ID R1AB_SARS2 Reviewed; 7096 AA.
AC P0DTD1;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 1.
DT 02-DEC-2020, entry version 5.
DE RecName: Full=Replicase polyprotein 1ab;
DE Short=pp1ab;
DE AltName: Full=ORF1ab polyprotein;
DE Contains:
DE RecName: Full=Host translation inhibitor nsp1;
DE AltName: Full=Leader protein;
DE AltName: Full=Non-structural protein 1;
DE Short=nsp1;
DE Contains:
DE RecName: Full=Non-structural protein 2;
DE Short=nsp2;
DE AltName: Full=p65 homolog;
DE Contains:
DE RecName: Full=Non-structural protein 3;
DE Short=nsp3;
DE EC=3.4.19.12 {ECO:0000269|PubMed:32726803};
DE EC=3.4.22.-;
DE AltName: Full=PL2-PRO;
DE AltName: Full=Papain-like protease {ECO:0000303|PubMed:32726803};
DE AltName: Full=Papain-like proteinase;
DE Short=PL-PRO;
DE Contains:
DE RecName: Full=Non-structural protein 4;
DE Short=nsp4;
DE Contains:
DE RecName: Full=3C-like proteinase;
DE Short=3CL-PRO;
DE Short=3CLp;
DE EC=3.4.22.69 {ECO:0000269|PubMed:32198291, ECO:0000269|PubMed:32272481};
DE AltName: Full=Main protease;
DE Short=Mpro {ECO:0000303|PubMed:32272481};
DE AltName: Full=Non-structural protein 5;
DE Short=nsp5;
DE AltName: Full=SARS coronavirus main proteinase;
DE Contains:
DE RecName: Full=Non-structural protein 6;
DE Short=nsp6;
DE Contains:
DE RecName: Full=Non-structural protein 7;
DE Short=nsp7;
DE Contains:
DE RecName: Full=Non-structural protein 8;
DE Short=nsp8;
DE Contains:
DE RecName: Full=Non-structural protein 9;
DE Short=nsp9;
DE Contains:
DE RecName: Full=Non-structural protein 10;
DE Short=nsp10;
DE AltName: Full=Growth factor-like peptide;
DE Short=GFL;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE Short=Pol;
DE Short=RdRp;
DE EC=2.7.7.48;
DE AltName: Full=Non-structural protein 12;
DE Short=nsp12;
DE Contains:
DE RecName: Full=Helicase;
DE Short=Hel;
DE EC=3.6.4.12;
DE EC=3.6.4.13;
DE AltName: Full=Non-structural protein 13;
DE Short=nsp13;
DE Contains:
DE RecName: Full=Proofreading exoribonuclease;
DE Short=ExoN;
DE EC=3.1.13.-;
DE AltName: Full=Guanine-N7 methyltransferase;
DE AltName: Full=Non-structural protein 14;
DE Short=nsp14;
DE Contains:
DE RecName: Full=Uridylate-specific endoribonuclease;
DE EC=3.1.-.-;
DE AltName: Full=NendoU;
DE AltName: Full=Non-structural protein 15;
DE Short=nsp15;
DE Contains:
DE RecName: Full=2'-O-methyltransferase;
DE EC=2.1.1.-;
DE AltName: Full=Non-structural protein 16;
DE Short=nsp16;
GN Name=rep; ORFNames=1a-1b;
OS Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Sarbecovirus.
OX NCBI_TaxID=2697049;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=32015508; DOI=10.1038/s41586-020-2008-3;
RA Wu F., Zhao S., Yu B., Chen Y.-M., Wang W., Song Z.-G., Hu Y., Tao Z.-W.,
RA Tian J.-H., Pei Y.-Y., Yuan M.-L., Zhang Y.-L., Dai F.-H., Liu Y.,
RA Wang Q.-M., Zheng J.-J., Xu L., Holmes E.C., Zhang Y.-Z.;
RT "A new coronavirus associated with human respiratory disease in China.";
RL Nature 579:265-269(2020).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 3C-LIKE PROTEINASE AND IN COMPLEX
RP WITH MICHAEL ACCEPTOR INHIBITOR N3.
RA Liu X., Zhang B., Jin Z., Yang H., Rao Z.;
RT "The crystal structure of 2019-nCoV main protease in complex with an
RT inhibitor N3.";
RL Submitted (FEB-2020) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 3C-LIKE PROTEINASE APOENZYME AND
RP IN COMPLEX WITH ALPHA-KETOAMIDE 13B INHIBITOR, SUBUNIT (3C-LIKE
RP PROTEINASE), FUNCTION (3C-LIKE PROTEINASE), CATALYTIC ACTIVITY (3C-LIKE
RP PROTEINASE), ACTIVE SITE (3C-LIKE PROTEINASE), AND ACTIVITY REGULATION
RP (3C-LIKE PROTEINASE).
RX PubMed=32198291; DOI=10.1126/science.abb3405;
RA Zhang L., Lin D., Sun X., Curth U., Drosten C., Sauerhering L., Becker S.,
RA Rox K., Hilgenfeld R.;
RT "Crystal structure of SARS-CoV-2 main protease provides a basis for design
RT of improved alpha-ketoamide inhibitors.";
RL Science 0:0-0(2020).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 3C-LIKE PROTEINASE APOENZYME AND
RP IN COMPLEX WITH MICHAEL ACCEPTOR INHIBITOR N3, FUNCTION (3C-LIKE
RP PROTEINASE) (3C-LIKE PROTEINASE), CATALYTIC ACTIVITY (3C-LIKE PROTEINASE),
RP AND ACTIVITY REGULATION (3C-LIKE PROTEINASE).
RX PubMed=32272481; DOI=10.1038/s41586-020-2223-y;
RA Jin Z., Du X., Xu Y., Deng Y., Liu M., Zhao Y., Zhang B., Li X., Zhang L.,
RA Peng C., Duan Y., Yu J., Wang L., Yang K., Liu F., Jiang R., Yang X.,
RA You T., Liu X., Yang X., Bai F., Liu H., Liu X., Guddat L.W., Xu W.,
RA Xiao G., Qin C., Shi Z., Jiang H., Rao Z., Yang H.;
RT "Structure of Mpro from COVID-19 virus and discovery of its inhibitors.";
RL Nature 0:0-0(2020).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) OF NON-STRUCTURAL PROTEIN
RP 7; NON-STRUCTURAL PROTEIN 8 AND RNA-DIRECTED RNA POLYMERASE, SUBUNIT
RP (NON-STRUCTURAL PROTEIN 7), SUBUNIT (NON-STRUCTURAL PROTEIN 8), SUBUNIT
RP (RNA-DIRECTED RNA POLYMERASE), FUNCTION (NON-STRUCTURAL PROTEIN 7),
RP FUNCTION (NON-STRUCTURAL PROTEIN 8), AND FUNCTION (RNA-DIRECTED RNA
RP POLYMERASE).
RX PubMed=32277040; DOI=10.1126/science.abb7498;
RA Gao Y., Yan L., Huang Y., Liu F., Zhao Y., Cao L., Wang T., Sun Q.,
RA Ming Z., Zhang L., Ge J., Zheng L., Zhang Y., Wang H., Zhu Y., Zhu C.,
RA Hu T., Hua T., Zhang B., Yang X., Li J., Yang H., Liu Z., Xu W.,
RA Guddat L.W., Wang Q., Lou Z., Rao Z.;
RT "Structure of the RNA-dependent RNA polymerase from COVID-19 virus.";
RL Science 0:0-0(2020).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.5 ANGSTROMS) OF NON-STRUCTURAL PROTEIN
RP 7; NON-STRUCTURAL PROTEIN 8 AND RNA-DIRECTED RNA POLYMERASE IN COMPLEX WITH
RP REMDESIVIR ANTIVIRAL DRUG AND IN COMPLEX WITH ZINC ION, SUBUNIT
RP (NON-STRUCTURAL PROTEIN 7), SUBUNIT (NON-STRUCTURAL PROTEIN 8), SUBUNIT
RP (RNA-DIRECTED RNA POLYMERASE), FUNCTION (NON-STRUCTURAL PROTEIN 7),
RP FUNCTION (NON-STRUCTURAL PROTEIN 8), FUNCTION (RNA-DIRECTED RNA
RP POLYMERASE), CATALYTIC ACTIVITY (RNA-DIRECTED RNA POLYMERASE), AND ACTIVITY
RP REGULATION (RNA-DIRECTED RNA POLYMERASE).
RX PubMed=32358203; DOI=10.1126/science.abc1560;
RA Yin W., Mao C., Luan X., Shen D.D., Shen Q., Su H., Wang X., Zhou F.,
RA Zhao W., Gao M., Chang S., Xie Y.C., Tian G., Jiang H.W., Tao S.C.,
RA Shen J., Jiang Y., Jiang H., Xu Y., Zhang S., Zhang Y., Xu H.E.;
RT "Structural basis for inhibition of the RNA-dependent RNA polymerase from
RT SARS-CoV-2 by remdesivir.";
RL Science 0:0-0(2020).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 3C-LIKE PROTEINASE APOENZYME IN
RP COMPLEX WITH COMPOUND 11A AND COMPOUND 11B, FUNCTION (3C-LIKE PROTEINASE),
RP CATALYTIC ACTIVITY (3C-LIKE PROTEINASE), AND ACTIVITY REGULATION (3C-LIKE
RP PROTEINASE).
RX PubMed=32321856; DOI=10.1126/science.abb4489;
RA Dai W., Zhang B., Su H., Li J., Zhao Y., Xie X., Jin Z., Liu F., Li C.,
RA Li Y., Bai F., Wang H., Cheng X., Cen X., Hu S., Yang X., Wang J., Liu X.,
RA Xiao G., Jiang H., Rao Z., Zhang L.K., Xu Y., Yang H., Liu H.;
RT "Structure-based design of antiviral drug candidates targeting the SARS-
RT CoV-2 main protease.";
RL Science 0:0-0(2020).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) OF NON-STRUCTURAL PROTEIN
RP 7; NON-STRUCTURAL PROTEIN 8 AND RNA-DIRECTED RNA POLYMERASE, SUBUNIT
RP (NON-STRUCTURAL PROTEIN 7), SUBUNIT (NON-STRUCTURAL PROTEIN 8), SUBUNIT
RP (RNA-DIRECTED RNA POLYMERASE), FUNCTION (NON-STRUCTURAL PROTEIN 7),
RP FUNCTION (NON-STRUCTURAL PROTEIN 8), FUNCTION (RNA-DIRECTED RNA
RP POLYMERASE), AND CATALYTIC ACTIVITY (RNA-DIRECTED RNA POLYMERASE).
RX PubMed=32438371; DOI=10.1038/s41586-020-2368-8;
RA Hillen H.S., Kokic G., Farnung L., Dienemann C., Tegunov D., Cramer P.;
RT "Structure of replicating SARS-CoV-2 polymerase.";
RL Nature 0:0-0(2020).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS) OF NON-STRUCTURAL PROTEIN 3 MACRO
RP DOMAIN, AND FUNCTION OF NON-STRUCTURAL PROTEIN 3.
RX PubMed=32578982; DOI=10.1021/acs.biochem.0c00309;
RA Frick D.N., Virdi R.S., Vuksanovic N., Dahal N., Silvaggi N.R.;
RT "Molecular Basis for ADP-ribose Binding to the Mac1 Domain of SARS-CoV-2
RT Nsp3.";
RL Biochemistry 0:0-0(2020).
RN [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.93 ANGSTROMS) OF NON-STRUCTURAL PROTEIN
RP 7; NON-STRUCTURAL PROTEIN 8 AND RNA-DIRECTED RNA POLYMERASE IN COMPLEX WITH
RP ZINC ION, SUBUNIT (NON-STRUCTURAL PROTEIN 7), SUBUNIT (NON-STRUCTURAL
RP PROTEIN 8), SUBUNIT (RNA-DIRECTED RNA POLYMERASE), FUNCTION (NON-STRUCTURAL
RP PROTEIN 7), FUNCTION (NON-STRUCTURAL PROTEIN 8), FUNCTION (RNA-DIRECTED RNA
RP POLYMERASE), CATALYTIC ACTIVITY (RNA-DIRECTED RNA POLYMERASE), ACTIVITY
RP REGULATION (RNA-DIRECTED RNA POLYMERASE), AND MUTAGENESIS OF SER-5253.
RX PubMed=32526208; DOI=10.1016/j.cell.2020.05.034;
RA Wang Q., Wu J., Wang H., Gao Y., Liu Q., Mu A., Ji W., Yan L., Zhu Y.,
RA Zhu C., Fang X., Yang X., Huang Y., Gao H., Liu F., Ge J., Sun Q., Yang X.,
RA Xu W., Liu Z., Yang H., Lou Z., Jiang B., Guddat L.W., Gong P., Rao Z.;
RT "Structural Basis for RNA Replication by the SARS-CoV-2 Polymerase.";
RL Cell 182:417-428(2020).
RN [11] {ECO:0000244|PDB:6YVA}
RP X-RAY CRYSTALLOGRAPHY (3.18 ANGSTROMS) OF NON-STRUCTURAL PROTEIN 3,
RP FUNCTION (NON-STRUCTURAL PROTEIN 3), CATALYTIC ACTIVITY (NON-STRUCTURAL
RP PROTEIN 3), ACTIVITY REGULATION (NON-STRUCTURAL PROTEIN 3), AND MUTAGENESIS
RP OF VAL-1629; PHE-1632; THR-1638; CYS-1674 AND TYR-1831.
