ID   POLG_FCVUR              Reviewed;        1763 AA.
AC   Q66914;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 125.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=Protein p5.6;
DE     AltName: Full=NS1;
DE   Contains:
DE     RecName: Full=Protein p32;
DE     AltName: Full=NS2;
DE   Contains:
DE     RecName: Full=NTPase;
DE              EC=3.6.1.15;
DE     AltName: Full=NS3;
DE     AltName: Full=p39;
DE   Contains:
DE     RecName: Full=Protein p30;
DE     AltName: Full=NS4;
DE   Contains:
DE     RecName: Full=Viral genome-linked protein;
DE     AltName: Full=NS5;
DE     AltName: Full=VPg;
DE     AltName: Full=p13;
DE   Contains:
DE     RecName: Full=Protease-polymerase p76;
DE              Short=Pro-Pol;
DE              EC=2.7.7.48;
DE              EC=3.4.22.66;
DE     AltName: Full=NS6-7;
GN   ORFNames=ORF1;
OS   Feline calicivirus (strain Cat/United States/Urbana/1960) (FCV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Caliciviridae; Vesivirus; Feline calicivirus.
OX   NCBI_TaxID=292349;
OH   NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7618275; DOI=10.1006/viro.1995.1354;
RA   Sosnovtsev S.V., Green K.Y.;
RT   "RNA transcripts derived from a cloned full-length copy of the feline
RT   calicivirus genome do not require VpG for infectivity.";
RL   Virology 210:383-390(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 686-695, PROTEOLYTIC PROCESSING (GENOME POLYPROTEIN),
RP   MUTAGENESIS OF GLU-46; GLU-331; GLU-683; GLU-685; GLU-960; GLU-1071;
RP   GLU-1345 AND GLU-1419, AND FUNCTION (PROTEASE-POLYMERASE P76).
RX   PubMed=12072506; DOI=10.1128/jvi.76.14.7060-7072.2002;
RA   Sosnovtsev S.V., Garfield M., Green K.Y.;
RT   "Processing map and essential cleavage sites of the nonstructural
RT   polyprotein encoded by ORF1 of the feline calicivirus genome.";
RL   J. Virol. 76:7060-7072(2002).
RN   [3]
RP   PROTEIN SEQUENCE OF 961-969 AND 1072-1080, PROTEOLYTIC PROCESSING (GENOME
RP   POLYPROTEIN), MUTAGENESIS OF CYS-1193, AND FUNCTION (PROTEASE-POLYMERASE
RP   P76).
RX   PubMed=10400760; DOI=10.1128/jvi.73.8.6626-6633.1999;
RA   Sosnovtseva S.A., Sosnovtsev S.V., Green K.Y.;
RT   "Mapping of the feline calicivirus proteinase responsible for autocatalytic
RT   processing of the nonstructural polyprotein and identification of a stable
RT   proteinase-polymerase precursor protein.";
RL   J. Virol. 73:6626-6633(1999).
RN   [4]
RP   PROTEIN SEQUENCE OF 961-980.
RX   PubMed=11062050; DOI=10.1006/viro.2000.0579;
RA   Sosnovtsev S.V., Green K.Y.;
RT   "Identification and genomic mapping of the ORF3 and VPg proteins in feline
RT   calicivirus virions.";
RL   Virology 277:193-203(2000).
RN   [5]
RP   FUNCTION (PROTEASE-POLYMERASE P76).
RX   PubMed=15254188; DOI=10.1128/jvi.78.15.8172-8182.2004;
RA   Kuyumcu-Martinez M., Belliot G., Sosnovtsev S.V., Chang K.O., Green K.Y.,
RA   Lloyd R.E.;
RT   "Calicivirus 3C-like proteinase inhibits cellular translation by cleavage
RT   of poly(A)-binding protein.";
RL   J. Virol. 78:8172-8182(2004).
RN   [6]
RP   FUNCTION (PROTEASE-POLYMERASE P76).
