R1AB_IBVB
ID R1AB_IBVB Reviewed; 6629 AA.
AC P0C6Y1; P26314; P27920; Q4ZJT1; Q4ZJT2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Replicase polyprotein 1ab;
DE Short=pp1ab;
DE AltName: Full=ORF1ab 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:0000269|PubMed:25609249};
DE EC=3.4.22.-;
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=RNA-directed RNA polymerase;
DE Short=Pol;
DE Short=RdRp;
DE EC=2.7.7.48;
DE AltName: Full=nsp12;
DE AltName: Full=p100;
DE Contains:
DE RecName: Full=Helicase;
DE Short=Hel;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P0C6X7};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P0C6X7};
DE AltName: Full=nsp13;
DE AltName: Full=p68;
DE Contains:
DE RecName: Full=Proofreading exoribonuclease {ECO:0000250|UniProtKB:P0C6X7};
DE Short=ExoN;
DE EC=2.1.1.-;
DE EC=3.1.13.-;
DE AltName: Full=Guanine-N7 methyltransferase {ECO:0000250|UniProtKB:P0C6X7};
DE AltName: Full=Non-structural protein 14;
DE Short=nsp14;
DE AltName: Full=p58;
DE Contains:
DE RecName: Full=Uridylate-specific endoribonuclease;
DE EC=4.6.1.- {ECO:0000250|UniProtKB:P0C6X7};
DE AltName: Full=NendoU;
DE AltName: Full=Non-structural protein 15;
DE Short=nsp15;
DE AltName: Full=p39;
DE Contains:
DE RecName: Full=2'-O-methyl transferase;
DE EC=2.1.1.57;
DE AltName: Full=Non-structural protein 16;
DE Short=nsp16;
DE AltName: Full=p35;
GN Name=rep; ORFNames=1a-1b;
OS Avian infectious bronchitis virus (strain Beaudette) (IBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Gammacoronavirus; Igacovirus.
OX NCBI_TaxID=11122;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3027249; DOI=10.1099/0022-1317-68-1-57;
RA Boursnell M.E.G., Brown T.D.K., Foulds I.J., Green P.F., Tomley F.M.,
RA Binns M.M.;
RT "Completion of the sequence of the genome of the coronavirus avian
RT infectious bronchitis virus.";
RL J. Gen. Virol. 68:57-77(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Vero cell-adapted p65;
RX PubMed=16137658; DOI=10.1016/j.bbrc.2005.08.105;
RA Fang S.G., Shen S., Tay F.P., Liu D.X.;
RT "Selection of and recombination between minor variants lead to the
RT adaptation of an avian coronavirus to primate cells.";
RL Biochem. Biophys. Res. Commun. 336:417-423(2005).
RN [3]
RP PROTEOLYTIC CLEAVAGE (ISOFORM REPLICASE POLYPROTEIN 1AB).
RX PubMed=11831730; DOI=10.1006/viro.1995.1128;
RA Liu D.X., Tibbles K.W., Cavanagh D., Brown T.D.K., Brierley I.;
RT "Identification, expression, and processing of an 87-kDa polypeptide
RT encoded by ORF 1a of the coronavirus infectious bronchitis virus.";
RL Virology 208:48-57(1995).
RN [4]
RP CHARACTERIZATION (3C-LIKE PROTEINASE), AND MUTAGENESIS OF HIS-2820;
RP GLU-2841; GLU-2843; CYS-2922; GLN-3928; GLN-4868 AND SER-4869.
RX PubMed=7778277; DOI=10.1006/viro.1995.1274;
RA Liu D.X., Brown T.D.K.;
RT "Characterisation and mutational analysis of an ORF 1a-encoding proteinase
RT domain responsible for proteolytic processing of the infectious bronchitis
RT virus 1a/1b polyprotein.";
RL Virology 209:420-427(1995).
RN [5]
RP PROTEOLYTIC CLEAVAGE (ISOFORM REPLICASE POLYPROTEIN 1AB), AND MUTAGENESIS
RP OF GLN-3672 AND GLN-3783.
RX PubMed=9032311; DOI=10.1128/jvi.71.3.1814-1820.1997;
RA Liu D.X., Xu H.Y., Brown T.D.K.;
RT "Proteolytic processing of the coronavirus infectious bronchitis virus 1a
RT polyprotein: identification of a 10-kilodalton polypeptide and
RT determination of its cleavage sites.";
RL J. Virol. 71:1814-1820(1997).
RN [6]
RP PROTEOLYTIC CLEAVAGE (ISOFORM REPLICASE POLYPROTEIN 1AB), AND MUTAGENESIS
RP OF GLN-3462; GLN-3672 AND GLN-3783.
RX PubMed=9568037; DOI=10.1006/viro.1998.9058;
RA Ng L.F.P., Liu D.X.;
RT "Identification of a 24-kDa polypeptide processed from the coronavirus
RT infectious bronchitis virus 1a polyprotein by the 3C-like proteinase and
RT determination of its cleavage sites.";
RL Virology 243:388-395(1998).
RN [7]
RP PROTEOLYTIC CLEAVAGE (ISOFORM REPLICASE POLYPROTEIN 1AB), CHARACTERIZATION
RP (PAPAIN-LIKE PROTEINASE), AND MUTAGENESIS OF GLY-673; THR-676; CYS-1274 AND
RP HIS-1437.
RX PubMed=9636369; DOI=10.1006/viro.1998.9164;
RA Lim K.P., Liu D.X.;
RT "Characterization of the two overlapping papain-like proteinase domains
RT encoded in gene 1 of the coronavirus infectious bronchitis virus and
RT determination of the C-terminal cleavage site of an 87-kDa protein.";
RL Virology 245:303-312(1998).
RN [8]
RP PROTEOLYTIC CLEAVAGE (ISOFORM REPLICASE POLYPROTEIN 1AB), AND MUTAGENESIS
RP OF GLN-4868; GLN-5468; GLN-5989 AND GLN-6327.
RX PubMed=9657947; DOI=10.1006/viro.1998.9199;
RA Liu D.X., Shen S., Xu H.Y., Wang S.F.;
RT "Proteolytic mapping of the coronavirus infectious bronchitis virus 1b
RT polyprotein: evidence for the presence of four cleavage sites of the 3C-
RT like proteinase and identification of two novel cleavage products.";
RL Virology 246:288-297(1998).
RN [9]
RP PROTEOLYTIC CLEAVAGE (ISOFORM REPLICASE POLYPROTEIN 1AB), GLYCOSYLATION
RP (NON-STRUCTURAL PROTEIN 4), AND MUTAGENESIS OF ALA-2264; GLY-2265 AND
RP GLY-2266.
