ID C7S857_9GAMC Unreviewed; 6611 AA.
AC C7S857;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=ORF1ab polyprotein {ECO:0000256|PROSITE-ProRule:PRU01344};
GN Name=1 {ECO:0000313|EMBL:ACJ12832.1};
OS Infectious bronchitis virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Gammacoronavirus; Igacovirus; Avian coronavirus.
OX NCBI_TaxID=11120 {ECO:0000313|EMBL:ACJ12832.1, ECO:0000313|Proteomes:UP000107830};
RN [1] {ECO:0000313|EMBL:ACJ12832.1, ECO:0000313|Proteomes:UP000107830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H52 {ECO:0000313|EMBL:ACJ12832.1};
RA Xiao C.T., Shi L., Zhou J.Y.;
RT "Comparative full-length genome sequence analysis of infectious bronchitis
RT virus islolates with different tissue tropism.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms a hexadecamer with nsp7 (8 subunits of each) that may
CC participate in viral replication by acting as a primase. Alternatively,
CC may synthesize substantially longer products than oligonucleotide
CC primers. {ECO:0000256|ARBA:ARBA00002182}.
CC -!- FUNCTION: Forms a hexadecamer with nsp8 (8 subunits of each) that may
CC participate in viral replication by acting as a primase. Alternatively,
CC may synthesize substantially longer products than oligonucleotide
CC primers. {ECO:0000256|ARBA:ARBA00003443}.
CC -!- FUNCTION: May play a role in the modulation of host cell survival
CC signaling pathway by interacting with host PHB and PHB2 (By
CC similarity). Indeed, these two proteins play a role in maintaining the
CC functional integrity of the mitochondria and protecting cells from
CC various stresses. {ECO:0000256|ARBA:ARBA00025450}.
CC -!- FUNCTION: Multifunctional protein involved in the transcription and
CC replication of viral RNAs. Contains the proteinases responsible for the
CC cleavages of the polyprotein. {ECO:0000256|ARBA:ARBA00024700}.
CC -!- FUNCTION: Plays a pivotal role in viral transcription by stimulating
CC both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase
CC activities (By similarity). Therefore plays an essential role in viral
CC mRNAs cap methylation. {ECO:0000256|ARBA:ARBA00024914}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Eight copies of nsp7 and eight copies of nsp8 assemble to form
CC a heterohexadecamer dsRNA-encircling ring structure (By similarity).
CC Interacts with ORF6 protein. {ECO:0000256|ARBA:ARBA00026001}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBUNIT: Interacts with host PHB and PHB2.
CC {ECO:0000256|ARBA:ARBA00025984}.
CC -!- SUBUNIT: Interacts with papain-like protease and non-structural protein
CC 6. {ECO:0000256|ARBA:ARBA00025840}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Endoplasmic
CC reticulum-Golgi intermediate compartment
CC {ECO:0000256|ARBA:ARBA00004399}. Host cytoplasm, host perinuclear
CC region {ECO:0000256|ARBA:ARBA00004407}. Host endoplasmic reticulum
CC membrane {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004153}. Host endoplasmic reticulum-Golgi
CC intermediate compartment {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}.
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DR EMBL; EU817497; ACJ12832.1; -; Genomic_RNA.
DR MEROPS; C30.002; -.
DR Proteomes; UP000107830; Genome.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; 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: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; cd21559; gammaCoV-Nsp6; 1.
DR CDD; cd21902; gammaCoV_Nsp10; 1.
DR CDD; cd21720; gammaCoV_Nsp13-helicase; 1.
DR CDD; cd21658; gammaCoV_Nsp14; 1.
DR CDD; cd21667; gammaCoV_Nsp5_Mpro; 1.
DR CDD; cd21828; gammaCoV_Nsp7; 1.
DR CDD; cd21832; gammaCoV_Nsp8; 1.
DR CDD; cd21899; gammaCoV_Nsp9; 1.
DR CDD; cd21733; gammaCoV_PLPro; 1.
DR CDD; cd21587; gammaCoV_RdRp; 1.
