ID A0A0U1WHG1_9ALPC Unreviewed; 6598 AA.
AC A0A0U1WHG1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=ORF1ab polyprotein {ECO:0000256|PROSITE-ProRule:PRU01344};
OS BtNv-AlphaCoV/SC2013.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Nyctacovirus;
OC Nyctalus velutinus alphacoronavirus SC-2013.
OX NCBI_TaxID=1503291 {ECO:0000313|EMBL:AIA62264.1, ECO:0000313|Proteomes:UP000103794};
RN [1] {ECO:0000313|EMBL:AIA62264.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BtNv-SC2013 {ECO:0000313|EMBL:AIA62264.1};
RX PubMed=26262818; DOI=10.1038/ismej.2015.138;
RA Wu Z., Yang L., Ren X., He G., Zhang J., Yang J., Qian Z., Dong J., Sun L.,
RA Zhu Y., Du J., Yang F., Zhang S., Jin Q.;
RT "Deciphering the bat virome catalog to better understand the ecological
RT diversity of bat viruses and the bat origin of emerging infectious
RT diseases.";
RL ISME J. 10:609-620(2016).
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; KJ473809; AIA62264.1; -; Genomic_RNA.
DR RefSeq; YP_009201729.1; NC_028833.1.
DR GeneID; 26628975; -.
DR KEGG; vg:26628975; -.
DR Proteomes; UP000103794; 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: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; 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; 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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000103794};
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 1782..1801
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1847..1866
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1921..1942
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1949..1968
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1980..2000
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2344..2364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2605..2623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2659..2681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2693..2712
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3124..3142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3148..3172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3179..3199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3211..3234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3246..3264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3284..3309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3316..3337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 110..352
FT /note="CoV Nsp2 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51989"