RX PubMed=32726803; DOI=10.1038/s41586-020-2601-5;
RA Shin D., Mukherjee R., Grewe D., Bojkova D., Baek K., Bhattacharya A.,
RA Schulz L., Widera M., Mehdipour A.R., Tascher G., Geurink P.P., Wilhelm A.,
RA van der Heden van Noort G.J., Ovaa H., Mueller S., Knobeloch K.P.,
RA Rajalingam K., Schulman B.A., Cinatl J., Hummer G., Ciesek S., Dikic I.;
RT "Papain-like protease regulates SARS-CoV-2 viral spread and innate
RT immunity.";
RL Nature 0:0-0(2020).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.6 ANGSTROMS) OF NON-STRUCTURAL PROTEIN
RP 1, FUNCTION (NON-STRUCTURAL PROTEIN 1), AND MUTAGENESIS OF LYS-164 AND
RP HIS-165.
RX PubMed=32680882; DOI=10.1126/science.abc8665;
RA Thoms M., Buschauer R., Ameismeier M., Koepke L., Denk T.,
RA Hirschenberger M., Kratzat H., Hayn M., Mackens-Kiani T., Cheng J.,
RA Straub J.H., Stuerzel C.M., Froehlich T., Berninghausen O., Becker T.,
RA Kirchhoff F., Sparrer K.M.J., Beckmann R.;
RT "Structural basis for translational shutdown and immune evasion by the Nsp1
RT protein of SARS-CoV-2.";
RL Science 0:0-0(2020).
RN [13]
RP FUNCTION (NON-STRUCTURAL PROTEIN 1).
RX PubMed=32733001; DOI=10.1038/s41467-020-17665-9;
RA Lei X., Dong X., Ma R., Wang W., Xiao X., Tian Z., Wang C., Wang Y., Li L.,
RA Ren L., Guo F., Zhao Z., Zhou Z., Xiang Z., Wang J.;
RT "Activation and evasion of type I interferon responses by SARS-CoV-2.";
RL Nat. Commun. 11:3810-3810(2020).
CC -!- FUNCTION: [Replicase polyprotein 1ab]: Multifunctional protein involved
CC in the transcription and replication of viral RNAs. Contains the
CC proteinases responsible for the cleavages of the polyprotein.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Host translation inhibitor nsp1]: Inhibits host translation
CC by interacting with the 40S ribosomal subunit (PubMed:32680882). Nsp1 C
CC terminus binds to and obstructs ribosomal mRNA entry tunnel
CC (PubMed:32680882). Thereby inhibits antiviral response triggered by
CC innate immunity or interferons (PubMed:32680882). The nsp1-40S ribosome
CC complex further induces an endonucleolytic cleavage near the 5'UTR of
CC host mRNAs, targeting them for degradation (By similarity). Viral mRNAs
CC are not susceptible to nsp1-mediated endonucleolytic RNA cleavage
CC thanks to the presence of a 5'-end leader sequence and are therefore
CC protected from degradation (By similarity). By suppressing host gene
CC expression, nsp1 facilitates efficient viral gene expression in
CC infected cells and evasion from host immune response (By similarity).
CC {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32680882}.
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. Indeed, these two proteins play a role in maintaining the
CC functional integrity of the mitochondria and protecting cells from
CC various stresses. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 3]: Responsible for the cleavages
CC located at the N-terminus of the replicase polyprotein. Participates
CC together with nsp4 in the assembly of virally-induced cytoplasmic
CC double-membrane vesicles necessary for viral replication (By
CC similarity). Antagonizes innate immune induction of type I interferon
CC by blocking the phosphorylation, dimerization and subsequent nuclear
CC translocation of host IRF3 (PubMed:32733001). Prevents also host NF-
CC kappa-B signaling (By similarity). In addition, PL-PRO possesses a
CC deubiquitinating/deISGylating activity and processes both 'Lys-48'- and
CC 'Lys-63'-linked polyubiquitin chains from cellular substrates
CC (PubMed:32726803). Cleaves preferentially ISG15 from substrates in
CC vitro (PubMed:32726803). Can play a role in host ADP-ribosylation by
CC binding ADP-ribose (PubMed:32578982). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:32578982, ECO:0000269|PubMed:32726803,
CC ECO:0000269|PubMed:32733001}.
CC -!- FUNCTION: [Non-structural protein 4]: Participates in the assembly of
CC virally-induced cytoplasmic double-membrane vesicles necessary for
CC viral replication. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [3C-like proteinase]: Cleaves the C-terminus of replicase
CC polyprotein at 11 sites (PubMed:32321856). Recognizes substrates
CC containing the core sequence [ILMVF]-Q-|-[SGACN] (PubMed:32198291,
CC PubMed:32272481). Also able to bind an ADP-ribose-1''-phosphate (ADRP)
CC (By similarity) (PubMed:32198291, PubMed:32272481).
CC {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32198291,
CC ECO:0000269|PubMed:32272481, ECO:0000269|PubMed:32321856}.
CC -!- FUNCTION: [Non-structural protein 6]: Plays a role in the initial
CC induction of autophagosomes from host reticulum endoplasmic. Later,
CC limits the expansion of these phagosomes that are no longer able to
CC deliver viral components to lysosomes. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Non-structural protein 7]: Plays a role in viral RNA
CC synthesis (PubMed:32358203, PubMed:32277040, PubMed:32438371,
CC PubMed:32526208). Forms a hexadecamer with nsp8 (8 subunits of each)
CC that may participate in viral replication by acting as a primase.
CC Alternatively, may synthesize substantially longer products than
CC oligonucleotide primers (By similarity). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:32277040, ECO:0000269|PubMed:32358203,
CC ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208}.
CC -!- FUNCTION: [Non-structural protein 8]: Plays a role in viral RNA
CC synthesis (PubMed:32358203, PubMed:32277040, PubMed:32438371,
CC PubMed:32526208). Forms a hexadecamer with nsp7 (8 subunits of each)
CC that may participate in viral replication by acting as a primase.
CC Alternatively, may synthesize substantially longer products than
CC oligonucleotide primers (By similarity). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:32277040, ECO:0000269|PubMed:32358203,
CC ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208}.
CC -!- FUNCTION: [Non-structural protein 9]: May participate in viral
CC replication by acting as a ssRNA-binding protein.
CC {ECO:0000250|UniProtKB:P0C6X7}.
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. Therefore plays an essential role in
CC viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Responsible for replication
CC and transcription of the viral RNA genome.
CC {ECO:0000305|PubMed:32277040, ECO:0000305|PubMed:32358203,
CC ECO:0000305|PubMed:32438371, ECO:0000305|PubMed:32526208}.
CC -!- FUNCTION: [Helicase]: Multi-functional protein with a zinc-binding
CC domain in N-terminus displaying RNA and DNA duplex-unwinding activities
CC with 5' to 3' polarity. Activity of helicase is dependent on magnesium.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Proofreading exoribonuclease]: Enzyme possessing two
CC different activities: an exoribonuclease activity acting on both ssRNA
CC and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase
CC activity. Acts as a proofreading exoribonuclease for RNA replication,
CC thereby lowering The sensitivity of the virus to RNA mutagens.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Uridylate-specific endoribonuclease]: Mn(2+)-dependent,
CC uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to
CC the cleaved bond. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [2'-O-methyltransferase]: Methyltransferase that mediates
CC mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral
CC mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16.
CC Therefore plays an essential role in viral mRNAs cap methylation which
CC is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
CC EC=2.7.7.48; Evidence={ECO:0000269|PubMed:32358203,
CC ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208};
CC -!- CATALYTIC ACTIVITY: [Helicase]:
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:0000250|UniProtKB:P0C6X7};
CC -!- CATALYTIC ACTIVITY: [Helicase]:
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:0000250|UniProtKB:P0C6X7};
CC -!- CATALYTIC ACTIVITY: [3C-like proteinase]:
CC Reaction=TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides
CC corresponding to the two self-cleavage sites of the SARS 3C-like
CC proteinase are the two most reactive peptide substrates. The enzyme
CC exhibits a strong preference for substrates containing Gln at P1
CC position and Leu at P2 position.; EC=3.4.22.69;
CC Evidence={ECO:0000269|PubMed:32198291, ECO:0000269|PubMed:32272481,
CC ECO:0000269|PubMed:32321856};
CC -!- CATALYTIC ACTIVITY: [Non-structural protein 3]:
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:0000269|PubMed:32726803};
CC -!- ACTIVITY REGULATION: [Non-structural protein 3]: Inhibited in vitro by
CC GRL-0617. {ECO:0000269|PubMed:32726803}.
CC -!- ACTIVITY REGULATION: [Proofreading exoribonuclease]: Inhibited by
CC Remdesivir antiviral drug (GS-5734). {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- ACTIVITY REGULATION: [RNA-directed RNA polymerase]: Inhibited by
CC Remdesivir antiviral drug (GS-5734) through non-obligate RNA chain
CC termination. {ECO:0000269|PubMed:32358203,
CC ECO:0000269|PubMed:32526208}.
CC -!- ACTIVITY REGULATION: [3C-like proteinase]: Inhibited by pyridone-
CC containing alpha-ketoamides compounds 13a and 13b. In turn, alpha-
CC ketoamide 13b (tert-butyl (1-((S)-1-(((S)-4-(benzylamino)-3,4-dioxo-1-
CC ((S)-2-oxopyrrolidin-3-yl)butan-2-yl)amino)-3-cyclopropyl-1-oxopropan-
CC 2-yl)-2-oxo-1,2-dihydropyridin-3-yl)carbamate) inhibits SARS-CoV-2
CC replication in human lung cells (PubMed:32198291). Inhibited ex vivo by
CC michael acceptor inhibitor N3 (PubMed:32272481). Inhibited ex vivo by
CC compound 11a and 11b (PubMed:32321856). {ECO:0000269|PubMed:32198291,
CC ECO:0000269|PubMed:32272481, ECO:0000269|PubMed:32321856}.
CC -!- SUBUNIT: [Non-structural protein 2]: Interacts with host PHB and PHB2.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [3C-like proteinase]: 3CL-PRO exists as monomer and homodimer.
CC Only the homodimer shows catalytic activity.
CC {ECO:0000269|PubMed:32198291}.
CC -!- SUBUNIT: [Non-structural protein 4]: Interacts with PL-PRO and nsp6.
CC {ECO:0000250|UniProtKB:P0C6X7}.
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 (By similarity). Interacts with RNA-directed RNA
CC polymerase (PubMed:32277040, PubMed:32358203, PubMed:32438371,
CC PubMed:32526208). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:32277040, ECO:0000269|PubMed:32358203,
CC ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208}.
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 RNA-directed RNA
CC polymerase (PubMed:32277040, PubMed:32358203, PubMed:32438371,
CC PubMed:32526208). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:32277040, ECO:0000269|PubMed:32358203,
CC ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208}.
CC -!- SUBUNIT: [Non-structural protein 9]: Is a dimer.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [Non-structural protein 10]: Forms a dodecamer and interacts
CC with nsp14 and nsp16; these interactions enhance nsp14 and nsp16
CC enzymatic activities. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase]: Interacts with nsp7 and nsp8.
CC {ECO:0000269|PubMed:32277040, ECO:0000269|PubMed:32358203,
CC ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208}.
CC -!- SUBUNIT: [Proofreading exoribonuclease]: Interacts (via N-terminus)
CC with DDX1. Interacts with nsp10. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [2'-O-methyltransferase]: Interacts with nsp10.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- INTERACTION:
CC PRO_0000449623; PRO_0000449623 [P0DTD1]: rep; NbExp=2; IntAct=EBI-25475864, EBI-25475864;
CC PRO_0000449625; PRO_0000449626 [P0DTD1]: rep; NbExp=13; IntAct=EBI-25475871, EBI-25475874;
CC PRO_0000449626; P04439: HLA-A; Xeno; NbExp=3; IntAct=EBI-25475874, EBI-1042870;
CC PRO_0000449627; PRO_0000449627 [P0DTD1]: rep; NbExp=2; IntAct=EBI-25475877, EBI-25475877;
CC PRO_0000449628; PRO_0000449633 [P0DTD1]: rep; NbExp=4; IntAct=EBI-25475880, EBI-25492395;
CC PRO_0000449629; PRO_0000449626 [P0DTD1]: rep; NbExp=2; IntAct=EBI-25475885, EBI-25475874;
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane
CC {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P0C6X7}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane
CC {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P0C6X7}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P0C6X7}. Note=Localizes in virally-induced
CC cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane
CC {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host
CC perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Note=nsp7, nsp8,
CC nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear.
CC Late in infection, they merge into confluent complexes.
CC {ECO:0000250|UniProtKB:P0C6X9}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host
CC perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Note=nsp7, nsp8,
CC nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear.
CC Late in infection, they merge into confluent complexes.
CC {ECO:0000250|UniProtKB:P0C6X9}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 9]: Host cytoplasm, host
CC perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Note=nsp7, nsp8,
CC nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear.
CC Late in infection, they merge into confluent complexes.
CC {ECO:0000250|UniProtKB:P0C6X9}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host
CC perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Note=nsp7, nsp8,
CC nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear.
CC Late in infection, they merge into confluent complexes.
CC {ECO:0000250|UniProtKB:P0C6X9}.
CC -!- SUBCELLULAR LOCATION: [Helicase]: Host endoplasmic reticulum-Golgi
CC intermediate compartment {ECO:0000250|UniProtKB:P0C6X7}. Note=The
CC helicase interacts with the N protein in membranous complexes and
CC colocalizes with sites of synthesis of new viral RNA.
