ID A8JP06_9ALPC Unreviewed; 6727 AA.
AC A8JP06;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=ORF1ab polyprotein {ECO:0000256|PROSITE-ProRule:PRU01344};
OS Rhinolophus bat coronavirus HKU2.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Rhinacovirus.
OX NCBI_TaxID=693998 {ECO:0000313|EMBL:ABQ57223.1, ECO:0000313|Proteomes:UP000130662};
RN [1] {ECO:0000313|EMBL:ABQ57223.1, ECO:0000313|Proteomes:UP000130662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKU2/HK/298/2006 {ECO:0000313|EMBL:ABQ57223.1};
RX PubMed=17617433; DOI=10.1016/j.virol.2007.06.009;
RA Lau S.K., Woo P.C., Li K.S., Huang Y., Wang M., Lam C.S., Xu H., Guo R.,
RA Chan K.H., Zheng B.J., Yuen K.Y.;
RT "Complete genome sequence of bat coronavirus HKU2 from Chinese horseshoe
RT bats revealed a much smaller spike gene with a different evolutionary
RT lineage from the rest of the genome.";
RL Virology 367:428-439(2007).
CC -!- FUNCTION: Forms a primer, NSP9-pU, which is utilized by the polymerase
CC for the initiation of RNA chains. Interacts with ribosome signal
CC recognition particle RNA (SRP). Together with NSP8, suppress protein
CC integration into the cell membrane, thereby disrupting host immune
CC defenses. {ECO:0000256|ARBA:ARBA00043928}.
CC -!- FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription
CC of viral genomic and subgenomic RNAs. Acts in complex with nsp7 and
CC nsp8 to transcribe both the minus and positive strands of genomic RNA.
CC The kinase-like NiRAN domain of NSP12 attaches one or more nucleotides
CC to the amino terminus of NSP9, forming a covalent RNA-protein
CC intermediate that serves as transcription/replication primer.
CC Subgenomic RNAs (sgRNAs) are formed by discontinuous transcription: The
CC polymerase has the ability to pause at transcription-regulating
CC sequences (TRS) and jump to the leader TRS, resulting in a major
CC deletion. This creates a series of subgenomic RNAs that are replicated,
CC transcribed and translated. In addition, Nsp12 is a subunit of the
CC viral RNA capping enzyme that catalyzes the RNA guanylyltransferase
CC reaction for genomic and sub-genomic RNAs. Subsequently, the NiRAN
CC domain transfers RNA to GDP, and forms the core cap structure GpppA-
CC RNA. {ECO:0000256|ARBA:ARBA00043918}.
CC -!- 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}. Host membrane
CC {ECO:0000256|ARBA:ARBA00004301}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004301}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000256|ARBA:ARBA00008087, ECO:0000256|PROSITE-ProRule:PRU01294}.
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DR EMBL; EF203066; ABQ57223.1; -; Genomic_RNA.
DR MEROPS; C30.003; -.
DR Proteomes; UP000130662; Genome.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO: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:0039648; P:modulation by symbiont of host protein ubiquitination; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; 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; cd21558; alphaCoV-Nsp6; 1.
DR CDD; cd21723; alphaCoV_Nsp13-helicase; 1.
DR CDD; cd21660; alphaCoV_Nsp14; 1.
DR CDD; cd21514; alphaCoV_Nsp2_HCoV-229E-like; 1.
DR CDD; cd21665; alphaCoV_Nsp5_Mpro; 1.
DR CDD; cd21826; alphaCoV_Nsp7; 1.
DR CDD; cd21830; alphaCoV_Nsp8; 1.
DR CDD; cd21897; alphaCoV_Nsp9; 1.
DR CDD; cd21731; alphaCoV_PLPro; 1.
DR CDD; cd21588; alphaCoV_RdRp; 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; 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; cd21875; PEDV-like_alphaCoV_Nsp1; 1.
DR CDD; cd21689; stalk_CoV_Nsp13-like; 1.
DR CDD; cd21712; TM_Y_alphaCoV_Nsp3_C; 1.
DR CDD; cd21401; ZBD_cv_Nsp13-like; 1.
DR Gene3D; 1.10.8.1190; -; 2.
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; IPR046443; a/bCoV_NSP1_glob.
DR InterPro; IPR003593; AAA+_ATPase.