FT DOMAIN 655..771
FT /note="CoV Nsp2 C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51991"
FT DOMAIN 772..868
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS51943"
FT DOMAIN 892..1143
FT /note="Peptidase C16"
FT /evidence="ECO:0000259|PROSITE:PS51124"
FT DOMAIN 1121..1289
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1449..1504
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS51944"
FT DOMAIN 1511..1768
FT /note="Peptidase C16"
FT /evidence="ECO:0000259|PROSITE:PS51124"
FT DOMAIN 2234..2338
FT /note="CoV Nsp3 Y"
FT /evidence="ECO:0000259|PROSITE:PS51992"
FT DOMAIN 2720..2815
FT /note="Nsp4C"
FT /evidence="ECO:0000259|PROSITE:PS51946"
FT DOMAIN 2816..3117
FT /note="Peptidase C30"
FT /evidence="ECO:0000259|PROSITE:PS51442"
FT DOMAIN 3396..3478
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51949"
FT DOMAIN 3479..3673
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51950"
FT DOMAIN 3674..3781
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS51951"
FT DOMAIN 3782..3920
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000259|PROSITE:PS51952"
FT DOMAIN 3922..4171
FT /note="NiRAN"
FT /evidence="ECO:0000259|PROSITE:PS51947"
FT DOMAIN 4177..4275
FT /note="Nsp12 Interface"
FT /evidence="ECO:0000259|PROSITE:PS52000"
FT DOMAIN 4276..4843
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000259|PROSITE:PS51948"
FT DOMAIN 4523..4685
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT DOMAIN 4844..4927
FT /note="CV ZBD"
FT /evidence="ECO:0000259|PROSITE:PS51653"
FT DOMAIN 5101..5452
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51657"
FT DOMAIN 5512..5726
FT /note="ExoN"
FT /evidence="ECO:0000259|PROSITE:PS51953"
FT DOMAIN 5735..5956
FT /note="N7-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51954"
FT DOMAIN 5959..6019
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000259|PROSITE:PS51960"
FT DOMAIN 6020..6137
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000259|PROSITE:PS51961"
FT DOMAIN 6154..6294
FT /note="NendoU"
FT /evidence="ECO:0000259|PROSITE:PS51958"
FT DOMAIN 6298..6594
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51955"
FT REGION 5847..5861
FT /note="GpppA-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
FT ACT_SITE 5530
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5532
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5631
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5707
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5712
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6184