RX   PubMed=15105529; DOI=10.1099/vir.0.19564-0;
RA   Willcocks M.M., Carter M.J., Roberts L.O.;
RT   "Cleavage of eukaryotic initiation factor eIF4G and inhibition of host-cell
RT   protein synthesis during feline calicivirus infection.";
RL   J. Gen. Virol. 85:1125-1130(2004).
RN   [7]
RP   INTERACTION WITH NTPASE (PROTEIN P32), INTERACTION WITH PROTEIN P30
RP   (PROTEIN P32), INTERACTION WITH PROTEASE-POLYMERASE P76 (PROTEIN P32),
RP   INTERACTION WITH PROTEASE-POLYMERASE P76 (VIRAL GENOME-LINKED PROTEIN),
RP   INTERACTION WITH CAPSID PROTEIN VP1 (VIRAL GENOME-LINKED PROTEIN),
RP   INTERACTION WITH VIRAL GENOME-LINKED PROTEIN (PROTEASE-POLYMERASE P76),
RP   INTERACTION WITH PROTEIN P32 (PROTEASE-POLYMERASE P76), INTERACTION WITH
RP   CAPSID PROTEIN VP1 (PROTEASE-POLYMERASE P76), SUBUNIT (PROTEIN P32), AND
RP   SUBUNIT (PROTEASE-POLYMERASE P76).
RX   PubMed=16432023; DOI=10.1099/vir.0.81456-0;
RA   Kaiser W.J., Chaudhry Y., Sosnovtsev S.V., Goodfellow I.G.;
RT   "Analysis of protein-protein interactions in the feline calicivirus
RT   replication complex.";
RL   J. Gen. Virol. 87:363-368(2006).
RN   [8]
RP   FUNCTION (PROTEASE-POLYMERASE P76).
RX   PubMed=27147742; DOI=10.1128/jvi.00647-16;
RA   Humoud M.N., Doyle N., Royall E., Willcocks M.M., Sorgeloos F.,
RA   van Kuppeveld F., Roberts L.O., Goodfellow I.G., Langereis M.A., Locker N.;
RT   "Feline Calicivirus Infection Disrupts Assembly of Cytoplasmic Stress
RT   Granules and Induces G3BP1 Cleavage.";
RL   J. Virol. 90:6489-6501(2016).
CC   -!- FUNCTION: [NTPase]: NTPase presumably plays a role in replication.
CC       Despite having similarities with helicases, does not seem to display
CC       any helicase activity.
CC   -!- FUNCTION: [Viral genome-linked protein]: Viral genome-linked protein is
CC       covalently linked to the 5'-end of the positive-strand, negative-strand
CC       genomic RNAs and subgenomic RNA. Acts as a genome-linked replication
CC       primer. May recruit ribosome to viral RNA thereby promoting viral
CC       proteins translation (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:15254188}.
CC   -!- FUNCTION: [Protease-polymerase p76]: The protease activity processes
CC       the polyprotein: Pro-Pol is first released by autocleavage, then all
CC       other proteins are cleaved (PubMed:12072506, PubMed:10400760). Cleaves
CC       host translation initiation factor eIF4G1, eIF4G2 and PABP1 thereby
CC       inducing a shutdown of host protein synthesis (PubMed:15105529). This
CC       shutdown may not prevent viral mRNA from being translated since viral
CC       Vpg replaces the cap (PubMed:15105529). May cleave host polyadenylate-
CC       binding protein thereby inhibiting cellular translation
CC       (PubMed:15254188). Seems to act as a RNase and degrades host Pol II-
CC       driven mRNAs with the help of host XRN1 (By similarity). Inhibits the
CC       integrated stress response (ISR) in the infected cell by cleaving host
CC       G3BP1 and G3BP2 (PubMed:27147742). Stress granule formation is thus
CC       inhibited, which allows protein synthesis and viral replication
CC       (PubMed:27147742). The RNA-directed RNA polymerase activity replicates
CC       genomic and antigenomic viral RNA by recognizing specific signals.
CC       Transcribes also a subgenomic mRNA by initiating RNA synthesis
CC       internally on antigenomic RNA. This sgRNA codes for structural
CC       proteins. Catalyzes the covalent attachment VPg with viral RNAs.