RX PubMed=10644337; DOI=10.1128/jvi.74.4.1674-1685.2000;
RA Lim K.P., Ng L.F.P., Liu D.X.;
RT "Identification of a novel cleavage activity of the first papain-like
RT proteinase domain encoded by open reading frame 1a of the coronavirus avian
RT infectious bronchitis virus and characterization of the cleavage
RT products.";
RL J. Virol. 74:1674-1685(2000).
RN [10]
RP PROTEOLYTIC CLEAVAGE (ISOFORM REPLICASE POLYPROTEIN 1AB), AND MUTAGENESIS
RP OF GLN-3086; GLN-3365 AND GLN-3379.
RX PubMed=10873746; DOI=10.1006/viro.2000.0330;
RA Ng L.F.P., Liu D.X.;
RT "Further characterization of the coronavirus infectious bronchitis virus
RT 3C-like proteinase and determination of a new cleavage site.";
RL Virology 272:27-39(2000).
RN [11]
RP PROTEOLYTIC CLEAVAGE (REPLICASE POLYPROTEIN 1AB), AND SUBCELLULAR LOCATION.
RX PubMed=11601893; DOI=10.1006/viro.2001.1098;
RA Xu H.Y., Lim K.P., Shen S., Liu D.X.;
RT "Further identification and characterization of novel intermediate and
RT mature cleavage products released from the ORF 1b region of the avian
RT coronavirus infectious bronchitis virus 1a/1b polyprotein.";
RL Virology 288:212-222(2001).
RN [12]
RP APOPTOTIC FUNCTION (NON-STRUCTURAL PROTEIN 14).
RX PubMed=11413307; DOI=10.1128/jvi.75.14.6402-6409.2001;
RA Liu C., Xu H.Y., Liu D.X.;
RT "Induction of caspase-dependent apoptosis in cultured cells by the avian
RT coronavirus infectious bronchitis virus.";
RL J. Virol. 75:6402-6409(2001).
RN [13]
RP CHARACTERIZATION (NON-STRUCTURAL PROTEIN 10), AND MUTAGENESIS.
RX PubMed=12021359; DOI=10.1128/jvi.76.12.6257-6267.2002;
RA Ng L.F.P., Liu D.X.;
RT "Membrane association and dimerization of a cysteine-rich, 16-kilodalton
RT polypeptide released from the C-terminal region of the coronavirus
RT infectious bronchitis virus 1a polyprotein.";
RL J. Virol. 76:6257-6267(2002).
RN [14]
RP INTERACTION WITH DDX1 (PROOFREADING EXORIBONUCLEASE).
RX PubMed=20573827; DOI=10.1128/jvi.00392-10;
RA Xu L., Khadijah S., Fang S., Wang L., Tay F.P., Liu D.X.;
RT "The cellular RNA helicase DDX1 interacts with coronavirus nonstructural
RT protein 14 and enhances viral replication.";
RL J. Virol. 84:8571-8583(2010).
RN [15] {ECO:0007744|PDB:4X2Z}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1174-1483 IN COMPLEX WITH ZINC,
RP FUNCTION (PAPAIN-LIKE PROTEASE), AND ACTIVE SITE (PAPAIN-LIKE PROTEASE).
RX PubMed=25609249; DOI=10.1074/jbc.m114.628636;
RA Kong L., Shaw N., Yan L., Lou Z., Rao Z.;
RT "Structural view and substrate specificity of papain-like protease from
RT avian infectious bronchitis virus.";
RL J. Biol. Chem. 290:7160-7168(2015).
CC -!- FUNCTION: [Isoform Replicase polyprotein 1ab]: 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:P0C6X7}.
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 (PubMed:25609249). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:25609249}.
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:P0C6Y3}.
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:P0C6X7}.
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:P0C6X7}.
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:P0C6Y3}.
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:P0C6X7}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Responsible for replication
CC and transcription of the viral RNA genome.
CC {ECO:0000250|UniProtKB:P0C6X7}.
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 (By similarity). Acts as a proofreading exoribonuclease for
CC RNA replication, thereby lowering The sensitivity of the virus to RNA
CC mutagens (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [Uridylate-specific endoribonuclease]: Plays a role in viral
CC transcription/replication and prevents the simultaneous activation of
CC host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By
CC similarity). Acts by degrading the 5'-polyuridines generated during
CC replication of the poly(A) region of viral genomic and subgenomic RNAs
CC (By similarity). Catalyzes a two-step reaction in which a 2'3'-cyclic
CC phosphate (2'3'-cP) is first generated by 2'-O transesterification,
CC which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If
CC not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and
CC activate host dsRNA sensors (By similarity).
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- FUNCTION: [2'-O-methyl transferase]: 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: [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:0000269|PubMed:25609249};
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:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
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: [Uridylate-specific endoribonuclease]:
CC Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-
CC 2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-
CC RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-
CC COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173079, ChEBI:CHEBI:173080;
CC Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC -!- CATALYTIC ACTIVITY: [2'-O-methyl transferase]:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC EC=2.1.1.57; Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC -!- COFACTOR: [Uridylate-specific endoribonuclease]:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC Note=Likely affects Nsp15 binding to RNA.
CC {ECO:0000250|UniProtKB:P0C6X7};
CC -!- COFACTOR: [Papain-like protease]:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P0C6X7};
CC -!- SUBUNIT: [Non-structural protein 2]: Interacts with host PHB and PHB2.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [Non-structural protein 4]: Interacts with papain-like
CC protease and non-structural protein 6. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [3C-like proteinase]: Monomer. Homodimer. Only the homodimer
CC shows catalytic activity. {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. {ECO:0000250|UniProtKB:P0C6X7}.
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:P0C6X7}.
CC -!- SUBUNIT: [Non-structural protein 9]: Homodimer.
CC {ECO:0000250|UniProtKB:P0C6Y3}.
CC -!- SUBUNIT: [Non-structural protein 10]: Homododecamer (By similarity).
CC Interacts with proofreading exoribonuclease nsp14 and 2'-O-
CC methyltransferase nsp16; these interactions enhance nsp14 and nsp16
CC enzymatic activities (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [Proofreading exoribonuclease]: Interacts with host DDX1 (via
CC C-terminus) (PubMed:20573827). Interacts with non-structural protein 10
CC (By similarity). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000269|PubMed:20573827}.
CC -!- SUBUNIT: [Uridylate-specific endoribonuclease]: Homohexamer.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- SUBUNIT: [2'-O-methyl transferase]: Interacts with non-structural
CC protein 10. {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- INTERACTION:
CC PRO_0000037415; Q92499: DDX1; Xeno; NbExp=5; IntAct=EBI-25826989, EBI-358474;
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:P0C6X7}.