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6199
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6240
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT BINDING 5770..5776
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
SQ SEQUENCE 6598 AA; 733363 MW; F174D8DA8950BBB6 CRC64;
MARNPITVAK AAVCEISAIG FGDIGEAVLH YSNAAADGFI KCRFVPLSMA DCVEGLLSDE
FVVLVNNDTS CLTVGTFGER PPDLKGWLLF SNCDVDGTAI VSFDGLAGAE VYVDNYMCDQ
TGKPVLAADV WTFKDYFGES DTIVIDGVVY RKAWEVVRLD VPYKAQSVSA ISSIEWLCGV
QHVLPSGTVL DVAKSVSKSK VVLLSDPYAD IYDQVGSPFM TNGKNLLEIV VKPCFLHGYV
KCNCGNTHWA VGDWRAGYKS VCCGLNCNPI CVAAGYVEPG DVLFTSKGAG TGLKYYKGLT
LKFVGEVENV AVWRIQKVHH VDGFVACNRF KDDFCSTMES CGVENVSATA NALKFSLISG
CCQEVTLRSI VSGQLSVGFA VFDTFEDIFS MPKWMQRLGA LGSTLWSQFK SFARETFKTS
TSLVEFVNFL RDVSCVVMNG ALELVANVPN HFASLFDHLR VLVASVTTLF IEEFKVAGVA
FKRLGDYVLF DNALCQLASV KLKGFKQDGL KTATYVSTVY GPSKRVKVKR VEKCDANLVL
CDSAPLVDEG YACVIQGQAF YTNGTYYWFM TDHTSVLESP VFKKDTIVCP DVLLAVDGGD
IFHKFLSTVT DVVEFCASIK VHFGLEGFVI TAAKKFKAFA RTLTELYNEF AIAVSDVVKI
ACMNFTYYAF NKPMVAVNGT LCPVELVEPP SDVSKEALVT DFMVFKSPDT HVKPIRIETE
SCELHEVDFV TPRDGGVVKI IDGYAFYESN GNYYPSSVDG VKNVTYRKKG GGVVTFSETN
SVKEVDPVHK VYLTYEFEDE VVVEVLKQTV GYKMTFEGQE WADFEATLRG VLSVVSTKLP
IPEYFVYDEE GGFDYTKPVM VSQWPIQVSD SVDHETVDDT VDTTPRSDED EVREALSFIK
EVEPQPLNPF AFEFTDYCGL KVLKQVNNNC WVASACLHMQ LLDLLDTPAM DLYKCGRVGP
LVQSCYESVK QLVGSMGDVT ECLEHMLKDV KSCVVVCDAV CDCGTKDLTI EGCVFRFMPC
SEPLERWCAV CNSMAACTIK GIKGTAIFCQ KPGPANDLYV EPYCAASFIG SVTSGHYRTN
VYHTGKAVDG FGVHDIDNTN LHTYAVKNVD WTRSHTPADN SPALVEPFLV YKNVQFFQGD
FKDLVGGVQH DFVVNAANER LQHGGGVAKA INDYTNNELQ HLSSAHVKKH GKVSVGSGVM
LQCSGVKVLN VVGPRHGAGE VALLENAYNC IFDQDGVPLT PLIGVGIFKV PITTSLKALL
DVVGDRQCRC FCYSDSEVAA IVAYVNNMSA VDDVQLPVCP PLTPCRVEGD VSFYMGSVDV
LLQQSFDRFV FFVSEDLQLC VLASALDVYL NGCVTEALNK SGPLPAGNIV SYKHPKGDGF
VVVTFAVLPA VGSKDFDKNV KRVFNKLSKL KGNILSTVSS VMFARLTRVW KSFWLCDSSV
SVVDEHFSET SVFVVVTENG RDFETVALDT AKTFVEQVGV CTIDNVDVTN AVVTPTDEPV
SVATPSVDWD AFYGFENASV FHTLDHSGFE FESTVVEGKR TLKSSDNNCW VNAVCLQLQY
LDAKFVSEGL NAMWDSYVTG NVSKFVHWLY WITDHSKNDR NDAESVLLRL SVYLCKSCVF
TIERETSSLC CSELRTYNAC VVSASVLRNG VSDGVCKHGD AYKSRVSAVD GIGIVVSVSI
PDPVPKSALL DGVSYTTFTG DVGSGHYAVV DRKLYKSFDG FDVKPASLSS VSVTGVVVKT
AKFTRKVKQV ATPTVSSGDA PLDLSTTLNT AASKFFSVGD VVARNVGMFC VWLFSMLTLL
FKTFKKRDFS VLALAPQRTG VIFRRSLKYN SKAAYKHLNS KWGTVKFVMK LLVMFYTLYM
LLFLTVRFSP LNSVFCDDYV DGYYNSTFVK SDYCDGLVCK VCLYGYQELS DFPHLDLTWE
FITHPLLVSF MPLLYMAFLL CFGNKWVRFL MCYFILQYVN AAGVVLGLQD SIWALHLVPF