CC       {ECO:0000250|UniProtKB:N0A3C0, ECO:0000269|PubMed:10400760,
CC       ECO:0000269|PubMed:12072506, ECO:0000269|PubMed:15105529,
CC       ECO:0000269|PubMed:15254188, ECO:0000269|PubMed:27147742}.
CC   -!- CATALYTIC ACTIVITY: [NTPase]:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC   -!- CATALYTIC ACTIVITY: [Protease-polymerase p76]:
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: [Protease-polymerase p76]:
CC       Reaction=Endopeptidase with a preference for cleavage when the P1
CC         position is occupied by Glu-|-Xaa and the P1' position is occupied by
CC         Gly-|-Yaa.; EC=3.4.22.66; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU01242};
CC   -!- SUBUNIT: Protein p32: Homodimer (PubMed:16432023). Interacts with
CC       NTPase, protein p30 and protease-polymerase p76 (PubMed:16432023).
CC       {ECO:0000269|PubMed:16432023}.
CC   -!- SUBUNIT: [Viral genome-linked protein]: Interacts with capsid protein
CC       VP1 and protease-polymerase p76. {ECO:0000269|PubMed:16432023}.
CC   -!- SUBUNIT: [Protease-polymerase p76]: Homooligomer. Interacts with Vpg,
CC       protein p32 and may interact with capsid protein VP1.
CC       {ECO:0000269|PubMed:16432023}.
CC   -!- DOMAIN: [Protease-polymerase p76]: Protease-polymerase is composed of
CC       two domains displaying two different catalytic activity. These
CC       activities may act independently.
CC   -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield
CC       mature proteins. Pro-Pol is first autocatalytically cleaved, then
CC       processes the whole polyprotein. {ECO:0000269|PubMed:10400760,
CC       ECO:0000269|PubMed:12072506}.
CC   -!- PTM: [Viral genome-linked protein]: VPg is uridylylated by the
CC       polymerase and is covalently attached to the 5'-end of the
CC       polyadenylated genomic and subgenomic RNAs. This uridylylated form acts
CC       as a nucleotide-peptide primer for the polymerase (By similarity).
CC       {ECO:0000250}.
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DR   EMBL; L40021; AAA79323.1; -; Genomic_RNA.
DR   RefSeq; NP_783196.1; NC_001481.2.
DR   SMR; Q66914; -.
DR   MEROPS; C24.002; -.
DR   GeneID; 1502252; -.
DR   KEGG; vg:1502252; -.
DR   BRENDA; 3.4.22.66; 8732.
DR   BRENDA; 3.4.23.B4; 8732.
DR   Proteomes; UP000001098; Segment.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd23192; Caliciviridae_RdRp; 1.
DR   Gene3D; 1.10.260.110; -; 1.
DR   Gene3D; 1.20.960.20; -; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 6.10.140.320; -; 1.
DR   Gene3D; 6.10.250.3230; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR   InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR   InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000317; Peptidase_C24.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR049434; VPg.
DR   Pfam; PF03510; Peptidase_C24; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   Pfam; PF00910; RNA_helicase; 1.
DR   Pfam; PF20915; VPg; 1.
DR   PRINTS; PR00916; 2CENDOPTASE.
DR   PRINTS; PR00918; CALICVIRUSNS.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51894; CV_3CL_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51218; SF3_HELICASE_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Covalent protein-RNA linkage; Direct protein sequencing;
KW   Eukaryotic host gene expression shutoff by virus;
KW   Eukaryotic host translation shutoff by virus;
KW   Host gene expression shutoff by virus; Host-virus interaction; Hydrolase;
KW   Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease;
KW   Reference proteome; RNA-directed RNA polymerase; Thiol protease;
KW   Transferase; Viral RNA replication.