CC {ECO:0000250|UniProtKB:P0C6X9}.
CC -!- SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease]: Host
CC cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=Normal translation results in Replicase polyprotein 1a.
CC Ribosomal frameshifting at the end of this protein occurs at low
CC frequency and produces Replicase polyprotein 1ab.;
CC Name=Replicase polyprotein 1ab;
CC IsoId=P0DTD1-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a;
CC IsoId=P0DTC1-1; Sequence=External;
CC -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC association of the replication complex and thereby alter the
CC architecture of the host cell membrane. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically
CC processed. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- MISCELLANEOUS: [Replicase polyprotein 1ab]: Produced by -1 ribosomal
CC frameshifting at the 1a-1b genes boundary.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MN908947; QHD43415.1; -; Genomic_RNA.
DR RefSeq; YP_009724389.1; NC_045512.2.
DR PDB; 5R7Y; X-ray; 1.65 A; A=3264-3569.
DR PDB; 5R7Z; X-ray; 1.59 A; A=3264-3569.
DR PDB; 5R80; X-ray; 1.93 A; A=3264-3569.
DR PDB; 5R81; X-ray; 1.95 A; A=3264-3569.
DR PDB; 5R82; X-ray; 1.31 A; A=3264-3569.
DR PDB; 5R83; X-ray; 1.58 A; A=3264-3569.
DR PDB; 5R84; X-ray; 1.83 A; A=3264-3569.
DR PDB; 5R8T; X-ray; 1.27 A; A=3264-3569.
DR PDB; 5RE4; X-ray; 1.88 A; A=3264-3569.
DR PDB; 5RE5; X-ray; 2.07 A; A=3264-3569.
DR PDB; 5RE6; X-ray; 1.87 A; A=3264-3569.
DR PDB; 5RE7; X-ray; 1.79 A; A=3264-3569.
DR PDB; 5RE8; X-ray; 1.81 A; A=3264-3569.
DR PDB; 5RE9; X-ray; 1.72 A; A=3264-3569.
DR PDB; 5REA; X-ray; 1.63 A; A=3264-3569.
DR PDB; 5REB; X-ray; 1.68 A; A=3264-3569.
DR PDB; 5REC; X-ray; 1.73 A; A=3264-3569.
DR PDB; 5RED; X-ray; 1.47 A; A=3264-3569.
DR PDB; 5REE; X-ray; 1.77 A; A=3264-3569.
DR PDB; 5REF; X-ray; 1.61 A; A=3264-3569.
DR PDB; 5REG; X-ray; 1.67 A; A=3264-3569.
DR PDB; 5REH; X-ray; 1.80 A; A=3264-3569.
DR PDB; 5REI; X-ray; 1.82 A; A=3264-3569.
DR PDB; 5REJ; X-ray; 1.72 A; A=3264-3569.
DR PDB; 5REK; X-ray; 1.74 A; A=3264-3569.
DR PDB; 5REL; X-ray; 1.62 A; A=3264-3569.
DR PDB; 5REM; X-ray; 1.96 A; A=3264-3569.
DR PDB; 5REN; X-ray; 2.15 A; A=3264-3569.
DR PDB; 5REO; X-ray; 1.88 A; A=3264-3569.
DR PDB; 5REP; X-ray; 1.81 A; A=3264-3569.
DR PDB; 5RER; X-ray; 1.88 A; A=3264-3569.
DR PDB; 5RES; X-ray; 1.65 A; A=3264-3569.
DR PDB; 5RET; X-ray; 1.68 A; A=3264-3569.
DR PDB; 5REU; X-ray; 1.69 A; A=3264-3569.
DR PDB; 5REV; X-ray; 1.60 A; A=3264-3569.
DR PDB; 5REW; X-ray; 1.55 A; A=3264-3569.
DR PDB; 5REX; X-ray; 2.07 A; A=3264-3569.
DR PDB; 5REY; X-ray; 1.96 A; A=3264-3569.
DR PDB; 5REZ; X-ray; 1.79 A; A=3264-3569.
DR PDB; 5RF0; X-ray; 1.65 A; A=3264-3569.
DR PDB; 5RF1; X-ray; 1.73 A; A=3264-3569.
DR PDB; 5RF2; X-ray; 1.53 A; A=3264-3569.
DR PDB; 5RF3; X-ray; 1.50 A; A=3264-3569.
DR PDB; 5RF4; X-ray; 1.61 A; A=3264-3569.
DR PDB; 5RF5; X-ray; 1.74 A; A=3264-3569.
DR PDB; 5RF6; X-ray; 1.45 A; A=3264-3569.
DR PDB; 5RF7; X-ray; 1.54 A; A=3264-3569.
DR PDB; 5RF8; X-ray; 1.44 A; A=3264-3569.
DR PDB; 5RF9; X-ray; 1.43 A; A=3264-3569.
DR PDB; 5RFA; X-ray; 1.52 A; A=3264-3569.
DR PDB; 5RFB; X-ray; 1.48 A; A=3264-3569.
DR PDB; 5RFC; X-ray; 1.40 A; A=3264-3569.
DR PDB; 5RFD; X-ray; 1.41 A; A=3264-3569.
DR PDB; 5RFE; X-ray; 1.46 A; A=3264-3569.
DR PDB; 5RFF; X-ray; 1.78 A; A=3264-3569.
DR PDB; 5RFG; X-ray; 2.32 A; A=3264-3569.
DR PDB; 5RFH; X-ray; 1.58 A; A=3264-3569.
DR PDB; 5RFI; X-ray; 1.69 A; A=3264-3569.
DR PDB; 5RFJ; X-ray; 1.80 A; A=3264-3569.
DR PDB; 5RFK; X-ray; 1.75 A; A=3264-3569.
DR PDB; 5RFL; X-ray; 1.64 A; A=3264-3569.
DR PDB; 5RFM; X-ray; 2.06 A; A=3264-3569.
DR PDB; 5RFN; X-ray; 1.80 A; A=3264-3569.
DR PDB; 5RFO; X-ray; 1.83 A; A=3264-3569.
DR PDB; 5RFP; X-ray; 2.03 A; A=3264-3569.
DR PDB; 5RFQ; X-ray; 1.76 A; A=3264-3569.
DR PDB; 5RFR; X-ray; 1.71 A; A=3264-3569.
DR PDB; 5RFS; X-ray; 1.70 A; A=3264-3569.
DR PDB; 5RFT; X-ray; 1.58 A; A=3264-3569.
DR PDB; 5RFU; X-ray; 1.53 A; A=3264-3569.
DR PDB; 5RFV; X-ray; 1.48 A; A=3264-3569.
DR PDB; 5RFW; X-ray; 1.43 A; A=3264-3569.
DR PDB; 5RFX; X-ray; 1.55 A; A=3264-3569.
DR PDB; 5RFY; X-ray; 1.90 A; A=3264-3569.
DR PDB; 5RFZ; X-ray; 1.68 A; A=3264-3569.
DR PDB; 5RG0; X-ray; 1.72 A; A=3264-3569.
DR PDB; 5RG1; X-ray; 1.65 A; A=3264-3569.
DR PDB; 5RG2; X-ray; 1.63 A; A=3264-3569.
DR PDB; 5RG3; X-ray; 1.58 A; A=3264-3569.
DR PDB; 5RGG; X-ray; 2.26 A; A=3264-3569.
DR PDB; 5RGH; X-ray; 1.70 A; A=3264-3569.
DR PDB; 5RGI; X-ray; 1.57 A; A=3264-3569.
DR PDB; 5RGJ; X-ray; 1.34 A; A=3264-3569.
DR PDB; 5RGK; X-ray; 1.43 A; A=3264-3569.
DR PDB; 5RGL; X-ray; 1.76 A; A=3264-3569.
DR PDB; 5RGM; X-ray; 2.04 A; A=3264-3569.
DR PDB; 5RGN; X-ray; 1.86 A; A=3264-3569.
DR PDB; 5RGO; X-ray; 1.74 A; A=3264-3569.
DR PDB; 5RGP; X-ray; 2.07 A; A=3264-3569.
DR PDB; 5RGQ; X-ray; 2.15 A; A=3264-3569.
DR PDB; 5RGR; X-ray; 1.41 A; A=3264-3569.
DR PDB; 5RGS; X-ray; 1.72 A; A=3264-3569.
DR PDB; 5RGT; X-ray; 2.22 A; A=3264-3569.
DR PDB; 5RGU; X-ray; 2.11 A; A=3264-3569.
DR PDB; 5RGV; X-ray; 1.82 A; A=3264-3569.
DR PDB; 5RGW; X-ray; 1.43 A; A=3264-3569.
DR PDB; 5RGX; X-ray; 1.69 A; A=3264-3569.
DR PDB; 5RGY; X-ray; 1.98 A; A=3264-3569.
DR PDB; 5RGZ; X-ray; 1.52 A; A=3264-3569.
DR PDB; 5RH0; X-ray; 1.92 A; A=3264-3569.
DR PDB; 5RH1; X-ray; 1.96 A; A=3264-3569.
DR PDB; 5RH2; X-ray; 1.83 A; A=3264-3569.
DR PDB; 5RH3; X-ray; 1.69 A; A=3264-3569.
DR PDB; 5RH4; X-ray; 1.34 A; A=3264-3569.
DR PDB; 5RH5; X-ray; 1.72 A; A=3264-3569.
DR PDB; 5RH6; X-ray; 1.60 A; A=3264-3569.
DR PDB; 5RH7; X-ray; 1.71 A; A=3264-3569.
DR PDB; 5RH8; X-ray; 1.81 A; A=3264-3569.
DR PDB; 5RH9; X-ray; 1.91 A; A=3264-3569.
DR PDB; 5RHA; X-ray; 1.51 A; A=3264-3569.
DR PDB; 5RHB; X-ray; 1.43 A; A=3264-3569.
DR PDB; 5RHC; X-ray; 1.58 A; A=3264-3569.
DR PDB; 5RHD; X-ray; 1.57 A; A=3264-3569.
DR PDB; 5RHE; X-ray; 1.56 A; A=3264-3569.
DR PDB; 5RHF; X-ray; 1.76 A; A=3264-3569.
DR PDB; 6LU7; X-ray; 2.16 A; A=3264-3569.
DR PDB; 6LZE; X-ray; 1.50 A; A=3264-3566.
DR PDB; 6M03; X-ray; 2.00 A; A=3264-3569.
DR PDB; 6M0K; X-ray; 1.50 A; A=3264-3567.
DR PDB; 6M2N; X-ray; 2.20 A; A/B/C/D=3264-3569.
DR PDB; 6M2Q; X-ray; 1.70 A; A=3264-3569.
DR PDB; 6M71; EM; 2.90 A; C=3860-3942, D=3943-4090, A=4393-5324.
DR PDB; 6VWW; X-ray; 2.20 A; A/B=6453-6798.
DR PDB; 6VXS; X-ray; 2.03 A; A/B=1024-1192.
DR PDB; 6W01; X-ray; 1.90 A; A/B=6453-6798.
DR PDB; 6W02; X-ray; 1.50 A; A/B=1024-1192.
DR PDB; 6W4B; X-ray; 2.95 A; A/B=4141-4253.
DR PDB; 6W4H; X-ray; 1.80 A; A=6799-7096, B=4254-4392.
DR PDB; 6W61; X-ray; 2.00 A; B=4254-4392, A=6799-7096.
DR PDB; 6W63; X-ray; 2.10 A; A=3264-3569.
DR PDB; 6W6Y; X-ray; 1.45 A; A/B=1024-1192.
DR PDB; 6W75; X-ray; 1.95 A; B/D=4254-4392, A/C=6799-7096.
DR PDB; 6W9C; X-ray; 2.70 A; A/B/C=1564-1878.
DR PDB; 6W9Q; X-ray; 2.05 A; A=4141-4253.
DR PDB; 6WC1; X-ray; 2.40 A; A/B=4141-4253.
DR PDB; 6WCF; X-ray; 1.06 A; A=1024-1192.
DR PDB; 6WEN; X-ray; 1.35 A; A=1024-1192.
DR PDB; 6WEY; X-ray; 0.95 A; A=1025-1195.
DR PDB; 6WIQ; X-ray; 2.85 A; A=3860-3942, B=4019-4140.
DR PDB; 6WJT; X-ray; 2.00 A; A/C=6799-7096, B/D=4254-4392.
DR PDB; 6WKQ; X-ray; 1.98 A; A/C=6799-7096, B/D=4254-4392.
DR PDB; 6WKS; X-ray; 1.80 A; AAA=6799-7096, BBB=4254-4392.
DR PDB; 6WLC; X-ray; 1.82 A; A/B=6453-6798.
DR PDB; 6WNP; X-ray; 1.44 A; A=3264-3569.
DR PDB; 6WOJ; X-ray; 2.20 A; A/B/C/D=1023-1197.
DR PDB; 6WQ3; X-ray; 2.10 A; A=6799-7096, B=4254-4392.
DR PDB; 6WQD; X-ray; 1.95 A; A/C=3860-3942, B/D=4019-4140.
DR PDB; 6WQF; X-ray; 2.30 A; A=3264-3569.
DR PDB; 6WRH; X-ray; 1.60 A; A=1564-1878.
DR PDB; 6WRZ; X-ray; 2.25 A; A=6799-7096, B=4254-4392.
DR PDB; 6WTC; X-ray; 1.85 A; A/C=3860-3942, B/D=4019-4140.