DR CDD; cd21168; M_gcv_Nsp15-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR CDD; cd22650; NTD_gammaCoV_Nsp15-like; 1.
DR CDD; cd21689; stalk_CoV_Nsp13-like; 1.
DR CDD; cd21710; TM_Y_gammaCoV_Nsp3_C; 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; 3.40.50.11580; -; 1.
DR Gene3D; 6.10.250.2820; -; 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; IPR003593; AAA+_ATPase.
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; 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; IPR044316; NSP14_gammaCoV.
DR InterPro; IPR044328; NSP15_gammaCoV_N.
DR InterPro; IPR044325; NSP15_M_gammaCoV.
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; IPR040795; NSP2_gammaCoV.
DR InterPro; IPR044383; NSP2_IBV-like.
DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR044308; NSP5_Mpro_GammaCoV.
DR InterPro; IPR043610; NSP6_CoV.
DR InterPro; IPR044368; NSP6_gammaCoV.
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; IPR043503; PLpro_palm_finger_dom_CoV.
DR InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR InterPro; IPR046441; RdRp_CoV.
DR InterPro; IPR044358; RdRp_gammaCoV.
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; 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; 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; PF17896; NSP2_gammaCoV; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF01443; Viral_helicase1; 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; 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; 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 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 endoplasmic reticulum {ECO:0000256|ARBA:ARBA00023184};
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:PRU00444}.
FT TRANSMEM 1698..1716
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1728..1744
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1825..1852
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1864..1889
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2539..2561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2567..2588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2595..2612
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2618..2646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3078..3098
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3104..3121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3133..3153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3173..3190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3202..3220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3240..3263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3275..3302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 675..780
