFFHFLFNT FLFVLAMLHV LPVDLYPIGL PVVVSLAFLI
TLSVKHSVVF TTTYLLPAFL MFVVKAPTLW IPNTYLRSAY EWVFGLSMSE RLTTYTVGCY
IAVYAFIAIN YTLRCLRYRS TSVLSFCMQM LQYGYIAQIT YRLMTQAWTE RLLFTAFSLL
TSHPLLAGFS WYVAGKFTVP LILPDLAIRI TIYVCIGYVM CMRFGLLWIL NKFTTVPMGT
YNYMVSIDQL KYMMAIKMSP PRNVFEVIIA NIRLIGLGGV RNIAVSTVQN KLLDAKAAAV
VVANLLDKAG VTNKHAVCKK IVKLHNDTLK ASTYEEAEMS LVKLLTHIIE FLPTDQVDAY
LADTVKVQAL NTYFDHLLEN KLVLQAVVDA NINLDSYRVY KEADATYRKS VEMDEPLQIQ
KKKLKAVNIA KAEWEREAAS QRKLEKLADA AMKSMYLAER AEDRRIKLTS GLTAMLYHML
RRLDSDRVKA LFECAKQQIL PIHAVVGVSN DNLKVIFNDK DSYLQYVDGN TLIFKGQRYN
IVKKLSLDNT PIEGIPEEYP VAVETIKEGV PQIQNNELCL RNVFTAQAPV LDGNGKETTA
KSFYVSRAGK KILVAVTSTK DDLKTVTCST DQGKVVLNLD PPMRFSHVVG GKQNLVYLYF
IQNISSLNRG MVIGHISGTT ILQANGTQIE YQENASLLTY LAFAVNPKEA YLKHLADGGK
PIQGCIQMIA SLGPGFAVTT KPQPNEHQFS YGGASICLYC RAHIPHPGVD GRCVYKGRFV
HIDKDKEPVS FALTHEPCNS CQRWSNYDCT CGTILQNSPY LNRVTGSSGA RLEPQQPGVT
PDAVKRAFHV HNNTTSGIFL STKTNCSRFR TTKQNLPLPN KGSVELYFVS KQCSQQVFEI
EETCYNMFDD SLKSTPEKFG VLARTEFFKF DKIPNVNRQF LTKYTLLDLA YALRHLSTSR
DVIKEILITI CGTTEEWFGD SWFDPIENPT FYREFHKLGS VLNRCVLNAN AFAKACSELG
IVGILTPDNQ DLLGQIYDFG DFIITQPGNG CVDLSSYYSY LMPIMSMTHM LKCECYDNDG
NEIDYDGFQY DFTDFKLSLF SKYFTYWDRP YHPNTVDCPD DRCVLHCANF NVLFAMCIPS
TAFGNLCSQA TVDGHKIIQT VGVHLKELGI VLNQDVNTHM SNINLNTLLR LVGDPTTIAS
VSDKCLDFRT PCQTLATMSS GITKQSVKPG HFNQHFYKHL LDSDILNQLG IDLKHFYYMQ
DGEAAITDYS YYRYNTPTMV DIKMFLFVLE VADKYLQPYE GGCLNAQSVV VNNLDKYAGY
PFNKLGKARN YYDMTYAEQN QLFEYTKRNV LPTLTQMNLK YAISAKDRAR TVAGVSIIST
MTNRQYHQKM LKSISLARNQ TIVIGTTKFY GGWDNMLRRL MNGINNPILV GWDYPKCDRS
MPNMLRIAAS CLLARKHTCC NQSQRFYRLA NECCQVLSEV VVSGNNLYVK PGGTSSGDAT
TAYANSVFNI LQVVSANVAT FLSTSTSSHN SREIADLHRN LYEDIYRGDS NNTTIIDQFY
QHLQKYFGLM ILSDDGVACI DTEAAASGVV SNLDGFRDIL FYQNNVYMAD SKCWTETDMT
VGPHEFCSQH TVLAEHEGKP YYLPYPDVSR ILGACIFVDD VNKADPIQNL ERYISLAIDA
YPLTKVDPIK GKVFYLLLDY IRILAQELQD GILDTFQSMT DMSYVNNFVQ EAFYAQMYEQ