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:P0C6X7}.
CC Note=Gammacoronaviruses induce membrane zippering to form zippered
CC endoplasmic reticulum (zER). {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:P0C6X7}. 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 -!- SUBCELLULAR LOCATION: [Helicase]: Host endoplasmic reticulum-Golgi
CC intermediate compartment {ECO:0000305}. Note=The helicase interacts
CC with the N protein in membranous complexes and colocalizes with sites
CC of synthesis of new viral RNA.
CC -!- SUBCELLULAR LOCATION: [Proofreading exoribonuclease]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}.
CC -!- SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease]: Host
CC cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DTD1}.
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 1ab; Synonyms=pp1ab;
CC IsoId=P0C6Y1-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P0C6V3-1; 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:P0C6X7}.
CC -!- DOMAIN: [Non-structural protein 4]: The hydrophobic region HD2 probably
CC mediates the membrane association of the replication complex.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- DOMAIN: [Non-structural protein 6]: The hydrophobic region HD3 probably
CC mediates the membrane association of the replication complex.
CC {ECO:0000250|UniProtKB:P0C6X7}.
CC -!- PTM: [Isoform Replicase polyprotein 1ab]: 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:P0C6X7}.
CC -!- PTM: [Non-structural protein 4]: N-glycosylated.
CC {ECO:0000269|PubMed:10644337}.
CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA46223.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAA46224.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAA70233.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAA70234.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAY24431.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAY24432.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M94356; AAA46223.1; ALT_SEQ; Genomic_RNA.
DR EMBL; M94356; AAA46224.1; ALT_SEQ; Genomic_RNA.
DR EMBL; M95169; AAA70233.1; ALT_SEQ; Genomic_RNA.
DR EMBL; M95169; AAA70234.1; ALT_SEQ; Genomic_RNA.
DR EMBL; DQ001339; AAY24431.1; ALT_SEQ; Genomic_RNA.
DR EMBL; DQ001339; AAY24432.1; ALT_SEQ; Genomic_RNA.
DR PIR; A33094; VFIHB1.
DR PIR; B33094; VFIHB2.
DR PDB; 3EJF; X-ray; 1.60 A; A=1005-1176.
DR PDB; 3EKE; X-ray; 2.10 A; A=1005-1176.
DR PDB; 4X2Z; X-ray; 2.15 A; A=1174-1483.
DR PDB; 5BZ0; X-ray; 2.10 A; A=1174-1483.
DR PDBsum; 3EJF; -.
DR PDBsum; 3EKE; -.
DR PDBsum; 4X2Z; -.
DR PDBsum; 5BZ0; -.
DR SMR; P0C6Y1; -.
DR IntAct; P0C6Y1; 6.
DR MEROPS; C16.005; -.
DR BRENDA; 3.4.22.B14; 8728.
DR BRENDA; 3.4.22.B50; 8728.
DR SABIO-RK; P0C6Y1; -.
DR EvolutionaryTrace; P0C6Y1; -.
DR Proteomes; UP000006717; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004532; F:exoribonuclease activity; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase 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:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd21409; 1B_cv_Nsp13-like; 1.
DR CDD; cd20762; capping_2-OMTase_Nidovirales; 1.
DR CDD; cd21512; cv_gamma-delta_Nsp2_IBV-like; 1.
DR CDD; cd21473; cv_Nsp4_TM; 1.
DR CDD; cd21559; gammaCoV-Nsp6; 1.
DR CDD; cd21658; gammaCoV_Nsp14; 1.
DR CDD; cd21667; gammaCoV_Nsp5_Mpro; 1.
DR CDD; cd21587; gammaCoV_RdRp; 1.
DR CDD; cd21168; M_gcv_Nsp15-like; 1.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR CDD; cd21161; NendoU_cv_Nsp15-like; 1.
DR CDD; cd21170; NTD_cv_Nsp15-like; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR CDD; cd21401; ZBD_cv_Nsp13-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; 3.30.160.820; -; 1.
DR Gene3D; 3.30.70.3540; -; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.50.11580; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR043608; CoV_NSP15_M.
DR InterPro; IPR043606; CoV_NSP15_N.
DR InterPro; IPR043611; CoV_NSP3_C.
DR InterPro; IPR032505; CoV_NSP4_C.
DR InterPro; IPR043612; CoV_NSP4_N.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR044371; Macro_X_NSP3-like.
DR InterPro; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR036333; NSP10_sf_CoV.
DR InterPro; IPR044343; NSP13_1B_dom_CoV.
DR InterPro; IPR027352; NSP13_ZBD_CoV-like.
DR InterPro; IPR009466; NSP14_CoV.
DR InterPro; IPR044316; NSP14_gammaCoV.
DR InterPro; IPR044328; NSP15_gammaCoV_N.
DR InterPro; IPR044325; NSP15_M_gammaCoV.
DR InterPro; IPR043174; NSP15_middle_sf.
DR InterPro; IPR042515; NSP15_N_CoV.
DR InterPro; IPR044401; NSP15_NendoU_CoV.
DR InterPro; IPR009461; NSP16_CoV-like.
DR InterPro; IPR040795; NSP2_gammaCoV.
DR InterPro; IPR044383; NSP2_IBV-like.
DR InterPro; IPR044357; NSP3_Ubl1_dom_CoV.
DR InterPro; IPR044353; Nsp3_Ubl2_dom_CoV.
DR InterPro; IPR038123; NSP4_C_sf_CoV.
DR InterPro; IPR044308; NSP5_Mpro_GammaCoV.
DR InterPro; IPR043610; NSP6_CoV.
DR InterPro; IPR044368; NSP6_gammaCoV.
DR InterPro; IPR014828; NSP7_CoV.
DR InterPro; IPR037204; NSP7_sf_CoV.
DR InterPro; IPR014829; NSP8_CoV.
DR InterPro; IPR037230; NSP8_sf_CoV.
DR InterPro; IPR014822; NSP9_CoV.
DR InterPro; IPR036499; NSP9_sf_CoV.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013016; Peptidase_C16_CoV.
DR InterPro; IPR008740; Peptidase_C30_CoV.
DR InterPro; IPR043477; Peptidase_C30_dom3_CoV.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043503; PLpro_palm_finger_dom_CoV.
DR InterPro; IPR043178; PLpro_thumb_sf_CoV.
DR InterPro; IPR044358; RdRp_gammaCoV.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR009469; RNA_pol_N_CoV.