DR PDB; 6WTJ; X-ray; 1.90 A; A=3264-3569.
DR PDB; 6WTK; X-ray; 2.00 A; A=3264-3569.
DR PDB; 6WTM; X-ray; 1.85 A; A/B=3264-3569.
DR PDB; 6WTT; X-ray; 2.15 A; A/B/C=3264-3567.
DR PDB; 6WUU; X-ray; 2.79 A; A/B/C/D=1562-1879.
DR PDB; 6WVN; X-ray; 2.00 A; A=6799-7096, B=4254-4392.
DR PDB; 6WX4; X-ray; 1.66 A; D=1562-1879.
DR PDB; 6WXC; X-ray; 1.85 A; A/B=6453-6798.
DR PDB; 6WXD; X-ray; 2.00 A; A/B=4141-4253.
DR PDB; 6WZU; X-ray; 1.79 A; A=1564-1878.
DR PDB; 6X1B; X-ray; 1.97 A; A/B=6453-6798.
DR PDB; 6X4I; X-ray; 1.85 A; A/B=6453-6798.
DR PDB; 6XA4; X-ray; 1.65 A; A=3264-3569.
DR PDB; 6XA9; X-ray; 2.90 A; A/C/E=1563-1878.
DR PDB; 6XAA; X-ray; 2.70 A; A=1563-1878.
DR PDB; 6XB0; X-ray; 1.80 A; A=3264-3569.
DR PDB; 6XB1; X-ray; 1.80 A; A=3264-3569.
DR PDB; 6XB2; X-ray; 2.10 A; A=3264-3569.
DR PDB; 6XBG; X-ray; 1.45 A; A/B=3264-3569.
DR PDB; 6XBH; X-ray; 1.60 A; A=3264-3569.
DR PDB; 6XBI; X-ray; 1.70 A; A/B=3264-3569.
DR PDB; 6XCH; X-ray; 2.20 A; A=3264-3569.
DR PDB; 6XDH; X-ray; 2.35 A; A/B=6453-6798.
DR PDB; 6XFN; X-ray; 1.70 A; A=3264-3569.
DR PDB; 6XG3; X-ray; 2.48 A; A=1564-1878.
DR PDB; 6XHM; X-ray; 1.41 A; A/B=3264-3569.
DR PDB; 6XHU; X-ray; 1.80 A; A/C=3264-3569.
DR PDB; 6XIP; X-ray; 1.50 A; A/C=3860-3942, B/D=4019-4140.
DR PDB; 6XKF; X-ray; 1.80 A; A/B=3264-3569.
DR PDB; 6XKH; X-ray; 1.28 A; A=3264-3569.
DR PDB; 6XKM; X-ray; 2.25 A; A=6799-7096, B=4254-4392.
DR PDB; 6XMK; X-ray; 1.70 A; A/B=3264-3568.
DR PDB; 6XOA; X-ray; 2.10 A; A/B/C/D=3264-3569.
DR PDB; 6XQS; X-ray; 1.90 A; A=3264-3569.
DR PDB; 6XQT; X-ray; 2.30 A; A/B=3264-3569.
DR PDB; 6XQU; X-ray; 2.20 A; A=3264-3569.
DR PDB; 6XR3; X-ray; 1.45 A; A=3264-3569.
DR PDB; 6Y2E; X-ray; 1.75 A; A=3264-3569.
DR PDB; 6Y2F; X-ray; 2.16 A; A=3264-3569.
DR PDB; 6Y2G; X-ray; 2.16 A; A=3264-3569.
DR PDB; 6Y84; X-ray; 1.39 A; A=3264-3569.
DR PDB; 6YB7; X-ray; 1.25 A; A=3264-3569.
DR PDB; 6YNQ; X-ray; 1.80 A; A=3264-3569.
DR PDB; 6YT8; X-ray; 2.05 A; A=3264-3569.
DR PDB; 6YVA; X-ray; 3.18 A; A=1564-1878.
DR PDB; 6YVF; X-ray; 1.60 A; A=3264-3569.
DR PDB; 6YWK; X-ray; 2.20 A; A/B/C/D/E=1025-1194.
DR PDB; 6YWL; X-ray; 2.50 A; A/B/C/D/E=1025-1194.
DR PDB; 6YWM; X-ray; 2.16 A; A/B/C=1025-1194.
DR PDB; 6YYT; EM; 2.90 A; A=4424-5321, B=3948-4133, C=3860-3932.
DR PDB; 6YZ1; X-ray; 2.40 A; A=6798-7096, B=4263-4384.
DR PDB; 6YZ6; X-ray; 1.70 A; A=3264-3569.
DR PDB; 6Z2E; X-ray; 1.70 A; AAA=3264-3569.
DR PDB; 6ZCT; X-ray; 2.55 A; A=4263-4384.
DR PDB; 6ZLW; EM; 2.60 A; i=1-180.
DR PDB; 6ZM7; EM; 2.70 A; CF=1-180.
DR PDB; 6ZME; EM; 3.00 A; CF=1-180.
DR PDB; 6ZMI; EM; 2.60 A; i=1-180.
DR PDB; 6ZMO; EM; 3.10 A; i=1-180.
DR PDB; 6ZMT; EM; 3.00 A; i=1-180.
DR PDB; 6ZN5; EM; 3.20 A; i=1-180.
DR PDB; 6ZOJ; EM; 2.80 A; j=1-180.
DR PDB; 6ZOK; EM; 2.80 A; j=1-180.
DR PDB; 6ZON; EM; 3.00 A; J=1-180.
DR PDB; 6ZP4; EM; 2.90 A; J=1-180.
DR PDB; 6ZRT; X-ray; 2.10 A; A=3264-3569.
DR PDB; 6ZRU; X-ray; 2.10 A; A=3264-3569.
DR PDB; 6ZSL; X-ray; 1.94 A; A/B=5325-5925.
DR PDB; 7BQ7; X-ray; 2.37 A; A=6799-7096, B=4254-4392.
DR PDB; 7BQY; X-ray; 1.70 A; A=3264-3569.
DR PDB; 7BRO; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7BRP; X-ray; 1.80 A; A/B=3264-3569.
DR PDB; 7BRR; X-ray; 1.40 A; A/B=3264-3569.
DR PDB; 7BTF; EM; 2.95 A; A=4393-5324, B=3943-4090, C=3860-3942.
DR PDB; 7BUY; X-ray; 1.60 A; A=3264-3569.
DR PDB; 7BV1; EM; 2.80 A; C=3860-3942, B=3943-4140, A=4393-5324.
DR PDB; 7BV2; EM; 2.50 A; C=3860-3942, B=3943-4140, A=4393-5324.
DR PDB; 7BZF; EM; 3.26 A; A=4393-5324, B=3943-4140, D=3943-4140, E=3860-3942.
DR PDB; 7C2I; X-ray; 2.50 A; A=6799-7096, B=4254-4392.
DR PDB; 7C2J; X-ray; 2.80 A; A=6799-7096, B=4254-4392.
DR PDB; 7C2K; EM; 2.93 A; A=4393-5324, B=3943-4140, D=3943-4140, E=3860-3942.
DR PDB; 7C2Q; X-ray; 1.93 A; A/B=3266-3561.
DR PDB; 7C2Y; X-ray; 1.91 A; A/B=3264-3561.
DR PDB; 7C6S; X-ray; 1.60 A; A=3264-3569.
DR PDB; 7C6U; X-ray; 2.00 A; A=3264-3569.
DR PDB; 7C7P; X-ray; 1.74 A; A/B=3264-3569.
DR PDB; 7C8B; X-ray; 2.20 A; A=3264-3569.
DR PDB; 7C8R; X-ray; 2.30 A; A=3264-3569.
DR PDB; 7C8T; X-ray; 2.05 A; A=3264-3569.
DR PDB; 7C8U; X-ray; 2.35 A; A=3264-3569.
DR PDB; 7CBT; X-ray; 2.35 A; A/B=3264-3569.
DR PDB; 7CJD; X-ray; 2.50 A; A/B/C/D=1564-1881.
DR PDB; 7CJM; X-ray; 3.20 A; B=1564-1878.
DR PDB; 7CMD; X-ray; 2.59 A; A/B/C/D=1564-1881.
DR PDB; 7COM; X-ray; 2.25 A; A/B=3264-3569.
DR PDB; 7JFQ; X-ray; 1.55 A; A=3264-3569.
DR PDB; 7JHE; X-ray; 2.25 A; A=6799-7096, B=4254-4392.
DR PDB; 7JIB; X-ray; 2.65 A; A=6799-7096, B=4254-4392.
DR PDB; 7JME; X-ray; 1.55 A; A=1025-1195.
DR PDB; 7JPE; X-ray; 2.18 A; A=6799-7096, B=4254-4392.
DR PDB; 7JR3; X-ray; 1.55 A; A=3264-3569.
DR PDB; 7JR4; X-ray; 1.55 A; A=3264-3569.
DR PDB; 7JU7; X-ray; 1.60 A; A=3264-3569.
DR PDB; 7JUN; Other; 2.30 A; A=3264-3569.
DR PDB; 7JYC; X-ray; 1.79 A; A=3264-3569.
DR PDBsum; 5R7Y; -.
DR PDBsum; 5R7Z; -.
DR PDBsum; 5R80; -.
DR PDBsum; 5R81; -.
DR PDBsum; 5R82; -.
DR PDBsum; 5R83; -.
DR PDBsum; 5R84; -.
DR PDBsum; 5R8T; -.
DR PDBsum; 5RE4; -.
DR PDBsum; 5RE5; -.
DR PDBsum; 5RE6; -.
DR PDBsum; 5RE7; -.
DR PDBsum; 5RE8; -.
DR PDBsum; 5RE9; -.
DR PDBsum; 5REA; -.
DR PDBsum; 5REB; -.
DR PDBsum; 5REC; -.
DR PDBsum; 5RED; -.
DR PDBsum; 5REE; -.
DR PDBsum; 5REF; -.
DR PDBsum; 5REG; -.
DR PDBsum; 5REH; -.
DR PDBsum; 5REI; -.
DR PDBsum; 5REJ; -.
DR PDBsum; 5REK; -.
DR PDBsum; 5REL; -.
DR PDBsum; 5REM; -.
DR PDBsum; 5REN; -.
DR PDBsum; 5REO; -.
DR PDBsum; 5REP; -.
DR PDBsum; 5RER; -.
DR PDBsum; 5RES; -.
DR PDBsum; 5RET; -.
DR PDBsum; 5REU; -.
DR PDBsum; 5REV; -.
DR PDBsum; 5REW; -.
DR PDBsum; 5REX; -.
DR PDBsum; 5REY; -.
DR PDBsum; 5REZ; -.
DR PDBsum; 5RF0; -.
DR PDBsum; 5RF1; -.
DR PDBsum; 5RF2; -.
DR PDBsum; 5RF3; -.
DR PDBsum; 5RF4; -.
DR PDBsum; 5RF5; -.
DR PDBsum; 5RF6; -.
DR PDBsum; 5RF7; -.
DR PDBsum; 5RF8; -.
DR PDBsum; 5RF9; -.
DR PDBsum; 5RFA; -.
DR PDBsum; 5RFB; -.
DR PDBsum; 5RFC; -.
DR PDBsum; 5RFD; -.
DR PDBsum; 5RFE; -.
DR PDBsum; 5RFF; -.
DR PDBsum; 5RFG; -.
DR PDBsum; 5RFH; -.
DR PDBsum; 5RFI; -.
DR PDBsum; 5RFJ; -.
DR PDBsum; 5RFK; -.
DR PDBsum; 5RFL; -.
DR PDBsum; 5RFM; -.
DR PDBsum; 5RFN; -.
DR PDBsum; 5RFO; -.
DR PDBsum; 5RFP; -.
DR PDBsum; 5RFQ; -.
DR PDBsum; 5RFR; -.
DR PDBsum; 5RFS; -.
DR PDBsum; 5RFT; -.
DR PDBsum; 5RFU; -.
DR PDBsum; 5RFV; -.
DR PDBsum; 5RFW; -.
DR PDBsum; 5RFX; -.
DR PDBsum; 5RFY; -.
DR PDBsum; 5RFZ; -.
DR PDBsum; 5RG0; -.
DR PDBsum; 5RG1; -.
DR PDBsum; 5RG2; -.
DR PDBsum; 5RG3; -.
DR PDBsum; 5RGG; -.
DR PDBsum; 5RGH; -.
DR PDBsum; 5RGI; -.
DR PDBsum; 5RGJ; -.
DR PDBsum; 5RGK; -.
DR PDBsum; 5RGL; -.
DR PDBsum; 5RGM; -.
DR PDBsum; 5RGN; -.
DR PDBsum; 5RGO; -.
DR PDBsum; 5RGP; -.
DR PDBsum; 5RGQ; -.
DR PDBsum; 5RGR; -.
DR PDBsum; 5RGS; -.
DR PDBsum; 5RGT; -.
DR PDBsum; 5RGU; -.
DR PDBsum; 5RGV; -.
DR PDBsum; 5RGW; -.
DR PDBsum; 5RGX; -.
DR PDBsum; 5RGY; -.
DR PDBsum; 5RGZ; -.
DR PDBsum; 5RH0; -.
DR PDBsum; 5RH1; -.
DR PDBsum; 5RH2; -.
DR PDBsum; 5RH3; -.
DR PDBsum; 5RH4; -.
DR PDBsum; 5RH5; -.
DR PDBsum; 5RH6; -.