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS51943"
FT DOMAIN 984..1160
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1156..1208
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS51944"
FT DOMAIN 1217..1478
FT /note="Peptidase C16"
FT /evidence="ECO:0000259|PROSITE:PS51124"
FT DOMAIN 2142..2244
FT /note="CoV Nsp3 Y"
FT /evidence="ECO:0000259|PROSITE:PS51992"
FT DOMAIN 2665..2760
FT /note="Nsp4C"
FT /evidence="ECO:0000259|PROSITE:PS51946"
FT DOMAIN 2761..3067
FT /note="Peptidase C30"
FT /evidence="ECO:0000259|PROSITE:PS51442"
FT DOMAIN 3362..3444
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51949"
FT DOMAIN 3445..3654
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000259|PROSITE:PS51950"
FT DOMAIN 3655..3765
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS51951"
FT DOMAIN 3767..3908
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000259|PROSITE:PS51952"
FT DOMAIN 3922..4180
FT /note="NiRAN"
FT /evidence="ECO:0000259|PROSITE:PS51947"
FT DOMAIN 4185..4283
FT /note="Nsp12 Interface"
FT /evidence="ECO:0000259|PROSITE:PS52000"
FT DOMAIN 4284..4850
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000259|PROSITE:PS51948"
FT DOMAIN 4530..4692
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT DOMAIN 4851..4934
FT /note="CV ZBD"
FT /evidence="ECO:0000259|PROSITE:PS51653"
FT DOMAIN 5107..5459
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51657"
FT DOMAIN 5521..5735
FT /note="ExoN"
FT /evidence="ECO:0000259|PROSITE:PS51953"
FT DOMAIN 5744..5971
FT /note="N7-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51954"
FT DOMAIN 5972..6032
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000259|PROSITE:PS51960"
FT DOMAIN 6033..6148
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000259|PROSITE:PS51961"
FT DOMAIN 6165..6306
FT /note="NendoU"
FT /evidence="ECO:0000259|PROSITE:PS51958"
FT DOMAIN 6309..6608
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51955"
FT REGION 5859..5873
FT /note="GpppA-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
FT ACT_SITE 5539
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5541
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5640
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5716
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5721