DR InterPro; IPR018995; RNA_synth_NSP10_CoV.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF06471; CoV_ExoN; 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; PF19218; CoV_NSP3_C; 1.
DR Pfam; PF16348; CoV_NSP4_C; 1.
DR Pfam; PF19217; CoV_NSP4_N; 1.
DR Pfam; PF19213; CoV_NSP6; 1.
DR Pfam; PF08716; CoV_NSP7; 1.
DR Pfam; PF08717; CoV_NSP8; 1.
DR Pfam; PF08710; CoV_NSP9; 1.
DR Pfam; PF08715; CoV_peptidase; 1.
DR Pfam; PF06478; CoV_RPol_N; 1.
DR Pfam; PF01661; Macro; 1.
DR Pfam; PF17896; NSP2_gammaCoV; 1.
DR Pfam; PF05409; Peptidase_C30; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SMART; SM00506; A1pp; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; 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; 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; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; PS51952; COV_EXON_MTASE_COACT; 1.
DR PROSITE; PS51954; COV_N7_MTASE; 1.
DR PROSITE; PS51948; COV_NSP12_RDRP; 1.
DR PROSITE; PS51960; COV_NSP15_NTD; 1.
DR PROSITE; PS51992; COV_NSP3_Y3; 1.
DR PROSITE; PS51943; COV_NSP3A_UBL; 1.
DR PROSITE; PS51944; COV_NSP3D_UBL; 1.
DR PROSITE; PS51946; COV_NSP4C; 1.
DR PROSITE; PS51949; COV_NSP7; 1.
DR PROSITE; PS51950; COV_NSP8; 1.
DR PROSITE; PS51951; COV_NSP9_SSRNA_BD; 1.
DR PROSITE; PS51653; CV_ZBD; 1.
DR PROSITE; PS51442; M_PRO; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51958; NENDOU; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS51955; NIV_2_O_MTASE; 1.
DR PROSITE; PS51953; NIV_EXON; 1.
DR PROSITE; PS51124; PEPTIDASE_C16; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Endonuclease; Exonuclease; Helicase; Host cytoplasm;
KW Host endoplasmic reticulum; Host membrane; Host-virus interaction;
KW Hydrolase; Lyase; Membrane; Metal-binding; Methyltransferase; 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 Viral RNA replication; Zinc; Zinc-finger.
FT CHAIN 1..673
FT /note="Non-structural protein 2"
FT /id="PRO_0000037404"
FT CHAIN 674..2265
FT /note="Papain-like protease"
FT /id="PRO_0000037405"
FT CHAIN 2266..2779
FT /note="Non-structural protein 4"
FT /id="PRO_0000037406"
FT CHAIN 2780..3086
FT /note="3C-like proteinase"
FT /id="PRO_0000037407"
FT CHAIN 3087..3379
FT /note="Non-structural protein 6"
FT /id="PRO_0000037408"
FT CHAIN 3380..3462
FT /note="Non-structural protein 7"
FT /id="PRO_0000037409"
FT CHAIN 3463..3672
FT /note="Non-structural protein 8"
FT /id="PRO_0000037410"
FT CHAIN 3673..3783
FT /note="Non-structural protein 9"
FT /id="PRO_0000037411"
FT CHAIN 3784..3928
FT /note="Non-structural protein 10"
FT /id="PRO_0000037412"
FT CHAIN 3929..4868
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000037413"
FT CHAIN 4869..5468
FT /note="Helicase"
FT /id="PRO_0000037414"
FT CHAIN 5469..5989
FT /note="Proofreading exoribonuclease"
FT /id="PRO_0000037415"
FT CHAIN 5990..6327
FT /note="Uridylate-specific endoribonuclease"
FT /id="PRO_0000037416"
FT CHAIN 6328..6629
FT /note="2'-O-methyl transferase"
FT /id="PRO_0000037417"
FT TOPO_DOM 1..1750
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 1751..1771
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1772..1843
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 1844..1864
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1865..2280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 2281..2301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2302..2559
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 2560..2580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2581..2611
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 2612..2632
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2633..2643
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 2644..2664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2665..3096
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 3097..3117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3118..3121
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 3122..3142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3143..3151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 3152..3172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3173..3188
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 3189..3209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3210..3257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 3258..3278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3279..3296
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT TRANSMEM 3297..3317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3318..6629
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT DOMAIN 675..780
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1003..1179
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 1175..1227
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 1236..1497
FT /note="Peptidase C16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT DOMAIN 2161..2263
FT /note="CoV Nsp3 Y3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01336"
FT DOMAIN 2684..2779
FT /note="Nsp4C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01291"
FT DOMAIN 2780..3086
FT /note="Peptidase C30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00772"
FT DOMAIN 3380..3462
FT /note="RdRp Nsp7 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01294"
FT DOMAIN 3463..3672
FT /note="RdRp Nsp8 cofactor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01295"
FT DOMAIN 3673..3783
FT /note="Nsp9 ssRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01296"
FT DOMAIN 3785..3926
FT /note="ExoN/MTase coactivator"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT DOMAIN 3940..4198
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 4302..4868
FT /note="Nsp12 RNA-dependent RNA polymerase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT DOMAIN 4548..4710
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 4869..4952
FT /note="CV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT DOMAIN 5125..5305
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 5306..5477
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 5539..5753
FT /note="ExoN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT DOMAIN 5762..5989
FT /note="N7-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT DOMAIN 5990..6050
FT /note="Nsp15 N-terminal oligomerization"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01305"
FT DOMAIN 6051..6166
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 6183..6324
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT DOMAIN 6327..6626
FT /note="Nidovirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ZN_FING 1353..1390
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"
FT ZN_FING 3858..3878
FT /evidence="ECO:0000250"
FT ZN_FING 3904..3917
FT /evidence="ECO:0000250"
FT REGION 783..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1751..1864
FT /note="HD1"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT REGION 2281..2664
FT /note="HD2"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT REGION 3097..3317
FT /note="HD3"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT REGION 5877..5891
FT /note="GpppA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT ACT_SITE 1274
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444,
FT ECO:0000269|PubMed:25609249"
FT ACT_SITE 1437
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00444,
FT ECO:0000269|PubMed:25609249"
FT ACT_SITE 1448
FT /note="For PL-PRO activity"
FT /evidence="ECO:0000269|PubMed:25609249"
FT ACT_SITE 2820
FT /note="For 3CL-PRO activity"
FT ACT_SITE 2922
FT /note="For 3CL-PRO activity"
FT ACT_SITE 4695
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 4696
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 4697
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01293"
FT ACT_SITE 5557
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5559
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5658