DR PDBsum; 5RH7; -.
DR PDBsum; 5RH8; -.
DR PDBsum; 5RH9; -.
DR PDBsum; 5RHA; -.
DR PDBsum; 5RHB; -.
DR PDBsum; 5RHC; -.
DR PDBsum; 5RHD; -.
DR PDBsum; 5RHE; -.
DR PDBsum; 5RHF; -.
DR PDBsum; 6LU7; -.
DR PDBsum; 6LZE; -.
DR PDBsum; 6M03; -.
DR PDBsum; 6M0K; -.
DR PDBsum; 6M2N; -.
DR PDBsum; 6M2Q; -.
DR PDBsum; 6M71; -.
DR PDBsum; 6VWW; -.
DR PDBsum; 6VXS; -.
DR PDBsum; 6W01; -.
DR PDBsum; 6W02; -.
DR PDBsum; 6W4B; -.
DR PDBsum; 6W4H; -.
DR PDBsum; 6W61; -.
DR PDBsum; 6W63; -.
DR PDBsum; 6W6Y; -.
DR PDBsum; 6W75; -.
DR PDBsum; 6W9C; -.
DR PDBsum; 6W9Q; -.
DR PDBsum; 6WC1; -.
DR PDBsum; 6WCF; -.
DR PDBsum; 6WEN; -.
DR PDBsum; 6WEY; -.
DR PDBsum; 6WIQ; -.
DR PDBsum; 6WJT; -.
DR PDBsum; 6WKQ; -.
DR PDBsum; 6WKS; -.
DR PDBsum; 6WLC; -.
DR PDBsum; 6WNP; -.
DR PDBsum; 6WOJ; -.
DR PDBsum; 6WQ3; -.
DR PDBsum; 6WQD; -.
DR PDBsum; 6WQF; -.
DR PDBsum; 6WRH; -.
DR PDBsum; 6WRZ; -.
DR PDBsum; 6WTC; -.
DR PDBsum; 6WTJ; -.
DR PDBsum; 6WTK; -.
DR PDBsum; 6WTM; -.
DR PDBsum; 6WTT; -.
DR PDBsum; 6WUU; -.
DR PDBsum; 6WVN; -.
DR PDBsum; 6WX4; -.
DR PDBsum; 6WXC; -.
DR PDBsum; 6WXD; -.
DR PDBsum; 6WZU; -.
DR PDBsum; 6X1B; -.
DR PDBsum; 6X4I; -.
DR PDBsum; 6XA4; -.
DR PDBsum; 6XA9; -.
DR PDBsum; 6XAA; -.
DR PDBsum; 6XB0; -.
DR PDBsum; 6XB1; -.
DR PDBsum; 6XB2; -.
DR PDBsum; 6XBG; -.
DR PDBsum; 6XBH; -.
DR PDBsum; 6XBI; -.
DR PDBsum; 6XCH; -.
DR PDBsum; 6XDH; -.
DR PDBsum; 6XFN; -.
DR PDBsum; 6XG3; -.
DR PDBsum; 6XHM; -.
DR PDBsum; 6XHU; -.
DR PDBsum; 6XIP; -.
DR PDBsum; 6XKF; -.
DR PDBsum; 6XKH; -.
DR PDBsum; 6XKM; -.
DR PDBsum; 6XMK; -.
DR PDBsum; 6XOA; -.
DR PDBsum; 6XQS; -.
DR PDBsum; 6XQT; -.
DR PDBsum; 6XQU; -.
DR PDBsum; 6XR3; -.
DR PDBsum; 6Y2E; -.
DR PDBsum; 6Y2F; -.
DR PDBsum; 6Y2G; -.
DR PDBsum; 6Y84; -.
DR PDBsum; 6YB7; -.
DR PDBsum; 6YNQ; -.
DR PDBsum; 6YT8; -.
DR PDBsum; 6YVA; -.
DR PDBsum; 6YVF; -.
DR PDBsum; 6YWK; -.
DR PDBsum; 6YWL; -.
DR PDBsum; 6YWM; -.
DR PDBsum; 6YYT; -.
DR PDBsum; 6YZ1; -.
DR PDBsum; 6YZ6; -.
DR PDBsum; 6Z2E; -.
DR PDBsum; 6ZCT; -.
DR PDBsum; 6ZLW; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZMT; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOK; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZRT; -.
DR PDBsum; 6ZRU; -.
DR PDBsum; 6ZSL; -.
DR PDBsum; 7BQ7; -.
DR PDBsum; 7BQY; -.
DR PDBsum; 7BRO; -.
DR PDBsum; 7BRP; -.
DR PDBsum; 7BRR; -.
DR PDBsum; 7BTF; -.
DR PDBsum; 7BUY; -.
DR PDBsum; 7BV1; -.
DR PDBsum; 7BV2; -.
DR PDBsum; 7BZF; -.
DR PDBsum; 7C2I; -.
DR PDBsum; 7C2J; -.
DR PDBsum; 7C2K; -.
DR PDBsum; 7C2Q; -.
DR PDBsum; 7C2Y; -.
DR PDBsum; 7C6S; -.
DR PDBsum; 7C6U; -.
DR PDBsum; 7C7P; -.
DR PDBsum; 7C8B; -.
DR PDBsum; 7C8R; -.
DR PDBsum; 7C8T; -.
DR PDBsum; 7C8U; -.
DR PDBsum; 7CBT; -.
DR PDBsum; 7CJD; -.
DR PDBsum; 7CJM; -.
DR PDBsum; 7CMD; -.
DR PDBsum; 7COM; -.
DR PDBsum; 7JFQ; -.
DR PDBsum; 7JHE; -.
DR PDBsum; 7JIB; -.
DR PDBsum; 7JME; -.
DR PDBsum; 7JPE; -.
DR PDBsum; 7JR3; -.
DR PDBsum; 7JR4; -.
DR PDBsum; 7JU7; -.
DR PDBsum; 7JUN; -.
DR PDBsum; 7JYC; -.
DR SMR; P0DTD1; -.
DR BioGRID; 4383850; 13.
DR BioGRID; 4383851; 27.
DR BioGRID; 4383852; 32.
DR BioGRID; 4383853; 61.
DR BioGRID; 4383854; 9.
DR BioGRID; 4383855; 85.
DR BioGRID; 4383856; 54.
DR BioGRID; 4383857; 61.
DR BioGRID; 4383858; 27.
DR BioGRID; 4383859; 36.
DR BioGRID; 4383860; 42.
DR BioGRID; 4383861; 67.
DR BioGRID; 4383862; 29.
DR BioGRID; 4383863; 62.
DR BioGRID; 4383864; 4.
DR ComplexPortal; CPX-5685; SARS-CoV-2 main protease complex.
DR ComplexPortal; CPX-5687; SARS-CoV-2 NSP9 complex.
DR ComplexPortal; CPX-5688; SARS-CoV-2 NSP10-NSP16 2'-O-methyltransferase complex.
DR ComplexPortal; CPX-5689; SARS-CoV-2 NSP15 complex.
DR ComplexPortal; CPX-5690; SARS-CoV-2 primase complex.
DR ComplexPortal; CPX-5691; SARS-CoV-2 NSP3-NSP4-NSP6 complex.
DR ComplexPortal; CPX-5692; SARS-CoV-2 3'-5' exoribonuclease proof-reading complex.
DR ComplexPortal; CPX-5742; SARS-CoV-2 polymerase complex.
DR IntAct; P0DTD1; 427.
DR GeneID; 43740578; -.
DR Proteomes; UP000464024; Genome.
DR GO; GO:0039714; C:cytoplasmic viral factory; ISS:UniProtKB.
DR GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019785; F:ISG15-specific protease activity; ISS:UniProtKB.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0039519; P:modulation by virus of host autophagy; ISS:UniProtKB.
DR GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR GO; GO:0039690; P:positive stranded viral RNA replication; ISS:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; ISS:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; ISS:UniProtKB.
DR GO; GO:0039548; P:suppression by virus of host IRF3 activity; ISS:UniProtKB.
DR GO; GO:0039579; P:suppression by virus of host ISG15 activity; ISS:UniProtKB.
DR GO; GO:0039644; P:suppression by virus of host NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0039722; P:suppression by virus of host toll-like receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0039547; P:suppression by virus of host TRAF activity; ISS:UniProtKB.
DR GO; GO:0039604; P:suppression by virus of host translation; ISS:UniProtKB.
DR GO; GO:0039501; P:suppression by virus of host type I interferon production; ISS:UniProtKB.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0001172; P:transcription, RNA-templated; ISS:UniProtKB.
DR GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; ISS:UniProtKB.
DR GO; GO:0019083; P:viral transcription; ISS:UniProtKB.
DR CDD; cd15239; 7tm_YRO2_fungal-like; 1.
DR CDD; cd18808; SF1_C_Upf1; 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; 2.20.25.360; -; 1.
DR Gene3D; 2.30.30.590; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.40.10.250; -; 1.
DR Gene3D; 2.40.10.290; -; 1.
DR Gene3D; 3.10.20.350; -; 1.
DR Gene3D; 3.10.20.540; -; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.220.20; -; 1.
DR Gene3D; 3.40.220.30; -; 1.
DR Gene3D; 3.40.50.11020; -; 1.
DR Gene3D; 3.40.50.11580; -; 1.
DR Gene3D; 3.90.70.90; -; 1.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR043609; CoV_NSP15_C.
DR InterPro; IPR043608; CoV_NSP15_M.
DR InterPro; IPR043606; CoV_NSP15_N.
DR InterPro; IPR043613; CoV_NSP2_C.
DR InterPro; IPR043615; CoV_NSP2_N.
DR InterPro; IPR043611; CoV_NSP3_C.
DR InterPro; IPR043612; CoV_NSP4_N.
DR InterPro; IPR043610; CoV_NSP6.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR022733; DPUP_SUD_C_bCoV.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR042570; NAR_sf.
DR InterPro; IPR036333; NSP10_sf_CoV.
DR InterPro; IPR009466; NSP14_CoV.
DR InterPro; IPR043174; NSP15_middle_sf.
DR InterPro; IPR042515; NSP15_N_CoV.
DR InterPro; IPR009461; NSP16_CoV-like.
DR InterPro; IPR021590; NSP1_bCoV.
DR InterPro; IPR038030; NSP1_sf_bCoV.
DR InterPro; IPR024375; NSP3_bCoV.
DR InterPro; IPR024358; NSP3_N_bCoV.
DR InterPro; IPR032592; NSP3_NAR_bCoV.
DR InterPro; IPR038166; NSP3_PL2pro_sf_CoV.
DR InterPro; IPR038400; NSP3_SUD-M_sf_bCoV.
DR InterPro; IPR043478; NSP3_SUD-N_bCoV.
DR InterPro; IPR038083; NSP3A-like.
DR InterPro; IPR032505; NSP4_C_CoV.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR014828; NSP7_CoV.
DR InterPro; IPR037204; NSP7_sf_CoV.
DR InterPro; IPR014829; NSP8_CoV-like.
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; IPR043177; PLpro_N_sf_CoV.
DR InterPro; IPR043503; PLpro_palm_finger_dom_CoV.
DR InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR009469; RNA_pol_N_coronovir.
DR InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR InterPro; IPR029063; SAM-dependent_MTases.
DR InterPro; IPR043476; Yro2-like_7TM.
DR Pfam; PF16251; bCoV_NAR; 1.
DR Pfam; PF11501; bCoV_NSP1; 1.
DR Pfam; PF12379; bCoV_NSP3_N; 1.
DR Pfam; PF12124; bCoV_SUD_C; 1.
DR Pfam; PF11633; bCoV_SUD_M; 1.
DR Pfam; PF06471; CoV_Methyltr_1; 1.
DR Pfam; PF06460; CoV_Methyltr_2; 1.
DR Pfam; PF09401; CoV_NSP10; 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; 1.
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; 1.
DR Pfam; PF06478; CoV_RPol_N; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF101816; SSF101816; 1.
DR SUPFAM; SSF140367; SSF140367; 1.
DR SUPFAM; SSF142877; SSF142877; 1.
DR SUPFAM; SSF143076; SSF143076; 1.
DR SUPFAM; SSF144246; SSF144246; 1.
DR SUPFAM; SSF159936; SSF159936; 1.
DR SUPFAM; SSF160099; SSF160099; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51653; CV_ZBD; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
DR PROSITE; PS51442; M_PRO; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51124; PEPTIDASE_C16; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Decay of host mRNAs by virus; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Exonuclease; Helicase;
KW Host cytoplasm; Host gene expression shutoff by virus; Host membrane;
KW Host mRNA suppression by virus; Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host ISG15 by virus; Inhibition of host NF-kappa-B by virus;
KW Leucine-rich repeat; Membrane; Metal-binding; Methyltransferase;
KW Modulation of host ubiquitin pathway by viral deubiquitinase;
KW Modulation of host ubiquitin pathway by virus; Nuclease;
KW Nucleotide-binding; Nucleotidyltransferase; Protease; Reference proteome;
KW Repeat; Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
KW Thiol protease; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Viral immunoevasion; Viral RNA replication; Zinc;
KW Zinc-finger.