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; 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; 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; IPR047912; Nsp13_helicase_alphaCoV.
DR InterPro; IPR048673; NSP13_stalk_CoV.
DR InterPro; IPR048672; NSP13_ZBD_CoV.
DR InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR InterPro; IPR044313; NSP14_alphaCoV.
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; IPR044385; NSP2_HCoV-229E-like.
DR InterPro; IPR043615; NSP2_N_CoV.
DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR044309; NSP5_Mpro_alphaCoV.
DR InterPro; IPR044369; NSP6_alphaCoV.
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; IPR043178; PLpro_thumb_sf_CoV.
DR InterPro; IPR044356; RdRp_alphaCoV.
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; 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; 2.
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; 2.
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 SMART; SM00382; AAA; 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; 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; 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; PS51989; COV_NSP2_N; 1.
DR PROSITE; PS51992; COV_NSP3_Y3; 1.
DR PROSITE; PS51943; COV_NSP3A_UBL; 1.
DR PROSITE; PS51944; COV_NSP3D_UBL; 1.
DR PROSITE; PS51946; COV_NSP4C; 1.
DR PROSITE; PS51949; COV_NSP7; 1.
DR PROSITE; PS51950; COV_NSP8; 1.
DR PROSITE; PS51951; COV_NSP9_SSRNA_BD; 1.
DR PROSITE; PS51653; CV_ZBD; 1.
DR PROSITE; PS51442; M_PRO; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51958; NENDOU; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS51955; NIV_2_O_MTASE; 1.
DR PROSITE; PS51953; NIV_EXON; 1.
DR PROSITE; PS51124; PEPTIDASE_C16; 2.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 3: Inferred from homology;
KW Activation of host autophagy by virus {ECO:0000256|ARBA:ARBA00023050};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW 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};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022632};
KW Inhibition of host IRF3 by virus {ECO:0000256|ARBA:ARBA00022931};
KW Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022482};
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: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 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 1910..1928
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1968..1989
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2051..2071
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2473..2493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2731..2749
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2761..2790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2810..2834