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5734
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 5739
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT ACT_SITE 6212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 6371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT ACT_SITE 6532
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01300"
FT BINDING 1353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="9"
FT /evidence="ECO:0000269|PubMed:25609249"
FT BINDING 1355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="9"
FT /evidence="ECO:0000269|PubMed:25609249"
FT BINDING 1387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="9"
FT /evidence="ECO:0000269|PubMed:25609249"
FT BINDING 1390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="9"
FT /evidence="ECO:0000269|PubMed:25609249"
FT BINDING 3858
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3861
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3867
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3878
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3904
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3907
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01297"
FT BINDING 3915
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 4873
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4876
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4887
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4897
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4901
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4907
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4918
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4923
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4940
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 4943
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00986"
FT BINDING 5150..5157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 5674
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5676
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5692
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5695
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5723
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5727
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5730
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5745
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01298"
FT BINDING 5797..5803
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 5915
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 5935
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 5946
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT BINDING 5949
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01299"
FT SITE 673..674
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 2265..2266
FT /note="Cleavage; by PL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 2779..2780
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 3086..3087
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 3379..3380
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 3462..3463
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 3672..3673
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 3783..3784
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 3928..3929
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 4868..4869
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 5468..5469
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 5989..5990
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT SITE 6327..6328
FT /note="Cleavage; by 3CL-PRO"
FT /evidence="ECO:0000250|UniProtKB:P0C6X7"
FT VARIANT 105
FT /note="P -> S (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 919
FT /note="K -> E (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 932
FT /note="L -> I (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 948
FT /note="D -> G (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 967
FT /note="A -> D (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 1133
FT /note="L -> S (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 1388
FT /note="P -> S (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 1753
FT /note="L -> F (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 2561
FT /note="Q -> H (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 3058
FT /note="Missing (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 3242
FT /note="N -> S (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 3409
FT /note="V -> A (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 3418
FT /note="I -> T (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 3471..3472
FT /note="IP -> MT (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 3751
FT /note="V -> D (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 3870
FT /note="S -> G (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 3935
FT /note="D -> G (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 5085
FT /note="A -> V (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 5968
FT /note="F -> S (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 6221
FT /note="P -> L (in strain: Isolate Vero cell-adapted p65)"
FT MUTAGEN 673
FT /note="G->A: No processing between p87 and p195."
FT /evidence="ECO:0000269|PubMed:9636369"
FT MUTAGEN 676
FT /note="T->S: No effect."
FT /evidence="ECO:0000269|PubMed:9636369"
FT MUTAGEN 1274
FT /note="C->S: Complete loss of PL-PRO activity."
FT /evidence="ECO:0000269|PubMed:9636369"
FT MUTAGEN 1437
FT /note="H->K: Complete loss of PL-PRO activity."
FT /evidence="ECO:0000269|PubMed:9636369"
FT MUTAGEN 2264
FT /note="A->N: Almost no processing between p195 and peptide
FT HD2."
FT /evidence="ECO:0000269|PubMed:10644337"
FT MUTAGEN 2265..2266
FT /note="Missing: No processing between p195 and peptide
FT HD2."
FT MUTAGEN 2265
FT /note="G->A: No effect."
FT /evidence="ECO:0000269|PubMed:10644337"
FT MUTAGEN 2265
FT /note="G->N: Almost no processing between p195 and peptide
FT HD2."
FT /evidence="ECO:0000269|PubMed:10644337"
FT MUTAGEN 2266
FT /note="G->N: No effect."
FT /evidence="ECO:0000269|PubMed:10644337"
FT MUTAGEN 2820
FT /note="H->K,G: Complete loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:7778277"
FT MUTAGEN 2841
FT /note="E->Q: No effect."
FT /evidence="ECO:0000269|PubMed:7778277"
FT MUTAGEN 2843
FT /note="E->D,N,Q: No effect."
FT /evidence="ECO:0000269|PubMed:7778277"
FT MUTAGEN 2922
FT /note="C->A: Complete loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:7778277"
FT MUTAGEN 2922
FT /note="C->S: Partial loss of 3CL-PRO activity."
FT /evidence="ECO:0000269|PubMed:7778277"
FT MUTAGEN 3086
FT /note="Q->E: No processing between 3CL-PRO and p34."
FT /evidence="ECO:0000269|PubMed:10873746"
FT MUTAGEN 3365
FT /note="Q->E: No effect."
FT /evidence="ECO:0000269|PubMed:10873746"
FT MUTAGEN 3379
FT /note="Q->E: No processing between p34 and p9."
FT /evidence="ECO:0000269|PubMed:10873746"
FT MUTAGEN 3462
FT /note="Q->E: No processing between p9 and p24."
FT /evidence="ECO:0000269|PubMed:9568037"
FT MUTAGEN 3672
FT /note="Q->E: No processing between p24 and p10."
FT /evidence="ECO:0000269|PubMed:9032311,
FT ECO:0000269|PubMed:9568037"
FT MUTAGEN 3783
FT /note="Q->E: No processing between p10 and p16."
FT /evidence="ECO:0000269|PubMed:9032311,
FT ECO:0000269|PubMed:9568037"
FT MUTAGEN 3928
FT /note="Q->E: No processing between p16 and p100."
FT /evidence="ECO:0000269|PubMed:7778277"
FT MUTAGEN 4868
FT /note="Q->E: No processing between p100 and p68."
FT /evidence="ECO:0000269|PubMed:7778277,
FT ECO:0000269|PubMed:9657947"
FT MUTAGEN 4869
FT /note="S->A,G: No effect."
FT /evidence="ECO:0000269|PubMed:7778277"
FT MUTAGEN 5468
FT /note="Q->M: No processing between p68 and p58."
FT /evidence="ECO:0000269|PubMed:9657947"
FT MUTAGEN 5989
FT /note="Q->E: No processing between p58 and p39."
FT /evidence="ECO:0000269|PubMed:9657947"
FT MUTAGEN 6327
FT /note="Q->E: No processing between p39 and p35."
