R1A_IBVM
ID R1A_IBVM Reviewed; 3953 AA.
AC P0C6V5; Q0GNB9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Replicase polyprotein 1a;
DE Short=pp1a;
DE AltName: Full=ORF1a polyprotein;
DE Contains:
DE RecName: Full=Non-structural protein 2;
DE Short=nsp2;
DE AltName: Full=p87;
DE Contains:
DE RecName: Full=Papain-like protease;
DE Short=PL-PRO;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:P0C6U8};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:P0C6U8};
DE AltName: Full=Non-structural protein 3;
DE Short=nsp3;
DE AltName: Full=p195;
DE Contains:
DE RecName: Full=Non-structural protein 4;
DE Short=nsp4;
DE AltName: Full=Peptide HD2;
DE AltName: Full=p41;
DE Contains:
DE RecName: Full=3C-like proteinase;
DE Short=3CL-PRO;
DE Short=3CLp;
DE EC=3.4.22.-;
DE AltName: Full=Main protease;
DE Short=Mpro;
DE AltName: Full=Non-structural protein 5;
DE Short=nsp5;
DE AltName: Full=p33;
DE Contains:
DE RecName: Full=Non-structural protein 6;
DE Short=nsp6;
DE AltName: Full=p34;
DE Contains:
DE RecName: Full=Non-structural protein 7;
DE Short=nsp7;
DE AltName: Full=p9;
DE Contains:
DE RecName: Full=Non-structural protein 8;
DE Short=nsp8;
DE AltName: Full=p24;
DE Contains:
DE RecName: Full=Non-structural protein 9;
DE Short=nsp9;
DE AltName: Full=p10;
DE Contains:
DE RecName: Full=Non-structural protein 10;
DE Short=nsp10;
DE AltName: Full=Growth factor-like peptide;
DE Short=GFL;
DE AltName: Full=p16;
DE Contains:
DE RecName: Full=Non-structural protein 11;
DE Short=nsp11;
GN ORFNames=1a;
OS Avian infectious bronchitis virus (strain M41) (IBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Gammacoronavirus; Igacovirus.
OX NCBI_TaxID=11127;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Mondal S.P., Buckles E.L.;
RT "Avian infectious bronchitis virus strain M41.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16934878; DOI=10.1016/j.jviromet.2006.07.018;
RA Callison S.A., Hilt D.A., Boynton T.O., Sample B.F., Robison R.,
RA Swayne D.E., Jackwood M.W.;
RT "Development and evaluation of a real-time Taqman RT-PCR assay for the
RT detection of infectious bronchitis virus from infected chickens.";
RL J. Virol. Methods 138:60-65(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2782-3088, AND SUBUNIT (3C-LIKE
RP PROTEINASE).
RX PubMed=18094151; DOI=10.1128/jvi.02114-07;
RA Xue X., Yu H., Yang H., Xue F., Wu Z., Shen W., Li J., Zhou Z., Ding Y.,
RA Zhao Q., Zhang X.C., Liao M., Bartlam M., Rao Z.;
RT "Structures of two coronavirus main proteases: implications for substrate
RT binding and antiviral drug design.";
RL J. Virol. 82:2515-2527(2008).
RN [4] {ECO:0007744|PDB:3EWO, ECO:0007744|PDB:3EWP}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1005-1178.
RX PubMed=18987156; DOI=10.1128/jvi.01862-08;
RA Xu Y., Cong L., Chen C., Wei L., Zhao Q., Xu X., Ma Y., Bartlam M., Rao Z.;
RT "Crystal structures of two coronavirus ADP-ribose-1''-monophosphatases and
RT their complexes with ADP-Ribose: a systematic structural analysis of the
RT viral ADRP domain.";
RL J. Virol. 83:1083-1092(2009).
RN [5] {ECO:0007744|PDB:3LD1}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 13-371.
RA Xu Y., Ye Z., Wei L., Cong L., Fu J., Chen C., Yang A., Wu W., Tang H.,
RA Bartlam M., Rao Z.;
RT "IBV nsp2 is an endosome-associated protein and viral pathogenicity
RT factor.";
RL Submitted (JAN-2010) to the PDB data bank.