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6194
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT BINDING 5779..5785
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01299"
SQ SEQUENCE 6611 AA; 741862 MW; B6A39116233949A7 CRC64;
MASSLKQGVS PKPRDVILVS KDIPEQLCDA LFFYTSHNPK DYADAFAFRQ KFDRNLQTGK
QFKFETVCGL FLLKGVDKIT PGVPAKVLKA TSKLADLEDI FGVSPFARKY RELLKTACQW
SLTVETLDAR AQTLDEIFDS TEILWLQVAA KIQVSAMAMR RLVGEVTAKV MEALGSNLSV
LFQIVKQQIA RIFQKALAIF ENVSELPQRI AALKMAFAKC AKSITVVVVE RTLVVREFAG
TCLASINGAV AKFFEELPNG FMGSKIFTTL AFFKEAAVKI VENIPNAPRG TRGFEVVGNA
KGTQVVVRGM RNDLTLLDQK ADIPVEKEGW SAILEGHLCY VFKSGDRFYA APLSGNFALH
DVHCCERVVC LSDGVTPEIN DGLILAAIYS SFSVSELVAA LKKGEPFKFL GHKFVYAKDA
AVSFTLAKAA TIADVLKLFQ SARVQTEDVW SAFTEKSFNF WKLAYGKVRN LEEVVKTHFC
KAQMSIIILA AVLGEGIWHL VSQVIYKVGG LFTRVVDFCE KHWKGFCAQL KKAKLVVTET
LCVLKGVAQH CFQLLLDAIH SLYMSFKKCA LGRIHGDLLF WKGGVHKIVQ DGDEVWFDAI
DSIDVEDLGV VQEKPIDFEV CEDVTLPENQ PGHMVQIEDD GKNYMFFRFK RDENIYYTPM
SQLGAINVVC KAGGKTVTFG DTIVKEIPPP DVVPIKVSIE CCGEPWNTIF KKAYKEPIEV
ETDLTVEQLL SVIYEKMCDD LKLFPEAPEP PPFENVALVD KNGKDLDCIK SCHLIYRDYE
SDDDIEEEDA EECDTDLECE EEDEDTKVLA LIQDPASNKY PLPLDDDYSV FNGCIVHKDA
LDVVNLPSGE ETFVVNNCFE GAVKPLPQKV VDVLGDWGEA VDAQEQIAQT TSEETPISSL
EATIEQVVVE EQKIISVVEE EQQVAVYTPA DLQVVEETPD EFILIADVST EEIVPHEEKE
SQIEQEPIQV VKSQREKKAK KFKVKSTTCE KPKFLEYTTC VGDLTVVIAK ALDEFKEFCI
VNAANEHMSH GGGVAKAIAD FCGPDFVEYC ADYVKKHGPQ QKLVTPSFVK GIQCVNNVVG
PRHGDSNLRE KLVAAYKSVL VGGVVNYVVP VLSSGIFGVD FKMSIDAMRE AFKGCAIRVL
LFSLSQEHID YFDATCKQKT IYLTEDGVKY RSVVLKPGDS LGQFGQVFAR NKVVFSADDV
EDKEILFIPT TDKTILEYYG LDAQKYVIYL QTLAQKWDVQ YRDNFVILEW RDGNCWISSA
IVLLQAAKIR FKGFLAEAWA QLLGGDPTDF VAWCYASCNA NVGEFSDANW LLANLAEYFD
ADYTNAFLKR RVSCNCGVKN CEVRGLEACI QPVKAPNLLH FKTQYTNCTV CDANSVDEVV
EASLPYLLLL ATDGPTTVDC DENAVGNVVF IGSTNSGHCY TQAIGKAFDN LAKDRKFSKN
SPYITAMYTR FSLKSESSLS VVKQSKSKTK VVKEDVANLV TSSKASFDDL TDFEHWYDSN
IYESLKVQEI PVNLDEYVSF TTKEDTKLPL TLKVRGIKSV VDFISRDGFS YKLTPDIEEN
SKAPVYYPVL DSISLKAIWV DGSANFVVGH PNYYSKSLRI PTFWENAESF VKIGDKVDGV
TMGLWRAEQL NKPNLERIFN IAKKAIVGSS VVTTQCSKLI SKAATFIADK VGGGVVRNIT
DRIKGLCGFT RGHFERKLSP QFIKTLIFFF FYFVKASAKS VATSYKRVLC KVVFTTLFIL
WFMYTSKPVT FTGTRVLDFL FEGSLCGPYN DYGKDSFDVL RYCGDDFTCR VCLHDKDSLH
LYKHAYSVEQ VYKDAASGIS FNWNWLYLVF LILFVKPVAG FVIICYCVKY LVLSSTVLQT
GVGFMDWFIQ TVFTHFNFMG AGFYFWLFYK LYIQVHHILY CKDITCEVCK RVARSNRHEV
SVVVGGRKQI VHVYTNSGYN FCKRHNWYCR NCDVYGHQNT FMSPEVAGEL SEKLKRHVKP
TAHAYHVVDE ACVVDDFVNL KYKAATPGKD GAPPAVKCFS VTDFLKKAVF LKDALKCEQI