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3254..3274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3280..3298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3305..3324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3348..3369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3376..3394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3414..3435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3442..3462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..109
FT /note="CoV Nsp1 globular"
FT /evidence="ECO:0000259|PROSITE:PS51962"
FT DOMAIN 112..358
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51989"
FT DOMAIN 775..896
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51991"
FT DOMAIN 898..992
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS51943"
FT DOMAIN 1029..1268
FT /note="Peptidase C16"
FT /evidence="ECO:0000259|PROSITE:PS51124"
FT DOMAIN 1246..1413
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1586..1641
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS51944"
FT DOMAIN 1649..1907
FT /note="Peptidase C16"
FT /evidence="ECO:0000259|PROSITE:PS51124"
FT DOMAIN 2358..2462
FT /note="CoV Nsp3 Y"
FT /evidence="ECO:0000259|PROSITE:PS51992"
FT DOMAIN 2846..2941
FT /note="Nsp4C"
FT /evidence="ECO:0000259|PROSITE:PS51946"
FT DOMAIN 2942..3243
FT /note="Peptidase C30"
FT /evidence="ECO:0000259|PROSITE:PS51442"
FT DOMAIN 3522..3604
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51949"
FT DOMAIN 3605..3799
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51950"
FT DOMAIN 3800..3907
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS51951"
FT DOMAIN 3908..4046
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000259|PROSITE:PS51952"
FT DOMAIN 4048..4297
FT /note="NiRAN"
FT /evidence="ECO:0000259|PROSITE:PS51947"
FT DOMAIN 4303..4401
FT /note="Nsp12 Interface"
FT /evidence="ECO:0000259|PROSITE:PS52000"
FT DOMAIN 4402..4969
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000259|PROSITE:PS51948"
FT DOMAIN 4649..4811
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT DOMAIN 4970..5053
FT /note="CV ZBD"
FT /evidence="ECO:0000259|PROSITE:PS51653"
FT DOMAIN 5217..5579
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51657"
FT DOMAIN 5638..5852
FT /note="ExoN"
FT /evidence="ECO:0000259|PROSITE:PS51953"
FT DOMAIN 5861..6082
FT /note="N7-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51954"
FT DOMAIN 6085..6145
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000259|PROSITE:PS51960"
FT DOMAIN 6146..6267
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000259|PROSITE:PS51961"
FT DOMAIN 6284..6424
FT /note="NendoU"
FT /evidence="ECO:0000259|PROSITE:PS51958"
FT DOMAIN 6428..6724