FT   CHAIN           1..1763
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000341636"
FT   CHAIN           1..46
FT                   /note="Protein p5.6"
FT                   /id="PRO_0000036907"
FT   CHAIN           47..331
FT                   /note="Protein p32"
FT                   /id="PRO_0000036908"
FT   CHAIN           332..685
FT                   /note="NTPase"
FT                   /id="PRO_0000036909"
FT   CHAIN           686..960
FT                   /note="Protein p30"
FT                   /id="PRO_0000036910"
FT   CHAIN           961..1071
FT                   /note="Viral genome-linked protein"
FT                   /id="PRO_0000036911"
FT   CHAIN           1072..1763
FT                   /note="Protease-polymerase p76"
FT                   /id="PRO_0000036912"
FT   DOMAIN          458..614
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1073..1229
FT                   /note="Peptidase C24"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT   DOMAIN          1478..1603
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   ACT_SITE        1110
FT                   /note="For 3CLpro activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT   ACT_SITE        1131
FT                   /note="For 3CLpro activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT   ACT_SITE        1193
FT                   /note="For 3CLpro activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT   BINDING         484..491
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   SITE            46..47
FT                   /note="Cleavage; by Pro-Pol"
FT                   /evidence="ECO:0000269|PubMed:12072506"
FT   SITE            331..332
FT                   /note="Cleavage; by Pro-Pol"
FT                   /evidence="ECO:0000269|PubMed:12072506"
FT   SITE            685..686
FT                   /note="Cleavage; by Pro-Pol"
FT                   /evidence="ECO:0000269|PubMed:10400760,
FT                   ECO:0000269|PubMed:12072506"
FT   SITE            960..961
FT                   /note="Cleavage; by Pro-Pol"
FT                   /evidence="ECO:0000269|PubMed:10400760,
FT                   ECO:0000269|PubMed:12072506"
FT   SITE            1071..1072
FT                   /note="Cleavage; by Pro-Pol"
FT                   /evidence="ECO:0000269|PubMed:10400760,
FT                   ECO:0000269|PubMed:12072506"
FT   MOD_RES         984
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P27409"
FT   MUTAGEN         46
FT                   /note="E->A: Complete loss of proteolytic processing
FT                   between P5.6 and P32; Complete loss of infectious clone
FT                   recovery."
FT                   /evidence="ECO:0000269|PubMed:12072506"
FT   MUTAGEN         331
FT                   /note="E->A: Complete loss of infectious clone recovery."
FT                   /evidence="ECO:0000269|PubMed:12072506"
FT   MUTAGEN         683
FT                   /note="E->A: Complete loss of infectious clone recovery."
FT                   /evidence="ECO:0000269|PubMed:12072506"
FT   MUTAGEN         685
FT                   /note="E->A: Complete loss of infectious clone recovery."
FT                   /evidence="ECO:0000269|PubMed:12072506"
FT   MUTAGEN         960
FT                   /note="E->A: Complete loss of infectious clone recovery."
FT                   /evidence="ECO:0000269|PubMed:12072506"
FT   MUTAGEN         1071
FT                   /note="E->A: Complete loss of infectious clone recovery."
FT                   /evidence="ECO:0000269|PubMed:12072506"
FT   MUTAGEN         1193
FT                   /note="C->G: Complete loss of proteolytic processing."
FT                   /evidence="ECO:0000269|PubMed:10400760"
FT   MUTAGEN         1345
FT                   /note="E->A: No effect on infectious clone recovery."
FT                   /evidence="ECO:0000269|PubMed:12072506"
FT   MUTAGEN         1419
FT                   /note="E->A: No effect on infectious clone recovery."