FT /evidence="ECO:0000269|PubMed:9657947"
FT STRAND 1015..1021
FT /evidence="ECO:0007829|PDB:3EJF"
FT HELIX 1023..1034
FT /evidence="ECO:0007829|PDB:3EJF"
FT STRAND 1035..1042
FT /evidence="ECO:0007829|PDB:3EJF"
FT HELIX 1052..1061
FT /evidence="ECO:0007829|PDB:3EJF"
FT HELIX 1063..1076
FT /evidence="ECO:0007829|PDB:3EJF"
FT STRAND 1080..1084
FT /evidence="ECO:0007829|PDB:3EJF"
FT STRAND 1091..1097
FT /evidence="ECO:0007829|PDB:3EJF"
FT HELIX 1107..1116
FT /evidence="ECO:0007829|PDB:3EJF"
FT STRAND 1125..1129
FT /evidence="ECO:0007829|PDB:3EJF"
FT STRAND 1133..1135
FT /evidence="ECO:0007829|PDB:3EKE"
FT TURN 1136..1139
FT /evidence="ECO:0007829|PDB:3EKE"
FT HELIX 1140..1151
FT /evidence="ECO:0007829|PDB:3EJF"
FT STRAND 1157..1163
FT /evidence="ECO:0007829|PDB:3EJF"
FT HELIX 1165..1173
FT /evidence="ECO:0007829|PDB:3EJF"
FT STRAND 1178..1188
FT /evidence="ECO:0007829|PDB:4X2Z"
FT STRAND 1190..1194
FT /evidence="ECO:0007829|PDB:4X2Z"
FT HELIX 1200..1203
FT /evidence="ECO:0007829|PDB:4X2Z"
FT STRAND 1209..1211
FT /evidence="ECO:0007829|PDB:4X2Z"
FT HELIX 1216..1218
FT /evidence="ECO:0007829|PDB:4X2Z"
FT STRAND 1224..1226
FT /evidence="ECO:0007829|PDB:4X2Z"
FT HELIX 1232..1235
FT /evidence="ECO:0007829|PDB:5BZ0"
FT TURN 1236..1239
FT /evidence="ECO:0007829|PDB:5BZ0"
FT HELIX 1242..1251
FT /evidence="ECO:0007829|PDB:5BZ0"
FT STRAND 1258..1261
FT /evidence="ECO:0007829|PDB:5BZ0"
FT STRAND 1264..1267
FT /evidence="ECO:0007829|PDB:5BZ0"
FT TURN 1271..1273
FT /evidence="ECO:0007829|PDB:5BZ0"
FT HELIX 1274..1285
FT /evidence="ECO:0007829|PDB:5BZ0"
FT HELIX 1294..1302
FT /evidence="ECO:0007829|PDB:5BZ0"
FT HELIX 1307..1316
FT /evidence="ECO:0007829|PDB:5BZ0"
FT HELIX 1327..1335
FT /evidence="ECO:0007829|PDB:5BZ0"
FT TURN 1342..1344
FT /evidence="ECO:0007829|PDB:5BZ0"
FT STRAND 1346..1353
FT /evidence="ECO:0007829|PDB:5BZ0"
FT STRAND 1356..1363
FT /evidence="ECO:0007829|PDB:5BZ0"
FT HELIX 1364..1368
FT /evidence="ECO:0007829|PDB:5BZ0"
FT STRAND 1369..1376
FT /evidence="ECO:0007829|PDB:5BZ0"
FT HELIX 1377..1381
FT /evidence="ECO:0007829|PDB:5BZ0"
FT STRAND 1382..1386
FT /evidence="ECO:0007829|PDB:5BZ0"
FT TURN 1388..1390
FT /evidence="ECO:0007829|PDB:5BZ0"
FT STRAND 1393..1413
FT /evidence="ECO:0007829|PDB:5BZ0"
FT STRAND 1415..1418
FT /evidence="ECO:0007829|PDB:5BZ0"
FT STRAND 1424..1431
FT /evidence="ECO:0007829|PDB:5BZ0"
FT STRAND 1435..1442
FT /evidence="ECO:0007829|PDB:5BZ0"
FT STRAND 1445..1447
FT /evidence="ECO:0007829|PDB:5BZ0"
FT STRAND 1458..1473
FT /evidence="ECO:0007829|PDB:5BZ0"
SQ SEQUENCE 6629 AA; 744540 MW; 887FCAF7EA68A270 CRC64;
MASSLKQGVS PKPRDVILVS KDIPEQLCDA LFFYTSHNPK DYADAFAVRQ KFDRSLQTGK
QFKFETVCGL FLLKGVDKIT PGVPAKVLKA TSKLADLEDI FGVSPLARKY RELLKTACQW
SLTVEALDVR AQTLDEIFDP TEILWLQVAA KIHVSSMAMR RLVGEVTAKV MDALGSNLSA
LFQIVKQQIA RIFQKALAIF ENVNELPQRI AALKMAFAKC ARSITVVVVE RTLVVKEFAG
TCLASINGAV AKFFEELPNG FMGSKIFTTL AFFKEAAVRV VENIPNAPRG TKGFEVVGNA
KGTQVVVRGM RNDLTLLDQK ADIPVEPEGW SAILDGHLCY VFRSGDRFYA APLSGNFALS
DVHCCERVVC LSDGVTPEIN DGLILAAIYS SFSVSELVTA LKKGEPFKFL GHKFVYAKDA
AVSFTLAKAA TIADVLRLFQ SARVIAEDVW SSFTEKSFEF WKLAYGKVRN LEEFVKTYVC
KAQMSIVILA AVLGEDIWHL VSQVIYKLGV LFTKVVDFCD KHWKGFCVQL KRAKLIVTET
FCVLKGVAQH CFQLLLDAIH SLYKSFKKCA LGRIHGDLLF WKGGVHKIVQ DGDEIWFDAI
DSVDVEDLGV VQEKSIDFEV CDDVTLPENQ PGHMVQIEDD GKNYMFFRFK KDENIYYTPM