FT CHAIN 1..7096
FT /note="Replicase polyprotein 1ab"
FT /id="PRO_0000449618"
FT CHAIN 1..180
FT /note="Host translation inhibitor nsp1"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449619"
FT CHAIN 181..818
FT /note="Non-structural protein 2"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449620"
FT CHAIN 819..2763
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449621"
FT CHAIN 2764..3263
FT /note="Non-structural protein 4"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449622"
FT CHAIN 3264..3569
FT /note="3C-like proteinase"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449623"
FT CHAIN 3570..3859
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449624"
FT CHAIN 3860..3942
FT /note="Non-structural protein 7"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449625"
FT CHAIN 3943..4140
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449626"
FT CHAIN 4141..4253
FT /note="Non-structural protein 9"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449627"
FT CHAIN 4254..4392
FT /note="Non-structural protein 10"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449628"
FT CHAIN 4393..5324
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449629"
FT CHAIN 5325..5925
FT /note="Helicase"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449630"
FT CHAIN 5926..6452
FT /note="Proofreading exoribonuclease"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449631"
FT CHAIN 6453..6798
FT /note="Uridylate-specific endoribonuclease"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449632"
FT CHAIN 6799..7096
FT /note="2'-O-methyltransferase"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT /id="PRO_0000449633"
FT TOPO_DOM 1..2225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2226..2246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2247..2317
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 2318..2338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2339..2775
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2776..2796
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2797..3044
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 3045..3065
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3066..3099
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3100..3120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3121..3127
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 3128..3148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3149..3586
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3587..3607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3608
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 3609..3629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3630..3634
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3635..3655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3656..3673
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 3674..3694
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3695..3729
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3730..3750
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3751..3778
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 3779..3799
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3800..7096
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 545..569
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 697..719
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT DOMAIN 1025..1194
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1634..1898
FT /note="Peptidase C16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT REPEAT 1680..1702
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 3185..3206
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT DOMAIN 3264..3569
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT REPEAT 3935..3959
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 3977..4004
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 4591..4616
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT DOMAIN 5004..5166
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 5325..5408
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT REPEAT 5552..5572
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT DOMAIN 5581..5762
FT /note="(+)RNA virus helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT DOMAIN 5763..5932
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT REPEAT 6817..6841
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT ZN_FING 1752..1789
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT NP_BIND 5606..5613
FT /note="NTP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00990"
FT REGION 154..180
FT /note="Binding to 40s ribosome mRNA entry channel"
FT /evidence="ECO:0000269|PubMed:32680882"
FT REGION 4937..4947
FT /note="Interaction with RMP Remdesivir"
FT /evidence="ECO:0000269|PubMed:32358203"
FT ACT_SITE 1674
FT /note="For PL1-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444,
FT ECO:0000269|PubMed:32726803"
FT ACT_SITE 1835
FT /note="For PL2-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ACT_SITE 3304
FT /note="For 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772,
FT ECO:0000305|PubMed:32198291"
FT ACT_SITE 3408
FT /note="Nucleophile; for 3CL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772,
FT ECO:0000269|PubMed:32198291"
FT METAL 4687
FT /note="Zinc 1; structural"
FT /evidence="ECO:0000269|PubMed:32358203,
FT ECO:0000269|PubMed:32526208"
FT METAL 4693
FT /note="Zinc 1; structural"
FT /evidence="ECO:0000269|PubMed:32358203,
FT ECO:0000269|PubMed:32526208"
FT METAL 4698
FT /note="Zinc 1; structural"
FT /evidence="ECO:0000269|PubMed:32358203,
FT ECO:0000269|PubMed:32526208"
FT METAL 4702
FT /note="Zinc 1; structural"
FT /evidence="ECO:0000269|PubMed:32358203,
FT ECO:0000269|PubMed:32526208"
FT METAL 4879
FT /note="Zinc 2; structural"
FT /evidence="ECO:0000269|PubMed:32358203,
FT ECO:0000269|PubMed:32526208"
FT METAL 5034
FT /note="Zinc 2; structural"
FT /evidence="ECO:0000269|PubMed:32358203,
FT ECO:0000269|PubMed:32526208"
FT METAL 5037
FT /note="Zinc 2; structural"
FT /evidence="ECO:0000269|PubMed:32358203,
FT ECO:0000269|PubMed:32526208"
FT METAL 5038
FT /note="Zinc 2; structural"
FT /evidence="ECO:0000269|PubMed:32358203,
FT ECO:0000269|PubMed:32526208"
FT METAL 5329
FT /note="Zinc 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT METAL 5332
FT /note="Zinc 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT METAL 5340
FT /note="Zinc 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT METAL 5343
FT /note="Zinc 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT METAL 5350
FT /note="Zinc 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT METAL 5353
FT /note="Zinc 4; via tele nitrogen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT METAL 5357
FT /note="Zinc 4; via pros nitrogen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT METAL 5363
FT /note="Zinc 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT METAL 5374
FT /note="Zinc 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT METAL 5379
FT /note="Zinc 5; via pros nitrogen"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT METAL 5396
FT /note="Zinc 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT METAL 5399
FT /note="Zinc 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT SITE 180..181
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 818..819
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 2763..2764
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 3263..3264
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 3569..3570
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 3859..3860
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 3942..3943
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 4140..4141
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 4253..4254
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 4392..4393
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 5324..5325
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 5925..5926
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 6452..6453
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT SITE 6798..6799
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6V3"
FT MUTAGEN 164
FT /note="K->A: Complete loss of ribosome binding and cellular
FT translation inhibition."
FT /evidence="ECO:0000269|PubMed:32680882"
FT MUTAGEN 165
FT /note="H->A: Complete loss of ribosome binding and cellular
FT translation inhibition."
FT /evidence="ECO:0000269|PubMed:32680882"
FT MUTAGEN 1629
FT /note="V->A: Partial loss of ISG15 cleavage in vitro."
FT /evidence="ECO:0000269|PubMed:32726803"
FT MUTAGEN 1632
FT /note="F->A: Partial loss of ISG15 cleavage in vitro."
FT /evidence="ECO:0000269|PubMed:32726803"
FT MUTAGEN 1638
FT /note="T->A: Partial loss of ubiquitin cleavage in vitro;
FT no effect on ISG15 cleavage in vitro."
FT /evidence="ECO:0000269|PubMed:32726803"
FT MUTAGEN 1638
FT /note="T->L: Increased cleavage of ubiquitin in vitro; no
FT effect on ISG15 cleavage in vitro."
FT /evidence="ECO:0000269|PubMed:32726803"
FT MUTAGEN 1674
FT /note="C->S: Complete loss of PL-pro activity."
FT /evidence="ECO:0000269|PubMed:32726803"
FT MUTAGEN 1831
FT /note="Y->G,T: Reduced inhibition by GRL-0617."
FT /evidence="ECO:0000269|PubMed:32726803"
FT MUTAGEN 5253
FT /note="S->A: Reduces RdRp inhibition by remdesivir."
FT /evidence="ECO:0000269|PubMed:32526208"
FT HELIX 153..160
FT /evidence="ECO:0000244|PDB:6ZOJ"
FT HELIX 166..178
FT /evidence="ECO:0000244|PDB:6ZOJ"
FT STRAND 1032..1042
FT /evidence="ECO:0000244|PDB:6WEY"
FT HELIX 1045..1052
FT /evidence="ECO:0000244|PDB:6WEY"
FT STRAND 1055..1060
FT /evidence="ECO:0000244|PDB:6WEY"
FT HELIX 1070..1078
FT /evidence="ECO:0000244|PDB:6WEY"
FT TURN 1079..1081
FT /evidence="ECO:0000244|PDB:6WEY"
FT HELIX 1082..1094
FT /evidence="ECO:0000244|PDB:6WEY"
FT STRAND 1102..1106
FT /evidence="ECO:0000244|PDB:6WEY"
FT TURN 1108..1110
FT /evidence="ECO:0000244|PDB:6WEY"
FT STRAND 1112..1117
FT /evidence="ECO:0000244|PDB:6WEY"
FT HELIX 1122..1124
FT /evidence="ECO:0000244|PDB:6WEY"
FT HELIX 1128..1130
FT /evidence="ECO:0000244|PDB:6WEY"
FT HELIX 1131..1136
FT /evidence="ECO:0000244|PDB:6WEY"
FT HELIX 1137..1140
FT /evidence="ECO:0000244|PDB:6WEY"
FT STRAND 1141..1146
FT /evidence="ECO:0000244|PDB:6WEY"
FT HELIX 1152..1154
FT /evidence="ECO:0000244|PDB:6WEN"
FT HELIX 1158..1168
FT /evidence="ECO:0000244|PDB:6WEY"
FT STRAND 1171..1177
FT /evidence="ECO:0000244|PDB:6WEY"
FT HELIX 1180..1191
FT /evidence="ECO:0000244|PDB:6WEY"
FT STRAND 1567..1578
FT /evidence="ECO:0000244|PDB:6WRH"
FT STRAND 1580..1585
FT /evidence="ECO:0000244|PDB:6WRH"
FT HELIX 1590..1594
FT /evidence="ECO:0000244|PDB:6WRH"
FT STRAND 1595..1599
FT /evidence="ECO:0000244|PDB:6WRH"
FT STRAND 1605..1607
FT /evidence="ECO:0000244|PDB:6W9C"
FT HELIX 1611..1613
FT /evidence="ECO:0000244|PDB:6WRH"
FT STRAND 1617..1620
FT /evidence="ECO:0000244|PDB:6WRH"
FT HELIX 1625..1635
FT /evidence="ECO:0000244|PDB:6WRH"
FT HELIX 1642..1653
FT /evidence="ECO:0000244|PDB:6WRH"
FT STRAND 1660..1665
FT /evidence="ECO:0000244|PDB:6W9C"
FT TURN 1671..1673
FT /evidence="ECO:0000244|PDB:6WX4"
FT HELIX 1674..1683
FT /evidence="ECO:0000244|PDB:6WRH"
FT STRAND 1690..1692
FT /evidence="ECO:0000244|PDB:6WRH"
FT HELIX 1693..1703
FT /evidence="ECO:0000244|PDB:6WRH"
FT HELIX 1708..1718