CC -!- FUNCTION: [Isoform Replicase polyprotein 1a]: Multifunctional protein
CC involved in the transcription and replication of viral RNAs. Contains
CC the proteinases responsible for the cleavages of the polyprotein.
CC {ECO:0000305}.
CC -!- FUNCTION: [Non-structural protein 2]: May play a role in the modulation
CC of host cell survival signaling pathway by interacting with host PHB
CC and PHB2 (By similarity). Indeed, these two proteins play a role in
CC maintaining the functional integrity of the mitochondria and protecting
CC cells from various stresses (By similarity).
CC {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- FUNCTION: [Papain-like protease]: Responsible for the cleavages located
CC at the N-terminus of the replicase polyprotein (By similarity). In
CC addition, PL-PRO possesses a deubiquitinating/deISGylating activity and
CC processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from
CC cellular substrates (By similarity). {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- FUNCTION: [Non-structural protein 4]: Plays a role in host membrane
CC rearrangement that leads to creation of cytoplasmic double-membrane
CC vesicles (DMV) necessary for viral replication (By similarity). Alone
CC is able to induce paired membranes (By similarity). Coexpression of
CC nsp3 and nsp4 does not result in the formation of DMVs (By similarity).
CC {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- FUNCTION: [3C-like proteinase]: Responsible for the majority of
CC cleavages as it cleaves the C-terminus of replicase polyprotein at 11
CC sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-
CC [SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-
CC CMK. {ECO:0000255|PROSITE-ProRule:PRU00772}.
CC -!- FUNCTION: [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8
CC subunits of each) that may participate in viral replication by acting
CC as a primase. Alternatively, may synthesize substantially longer
CC products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- FUNCTION: [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8
CC subunits of each) that may participate in viral replication by acting
CC as a primase. Alternatively, may synthesize substantially longer
CC products than oligonucleotide primers. {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- FUNCTION: [Non-structural protein 9]: Plays an essential role in viral
CC replication by forming a homodimer that binds single-stranded RNA.
CC {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- FUNCTION: [Non-structural protein 10]: Plays a pivotal role in viral
CC transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16
CC 2'-O-methyltransferase activities (By similarity). Therefore plays an
CC essential role in viral mRNAs cap methylation (By similarity).
CC {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- CATALYTIC ACTIVITY: [Papain-like protease]:
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:0000250|UniProtKB:P0C6U8};
CC -!- COFACTOR: [Papain-like protease]:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P0C6U8};
CC -!- SUBUNIT: [Non-structural protein 2]: Interacts with host PHB and PHB2.
CC {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- SUBUNIT: [Non-structural protein 4]: Interacts with papain-like
CC protease and non-structural protein 6. {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- SUBUNIT: [3C-like proteinase]: Monomer (PubMed:18987156). Homodimer
CC (PubMed:18987156). Only the homodimer shows catalytic activity (By
CC similarity). {ECO:0000250|UniProtKB:P0C6U8,
CC ECO:0000269|PubMed:18987156}.
CC -!- SUBUNIT: [Non-structural protein 7]: Eight copies of nsp7 and eight
CC copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling
CC ring structure. {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- SUBUNIT: [Non-structural protein 8]: Eight copies of nsp7 and eight
CC copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling
CC ring structure (By similarity). Interacts with ORF6 protein (By
CC similarity). {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- SUBUNIT: [Non-structural protein 9]: Homodimer.
CC {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- SUBUNIT: [Non-structural protein 10]: Homododecamer.
CC {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- SUBCELLULAR LOCATION: [Papain-like protease]: Host endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane
CC protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6U8}.
CC Note=Gammacoronaviruses induce membrane zippering to form zippered
CC endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane
CC protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6U8}.
CC Note=Localizes in virally-induced cytoplasmic double-membrane vesicles
CC (By similarity). Gammacoronaviruses induce membrane zippering to form
CC zippered endoplasmic reticulum (zER) (By similarity).
CC {ECO:0000250|UniProtKB:P0C6U8, ECO:0000250|UniProtKB:P0C6Y3}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 6]: Host endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane
CC protein {ECO:0000305}. Note=Gammacoronaviruses induce membrane
CC zippering to form zippered endoplasmic reticulum (zER).