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51955"
FT REGION 5973..5987
FT /note="GpppA-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
FT ACT_SITE 5656
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5658
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5757
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5833
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5838
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6314
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6329
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6370
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT BINDING 5896..5902
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
SQ SEQUENCE 6727 AA; 748739 MW; 66D58211091A670B CRC64;
MSINQLTLAI ASDQEISAHG YPTMSDAVEH FSSSASHGFK DCRFVAVGLQ DIVIGVEPSD
FVVALEGDEI LTAYIATFGA RPRCLRGWLI PSNSNYVLDE FQVIFGKRGG DVVSVDNYMC
GADGKPAVPS EQWSFVEHFD DDTDEITING VTFRHAWNTV RAADPYEKQG LLSIKSIEYI
SNVPHKLPNG SVLGVAGTPK KRNAVVLDEK YSKLYDACGV PFITNGKSIL EVVPKPLFLH
ALVECKCGNE SWTVGDWTGF KTTCCGCTGK VTTLTVGDVT PGDIVFTTPG AGKGTKFFCG
LVLTFVDTLE GVSAWRVIKA YTVDKFVASS NFDEHNHVMS LDQCSFDNFS PISVALKFSL
LCGKCCDDIK VAVATGVIDI GLGVFDVNDT VFENVPWFIQ KFEFLKPAWD ALKQAVINLG
VTSKAVLSFI KSLCSAAFSV VDGVPVIVCT VAERFSKAFT DFLSYTRECF TALCDDIVVF
GVKCKAVGDY IIFNNSVVKT VKAKIKGVKE AGLKTMTYTQ CLLGPTKPVK VKRVERSVAQ
LKVVDTAVPL KQEGECLVVG GRAMFRSDGY YRFMADADVV LESPVFTAGS QYNVVFETDA
LFIAPEIGTV FEGDNIDTVV QTVANKVQAF NNRFVVYNAH VVDGAINVFC DYKFTCPAFL
DGFPEWFSFC KNHFKDAGFV EFYDCIINSD STFQTTFQPY LDLKPSVDVY LGPEIVRAVD
GGRLWRTVIN GIGDAVNFCK NLRLHFEFGE LKGTVVKRFK GILKTLLTVY NEFIQTTVSV
LTICGISAKY YAFDKPMLCM HGITERVTSF DITSLGKPIL DGLSRCNVFA RGSNAVVVDS
VDHELLDLEE CDFVEPASHG VLVVSDDYGF YSCETGIYPY ASDGKVLPLR FRKKAGGKNV
AFDDNVTVTE IDPIFKVKLS FEFEDEKLIE LCKKVIGSKV KCSSWSQLVE IIDTALTATK
SYYNVPEYFI YDEEGGNDLN LDVMISEWPL QVDEVSELFS TDETVEEQAV EQVEPVVEDV
SDIIEVNKAF AIDDSPKRAI SPFGFDTNEI NGRRVLVQSN NNCWVNAACY QLQVLGFDSP
AMELYRVGGT HNLVKQCYEA TGAFLGSLGD VAHCLEVLLK DAKTAKVTVE VTCDCSSNFE
ELSGAFFRFL PLRSKFEYGS CFACHGTRYY RVCGIVGSAI FSQTLKPLDF NDLICDVASA
SVFLGDDCGH YLINDYDKRL CVDGMGVYKI RHNTIDTIVV KDADIKPSTV APFTEYCNVK
FYQGDFKDLA GLSHDFVVNA ANCNLAHGGG VAKAIDHHTG GKLQKLSTSF VKKNGKVATG
ECVMIDTGKL KVLNAVGPRK GKDAESLLNT VYTNIFARRG VPLMPLISCG IFGFDLKDSL
RAFLAACGDR HVKCFVYSDS ERESVMKFLT TPFEENAAPK EVLETPVVEI TTDVVAPFYT
IGSHKFYDCN SVEPILGLGV KNIVLFTDQV LSVKDFGVAV DKHLNGLLSD MSNKYVSDHK
AVPFGNILSL DCGAFTVVDA VSPFDGASFE KQSGRTIRKL ARLNGSTLCV LPNASALFDK
LFALGDNFSF LVLDNVRPLF DNYLKPKDVK VKVTADGRNV NDVVVTTAET FDAQLGPSAN
GVESLVGVVP TPMDSGRVVN TAPDVNWSKH FGFSDAAAFA VLDHSKFAFD SEVVDGKRAL
ADSDNNCWVN ATCLALQFLK PTFKYVGWED LWNKFVTGDV AGFVHLLYYI EGVDKGAKGD
VESTLSKLDK YIVSSGSVTV ERSTLCDRCN STVKTVTGAI AEASVILNGH ADGHCPHNFE