FT /evidence="ECO:0000244|PDB:6WRH"
FT HELIX 1728..1737
FT /evidence="ECO:0000244|PDB:6WRH"
FT STRAND 1745..1752
FT /evidence="ECO:0000244|PDB:6WRH"
FT TURN 1753..1755
FT /evidence="ECO:0000244|PDB:6WRH"
FT STRAND 1756..1763
FT /evidence="ECO:0000244|PDB:6WRH"
FT HELIX 1765..1768
FT /evidence="ECO:0000244|PDB:6WRH"
FT STRAND 1769..1772
FT /evidence="ECO:0000244|PDB:6WRH"
FT HELIX 1776..1781
FT /evidence="ECO:0000244|PDB:6WRH"
FT STRAND 1783..1786
FT /evidence="ECO:0000244|PDB:6WRH"
FT STRAND 1790..1816
FT /evidence="ECO:0000244|PDB:6WRH"
FT STRAND 1822..1830
FT /evidence="ECO:0000244|PDB:6WRH"
FT STRAND 1833..1849
FT /evidence="ECO:0000244|PDB:6WRH"
FT STRAND 1852..1869
FT /evidence="ECO:0000244|PDB:6WRH"
FT STRAND 1871..1874
FT /evidence="ECO:0000244|PDB:6WRH"
FT HELIX 3274..3277
FT /evidence="ECO:0000244|PDB:6YB7"
FT STRAND 3280..3285
FT /evidence="ECO:0000244|PDB:6YB7"
FT STRAND 3288..3295
FT /evidence="ECO:0000244|PDB:6YB7"
FT STRAND 3298..3302
FT /evidence="ECO:0000244|PDB:6YB7"
FT HELIX 3303..3306
FT /evidence="ECO:0000244|PDB:6YB7"
FT HELIX 3311..3313
FT /evidence="ECO:0000244|PDB:6YB7"
FT HELIX 3317..3322
FT /evidence="ECO:0000244|PDB:6YB7"
FT HELIX 3326..3328
FT /evidence="ECO:0000244|PDB:6YB7"
FT STRAND 3329..3333
FT /evidence="ECO:0000244|PDB:6YB7"
FT STRAND 3336..3338
FT /evidence="ECO:0000244|PDB:6YB7"
FT STRAND 3340..3346
FT /evidence="ECO:0000244|PDB:6YB7"
FT STRAND 3349..3356
FT /evidence="ECO:0000244|PDB:6YB7"
FT STRAND 3363..3366
FT /evidence="ECO:0000244|PDB:6YB7"
FT STRAND 3374..3381
FT /evidence="ECO:0000244|PDB:6YB7"
FT STRAND 3384..3392
FT /evidence="ECO:0000244|PDB:6YB7"
FT STRAND 3411..3416
FT /evidence="ECO:0000244|PDB:6YB7"
FT STRAND 3419..3429
FT /evidence="ECO:0000244|PDB:6YB7"
FT TURN 3431..3433
FT /evidence="ECO:0000244|PDB:7BRP"
FT STRAND 3435..3438
FT /evidence="ECO:0000244|PDB:6YB7"
FT STRAND 3444..3447
FT /evidence="ECO:0000244|PDB:7BRR"
FT STRAND 3450..3453
FT /evidence="ECO:0000244|PDB:6YB7"
FT HELIX 3464..3476
FT /evidence="ECO:0000244|PDB:6YB7"
FT HELIX 3490..3499
FT /evidence="ECO:0000244|PDB:6YB7"
FT HELIX 3507..3512
FT /evidence="ECO:0000244|PDB:6YB7"
FT HELIX 3514..3520
FT /evidence="ECO:0000244|PDB:6YB7"
FT HELIX 3524..3537
FT /evidence="ECO:0000244|PDB:6YB7"
FT STRAND 3547..3549
FT /evidence="ECO:0000244|PDB:6YB7"
FT HELIX 3556..3564
FT /evidence="ECO:0000244|PDB:6YB7"
FT HELIX 3565..3568
FT /evidence="ECO:0000244|PDB:7C8T"
FT HELIX 3860..3878
FT /evidence="ECO:0000244|PDB:6XIP"
FT HELIX 3881..3883
FT /evidence="ECO:0000244|PDB:6XIP"
FT HELIX 3885..3899
FT /evidence="ECO:0000244|PDB:6XIP"
FT HELIX 3904..3920
FT /evidence="ECO:0000244|PDB:6XIP"
FT TURN 3922..3924
FT /evidence="ECO:0000244|PDB:6XIP"
FT HELIX 3927..3930
FT /evidence="ECO:0000244|PDB:6WTC"
FT HELIX 3952..3970
FT /evidence="ECO:0000244|PDB:6YYT"
FT TURN 4011..4013
FT /evidence="ECO:0000244|PDB:7BTF"
FT HELIX 4021..4040
FT /evidence="ECO:0000244|PDB:6XIP"
FT HELIX 4043..4053
FT /evidence="ECO:0000244|PDB:6XIP"
FT STRAND 4058..4060
FT /evidence="ECO:0000244|PDB:6XIP"
FT HELIX 4061..4066
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4069..4074
FT /evidence="ECO:0000244|PDB:6XIP"
FT HELIX 4077..4083
FT /evidence="ECO:0000244|PDB:6XIP"
FT STRAND 4088..4091
FT /evidence="ECO:0000244|PDB:6XIP"
FT STRAND 4094..4102
FT /evidence="ECO:0000244|PDB:6XIP"
FT HELIX 4111..4113
FT /evidence="ECO:0000244|PDB:6XIP"
FT TURN 4116..4118
FT /evidence="ECO:0000244|PDB:6XIP"
FT HELIX 4119..4121
FT /evidence="ECO:0000244|PDB:6XIP"
FT STRAND 4124..4132
FT /evidence="ECO:0000244|PDB:6XIP"
FT STRAND 4144..4148
FT /evidence="ECO:0000244|PDB:6W9Q"
FT STRAND 4150..4160
FT /evidence="ECO:0000244|PDB:6WXD"
FT STRAND 4165..4175
FT /evidence="ECO:0000244|PDB:6WXD"
FT STRAND 4178..4187
FT /evidence="ECO:0000244|PDB:6WXD"
FT STRAND 4193..4197
FT /evidence="ECO:0000244|PDB:6WXD"
FT STRAND 4199..4202
FT /evidence="ECO:0000244|PDB:6W9Q"
FT STRAND 4204..4209
FT /evidence="ECO:0000244|PDB:6WXD"
FT STRAND 4213..4219
FT /evidence="ECO:0000244|PDB:6WXD"
FT STRAND 4222..4231
FT /evidence="ECO:0000244|PDB:6WXD"
FT HELIX 4236..4249
FT /evidence="ECO:0000244|PDB:6WXD"
FT HELIX 4264..4273
FT /evidence="ECO:0000244|PDB:6WVN"
FT HELIX 4276..4285
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 4307..4311
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 4318..4323
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 4324..4326
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 4328..4332
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 4339..4341
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 4348..4353
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 4354..4356
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 4360..4366
FT /evidence="ECO:0000244|PDB:6W4H"
FT TURN 4371..4373
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 4375..4377
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 4397..4404
FT /evidence="ECO:0000244|PDB:7BTF"
FT STRAND 4416..4418
FT /evidence="ECO:0000244|PDB:7BTF"
FT STRAND 4424..4430
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4435..4441
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4447..4451
FT /evidence="ECO:0000244|PDB:7BTF"
FT STRAND 4457..4466
FT /evidence="ECO:0000244|PDB:7BTF"
FT HELIX 4477..4481
FT /evidence="ECO:0000244|PDB:7BV2"
FT TURN 4482..4484
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4491..4511
FT /evidence="ECO:0000244|PDB:7BTF"
FT STRAND 4513..4515
FT /evidence="ECO:0000244|PDB:6M71"
FT HELIX 4516..4524
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4528..4530
FT /evidence="ECO:0000244|PDB:7BV1"
FT HELIX 4532..4540
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4546..4550
FT /evidence="ECO:0000244|PDB:7BV2"
FT TURN 4552..4555
FT /evidence="ECO:0000244|PDB:7BV2"
FT TURN 4557..4559
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4563..4567
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4568..4570
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4571..4591
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4593..4596
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4599..4601
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4602..4606
FT /evidence="ECO:0000244|PDB:6YYT"
FT STRAND 4623..4625
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4627..4639
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4642..4647
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4649..4651
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4653..4655
FT /evidence="ECO:0000244|PDB:6YYT"
FT HELIX 4668..4678
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4690..4692
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4696..4709
FT /evidence="ECO:0000244|PDB:7BV2"
FT TURN 4710..4712
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4715..4717
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4718..4727
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4730..4740
FT /evidence="ECO:0000244|PDB:7BV2"
FT TURN 4741..4743
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4744..4747
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4753..4756
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4760..4768
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4770..4776
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4777..4784
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4789..4796
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4809..4817
FT /evidence="ECO:0000244|PDB:7BV2"
FT TURN 4818..4821
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4840..4845
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4846..4850
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4858..4868
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4869..4872
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4873..4875
FT /evidence="ECO:0000244|PDB:6YYT"
FT HELIX 4882..4884
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4890..4893
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4898..4900
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4904..4910
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4913..4922
FT /evidence="ECO:0000244|PDB:7BV2"
FT TURN 4923..4925
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4931..4936
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4941..4943
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4948..4951
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4954..4973
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 4976..4979
FT /evidence="ECO:0000244|PDB:7BV2"
FT TURN 4986..4988
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 4989..4997
FT /evidence="ECO:0000244|PDB:7BV2"
FT TURN 4998..5000
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 5002..5008
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 5014..5017
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 5020..5030
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 5031..5033
FT /evidence="ECO:0000244|PDB:7BV2"
FT TURN 5035..5037
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 5040..5054
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 5058..5060
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 5062..5067
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 5074..5076
FT /evidence="ECO:0000244|PDB:6YYT"
FT HELIX 5079..5100
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 5104..5106
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 5110..5124
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 5131..5144
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 5145..5150
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 5153..5159
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 5160..5164
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 5166..5168
FT /evidence="ECO:0000244|PDB:6M71"
FT HELIX 5171..5181
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 5188..5190
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 5192..5194
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 5197..5199
FT /evidence="ECO:0000244|PDB:6M71"
FT STRAND 5204..5206
FT /evidence="ECO:0000244|PDB:6M71"
FT STRAND 5207..5214
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 5217..5223
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 5226..5234
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 5235..5237
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 5239..5242
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 5244..5258
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 5259..5263
FT /evidence="ECO:0000244|PDB:7BV2"
FT STRAND 5264..5266
FT /evidence="ECO:0000244|PDB:6YYT"
FT HELIX 5267..5286
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 5302..5308
FT /evidence="ECO:0000244|PDB:6YYT"
FT HELIX 5310..5314
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 5315..5317
FT /evidence="ECO:0000244|PDB:7BV2"
FT HELIX 6454..6464
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6476..6479
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6482..6487
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6490..6496
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6499..6501
FT /evidence="ECO:0000244|PDB:6WLC"
FT HELIX 6503..6511
FT /evidence="ECO:0000244|PDB:6WLC"
FT HELIX 6521..6526
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6531..6536
FT /evidence="ECO:0000244|PDB:6WLC"