SQLGAINVVC KAGGKTVTFG ETTVQEIPPP DVVPIKVSIE CCGEPWNTIF KKAYKEPIEV
DTDLTVEQLL SVIYEKMCDD LKLFPEAPEP PPFENVALVD KNGKDLDCIK SCHLIYRDYE
SDDDIEEEDA EECDTDSGEA EECDTNSECE EEDEDTKVLA LIQDPASIKY PLPLDEDYSV
YNGCIVHKDA LDVVNLPSGE ETFVVNNCFE GAVKPLPQKV VDVLGDWGEA VDAQEQLCQQ
EPLQHTFEEP VENSTGSSKT MTEQVVVEDQ ELPVVEQDQD VVVYTPTDLE VAKETAEEVD
EFILIFAVPK EEVVSQKDGA QIKQEPIQVV KPQREKKAKK FKVKPATCEK PKFLEYKTCV
GDLTVVIAKA LDEFKEFCIV NAANEHMTHG SGVAKAIADF CGLDFVEYCE DYVKKHGPQQ
RLVTPSFVKG IQCVNNVVGP RHGDNNLHEK LVAAYKNVLV DGVVNYVVPV LSLGIFGVDF
KMSIDAMREA FEGCTIRVLL FSLSQEHIDY FDVTCKQKTI YLTEDGVKYR SIVLKPGDSL
GQFGQVYAKN KIVFTADDVE DKEILYVPTT DKSILEYYGL DAQKYVIYLQ TLAQKWNVQY
RDNFLILEWR DGNCWISSAI VLLQAAKIRF KGFLTEAWAK LLGGDPTDFV AWCYASCTAK
VGDFSDANWL LANLAEHFDA DYTNAFLKKR VSCNCGIKSY ELRGLEACIQ PVRATNLLHF
KTQYSNCPTC GANNTDEVIE ASLPYLLLFA TDGPATVDCD EDAVGTVVFV GSTNSGHCYT
QAAGQAFDNL AKDRKFGKKS PYITAMYTRF AFKNETSLPV AKQSKGKSKS VKEDVSNLAT
SSKASFDNLT DFEQWYDSNI YESLKVQESP DNFDKYVSFT TKEDSKLPLT LKVRGIKSVV
DFRSKDGFIY KLTPDTDENS KAPVYYPVLD AISLKAIWVE GNANFVVGHP NYYSKSLHIP
TFWENAENFV KMGDKIGGVT MGLWRAEHLN KPNLERIFNI AKKAIVGSSV VTTQCGKLIG
KAATFIADKV GGGVVRNITD SIKGLCGITR GHFERKMSPQ FLKTLMFFLF YFLKASVKSV
VASYKTVLCK VVLATLLIVW FVYTSNPVMF TGIRVLDFLF EGSLCGPYKD YGKDSFDVLR
YCADDFICRV CLHDKDSLHL YKHAYSVEQV YKDAASGFIF NWNWLYLVFL ILFVKPVAGF
VIICYCVKYL VLNSTVLQTG VCFLDWFVQT VFSHFNFMGA GFYFWLFYKI YIQVHHILYC
KDVTCEVCKR VARSNRQEVS VVVGGRKQIV HVYTNSGYNF CKRHNWYCRN CDDYGHQNTF
MSPEVAGELS EKLKRHVKPT AYAYHVVDEA CLVDDFVNLK YKAATPGKDS ASSAVKCFSV
TDFLKKAVFL KEALKCEQIS NDGFIVCNTQ SAHALEEAKN AAIYYAQYLC KPILILDQAL
YEQLVVEPVS KSVIDKVCSI LSSIISVDTA ALNYKAGTLR DALLSITKDE EAVDMAIFCH
NHDVDYTGDG FTNVIPSYGI DTGKLTPRDR GFLINADASI ANLRVKNAPP VVWKFSELIK
LSDSCLKYLI SATVKSGVRF FITKSGAKQV IACHTQKLLV EKKAGGIVSG TFKCFKSYFK
WLLIFYILFT ACCSGYYYME VSKSFVHPMY DVNSTLHVEG FKVIDKGVLR EIVPEDTCFS
NKFVNFDAFW GRPYDNSRNC PIVTAVIDGD GTVATGVPGF VSWVMDGVMF IHMTQTERKP
WYIPTWFNRE IVGYTQDSII TEGSFYTSIA LFSARCLYLT ASNTPQLYCF NGDNDAPGAL
PFGSIIPHRV YFQPNGVRLI VPQQILHTPY VVKFVSDSYC RGSVCEYTRP GYCVSLNPQW
VLFNDEYTSK PGVFCGSTVR ELMFSMVSTF FTGVNPNIYM QLATMFLILV VVVLIFAMVI
KFQGVFKAYA TTVFITMLVW VINAFILCVH SYNSVLAVIL LVLYCYASLV TSRNTVIIMH
CWLVFTFGLI VPTWLACCYL GFIIYMYTPL FLWCYGTTKN TRKLYDGNEF VGNYDLAAKS
TFVIRGSEFV KLTNEIGDKF EAYLSAYARL KYYSGTGSEQ DYLQACRAWL AYALDQYRNS
GVEIVYTPPR YSIGVSRLQS GFKKLVSPSS AVEKCIVSVS YRGNNLNGLW LGDTIYCPRH
VLGKFSGDQW NDVLNLANNH EFEVTTQHGV TLNVVSRRLK GAVLILQTAV ANAETPKYKF
IKANCGDSFT IACAYGGTVV GLYPVTMRSN GTIRASFLAG ACGSVGFNIE KGVVNFFYMH
HLELPNALHT GTDLMGEFYG GYVDEEVAQR VPPDNLVTNN IVAWLYAAII SVKESSFSLP
KWLESTTVSV DDYNKWAGDN GFTPFSTSTA ITKLSAITGV DVCKLLRTIM VKNSQWGGDP
ILGQYNFEDE LTPESVFNQI GGVRLQSSFV RKATSWFWSR CVLACFLFVL CAIVLFTAVP
LKFYVYAAVI LLMAVLFISF TVKHVMAYMD TFLLPTLITV IIGVCAEVPF IYNTLISQVV
IFLSQWYDPV VFDTMVPWMF LPLVLYTAFK CVQGCYMNSF NTSLLMLYQF VKLGFVIYTS
SNTLTAYTEG NWELFFELVH TTVLANVSSN SLIGLFVFKC AKWMLYYCNA TYLNNYVLMA
VMVNCIGWLC TCYFGLYWWV NKVFGLTLGK YNFKVSVDQY RYMCLHKINP PKTVWEVFST
NILIQGIGGD RVLPIATVQA KLSDVKCTTV VLMQLLTKLN VEANSKMHVY LVELHNKILA
SDDVGECMDN LLGMLITLFC IDSTIDLSEY CDDILKRSTV LQSVTQEFSH IPSYAEYERA
KNLYEKVLVD SKNGGVTQQE LAAYRKAANI AKSVFDRDLA VQKKLDSMAE RAMTTMYKEA
RVTDRRAKLV SSLHALLFSM LKKIDSEKLN VLFDQASSGV VPLATVPIVC SNKLTLVIPD
PETWVKCVEG VHVTYSTVVW NIDTVIDADG TELHPTSTGS GLTYCISGAN IAWPLKVNLT