WRVQVVGVKG DIILLHSGSL LNGPYVYGDA YVAFSGNIDN GHYTVFDNKL SKMYDGIKCV
KTTLDTLVAS SVVIRNGSXA VKTEHVPLIK KLDDSAEKFF NVGDIVAHNI AYFFVWLLTT
LSTLYRCWRG GNFKLLSSIP ERSGIVLRRS FKYNFRALRS NVASKQKYCL MFAKLLLLLY
TIYAMLFILV RFSFFNDYIC GSAVRGYASS DFDKSKFCNG SLVCKTCLFG YQELSEFQHV
GVVWSYVREP LFASVLPLCY FAVIAIFGGV VERFALCYFA AQFINNVLSF LKLQDSFWLV
QLVPFDIFGD EILVMFLSYK AICFFKHVVF GCDKPSCVAC CKSAKLKRIA MDTIVNGSRR
SFYVNANGGA KLCKKHNFFC VACDSYGSGH TYINDHIANE LHNVTKLHVK PTGPAFINVD
RVEFSDGFYR IFSGDKFWKY NFDITDKKFS CKEVLKNCNI LDDFIVFDNN GSNLSQVQNA
CVYLSQLLCK PIKIIDSTLL SSLNVDFNGA LHKAFLDVLH NSFGKDFSSC KTMHDCKELL
ELDVSDDDFI KVVSDAHRFD VLITDTSFNN FCTSYAKPAE KLSSFDLAHC MRSGAKVVNH
NVLIKEKMPI VWNCVDFAKL SVDARKYIVK TAKVKGVTFL LTVNNNVMET TLPCVSVLQK
QGAGKLSSMW KNFWYACGAI LALFVLLNCV GFTEYASSLP GYDFKYIEDG QLKPFVNGLY
CVRNTFDTFM DWHAQKFGFK PSNSDKCPIV VGASDSGRVV PGVASDVYLL GKTLIFTLKT
VFGSAGHCYD VNGIADGDKC LFNSACTNLE GLGGTRTYCY KTGLIEGAMT YGDLQHDSYY
RLSGDNYVRL PYVVVQGLGF RAVRTQATTY CRVGECVDSK AGMCFGADRW MVYSNDIGSD
FICGSSLVDL LRNILSVFNY NFSTMIMSGQ VIFNCVLACV VVFGCYFVMK FRRVFGDMSL
AVFTVCAAVV VNNLSYFVSL NYVGMVVYSF LYFISTRGLK YCFIWDISYV VAYCLLAPWW
LLTWYICAAL IGLIPNLFKL KVSTTLFEGT KFVGTFDAAS VGTFVIDARS YERLINSTSI
EKIKQYASTF NKYKYYSGSA NEADYRCACY AHLAKALIDF STTRQDTLYT PPTVSINSTL
QAGLKKMAQP SGLVEPCVVR VSYGNTVLNG VWLDDKVYCP RHVLASDTTV TIDYDAVYHS
MRLHNFSISK GNVFLGVVGA VMQGANLVIT VSQANVNTPS YSFRTLKAGE CFNILACYDG
TPAGVYGVNL RSTHTIKGSF VNGACGSPGF VMNGYKVEFV YMHQIELGNA SHVGSDMFGN
IYGGFEDQPS IQLEGVATLI TENVVAFLYA ALINGERWWC SNERCTIDSF NEWALGNGFT
NLVSGDGFSM LAAKTGVDVC QLLSAIQRLA TGLGGKTILG YASLTDEYTL SEVVRQMYGV
NIQSTKTSSA LKNLLLMGFF FLLFWSEFFM YSTILWINPG LITTFLGLFV MLSMLLASCI
KHKMLFLQLF LLPSIIIAAC YNFAWDMEVT RMLATQFDYH VSFLNMDIQG AINIIVCFIG
ISLHTYRFLD TQLRSYSTYV LSMCTVLYTF YYGYDSLSLA IMLLGFGCRE WYVGTAAFRL
AQFIVPYCPG LISFVGDIKA VLVLYLVFGF VATVYFGLLY WLNRVLKLTL GCYDFKVSAA
EFKYMVANGY TAPRGPFDSV LLSLRLLGVG GQKTIKVSTV QSKLTDLKCA NVVLLGCLTN
MNIAANSREW SYCVNLHNEI NLTSDPEEAL EKLLALVAFF LSKQQNFGVD DLIDSFFENR
NVLQSVASAF ANMPSFIAYE KARMNYEDAI ANDAAPAVVK QLKKAMNTAK GEFDHEASVQ
KKIQRMADAA AAQMYKDARA VDRKSKVVSA MHSLLFGMLR KLDMSSINQL MELAKDGCIP
MAIIPAAAAT KLTVITPDLE SFSKIRVDNN IYYAGAAWSI TDVKDADGRV VILKEINADN
KDALVWPLHV TCERVVKLQN NEIIPGKLKQ RAVKAEGDGF STDAKALYNT EGGHCFVYAL
IADKPDLKVV KWEYDGGCKT IELEPPLKFA VEAPTGVQIK YLYYVKNLNN LRRGATLGYI
GATVRLQAGK QTELACNSSL LTLCAFAVDP AKAYVSAVKQ GAKPVGNCVK MLANGSGSGQ
AVTNGVEANM NQDSYGGASV CIYCRAHVDH PAMDGACRFK GKYVQIPIGV NDPIRFCIEN
EVCKVCGCWL NNGCSCDRSS VQSTDQAYLN RARGSSAARL EPCNGTEPEH CVRAFDVYNK
DVACIGKFLK VNCVRLKNLD KHDAFFVVKR CTKSVMEHEQ SMYNKLSGSN ALAVHDFFTW
KDGRSIYGNV CRQDLSKYTM MDLCYALRNF DERNCETLKE ILVLTGCCDQ SYFDNKVWYD
PVENEDLHRV YALLGQRVAN AMLKCVELCD EMVTKGVVGV LTLDNQDLNG NFYDFGDFVD