CC {ECO:0000250|UniProtKB:P0C6Y3}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host
CC perinuclear region {ECO:0000250|UniProtKB:P0C6U8}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 9]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host
CC perinuclear region {ECO:0000250}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are
CC localized in cytoplasmic foci, largely perinuclear. Late in infection,
CC they merge into confluent complexes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=Isoform Replicase polyprotein 1ab is produced by -1 ribosomal
CC frameshifting at the 1a-1b genes boundary. Isoform Replicase
CC polyprotein 1a is produced by conventional translation.
CC {ECO:0000305};
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6V5-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=P0C6Y3-1; Sequence=External;
CC -!- DOMAIN: [Papain-like protease]: The hydrophobic region HD1 probably
CC mediates the membrane association of the replication complex.
CC {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- DOMAIN: [Non-structural protein 4]: The hydrophobic region HD2 probably
CC mediates the membrane association of the replication complex.
CC {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- DOMAIN: [Non-structural protein 6]: The hydrophobic region HD3 probably
CC mediates the membrane association of the replication complex.
CC {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- PTM: [Isoform Replicase polyprotein 1a]: Specific enzymatic cleavages
CC in vivo by its own proteases yield mature proteins (By similarity). 3C-
CC like proteinase nsp5 liberates nsps 6-16 from the polyprotein (By
CC similarity). Papain-like and 3C-like proteinases are autocatalytically
CC processed. {ECO:0000250|UniProtKB:P0C6U8}.
CC -!- PTM: [Non-structural protein 4]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P0C6Y1}.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000305}.
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DR EMBL; DQ834384; ABI26421.1; -; Genomic_RNA.
DR EMBL; AY851295; AAW33784.1; -; Genomic_RNA.
DR PDB; 3EWO; X-ray; 1.80 A; A/B=1005-1178.
DR PDB; 3EWP; X-ray; 2.00 A; A/B=1005-1178.
DR PDB; 3LD1; X-ray; 2.50 A; A=13-371.
DR PDBsum; 3EWO; -.
DR PDBsum; 3EWP; -.
DR PDBsum; 3LD1; -.
DR SMR; P0C6V5; -.
DR MEROPS; C30.002; -.
DR PRIDE; P0C6V5; -.
DR SABIO-RK; P0C6V5; -.
DR EvolutionaryTrace; P0C6V5; -.
DR Proteomes; UP000007642; Genome.
DR Proteomes; UP000096468; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; 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:0019079; P:viral genome replication; IEA:InterPro.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
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; cd21667; gammaCoV_Nsp5_Mpro; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR Gene3D; 1.10.150.420; -; 1.
DR Gene3D; 1.10.1840.10; -; 1.
DR Gene3D; 1.10.8.1190; -; 1.
DR Gene3D; 1.10.8.370; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.40.10.250; -; 1.
DR Gene3D; 2.60.120.1680; -; 1.
DR Gene3D; 3.30.70.3540; -; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR InterPro; IPR043611; CoV_NSP3_C.
DR InterPro; IPR032505; CoV_NSP4_C.
DR InterPro; IPR043612; CoV_NSP4_N.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR044371; Macro_X_NSP3-like.
DR InterPro; IPR036333; NSP10_sf_CoV.
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; 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; IPR018995; RNA_synth_NSP10_CoV.
DR Pfam; PF09401; CoV_NSP10; 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; PF01661; Macro; 1.
DR Pfam; PF17896; NSP2_gammaCoV; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF101816; SSF101816; 1.
DR SUPFAM; SSF140367; SSF140367; 1.
DR SUPFAM; SSF143076; SSF143076; 1.