FT TURN 6540..6543
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6544..6548
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6550..6553
FT /evidence="ECO:0000244|PDB:6WLC"
FT TURN 6555..6557
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6558..6562
FT /evidence="ECO:0000244|PDB:6WLC"
FT HELIX 6566..6568
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6569..6571
FT /evidence="ECO:0000244|PDB:6X1B"
FT STRAND 6573..6576
FT /evidence="ECO:0000244|PDB:6WLC"
FT HELIX 6582..6588
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6590..6598
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6612..6614
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6617..6619
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6622..6624
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6629..6634
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6637..6639
FT /evidence="ECO:0000244|PDB:6X1B"
FT HELIX 6660..6667
FT /evidence="ECO:0000244|PDB:6WLC"
FT HELIX 6670..6676
FT /evidence="ECO:0000244|PDB:6WLC"
FT TURN 6680..6683
FT /evidence="ECO:0000244|PDB:6X4I"
FT HELIX 6684..6687
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6693..6696
FT /evidence="ECO:0000244|PDB:6WLC"
FT HELIX 6703..6712
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6715..6718
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6726..6734
FT /evidence="ECO:0000244|PDB:6WLC"
FT TURN 6735..6737
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6740..6747
FT /evidence="ECO:0000244|PDB:6WLC"
FT HELIX 6751..6758
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6765..6774
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6777..6786
FT /evidence="ECO:0000244|PDB:6WLC"
FT STRAND 6789..6795
FT /evidence="ECO:0000244|PDB:6WLC"
FT HELIX 6800..6803
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 6804..6808
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 6811..6814
FT /evidence="ECO:0000244|PDB:6W4H"
FT TURN 6826..6829
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 6840..6852
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 6864..6869
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 6878..6886
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 6892..6899
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 6905..6911
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 6913..6915
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 6916..6920
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 6922..6927
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 6932..6934
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 6947..6958
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 6959..6969
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 6971..6973
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 6976..6982
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 6985..6994
FT /evidence="ECO:0000244|PDB:6W4H"
FT TURN 6995..6998
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 7002..7009
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 7019..7032
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 7040..7043
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 7056..7058
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 7062..7064
FT /evidence="ECO:0000244|PDB:6W4H"
FT HELIX 7067..7074
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 7078..7081
FT /evidence="ECO:0000244|PDB:6W4H"
FT STRAND 7088..7090
FT /evidence="ECO:0000244|PDB:6W4H"
SQ SEQUENCE 7096 AA; 794058 MW; A4E62D97150BB8CC CRC64;
MESLVPGFNE KTHVQLSLPV LQVRDVLVRG FGDSVEEVLS EARQHLKDGT CGLVEVEKGV
LPQLEQPYVF IKRSDARTAP HGHVMVELVA ELEGIQYGRS GETLGVLVPH VGEIPVAYRK
VLLRKNGNKG AGGHSYGADL KSFDLGDELG TDPYEDFQEN WNTKHSSGVT RELMRELNGG
AYTRYVDNNF CGPDGYPLEC IKDLLARAGK ASCTLSEQLD FIDTKRGVYC CREHEHEIAW
YTERSEKSYE LQTPFEIKLA KKFDTFNGEC PNFVFPLNSI IKTIQPRVEK KKLDGFMGRI
RSVYPVASPN ECNQMCLSTL MKCDHCGETS WQTGDFVKAT CEFCGTENLT KEGATTCGYL
PQNAVVKIYC PACHNSEVGP EHSLAEYHNE SGLKTILRKG GRTIAFGGCV FSYVGCHNKC
AYWVPRASAN IGCNHTGVVG EGSEGLNDNL LEILQKEKVN INIVGDFKLN EEIAIILASF
SASTSAFVET VKGLDYKAFK QIVESCGNFK VTKGKAKKGA WNIGEQKSIL SPLYAFASEA
ARVVRSIFSR TLETAQNSVR VLQKAAITIL DGISQYSLRL IDAMMFTSDL ATNNLVVMAY
ITGGVVQLTS QWLTNIFGTV YEKLKPVLDW LEEKFKEGVE FLRDGWEIVK FISTCACEIV
GGQIVTCAKE IKESVQTFFK LVNKFLALCA DSIIIGGAKL KALNLGETFV THSKGLYRKC
VKSREETGLL MPLKAPKEII FLEGETLPTE VLTEEVVLKT GDLQPLEQPT SEAVEAPLVG
TPVCINGLML LEIKDTEKYC ALAPNMMVTN NTFTLKGGAP TKVTFGDDTV IEVQGYKSVN
ITFELDERID KVLNEKCSAY TVELGTEVNE FACVVADAVI KTLQPVSELL TPLGIDLDEW
SMATYYLFDE SGEFKLASHM YCSFYPPDED EEEGDCEEEE FEPSTQYEYG TEDDYQGKPL
EFGATSAALQ PEEEQEEDWL DDDSQQTVGQ QDGSEDNQTT TIQTIVEVQP QLEMELTPVV
QTIEVNSFSG YLKLTDNVYI KNADIVEEAK KVKPTVVVNA ANVYLKHGGG VAGALNKATN
NAMQVESDDY IATNGPLKVG GSCVLSGHNL AKHCLHVVGP NVNKGEDIQL LKSAYENFNQ
HEVLLAPLLS AGIFGADPIH SLRVCVDTVR TNVYLAVFDK NLYDKLVSSF LEMKSEKQVE
QKIAEIPKEE VKPFITESKP SVEQRKQDDK KIKACVEEVT TTLEETKFLT ENLLLYIDIN
GNLHPDSATL VSDIDITFLK KDAPYIVGDV VQEGVLTAVV IPTKKAGGTT EMLAKALRKV
PTDNYITTYP GQGLNGYTVE EAKTVLKKCK SAFYILPSII SNEKQEILGT VSWNLREMLA
HAEETRKLMP VCVETKAIVS TIQRKYKGIK IQEGVVDYGA RFYFYTSKTT VASLINTLND
LNETLVTMPL GYVTHGLNLE EAARYMRSLK VPATVSVSSP DAVTAYNGYL TSSSKTPEEH
FIETISLAGS YKDWSYSGQS TQLGIEFLKR GDKSVYYTSN PTTFHLDGEV ITFDNLKTLL
SLREVRTIKV FTTVDNINLH TQVVDMSMTY GQQFGPTYLD GADVTKIKPH NSHEGKTFYV
LPNDDTLRVE AFEYYHTTDP SFLGRYMSAL NHTKKWKYPQ VNGLTSIKWA DNNCYLATAL
LTLQQIELKF NPPALQDAYY RARAGEAANF CALILAYCNK TVGELGDVRE TMSYLFQHAN
LDSCKRVLNV VCKTCGQQQT TLKGVEAVMY MGTLSYEQFK KGVQIPCTCG KQATKYLVQQ
ESPFVMMSAP PAQYELKHGT FTCASEYTGN YQCGHYKHIT SKETLYCIDG ALLTKSSEYK
GPITDVFYKE NSYTTTIKPV TYKLDGVVCT EIDPKLDNYY KKDNSYFTEQ PIDLVPNQPY
PNASFDNFKF VCDNIKFADD LNQLTGYKKP ASRELKVTFF PDLNGDVVAI DYKHYTPSFK
KGAKLLHKPI VWHVNNATNK ATYKPNTWCI RCLWSTKPVE TSNSFDVLKS EDAQGMDNLA
CEDLKPVSEE VVENPTIQKD VLECNVKTTE VVGDIILKPA NNSLKITEEV GHTDLMAAYV
DNSSLTIKKP NELSRVLGLK TLATHGLAAV NSVPWDTIAN YAKPFLNKVV STTTNIVTRC
LNRVCTNYMP YFFTLLLQLC TFTRSTNSRI KASMPTTIAK NTVKSVGKFC LEASFNYLKS
PNFSKLINII IWFLLLSVCL GSLIYSTAAL GVLMSNLGMP SYCTGYREGY LNSTNVTIAT
YCTGSIPCSV CLSGLDSLDT YPSLETIQIT ISSFKWDLTA FGLVAEWFLA YILFTRFFYV
LGLAAIMQLF FSYFAVHFIS NSWLMWLIIN LVQMAPISAM VRMYIFFASF YYVWKSYVHV
VDGCNSSTCM MCYKRNRATR VECTTIVNGV RRSFYVYANG GKGFCKLHNW NCVNCDTFCA
GSTFISDEVA RDLSLQFKRP INPTDQSSYI VDSVTVKNGS IHLYFDKAGQ KTYERHSLSH
FVNLDNLRAN NTKGSLPINV IVFDGKSKCE ESSAKSASVY YSQLMCQPIL LLDQALVSDV
GDSAEVAVKM FDAYVNTFSS TFNVPMEKLK TLVATAEAEL AKNVSLDNVL STFISAARQG
FVDSDVETKD VVECLKLSHQ SDIEVTGDSC NNYMLTYNKV ENMTPRDLGA CIDCSARHIN
AQVAKSHNIA LIWNVKDFMS LSEQLRKQIR SAAKKNNLPF KLTCATTRQV VNVVTTKIAL
KGGKIVNNWL KQLIKVTLVF LFVAAIFYLI TPVHVMSKHT DFSSEIIGYK AIDGGVTRDI
ASTDTCFANK HADFDTWFSQ RGGSYTNDKA CPLIAAVITR EVGFVVPGLP GTILRTTNGD
FLHFLPRVFS AVGNICYTPS KLIEYTDFAT SACVLAAECT IFKDASGKPV PYCYDTNVLE
GSVAYESLRP DTRYVLMDGS IIQFPNTYLE GSVRVVTTFD SEYCRHGTCE RSEAGVCVST
SGRWVLNNDY YRSLPGVFCG VDAVNLLTNM FTPLIQPIGA LDISASIVAG GIVAIVVTCL
AYYFMRFRRA FGEYSHVVAF NTLLFLMSFT VLCLTPVYSF LPGVYSVIYL YLTFYLTNDV
SFLAHIQWMV MFTPLVPFWI TIAYIICIST KHFYWFFSNY LKRRVVFNGV SFSTFEEAAL
CTFLLNKEMY LKLRSDVLLP LTQYNRYLAL YNKYKYFSGA MDTTSYREAA CCHLAKALND
FSNSGSDVLY QPPQTSITSA VLQSGFRKMA FPSGKVEGCM VQVTCGTTTL NGLWLDDVVY
CPRHVICTSE DMLNPNYEDL LIRKSNHNFL VQAGNVQLRV IGHSMQNCVL KLKVDTANPK
TPKYKFVRIQ PGQTFSVLAC YNGSPSGVYQ CAMRPNFTIK GSFLNGSCGS VGFNIDYDCV
SFCYMHHMEL PTGVHAGTDL EGNFYGPFVD RQTAQAAGTD TTITVNVLAW LYAAVINGDR
WFLNRFTTTL NDFNLVAMKY NYEPLTQDHV DILGPLSAQT GIAVLDMCAS LKELLQNGMN
GRTILGSALL EDEFTPFDVV RQCSGVTFQS AVKRTIKGTH HWLLLTILTS LLVLVQSTQW
SLFFFLYENA FLPFAMGIIA MSAFAMMFVK HKHAFLCLFL LPSLATVAYF NMVYMPASWV
MRIMTWLDMV DTSLSGFKLK DCVMYASAVV LLILMTARTV YDDGARRVWT LMNVLTLVYK
VYYGNALDQA ISMWALIISV TSNYSGVVTT VMFLARGIVF MCVEYCPIFF ITGNTLQCIM
LVYCFLGYFC TCYFGLFCLL NRYFRLTLGV YDYLVSTQEF RYMNSQGLLP PKNSIDAFKL
NIKLLGVGGK PCIKVATVQS KMSDVKCTSV VLLSVLQQLR VESSSKLWAQ CVQLHNDILL
AKDTTEAFEK MVSLLSVLLS MQGAVDINKL CEEMLDNRAT LQAIASEFSS LPSYAAFATA
QEAYEQAVAN GDSEVVLKKL KKSLNVAKSE FDRDAAMQRK LEKMADQAMT QMYKQARSED
KRAKVTSAMQ TMLFTMLRKL DNDALNNIIN NARDGCVPLN IIPLTTAAKL MVVIPDYNTY
KNTCDGTTFT YASALWEIQQ VVDADSKIVQ LSEISMDNSP NLAWPLIVTA LRANSAVKLQ
NNELSPVALR QMSCAAGTTQ TACTDDNALA YYNTTKGGRF VLALLSDLQD LKWARFPKSD
GTGTIYTELE PPCRFVTDTP KGPKVKYLYF IKGLNNLNRG MVLGSLAATV RLQAGNATEV
PANSTVLSFC AFAVDAAKAY KDYLASGGQP ITNCVKMLCT HTGTGQAITV TPEANMDQES
FGGASCCLYC RCHIDHPNPK GFCDLKGKYV QIPTTCANDP VGFTLKNTVC TVCGMWKGYG
CSCDQLREPM LQSADAQSFL NRVCGVSAAR LTPCGTGTST DVVYRAFDIY NDKVAGFAKF
LKTNCCRFQE KDEDDNLIDS YFVVKRHTFS NYQHEETIYN LLKDCPAVAK HDFFKFRIDG
DMVPHISRQR LTKYTMADLV YALRHFDEGN CDTLKEILVT YNCCDDDYFN KKDWYDFVEN
PDILRVYANL GERVRQALLK TVQFCDAMRN AGIVGVLTLD NQDLNGNWYD FGDFIQTTPG
SGVPVVDSYY SLLMPILTLT RALTAESHVD TDLTKPYIKW DLLKYDFTEE RLKLFDRYFK
YWDQTYHPNC VNCLDDRCIL HCANFNVLFS TVFPPTSFGP LVRKIFVDGV PFVVSTGYHF
RELGVVHNQD VNLHSSRLSF KELLVYAADP AMHAASGNLL LDKRTTCFSV AALTNNVAFQ
TVKPGNFNKD FYDFAVSKGF FKEGSSVELK HFFFAQDGNA AISDYDYYRY NLPTMCDIRQ
LLFVVEVVDK YFDCYDGGCI NANQVIVNNL DKSAGFPFNK WGKARLYYDS MSYEDQDALF
AYTKRNVIPT ITQMNLKYAI SAKNRARTVA GVSICSTMTN RQFHQKLLKS IAATRGATVV
IGTSKFYGGW HNMLKTVYSD VENPHLMGWD YPKCDRAMPN MLRIMASLVL ARKHTTCCSL
SHRFYRLANE CAQVLSEMVM CGGSLYVKPG GTSSGDATTA YANSVFNICQ AVTANVNALL
STDGNKIADK YVRNLQHRLY ECLYRNRDVD TDFVNEFYAY LRKHFSMMIL SDDAVVCFNS
TYASQGLVAS IKNFKSVLYY QNNVFMSEAK CWTETDLTKG PHEFCSQHTM LVKQGDDYVY
LPYPDPSRIL GAGCFVDDIV KTDGTLMIER FVSLAIDAYP LTKHPNQEYA DVFHLYLQYI
RKLHDELTGH MLDMYSVMLT NDNTSRYWEP EFYEAMYTPH TVLQAVGACV LCNSQTSLRC
GACIRRPFLC CKCCYDHVIS TSHKLVLSVN PYVCNAPGCD VTDVTQLYLG GMSYYCKSHK
PPISFPLCAN GQVFGLYKNT CVGSDNVTDF NAIATCDWTN AGDYILANTC TERLKLFAAE
TLKATEETFK LSYGIATVRE VLSDRELHLS WEVGKPRPPL NRNYVFTGYR VTKNSKVQIG
EYTFEKGDYG DAVVYRGTTT YKLNVGDYFV LTSHTVMPLS APTLVPQEHY VRITGLYPTL
NISDEFSSNV ANYQKVGMQK YSTLQGPPGT GKSHFAIGLA LYYPSARIVY TACSHAAVDA
LCEKALKYLP IDKCSRIIPA RARVECFDKF KVNSTLEQYV FCTVNALPET TADIVVFDEI
SMATNYDLSV VNARLRAKHY VYIGDPAQLP APRTLLTKGT LEPEYFNSVC RLMKTIGPDM
FLGTCRRCPA EIVDTVSALV YDNKLKAHKD KSAQCFKMFY KGVITHDVSS AINRPQIGVV
REFLTRNPAW RKAVFISPYN SQNAVASKIL GLPTQTVDSS QGSEYDYVIF TQTTETAHSC
NVNRFNVAIT RAKVGILCIM SDRDLYDKLQ FTSLEIPRRN VATLQAENVT GLFKDCSKVI
TGLHPTQAPT HLSVDTKFKT EGLCVDIPGI PKDMTYRRLI SMMGFKMNYQ VNGYPNMFIT
REEAIRHVRA WIGFDVEGCH ATREAVGTNL PLQLGFSTGV NLVAVPTGYV DTPNNTDFSR
VSAKPPPGDQ FKHLIPLMYK GLPWNVVRIK IVQMLSDTLK NLSDRVVFVL WAHGFELTSM
KYFVKIGPER TCCLCDRRAT CFSTASDTYA CWHHSIGFDY VYNPFMIDVQ QWGFTGNLQS
NHDLYCQVHG NAHVASCDAI MTRCLAVHEC FVKRVDWTIE YPIIGDELKI NAACRKVQHM
VVKAALLADK FPVLHDIGNP KAIKCVPQAD VEWKFYDAQP CSDKAYKIEE LFYSYATHSD
KFTDGVCLFW NCNVDRYPAN SIVCRFDTRV LSNLNLPGCD GGSLYVNKHA FHTPAFDKSA
FVNLKQLPFF YYSDSPCESH GKQVVSDIDY VPLKSATCIT RCNLGGAVCR HHANEYRLYL
DAYNMMISAG FSLWVYKQFD TYNLWNTFTR LQSLENVAFN VVNKGHFDGQ QGEVPVSIIN
NTVYTKVDGV DVELFENKTT LPVNVAFELW AKRNIKPVPE VKILNNLGVD IAANTVIWDY
KRDAPAHIST IGVCSMTDIA KKPTETICAP LTVFFDGRVD GQVDLFRNAR NGVLITEGSV
KGLQPSVGPK QASLNGVTLI GEAVKTQFNY YKKVDGVVQQ LPETYFTQSR NLQEFKPRSQ
MEIDFLELAM DEFIERYKLE GYAFEHIVYG DFSHSQLGGL HLLIGLAKRF KESPFELEDF
IPMDSTVKNY FITDAQTGSS KCVCSVIDLL LDDFVEIIKS QDLSVVSKVV KVTIDYTEIS
FMLWCKDGHV ETFYPKLQSS QAWQPGVAMP NLYKMQRMLL EKCDLQNYGD SATLPKGIMM
NVAKYTQLCQ YLNTLTLAVP YNMRVIHFGA GSDKGVAPGT AVLRQWLPTG TLLVDSDLND
FVSDADSTLI GDCATVHTAN KWDLIISDMY DPKTKNVTKE NDSKEGFFTY ICGFIQQKLA
LGGSVAIKIT EHSWNADLYK LMGHFAWWTA FVTNVNASSS EAFLIGCNYL GKPREQIDGY
VMHANYIFWR NTNPIQLSSY SLFDMSKFPL KLRGTAVMSL KEGQINDMIL SLLSKGRLII
RENNRVVISS DVLVNN
//