RNGHNKVDVV LQNNELMPHG VKTKACVAGV DQAHCSVESK CYYTNISGNS VVAAITSSNP
NLKVASFLNE AGNQIYVDLD PPCKFGMKVG VKVEVVYLYF IKNTRSIVRG MVLGAISNVV
VLQSKGHETE EVDAVGILSL CSFAVDPADT YCKYVAAGNQ PLGNCVKMLT VHNGSGFAIT
SKPSPTPDQD SYGGASVCLY CRAHIAHPGS VGNLDGRCQF KGSFVQIPTT EKDPVGFCLR
NKVCTVCQCW IGYGCQCDSL RQPKSSVQSV AGASDFDKNY LNRVRGSSEA RLIPLASGCD
PDVVKRAFDV CNKESAGMFQ NLKRNCARFQ ELRDTEDGNL EYLDSYFVVK QTTPSNYEHE
KSCYEDLKSE VTADHDFFVF NKNIYNISRQ RLTKYTMMDF CYALRHFDPK DCEVLKEILV
TYGCIEDYHP KWFEENKDWY DPIENSKYYV MLAKMGPIVR RALLNAIEFG NLMVEKGYVG
VITLDNQDLN GKFYDFGDFQ KTAPGAGVPV FDTYYSYMMP IIAMTDALAP ERYFEYDVHK
GYKSYDLLKY DYTEEKQELF QKYFKYWDQE YHPNCRDCSD DRCLIHCANF NILFSTLIPQ
TSFGNLCRKV FVDGVPFIAT CGYHSKELGV IMNQDNTMSF SKMGLSQLMQ FVGDPALLVG
TSNNLVDLRT SCFSVCALTS GITHQTVKPG HFNKDFYDFA EKAGMFKEGS SIPLKHFFYP
QTGNAAINDY DYYRYNRPTM FDICQLLFCL EVTSKYFECY EGGCIPASQV VVNNLDKSAG
YPFNKFGKAR LYYEMSLEEQ DQLFEITKKN VLPTITQMNL KYAISAKNRA RTVAGVSILS
TMTNRQFHQK ILKSIVNTRN ASVVIGTTKF YGGWDNMLRN LIQGVEDPIL MGWDYPKCDR
AMPNLLRIAA SLVLARKHTN CCSWSERIYR LYNECAQVLS ETVLATGGIY VKPGGTSSGD
ATTAYANSVF NIIQATSANV ARLLSVITRD IVYDNIKSLQ YELYQQVYRR VNFDPAFVEK
FYSYLCKNFS LMILSDDGVV CYNNTLAKQG LVADISGFRE VLYYQNNVFM ADSKCWVEPD
LEKGPHEFCS QHTMLVEVDG EPKYLPYPDP SRILGACVFV DDVDKTEPVA VMERYIALAI
DAYPLVHHEN EEYKKVFFVL LAYIRKLYQE LSQNMLMDYS FVMDIDKGSK FWEQEFYENM
YRAPTTLQSC GVCVVCNSQT ILRCGNCIRK PFLCCKCCYD HVMHTDHKNV LSINPYICSQ
LGCGEADVTK LYLGGMSYFC GNHKPKLSIP LVSNGTVFGI YRANCAGSEN VDDFNQLATT
NWSIVEPYIL ANRCSDSLRR FAAETVKATE ELHKQQFASA EVREVFSDRE LILSWEPGKT
RPPLNRNYVF TGYHFTRTSK VQLGDFTFEK GEGKDVVYYK ATSTAKLSVG DIFVLTSHNV
VSLVAPTLCP QQTFSRFVNL RPNVMVPECF VNNIPLYHLV GKQKRTTVQG PPGSGKSHFA
IGLAVYFSSA RVVFTACSHA AVDALCEKAF KFLKVDDCTR IVPQRTTVDC FSKFKANDTG
KKYIFSTINA LPEVSCDILL VDEVSMLTNY ELSFINGKIN YQYVVYVGDP AQLPAPRTLL
NGSLSPKDYN VVTNLMVCVK PDIFLAKCYR CPKEIVDTVS TLVYDGKFIA NNPESRECFK
VIVNNGNSDV GHESGSAYNT TQLEFVKDFV CRNKQWREAI FISPYNAMNQ RAYRMLGLNV
QTVDSSQGSE YDYVIFCVTA DSQHALNINR FNVALTRAKR GILVVMRQRD ELYSALKFTE
LDSETSLQGT GLFKICNKEF SGVHPAYAVT TKALAATYKV NDELAALVNV EAGSEITYKH
LISLLGFKMS VNVEGCHNMF ITRDEAIRNV RGWVGFDVEA THACGTNIGT NLPFQVGFST
GADFVVTPEG LVDTSIGNNF EPVNSKAPPG EQFNHLRVLF KSAKPWHVIR PRIVQMLADN
LCNVSDCVVF VTWCHGLELT TLRYFVKIGK EQVCSCGSRA TTFNSHTQAY ACWKHCLGFD
FVYNPLLVDI QQWGYSGNLQ FNHDLHCNVH GHAHVASVDA IMTRCLAINN AFCQDVNWDL
TYPHIANEDE VNSSCRYLQR MYLNACVDAL KVNVVYDIGN PKGIKCVRRG DVNFRFYDKN
PIVRNVKQFE YDYNQHKDKF ADGLCMFWNC NVDCYPDNSL VCRYDTRNLS VFNLPGCNGG
SLYVNKHAFY TPKFDRISFR NLKAMPFFFY DSSPCETIQV DGVAQDLVSL ATKDCITKCN
IGGAVCKKHA QMYAEFVTSY NAAVTAGFTF WVTNKLNPYN LWKSFSALQS IDNIAYNMYK
GGHYDAIAGE MPTVITGDKV FVIDQGVEKA VFVNQTTLPT SVAFELYAKR NIRTLPNNRI
LKGLGVDVTN GFVIWDYANQ TPLYRNTVKV CAYTDIEPNG LVVLYDDRYG DYQSFLAADN
AVLVSTQCYK RYSYVEIPSN LLVQNGMPLK DGANLYVYKR VNGAFVTLPN TINTQGRSYE
TFEPRSDIER DFLAMSEESF VERYGKDLGL QHILYGEVDK PQLGGLHTVI GMYRLLRANK
LNAKSVTNSD SDVMQNYFVL SDNGSYKQVC TVVDLLLDDF LELLRNILKE YGTNKSKVVT
VSIDYHSINF MTWFEDGSIK TCYPQLQSAW TCGYNMPELY KVQNCVMEPC NIPNYGVGIT
LPSGILMNVA KYTQLCQYLS KTTICVPHNM RVMHFGAGSD KGVAPGSTVL KQWLPEGTLL
VDNDIVDYVS DAHVSVLSDC NKYNTEHKFD LVISDMYTDN DSKRKHEGVI ANNGNDDVFI
YLSSFLRNNL ALGGSFAVKV TETSWHEVLY DIAQDCAWWT MFCTAVNASS SEAFLIGVNY
LGASEKVKVS GKTLHANYIF WRNCNYLQTS AYSIFDVAKF DLRLKATPVV NLKTEQKTDL
VFNLIKCGKL LVRDVGNTSF TSDSFVCTM