DR SUPFAM; SSF144246; SSF144246; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS51952; COV_EXON_MTASE_COACT; 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; PS51442; M_PRO; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51124; PEPTIDASE_C16; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; Host cytoplasm;
KW Host endoplasmic reticulum; Host membrane; Host-virus interaction;
KW Hydrolase; Lyase; Membrane; Metal-binding; Protease; Repeat;
KW Ribosomal frameshifting; RNA-binding; Thiol protease; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..3953
FT /note="Replicase polyprotein 1a"
FT /id="PRO_0000338336"
FT CHAIN 1..673
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338337"
FT CHAIN 674..2267
FT /note="Papain-like protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338338"
FT CHAIN 2268..2781
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338339"
FT CHAIN 2782..3088
FT /note="3C-like proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338340"
FT CHAIN 3089..3381
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338341"
FT CHAIN 3382..3464
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338342"
FT CHAIN 3465..3674
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338343"
FT CHAIN 3675..3785
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338344"
FT CHAIN 3786..3930
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250"
FT /id="PRO_0000338345"
FT CHAIN 3931..3953
FT /note="Non-structural protein 11"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338346"
FT TOPO_DOM 1..1752
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT TRANSMEM 1753..1773
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1774..1845
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT TRANSMEM 1846..1866
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1867..2282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT TRANSMEM 2283..2303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2304..2561
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT TRANSMEM 2562..2582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2583..2613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT TRANSMEM 2614..2634
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2635..2645
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT TRANSMEM 2646..2666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2667..3098
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT TRANSMEM 3099..3119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3120..3123
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT TRANSMEM 3124..3144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3145..3153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT TRANSMEM 3154..3174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3175..3190
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT TRANSMEM 3191..3211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3212..3259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT TRANSMEM 3260..3280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3281..3298
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT TRANSMEM 3299..3319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3320..3953
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT DOMAIN 675..780
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1005..1181
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1177..1229
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1238..1499
FT /note="Peptidase C16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 2163..2265
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 2686..2781
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 2782..3088
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3382..3464
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3465..3674
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 3675..3785