SPTLQASGVC VVCASPTILR CGDCIRRPLL CCVCAYQHVT QTTHKRIIAI NNYICSVDNC
NEDNVEKLYI SGTAIYCENH KPTLCIPIVA NGTVFGIYRH TARGSDDIDL FNELATSNFD
TIEPYQKANR APLSLMLFAA ETIKALEESI KKSYATATVK DVYDQRYIKL VWEHGKKPPP
ITKNHIFTGY HFNKNGKTQV GDYILTKTDG SDSYTYRGTS TYKLQTGDVL VLMAHVVTPL
SAPPVLAQTT YVRKSLIPDT VNASFYVQHF KSYNEIALQK VTTVLGPPGT GKSTFAIGLA
KYYPNARICY TASSHAAIDA LCEKAFKTLP VGQCSRIVPT RTTVECFQDF VVNNTTAQYI
FSTINALPDI KCDIVVVDEV SMLTNYELSS VNARLVYNHI VYVGDPYQLP SPRTMLTTGQ
LAPADYNVVT DIMVHTGADV MLDMCYRCPR EIVDTVSKLV YDNKLKAAKP NSRQCYKTII
NFGSSDIAHE GQSAYNEPQL RFALAFRRYK RWDNVTFISP YNAMNVKAAM AGFSTQTVDS
SQGSEYDYVI FCVTTDSAHA LNMSRLNVAL TRAKVGILVV FRQANDLYNS LQFESIDPSL
VGQEGVLLMT DRRSTALAKS GSTPMTLQSS EDTTQEVFPE GSSSTRLLCP LFKRCSFEYS
GQHPAHALTW HDCGSEYRCD EPLAKLVGVS DGTLISYKTL VSALGFLPSL KIETYHNMFL
TKEACRIYVQ SWIGIDVEAA HAVKPNVGTN LPLQIGFSTG KNFSVIPEGI WVNEFGTCTE
PVPAKIPPGE QFRHLKKDMR QARPWKVVRN EIAAHLADVA PHTDHICFVT WAHQLELATM
RYFVKIGTEE KCFCGRRACF TNCNEYTCKA HRNLSSPSAD YVYNPFIIDV ATWGFSGRLS
TNHDEVCTYH SNAHVASADA IMTVCLAIHE LFKSVDWDLE FPVTPEQSQL NKACRLVQAN
YLNILLTTTK ATVVHDIGNP KGIPIVRRAG IKYHFYDQAP IVKHVQKLKY KPEMEARFME
GLTMFWNCNV DTYPANALVC RYDTHRQKHL IGPNGSALYI NKHAFLTPEM HTYATHKLTL
APLIYYSTTD CSTEQPIVVS YRDCVTRCNT GTTICPTHAL EYQEFINAYN LMARHGFNVY
IPRNVNVYNC WLTFTNLQNL ENLAYNCYYK NCNAHVDGQL DVVINNNAVY AKVDTQLVKL
FDNRTNLPVS TAFEHYTNRH TKSLPTTQLL AGLGVTATRN FTIWVDDDTA FQNTINVSTY
TDVDPTLHVV LCDDRYGTDW SQFNQLPNAV FLTKTKVKKT TPFICTALTL NGIAIDGDEL
YIYYRKDNQI VNFTTTLTQG RSVDKFITKT PMEKDFLEMS PEDFITNYQL QGLGVEHIIY
GDDTTPVIGG THAMISLVKN KFSFELVNHI YNPVQNCVVT SPNASTKQVC TLIDITLDDY
VNIIKTAHAN FSTKSKVFSV NIDCQNVNFM LWHDEQVKTC YPIVQSLTNG YQMPSIYKTL
VCDLEPCDIP NYHAYTPKVP GVVKNVLKYR QLFNYIIKKD RLAVPHNMTV LHLGAASVDG
TAPGTSVIKQ MLPEGTVIID LDIREFTSDA NQIIVSDYRT YMPPHHVDAI FSDLYSSDDI
HFFDNLVRIV KERLALGGSI FVKVTEHSYS PTLYQLAGYF DDYQFFCTAV NAASSEAFLC
CFNYLGTAKE SVEGHNLHAS YIKWRNEIAL TPTYSPLADN PATVCKLKAT PIISLKELEK
KPILKFLVSS GRLLVRPPEC RELY
//