SNDGFIVCNT QSAHALEEAK NAAIYYAQYL CKPILILDQA LYQNLIVEPV SKSVVNKVCD
ILSRIISVDT ASLDYKAGTI RDALLSVTKD EEAVDMAIFC HNHEVEYTGD GFTNVIPSYG
IDTDKLTPRD RGFLINADAS VANLRVKNAP PVVWKFSDLI KLSDSCLKYL ISATVKSGSR
FFITRSGAKQ IFSCSTQKLL VEKKAGGVIS GTFNWFKSCC KWLLIFYVLF TLCCLGCYHM
ETNKSFVHPM YDVNSTMHVE GFKVIDKGVI RDIVPEDACF SNKFANFDAF WGKPYVNSRD
CPIVTAVIDG AGTIAAGVPG FVDWVLDGVM FVHMTQTERK PWYIPTWFNR EIVGYTQDSI
ITEGSFYTSI ALFSARCLYL TASNTPQLYC FNGHNDAPGA LPFSSITPHR VYFQPNGVRL
IIPQQIMHTP YVVKFLSDSY CRGSVCEYTK PGYCVSLNSQ WVLFNDEYTS KPGVFCGSTV
RELMFNMVST FFTGVNPNIY MQLATMFLIL VVVVLIFAMV IKFQGVFKAY ATIVFTIMLV
WVVNAFILCV HSYNSVVAVI LLVIYCYASL VTSRNTAIIM HCWLVFTFGL IVPIWLACCY
LAFVLYMYTP LFFWCYGTTK NTRKLYDGNE FVGTYDLAAK STFVIRGPEF VKLTNEIGDK
FEHYLSAYAR LKYYSGTGSE QDYLQACRAW LAYALDQYRN SGVEIVYTPP RYSIGVSRLQ
AGFKKLVSPS SVVEKCIVSV SYRGNNLNGL WLGGTIYCPR HVLGKFSGDQ WNDVLNLANN
HEFEVVTQNN VTLNVVSRRL KGAVLILQTA VANAETPKYK FVKANCGDSF TIACSYGGTV
VGLYPVTMRS NGTIRASFLA GACGSPGFNI EKGVVNFYYM HHLELPNALH TGTDLMGEFY
GGYVDEEVAQ RVPPDNLVTN NIVAWLYAAI ISVKESSFSL PKWLDSTTVS VEDCNKWAGD
NGFTPFSTST AITKLSAITG VDVCKLLRTI MVKSSQWGSD PILGQYNFED ELTPESVFNQ
IGGVRLQSSF VRRATSWFWS RCVLACFLFV LCAIVLFTAV PLKYYVHAAV ILLTAVLFIS
FTVKHVMAYM DTFLLPTLLT VIIGVCAEVP FIYNTLISRI VVFVSQWYDP VVFDTMVPWM
FLPLVLYTAF KCVQGCYSVN SFNTSLLVLY QFLKLGFVIY ASSSTLAAYT EGNWDLFFEL
VHTTVLANVS SNSLIGLFVF KLAKWMLYYC NATYFNNYVL MAVIINGFGW LFTCYFGVYW
WINKVFGLTL GKYEFKVSVD QYRYMCLHKI NSPKTVWEVF STNILIQGIG GDRVLPIATV
QSKLSDVKCT TVVLMQLLTK LNVEANSKMH AYLVELHNKI LASDDVGECM DNLLGMLITL
FCIDSTIDLG EYCDDILKRS TVLQSVTQEF SHIPSYAEYE RAKSIYEKVL ADSKNGGVTQ
QELAAYRKAA NIAKSVFDRD LAVQKKLDSM AERAMTTMYK EARVTDRRAK LVSSLHALLF
SMLKKIDSEK LNVLFDQANS GVVPLATVPI VCSNKLTLVI PDPETWVKCV EGVHVTYSTV
VWNIDCVTDA DGTELHPTST GSGLTYCISG DNIAWPLKVN LTRNGHNKVD VALQNNELMP
HGVKTKACVA GVDQAHCSVE SKCYYTSISG SSVVAAITSS NPNLKVASFL NEAGNQIYVD
LDPPCKFGMK VGDKVEVVYL YFIKNTRSIV RGMVLGAISN VVVLQSKGHE TEEVDAVGIL
SLCSFAVDPA DTYCKYVAAG NQPLGNCVKM LTVHNGSGFA ITSKPSPTPD QDSYGGASVC
LYCRAHIAHP GGAGNLDGRC QFKGSFVQIP TTEKDPVGFC LRNKVCTVCQ CWIGYGCQCD
SLRQPKPSVQ SVAVASGFDK NYLNRVRGSS EARLIPLANG CDPDVVKRAF DVCNKESAGM
FQNLKRNCAR FQEVRDTEDG NLEYCDSYFV VKQTTPSNYE HEKACYEDLK SEVTADHDFF
VFNKNIYNIS RQRLTKYTMM DFCYALRHFD PKDCEVLKEI LVTYGCIEDY HPKWFEENKD
WYDPIENPKY YAMLAKMGPI VRRALLNAIE FGNLMVEKGY VGVITLDNQD LNGKFYDFGD
FQKTAPGAGV PVFDTYYSYM MPIIAMTDAL APERYFEYDV HKGYKSYDLL KYDYTEEKQE
LFQKYFKYWD QEYHPNCRDC SDDRCLIHCA NFNILFSTLV PQTSFGNLCR KVFVDGVPFI
ATCGYHSKEL GVIMNQDNTM SFSKMGLSQL MQFVGDPALL VGTSNKLVDL RTSCFSVCAL