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 3787..3928
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT ZN_FING 1355..1392
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 3860..3880
FT /evidence="ECO:0000250"
FT ZN_FING 3906..3919
FT /evidence="ECO:0000250"
FT REGION 1753..1866
FT /note="HD1"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT REGION 2283..2666
FT /note="HD2"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT REGION 3099..3319
FT /note="HD3"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT ACT_SITE 1276
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1439
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 1450
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000250|UniProtKB:P0C6Y1"
FT ACT_SITE 2822
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT ACT_SITE 2924
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT BINDING 3860
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3863
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3869
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3880
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3906
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3909
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3917
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3919
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT SITE 673..674
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT SITE 2267..2268
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT SITE 2781..2782
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT SITE 3088..3089
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT SITE 3381..3382
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT SITE 3464..3465
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT SITE 3674..3675
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT SITE 3785..3786
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT SITE 3930..3931
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6U8"
FT VARIANT 807
FT /note="L -> S"
FT VARIANT 1618
FT /note="S -> F"
FT VARIANT 1739
FT /note="S -> A"
FT VARIANT 2631
FT /note="M -> L"
FT VARIANT 2774
FT /note="S -> P"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:3LD1"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:3LD1"
FT HELIX 42..58
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3LD1"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:3LD1"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:3LD1"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:3LD1"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:3LD1"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3LD1"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:3LD1"
FT HELIX 152..174
FT /evidence="ECO:0007829|PDB:3LD1"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:3LD1"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:3LD1"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:3LD1"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:3LD1"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:3LD1"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:3LD1"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:3LD1"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 337..344
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 347..354
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:3LD1"
FT STRAND 1017..1023
FT /evidence="ECO:0007829|PDB:3EWO"
FT HELIX 1025..1035
FT /evidence="ECO:0007829|PDB:3EWO"
FT STRAND 1037..1044
FT /evidence="ECO:0007829|PDB:3EWO"
FT HELIX 1054..1063
FT /evidence="ECO:0007829|PDB:3EWO"
FT HELIX 1065..1078
FT /evidence="ECO:0007829|PDB:3EWO"
FT STRAND 1082..1086
FT /evidence="ECO:0007829|PDB:3EWO"
FT STRAND 1093..1099
FT /evidence="ECO:0007829|PDB:3EWO"
FT HELIX 1109..1120
FT /evidence="ECO:0007829|PDB:3EWO"
FT STRAND 1127..1131
FT /evidence="ECO:0007829|PDB:3EWO"
FT HELIX 1142..1153
FT /evidence="ECO:0007829|PDB:3EWO"
FT STRAND 1159..1165