VMPGMGIPCC TSYYSYMMPI MTMTNCLAYE CFMKSDIFGS DFKTYDLLEY DFTDHKVRLF
DKYFKYWGQD YHPNCSDCYD DMCLLHCSNF NTLFSTTIPN TAFGPLCRKV FVDGVPLIAT
AGYHFKQLGL VWNKDINTHN SRLSMTDLLQ FVTDPGLLIA SSPALVDQRT VCFSIAALST
GITHQTVKPG HFNKEFYDYL LSQGFFDEGS ELTLKHFFFA QKGDAAVADF DYYRYNKPTM
LDICMARFTY KVVQRYFECY DGGCITAREV VVTNLDKSAG YPLNRFGKAR LFYETFSYEE
QDALYAMTKR NILPTMTQLN LKYSISGKAR ARTVGGVSLL ATMTTRQFHQ KHLKSIVNTR
NAPVVIGTTK FYGGWDNMLK NLMNDVDNGA LMGWDYPKCD RAMPSMIRML AAMVLGSKHV
TCCTDSDRFY RLSNELAQVL NEVVHSNGGF YVKPGGTTSG DATTAYANSV FNIFQAVSSN
INRLLSVDSN VCNNLYVKKL QRSIYDNCYR SSAVDDNVVT DFYNYLKKHF SMMILSDDGV
VCYNKEYAAL GYVGDISAFK ATLYYQNNVF MSTAKCWVEE DLSVGPHEFC SQHTMQIVDS
DGDYYLPYPD PSRILSAGVF VDDIVKTDPV ILLERYVSLA IDAYPLSKHP NREYRKVFYV
LLDWVKHLHN TLNQGILETF SVTLLDDVQS KFWDEAFYAG MYEKSTVLQA AGMCIVCGSQ
TVLRCGDCLR RPLLCTKCAY DHVVGTTHRF ILSITPYVCN TSGCNVNDVT KLFLGGLNYY
CHDHKPQLSF PLCANGNIFG LYKNSAVGSL DVEVFNKLAM SDWSDVSDYK LANDVKESLR
LFAAETIKAR EESVKSSYAC ATLKEIIGPK ELLLQWEVGK ARPPLNRNSV FTCFQISKDS
KWQVGEFTFE KLDYGSDTVC YKSNVTAKLV PGMIFVLTSH NVLSLKAPTI ANQERYSTIY
KLYPSLNVDD AYSSLVPYYQ LIGKQKITTI QGPPGSGKSH CVIGLGLYYP SARIVFAACS
HAAVDSLCHK AAKAYSVDRC SRIIPARARV ECYSGFKPNN TSAQYIFSTV NALPEVNADI
VVIDEVSMCT NYDLSIVNAR VAYKHIVYVG DPQQLPAPRT MITRGVLQPE DYNVVTQRMC
GVGPDVFLHK CYRCPAEVVN TVSELVYENK FKPVKDHSKQ CFKMFVKGNV QIDNGSSVNK
RQLEVVKAFI AKNPKWSRAV FISPYNSQNY VAGRMLGLQT QTVDSAQGSE YDYVIYTQTS
DTSHALNVNR FNVAITRTKI GILCIMCDKA LYDTLKFFEI SQSDLQSNIG GCGLFKDCYK
FDQDLPPAYA TTYMALSDKF KIDKELAVNI GHSDVRYEHV VSYMGFRFDM NIPNFHSLFC
TRDFAMRNVR GWIGMDVEGA HVCGDNIGTN VPLQVGFSNG VDFVVQPEGC VVTNEGNIVK
PVKARAPPGE QFTHLVPLMR KGQPWYVVRR RIVQMVCDCL NGLSDVVIFV LWAGGLELTT
MKYFVKIGPS QHCDCGKEAR CYNSATHAYY CLAHALGCDY LYNPFVIDIQ QWGYTGSLSS
NHHEVCNVHR NEHVASGDAI MTRCLAIHDC FVKNVDWSIT YPFIANENAI NKSGRIVQSH
IMKAALKVYN PKAVHDIGNP KGIRCAATNV PWYCYDKQPI NSNVKMLEYD YMTHGQLDGM
CLFWNCNVDM YPEFSIVCRF DTRCRSHLSL EGVNGGALYV NNHAFHTPAY DKRAFAKLKP
MPFFFYDDGE CDVSQGQINY VPLRATVCIT KCNIGGAVCK RHASLYRAYV EAYNTFTQNG
FNIWCPNSFD VYNLWQTLVD TNLQGLENIA YNVVKKGSFV GEPGELPVAV VNDRVSVRDG
VSDNVIFVNK TSLPTNVAFE LYAKRKIGLT PPLTILKNMG VVATHGFVLW DYDADRPFSN
FTKSVCKYTD FDEDVCTCFD NSIQGAFERF TLCKNGVLIS NVAIKKLRGI RLNFGYLNGV
AVSSITEGET TKPVDWYIYQ RKDGSFVEPV DGYYSQGRNA STFLPRSQME KDFLELDTGL
FISKYGLEDF NFEHIVYGDV SKITLGGLHL LISQVRLARI GVLKVEDFVD SADDTLHSCS
VTYANDPSSK SVCTYMDILL DDFVVILKNL DLSVTSKVHD VIVDCKAWRW MLWCKDSKVA
TFYPQLQSAE WKCGYSMPSL YKIQNMCMDA CNLYNYGASI KLPDGIMFNV VKYTQLCQFL
NTTTMCVPHN MRVLHLGAGS DKGVAPGTAV LRRWLPDDAI IVDNDVNDYV SDADFSITGD
CTHVYVEDKF DLLISYMYDG KIKSIDGDNV SKDGFFTYIN GFIREKLALG GAMAVKITEY
SWNKQLYEIA QKFEYWTLFC TSVNTSSSEA FLIGINYLGD FSSASVIDGN VMHANYIFWR
NSTIMTMSYN SVLDLSKFRC KHKATVIITL KDKDITDMVL GLIKNGKLLI RNSQKLLNFS
NHLVTTK
//