ASGITHQTVK PGHFNKDFYD FAEKAGMFKE GSSIPLKHFF YPQTGNAAIN DYDYYRYNRP
TMFDIRQLLF CLEVTSKYFE CYEGGCIPAS QVVVNNLDKS AGYPFNKFGK ARLYYEMSLE
EQDQLFESTK KNVLPTITQM NLKYAISAKN RARTVAGVSI LSTMTNRQFH QKILKSIVNT
RNAPVVIGTT KFYGGWDNML RNLIQGVEDP ILMGWDYPKC DRAMPNLLRI AASLVLARKH
TNCCTWSERV YRLYNECAQV LSETVLATGG IYVKPGGTSS GDATTAYANS VFNIIQATSA
NVARLLSVIT RDIVYDDIKS LQYELYQQVY RRVNFDPAFV EKFYSYLCKN FSLMILSDDG
VVCYNNTLAK QGLVADISGF REVLYYQNNV FMADSKCWVE PDLEKGPHEF CSQHTMLVEV
DGEPRYLPYP DPSRILCACV FVDDLDKTES VAVMERYIAL AIDAYPLVHH ENEEYKKVFF
VLLSYIRKLY QELSQNMLMD YSFVMDIDKG SKFWEQEFYE NMYRAPTTLQ SCGVCVVCNS
QTILRCGNCI RKPFLCCKCC YDHVMHTDHK NVLSINPYIC SQPGCGEADV TKLYLGGMSY
FCGNHKPKLS IPLVSNGTVF GIYRANCAGS ENVDDFNQLA TTNWSTVEPY ILANRCVDSL
RRFAAETVKA TEELHKQQFA SAEVREVLSD RELILSWEPG KTRPPLNRNY VFTGFHFTRT
SKVQLGDFTF EKGEGKDVVY YRATSTAKLS VGDIFVLTSH NVVSLIAPTL CPQQTFSRFV
NLRPNVMVPA CFVNNIPLYH LVGKQKRTTV QGPPGSGKSH FAIGLAAYFS NARVVFTACS
HAAVDALCEE AFKFLKVDDC TRIVPQRTTI DCFSKFKAND TGKKYIFSTI NALPEVSCDI
LLVDEVSMLT NYELSFINGK INYQYVVYVG DPAQLPAPRT LLNGSLSPKD YNVVTNLMVC
VKPDIFLAKC YRCPKEIVDT VSTLVYDGKF IANNPESRQC FTVIVNNGNS DVGHESGSAY
NTTQLEFVKD FVCRNKEWRE ATFISPYNAM NQRAYRMLGL NVQTVDSSQG SEYDYVIFCV
TADSQHALNI NRFNVALTRA KRGILVVMRQ RDELYSALKF IELDSVASLQ GTGLFKICNK
EFSGVHPAYA VTTKALAATY KVNDELAALV NVEAGSEITY KHLISLLGFK MSVNVEGCHN
MFITRDEAIR NVRGWVGFDV EATHACGTNI GTNLPFQVGF STGAGFVVTP EGLVDTSIGN
NFEPVNSKAP PGEQFNHLRA LFKSAKPWHV VRPRIVQMLA DNLCNVSDCV VFVTWCHGLE
LTTLRYFVKI GKDQVCSCGS RATTFNSYTQ AYACWKHCLG FDFVYNPLLV DIQQWGYSGN
LQFNHDLHCN VHGHAHVASA DAIMTRCLAI NNAFCQDVNW DLTYPHIANE DEVNSSCRYL
QRMYLNACVD ALKVNVVYDI GNPKGIKCVR RGDLNFRFYD KNPIVPNVKQ FEYDYNQHKD
KFADGLCMFW NCNVDCYPDN SLVCRYDTRN LSVFNLPGCN GGSLYVNKHA FHTPKFDRTS
FRNLKAMPFF FYDSSPCETI QVDGVAQDLV SLATKDCITK CNIGGAVCKK HAQMYADFVT
SYNAAVTAGF TFWVTNNFNP YNLWKSFSAL QSIDNIAYNM YKGGHYDAIA GEMPTIVTGD
KVFVIDQGVE KAVFFNQTIL PTSVAFELYA KRNIRTLPNN RILKGLGVDV TNGFVIWDYT
NQTPLYRNTV KVCAYTDIEP NGLIVLYDDR YGDYQSFLAA DNAVLVSTQC YKRYSYVEIP
SNLLVQNGIP LKDGANLYVY KRVNGAFVTL PNTLNTQGRS YETFEPRSDV ERDFLDMSEE
SFVEKYGKEL GLQHILYGEV DKPQLGGLHT VIGMCRLLRA NKLNAKSVTN SDSDVMQNYF
VLADNGSYKQ VCTVVDLLLD DFLELLRNIL KEYGTNKSKV VTVSIDYHSI NFMTWFEDGI
IKTCYPQLQS AWTCGYNMPE LYKVQNCVME PCNIPNYGVG IALPSGIMMN VAKYTQLCQY
LSKTTMCVPH SMRVMHFGAG SDKGVAPGST VLKQWLPEGT LLVDNDIVDY VSDAHVSVLS
DCNKYKTEHK FDLVISDMYT DNDSKRKHEG VIANNGNDDV FIYLSSFLRN NLALGGSFAV
KLTETSWHES LYDIAQDCAW WTMFCTAVNA SSSEAFLIGV NYLGASAKVK VSGKTLHANY
IFWRNCNYLQ TSAYSIFDVA KFDLRLKATP VVNLKTEQKT DLVFNLIKCG KLLVRDVGNT
SFTSDSFVCT M
//