FT /evidence="ECO:0007829|PDB:3EWO"
FT HELIX 1167..1176
FT /evidence="ECO:0007829|PDB:3EWO"
SQ SEQUENCE 3953 AA; 441177 MW; 70AB99DED32F2B89 CRC64;
MASSLKQGVS PKLRDVILVS KDIPEQLCDA LFFYTSHNPK DYADAFAVRQ KFDRNLQTGK
QFKFETVCGL FLLKGVDKIT PGVPAKVLKA TSKLADLEDI FGVSPFARKY RELLKTACQW
SLTVETLDAR AQTLDEIFDP TEILWLQVAA KIQVSAMAMR RLVGEVTAKV MDALGSNMSA
LFQIFKQQIV RIFQKALAIF ENVSELPQRI AALKMAFAKC AKSITVVVME RTLVVREFAG
TCLASINGAV AKFFEELPNG FMGAKIFTTL AFFREAAVKI VDNIPNAPRG TKGFEVVGNA
KGTQVVVRGM RNDLTLLDQK AEIPVESEGW SAILGGHLCY VFKSGDRFYA APLSGNFALH
DVHCCERVVC LSDGVTPEIN DGLILAAIYS SFSVAELVAA IKRGEPFKFL GHKFVYAKDA
AVSFTLAKAA TIADVLKLFQ SARVKVEDVW SSLTEKSFEF WRLAYGKVRN LEEFVKTCFC
KAQMAIVILA TVLGEGIWHL VSQVIYKVGG LFTKVVDFCE KYWKGFCAQL KRAKLIVTET
LCVLKGVAQH CFQLLLDAIQ FMYKSFKKCA LGRIHGDLLF WKGGVHKIIQ EGDEIWFDAI
DSIDVEDLGV VQEKLIDFDV CDNVTLPENQ PGHMVQIEDD GKNYMFFRFK KDENIYYTPM
SQLGAINVVC KAGGKTVTFG ETTVQEIPPP DVVFIKVSIE CCGEPWNTIF KKAYKEPIEV
ETDLTVEQLL SVVYEKMCDD LKLFPEAPEP PPFENVTLVD KNGKDLDCIK SCHLIYRDYE
SDDDIEEEDA EECDTDSGDA EECDTNLECE EEDEDTKVLA LIQDPASNKY PLPLDDDYSV
YNGCIVHKDA LDVVNLPSGE ETFVVNNCFE GAVKALPQKV IDVLGDWGEA VDAQEQLCQQ
ESTRVISEKS VEGFTGSCDA MAEQAIVEEQ EIVPVVEQSQ DVVVFTPADL EVVKETAEEV
DEFILISAVP KEEVVSQEKE EPQVEQEPTL VVKAQREKKA KKFKVKPATC EKPKFLEYKT
CVGDLAVVIA KALDEFKEFC IVNAANEHMS HGGGVAKAIA DFCGPDFVEY CADYVKKHGP
QQKLVTPSFV KGIQCVNNVV GPRHGDSNLR EKLVAAYKSV LVGGVVNYVV PVLSSGIFGV
DFKISIDAMR EAFKGCAIRV LLFSLSQEHI DYFDATCKQK TIYLTEDGVK YRSVVLKPGD
SLGQFGQVFA RNKVVFSADD VEDKEILFIP TTDKTILEYY GLDAQKYVTY LQTLAQKWDV
QYRDNFVILE WRDGNCWISS AIVLLQAAKI RFKGFLAEAW AKLLGGDPTD FVAWCYASCN
AKVGDFSDAN WLLANLAEHF DADYTNALLK KCVSCNCGVK SYELRGLEAC IQPVRAPNLL
HFKTQYSNCP TCGASSTDEV IEASLPYLLL FATDGPATVD CDENAVGTVV FIGSTNSGHC
YTQADGKAFD NLAKDRKFGR KSPYITAMYT RFSLRSENPL LVVEHSKGKA KVVKEDVSNL
ATSSKASFDD LTDFEQWYDS NIYESLKVQE TPDNLDEYVS FTTKEDSKLP LTLKVRGIKS
VVDFRSKDGF TYKLTPDTDE NSKTPVYYPV LDSISLRAIW VEGSANFVVG HPNYYSKSLR
IPTFWENAES FVKMGYKIDG VTMGLWRAEH LNKPNLERIF NIAKKAIVGS SVVTTQCGKI
LVKAATYVAD KVGDGVVRNI TDRIKGLCGF TRGHFEKKMS LQFLKTLVFF FFYFLKASSK
SLVSSYKIVL CKVVFATLLI VWFIYTSNPV VFTGIRVLDF LFEGSLCGPY NDYGKDSFDV
LRYCAGDFTC RVCLHDRDSL HLYKHAYSVE QIYKDAASGI NFNWNWLYLV FLILFVKPVA
GFVIICYCVK YLVLSSTVLQ TGVGFLDWFV KTVFTHFNFM GAGFYFWLFY KIYVQVHHIL
YCKDVTCEVC KRVARSNRQE VSVVVGGRKQ IVHVYTNSGY NFCKRHNWYC RNCDDYGHQN
TFMSPEVAGE LSEKLKRHVK PTAYAYHVVY EACVVDDFVN LKYKAAIPGK DNASSAVKCF
SVTDFLKKAV FLKEALKCEQ ISNDGFIVCN TQSAHALEEA KNAAVYYAQY LCKPILILDQ
ALYEQLIVEP VSKSVIDKVC SILSNIISVD TAALNYKAGT LRDALLSITK DEEAVDMAIF
CHNHEVEYTG DGFTNVIPSY GMDTDKLTPR DRGFLINADA SIANLRVKNA PPVVWKFSDL
IKLSDSCLKY LISATVKSGG RFFITKSGAK QVISCHTQKL LVEKKAGGVI NNTFKWFMSC
FKWLFVFYIL FTACCLGYYY MEMNKSFVHP MYDVNSTLHV EGFKVIDKGV IREIVSEDNC
FSNKFVNFDA FWGKSYENNK NCPIVTVVID GDGTVAVGVP GFVSWVMDGV MFVHMTQTDR
RPWYIPTWFN REIVGYTQDS IITEGSFYTS IALFSARCLY LTASNTPQLY CFNGDNDAPG
ALPFGSIIPH RVYFQPNGVR LIVPQQILHT PYIVKFVSDS YCRGSVCEYT KPGYCVSLDS
QWVLFNDEYI SKPGVFCGST VRELMFNMVS TFFTGVNPNI YIQLATMFLI LVVIVLIFAM
VIKFQGVFKA YATIVFTIML VWVINAFVLC VHSYNSVLAV ILLVLYCYAS MVTSRNTAII
MHCWLVFTFG LIVPTWLACC YLGFILYMYT PLVFWCYGTT KNTRKLYDGN EFVGNYDLAA
KSTFVIRGTE FVKLTNEIGD KFEAYLSAYA RLKYYSGTGS EQDYLQACRA WLAYALDQYR
NSGVEVVYTP PRYSIGVSRL QAGFKKLVSP SSAVEKCIVS VSYRGNNLNG LWLGDSIYCP
RHVLGKFSGD QWGDVLNLAN NHEFEVVTQN GVTLNVVSRR LKGAVLILQT AVANAETPKY
KFVKANCGDS FTIACSYGGT VIGLYPVTMR SNGTIRASFL AGACGSVGFN IEKGVVNFFY
MHHLELPNAL HTGTDLMGEF YGGYVDEEVA QRVPPDNLVT NNIVAWLYAA IISVKESSFS
QPKWLESTTV SIEDYNRWAS DNGFTPFSTS TAITKLSAIT GVDVCKLLRT IMVKSAQWGS
DPILGQYNFE DELTPESVFN QVGGVRLQSS FVRKATSWFW SRCVLACFLF VLCAIVLFTA
VPLKFYVHAA VILLMAVLFI SFTVKHVMAY MDTFLLPTLI TVIIGVCAEV PFIYNTLISQ
VVIFLSQWYD PVVFDTMVPW MLLPLVLYTA FKCVQGCYMN SFNTSLLMLY QFMKLGFVIY
TSSNTLTAYT EGNWELFFEL VHTIVLANVS SNSLIGLIVF KCAKWMLYYC NATYFNNYVL
MAVMVNGIGW LCTCYFGLYW WVNKVFGLTL GKYNFKVSVD QYRYMCLHKV NPPKTVWEVF
TTNILIQGIG 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 NYLNGYGVAV RLG