DIFCDEIVVC WLVYVILAFL KHVCFGCEKP SCVACSKSAR LTRIPIQTVV NGSTKVVYVA
ANGGNRPFCK KHNFFCVNCD SYGVGCTFIN EHVARELANV TKTNVQPTGD AYIVIDKVEF
QNGFYYLYSG ETFWRYNFDI TSSKYSCKEV LKSCNILSDF IVFDNNGTNV SQVHNASVYL
SQLLCKPIKL VDSALLSTLD VDFNGALHSA FLEVLNNSFN KDFSGCATMS ECKSLLGFEV
SDEDFYNAVS DAHRFNILLT DISFNNFITT YAKPEEKFAT HDAAVCMRSG SKIVNHNVLI
KENAAVVWYQ RDFHALSEDC RKYIVKTSKQ KGVNIMITFN DTRMNVAIPA VNFVCKKGGA
IKPFGWLCIV FAFIFALYMS VGLFDFTESV PSYMGFDFKY IKEGRLHDFT ERLDCVYSVF
DNFDVWHESK FGTVPTKSIK CPIVVGVSDS VRTLPGVPAG VMLVGKTLVF AVKTVFGETG
NCYDTQGVTS TSSCLFTSAC TVLSGIGGTI TYCYKDGIVE GARTYSELVP NTYYKMEDGR
HVIFPEVLAR GFGFRAVRTL ATTYCRAGQC VDSKAGVCFG LDRFLVYSAD SGSDFVCGNG
LLSLLYNVLA IFSSSFSVAA LSGQIIFNLV VAAIAVFVCF TVVKFKRMFG DMSRGVCTVG
AAVLVNNLSY VVTQNTVGMI VYAVLYFLAT RGVTYSWIWY VSYVVAYSTL APWWLLSWYL
IAGLSGVIPS FIKLRVSSQL FDGDKFVGSF EAAAMGTFVL DMHSYEKLVN SLPADKLKQY
ASAFNRYKYY SGSASEADYR LACFSHLAKA MMDYGTTHQD CLYTPPTISY NSTLQAGLRK
MAQPSGMVEK CIVRVAYGNM VLNGVWLGDE VYCPRHVIAE NTTTLIDYDK AFSLIRLHNF
SVSVGNVFLG VVSCRMRGAL LCIKVNQANV NTPNYTFKTL KPGDSFNILA CYEGVASGVY
GVTLRNNSTV RGSFINGACG SPGYNLVGNT VEFCYFHQLE LGSGCHVGSD ANGVMYGNFD
DQPTLQIEGA SRLYTANVVS FLYGALLNGC NWWLTSDRLT LEAFNDWATS NDFTTLSSVD
MYTILSAKTG VDVARVLAAI QKLAKGFGGN KILGYSSLTD EFTAGEVIKQ MYGVTLQSSK
KSRFLGNLLS IGLFVFMFWS EFLSYSALFW INANVLTPIF LCLCGFSVVL TVGLKHKLLF
LYTFLIPTVV LLAAINLSWD FYLRALLSST VGYHTSLMSF DLQGVLNIAI CAFVSGLHLY
RFSPNVGSCA TLLMSLGVTV YNYWFDTDYF SIIMTLLLNM SSTWYIGAIA YKIASVMIVF
VPAPLIAAFG PIKTVLMVYV CIGYVFCMYW GFCYWLNRVS KLTLGVYDFK VSSAEFKYMV
ANGLSAPRSV LDTLYLSFRL LGVGGERTIK VATVQSKLTD LKCANVVLLG CLSAMNVSAN
SKEWAYCVDL HNKINLCDDP EKAQEMLLAL LAFFISKQKD FGVDDLLDSY FSNSALLQSV
AATFVNMPSY IAYETARQEY ENAVNTDASQ SVVKQLRKAM NVAKAEFDKE ASVQRKINRM
AEAAATQMYK EARAVNKKSK VISSLHAMLF SMLRRLDMSS IDNILSLARD GTVPLSIIPT
ACATKLTVVC SDIESFSKVV FDNCVQYAGV VWNIIDIRDG DGKIVHLKEV NKDNVDVLSW
PLFVNCERMV KLQNNEIMPG KLKQKAVRAE GEGVHCDGKA LYNNEGGKTF MYAFLADKPD
LKYVKWDFDG GCNVIELEPP CKFAVETSTG VQVRYLYFVK NLNTLRRGAV LGYIGATVRL
QAGKQTELAT NSSLLTLCAF AVDPPKMYID SVKAGIKPVG NCVKMLSNGA GNGQAITTSV
EANTNQDSYG GASVCLYCRA HVEHPGMDGR CQFKGRYVQV PLGTADPIRF CLENKVCSVC
GCWFGHGCTC DRTCLQAVDT AYLNRVRGSS AARLEPCNGS ETDHVVRAFD IYNKDVACIG
KFLKVNCVRM RNVDAKDAFF VVKRCVKGVM EHEQSMYDTL KHSGVLAPHD FYLWKNGRSV
YGNVSRQNLT KYTMMDLVFA LRNFDERNCD VLKEILVLVG ACDESYFENK CWYDPVENED
IHRVYAALGR IVNTAMLNCV KLCDAMVEKG IIGVLTLDNQ DLNGLFYDFG DFSFTMPGMG
VPCCTSYYSY MMPVMGMTNC LACECFVKSD IFGSDFKTFD LLEYDFTEHK SLLFEKYFKY
WGQDYHPNCV DCHDDMCVVH CANFNTLFST TIPITAFGPL CRKVFVDGVP LVTTAGYHFK
QLGIVWNKDI NTHSTRLSIN ELLQFVADPA LLVASSPALV DQRTCCFSVA ALGTGMTSQT