FT                   /evidence="ECO:0000269|PubMed:12072506"
SQ   SEQUENCE   1763 AA;  194911 MW;  7F105592DF0BF821 CRC64;
     MSQTLSFVLK THSVRKDFVH SVKRTLQRRR DLQYLYNKLS RPIRAEACPS CASYDVCPNC
     TSGSIPDDGS SKGQIPSWED VTKTSTYSLL LSEDTSDELH PDDLVNVAAH IRKALSTQSH
     PANVDMCKEQ LTSLLVMAEA MLPQRSRSTL PLHQKYVAAR LEWREKFFSK PLDFLLEKIG
     TSRDILQITA VWKIIIEKAC YCKSYGEHWF EAAKQKLREI KSYEHNTLKP LIGAFIDGLR
     LMTIDNPNPM GFLPKLIGLI KPLNLAMIID NHENTLSGWV ITLTAIMELY NITECTIDVI
     TSIITGFYDK IGKATKFYSQ IKALFTGFRS EDVANSFWYM AAAILCYLIT GLIPNNGRLS
     KIKACLAGAT TLVSGIVATQ KLAAMFATWN SESIVNELSA RTVAISELNN PTTTSDTDSV
     ERLLELAKIL HEEIKIHTLN PIMQSYNPIL RNLMSTLDGV ITSCNKRKAI AKKRPVPVCY
     ILTGPPGCGK TTAALALAKK LSDQEPSVIN LDVDHHDTYT GNEVCIVDEF DSSDKVDYAN
     FVIGMVNSAP MVLNCDMLEN KGKLFTSKYI IMTSNSETPV KPSSRRAGAF YRRVTIIDVA
     NPLAESHKRA RPGTSVPRSC YKKNFSHLSL AKRGAECWCK EYVLDPKGLQ HQSIKAPPPT
     FLNIDSLAQT MKQDFTLKNM AFEAENGHSE HRYGFVCQQG EVETVRRLLN AVRTRLNATF
     TVCVGSEASS SIGCTAHVLT PDEPFNGKKY VVSRCNEASL SALEGNCVQS ALGVCMSTKD
     LTHLCHFIRG KIVNDSVRLD ELPANQHVVT VNSVFDLAWA LRRHLTLAGQ FQAIRAAYDV
     LTAPDKVPAM LRHWMDETSF SDEHVVTQFV TPGGIVILES CGGARIWALG HNVIRAGGVT
     ATPTGGCIRF MGLSAQTMPW SEIFRELFSL LGRIWSSIKV STLVLTALGM YASRFRPKSE
     AKGKTKSKVG PYRGRGVALT DDEYDEWREH NATRKLDLSV EDFLMLRHRA ALGADDADAV
     KFRSWWNSRS RLADDYEDVT VIGKGGVKHE KIRTNTLRAV DRGYDVSFAE ESGPGTKFHK
     NAIGSVTDVC GEHKGYCVHM GHGVYATVAH VAKGDSFFLG ERIFDLKTNG EFCCFRSTKI
     LPSAAPFFPG KPTRDPWGSP VATEWKPKPY TTTSGKIVGC FATTSTETHP GDCGLPYIDD
     NGRVTGLHTG SGGPKTPSAK LVVPYVHIDM KTKSVTAQKY DVTKPDISYK GLICKQLDEI
     RIIPKGTRLH VSPAHTEDFE ECSHQPASLG SGDPRCPKSL TAIVVDSLKP YCDKVEGPPH
     DILHRVQKML IDHLSGFVPV NISSETSMLS AFHKLNHDTS CGPYLGGRKK DHMTNGEPDK
     PLLDLLSAKW KLATQGIALP HEYTIGLKDE LRPVEKVAEG KRRMIWGCDV GVATVCAAAF
     KGVSDAITAN HQYGPVQVGI NMDSPSVEAL HQRIKSAAKV YAVDYSKWDS TQSPRVSAAS
     IDILRYFSDR SPIVDSAANT LKSPPIAIFN GVAVKVSSGL PSGMPLTSVI NSLNHCLYVG
     CAILQSLEAR GVPVTWNLFS TFDMMTYGDD GVYMFPMMFA SVSDQIFANL SAYGLKPTRV
     DKSVGSIEPI DPESVVFLKR TITRTPQGIR GLLDRSSIIR QFYYIKGENS DDWKTPPKSI
     DPTSRGQQLW NACLYASQHG VEFYNKIYKL AQKAVEYEEL HLEPPTYHSA LEHYNNQFNG
     VEARSDQIDS SGMTALHCDV FEV
//