VKPGHFNREF YDFLRGQGFF EEGSDLTLKH FFFAQKGDAA IKDFDFYRYN RPTMLDICQA
RVTYQIVKRY FDIYDGGCIT AREVVVVNLN KSAGYPFNKL GKAGLYYEAL SYEEQDQLYA
VTKRNVMPTM TQLNLKYAIS GKERARTVGG VSLLSTMTTR QYHQKHLKSI VNTRNASVVI
GTTKFYGGWD NMLRTLIDGV DNPCLMGWDY PKCDRALPNM IRMISAMILG SKHVNCCTAS
DRYYRLCNEL AQVLTEVVYS NGGFYFKPGG TTSGDATTAY ANSVFNIFQA VSANINRLLG
VDSNACNNNT VKHLQRRLYD NCYRLSNVDD EFVNDYYGYL QKHFSMMILS DDGVVCYNKD
YADLGYVADI GAFKATLYYQ NNVFMSTAKC WVEPDVNKGP HEFCSQHTMQ VVDENGKYFL
PYPDPSRILS AGVFVDDVVK TDPVILLERY VSLAIDAYPL SKHENLEYRK VFYALLDWVK
HLHNTLNQGI LESFSVTLLE DQSAKFWSED FYANMYEKST ALQSAGMCVV CGSQTVLRCG
DCIRRPLLCT KCAYDHVVGT PHKFILSISP YVCNHSGCTV NDVTRLYLGG LSYYCVDHKP
QLAFPLCSAG NVFGLYKNSA TGSVDVDVFN TLSTSDWSDV RDYRLANECK DSLRLFAAET
VKAKEECIKS SYACATLREI IGPKELLLSW EPGKPRPPLN RNSVFTGFQI TKDSKMQLGE
FTFEKLDYDS DAVVYKSTTT CKLSPGVLFV LTSHNVAPLR APTMANQEKY STIVKLRPVF
NISDAYASLI PYYQLIGKQR ITTIQGPPGS GKSHCVIGLG LYYPGARILY TACSHAAVDS
LCAKAATAFN TDSCSRIIPA RARVECFSGF KVNNTSAQYI FATVNTIPEI NVDIVVLDEV
SMCTNYELSL LNQRVSYRHV VYVGDPQQLP APRTMISKGV LEPRDYNVVT QRMCAVGPDV
FLHKCYRCPA EIVKTVSELV YENKFKPVHP DSKECFKLYC KGSVHVDNGS SVNKRQLDVV
RMFLGKNPRW AKAVFISPYN SQNYVASRVL GLQTQTVDSS QGSEYDYVIY TQTSDTLHAC
NINRFNVAIT RAKKGILCVM CDRSLFDALK FYELKMTDLQ SSDGCGLFKD CHRGSDNLPP
SHAPTYMSLS DAFKTDKDLA VQIGVSGTIK YEHVISFMGF RFDVNVPGYH NLFCTRDFAM
RNVRGWIGMD VEGAHVCGDN LGTNVPLQIG FSNGVDFVVQ PEGCVITECG NKVTSVRARA
PPGEQFTHLI PLMRKGQPWS VVRKRIVQMC CDCMSGMSDI IIFVLWAGGL ELTTMRYFVK
TGPVTHCHCG KEATCYNSGS HAFYCFRHAL GCDYLYNPFV IDIQQWGYTG SLSFNHHQYC
NIHRNEHVAS GDAIMTRCLA VYDCFVKNVD WSITYPFISN ELAINKGGRV VQSHIVRAAL
KLYNPKAIHD IGNPKGIRCA STNISWYCYD KQPLNSNVRM LEYDYITHGQ MEGLCLFWNC
NVDMYPEFSI VCRFDTRTRS VLNLEGVNGG SLYVNNHAFH TPAYDRRAFA KLQPAPFFFY
DDGDCDIVQG ETNYVPLRSS SCITRCNVGG AVCSKHSNMY HAYVNAYNVF TQAGFTIWVP
KSFELFNLWQ TFLDTNLQGL ENIAYNVVKK GSFVGASGEL PVAVVNDRVL VREDLSDNVV
FVNKTSLPTN VAFELYAKRA TGLTPPLTIL RNLGVVSTYK FCLWDYEAER PFTSFTKSVC
SYTDFDEDVC TCYDASIPGS LERFTLANNA VLFSRQPIKK LTGFKINYGF LNGVPVSTTE
GKPVVWYFYV RSNGVNVDYV DGYYTQGRTI STFLPRSQME EDFLNMDEGF FISKYGLEDF
AFEHVVYGDV SKTTLGGLHL LISQVRLGKM GVLNVEDFVS SNDSTLKSCT VTYANDPSSK
MVCTYVDLLL DDFVCLLKSL DLSVVSKVHE VVLDCKIWRW MLWCKDNKVQ TFYPQLQSAE
WKCGYSMPTL YKIQRMCLEP CNLYNYGEGV RLPEGIMFNV VKYTQLCQYL NSTTMCVPHN
MRVLHLGAGS DKGVAPGTAV LRRWLPSDAV ILDNDVNTYV SDADFSHTGD CSTLYLTDKF
DLVISDMYDG RIKAIDGANV SKDGFFTYIN GVICEKLALG GTAAIKITEY SWNRKLYELM
QKFAYWTLFC TSVNTSSSEA FLIGVNYLGD FSETPVIDGA TCHANYIFWR NSTLMAMSYN
SVLDLTRFEC KHKATVVVNL KESDVNEVVL GLVKSGKLLI RNTGVVCGYA QPPHLSHV
//
