ID   SUVH9_ARATH             Reviewed;         650 AA.
AC   Q9T0G7;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=Histone-lysine N-methyltransferase family member SUVH9;
DE   AltName: Full=Histone H3-K9 methyltransferase 9;
DE            Short=H3-K9-HMTase 9;
DE   AltName: Full=Protein SET DOMAIN GROUP 22;
DE   AltName: Full=Suppressor of variegation 3-9 homolog protein 9;
DE            Short=Su(var)3-9 homolog protein 9;
GN   Name=SUVH9; Synonyms=SDG22, SET22; OrderedLocusNames=At4g13460;
GN   ORFNames=T6G15.10;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND NOMENCLATURE.
RX   PubMed=11691919; DOI=10.1093/nar/29.21.4319;
RA   Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K.,
RA   Assalkhou R., Schulz I., Reuter G., Aalen R.B.;
RT   "The Arabidopsis thaliana genome contains at least 29 active genes encoding
RT   SET domain proteins that can be assigned to four evolutionarily conserved
RT   classes.";
RL   Nucleic Acids Res. 29:4319-4333(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   GENE FAMILY.
RX   PubMed=16384625; DOI=10.1016/j.jplph.2005.10.015;
RA   Fischer A., Hofmann I., Naumann K., Reuter G.;
RT   "Heterochromatin proteins and the control of heterochromatic gene silencing
RT   in Arabidopsis.";
RL   J. Plant Physiol. 163:358-368(2006).
RN   [5]
RP   FUNCTION, DNA-BINDING, LACK OF METHYLTRANSFERASE ACTIVITY, AND LACK OF
RP   S-ADENOSYL-L-METHIONINE BINDING.
RX   PubMed=19043555; DOI=10.1371/journal.pgen.1000280;
RA   Johnson L.M., Law J.A., Khattar A., Henderson I.R., Jacobsen S.E.;
RT   "SRA-domain proteins required for DRM2-mediated de novo DNA methylation.";
RL   PLoS Genet. 4:E1000280-E1000280(2008).
RN   [6]
RP   SUBUNIT, AND INTERACTION WITH MORC6; MORC2 AND MORC1/CRT1.
RX   PubMed=24465213; DOI=10.1371/journal.pgen.1003948;
RA   Liu Z.-W., Shao C.-R., Zhang C.-J., Zhou J.-X., Zhang S.-W., Li L.,
RA   Chen S., Huang H.-W., Cai T., He X.-J.;
RT   "The SET domain proteins SUVH2 and SUVH9 are required for Pol V occupancy
RT   at RNA-directed DNA methylation loci.";
RL   PLoS Genet. 10:E1003948-E1003948(2014).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH SWI3B; SWI3C AND
RP   SWI3D.
RX   PubMed=27171427; DOI=10.1371/journal.pgen.1006026;
RA   Liu Z.-W., Zhou J.-X., Huang H.-W., Li Y.-Q., Shao C.-R., Li L., Cai T.,
RA   Chen S., He X.-J.;
RT   "Two components of the RNA-Directed DNA methylation pathway associate with
RT   MORC6 and silence loci targeted by MORC6 in Arabidopsis.";
RL   PLoS Genet. 12:E1006026-E1006026(2016).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 134-650 IN COMPLEX WITH ZINC
RP   IONS, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=24463519; DOI=10.1038/nature12931;
RA   Johnson L.M., Du J., Hale C.J., Bischof S., Feng S., Chodavarapu R.K.,
RA   Zhong X., Marson G., Pellegrini M., Segal D.J., Patel D.J., Jacobsen S.E.;
RT   "SRA- and SET-domain-containing proteins link RNA polymerase V occupancy to
RT   DNA methylation.";
RL   Nature 507:124-128(2014).
CC   -!- FUNCTION: Histone methyltransferase family member that plays a role in
CC       gene silencing (PubMed:19043555, PubMed:24463519, PubMed:27171427).
CC       Together with MORC6 and SUVH2, regulates the silencing of some
CC       transposable elements (TEs) (PubMed:27171427). According to
CC       PubMed:19043555, the protein does not bind S-adenosyl-L-methionine and
CC       lacks methyltransferase activity. Instead, it may function downstream
CC       of DRM2 in RNA-directed DNA methylation, binding to methylated DNA and
CC       recruiting DNA-directed RNA polymerase V to chromatin (PubMed:24463519,
CC       PubMed:27171427). {ECO:0000269|PubMed:19043555,
CC       ECO:0000269|PubMed:24463519, ECO:0000269|PubMed:27171427}.
CC   -!- SUBUNIT: Component of an RNA-directed DNA methylation (RdDM) complex
CC       that contains at least MORC6, MORC1/CRT1, MORC2, SWI3D and SUVH9.
CC       Interacts directly with MORC6, MORC2 and MORC1/CRT1. Interacts with
CC       SWI3B, SWI3C and SWI3D (PubMed:27171427). {ECO:0000269|PubMed:24465213,
CC       ECO:0000269|PubMed:27171427}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:24463519}.
CC       Chromosome, centromere {ECO:0000250}. Note=Associates with centromeric
CC       constitutive heterochromatin. {ECO:0000305}.
CC   -!- DOMAIN: Although both SET and pre-SET domains are present, the absence
CC       of the post-SET domain may explain the lack of methyltransferase
CC       activity. Besides, the Cys residues in the SET domain that normally
CC       bind a zinc ion are not conserved.
CC   -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are
CC       arranged in a triangular cluster; some of these Cys residues contribute
CC       to the binding of two zinc ions within the cluster.
CC   -!- DISRUPTION PHENOTYPE: Impaired gene silencing due to decondensation of
CC       chromocenters leading to the derepression of DNA-methylated genes and
CC       transposable elements (TEs). {ECO:0000269|PubMed:27171427}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. Histone-lysine methyltransferase family. Suvar3-9
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00908}.
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DR   EMBL; AF344452; AAK28974.1; -; mRNA.
DR   EMBL; AL049656; CAB41104.1; -; Genomic_DNA.
DR   EMBL; AL161536; CAB78388.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83282.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83283.1; -; Genomic_DNA.
DR   PIR; T06648; T06648.
DR   RefSeq; NP_001031625.1; NM_001036548.2.
DR   RefSeq; NP_193082.1; NM_117420.3.
DR   PDB; 4NJ5; X-ray; 2.40 A; A=134-650.
DR   PDBsum; 4NJ5; -.
DR   AlphaFoldDB; Q9T0G7; -.
DR   SMR; Q9T0G7; -.
DR   BioGRID; 12275; 1.
DR   STRING; 3702.Q9T0G7; -.
DR   PaxDb; 3702-AT4G13460-2; -.
DR   ProteomicsDB; 226525; -.
DR   EnsemblPlants; AT4G13460.1; AT4G13460.1; AT4G13460.
DR   EnsemblPlants; AT4G13460.2; AT4G13460.2; AT4G13460.
DR   GeneID; 826978; -.
DR   Gramene; AT4G13460.1; AT4G13460.1; AT4G13460.
DR   Gramene; AT4G13460.2; AT4G13460.2; AT4G13460.
DR   KEGG; ath:AT4G13460; -.
DR   Araport; AT4G13460; -.
DR   TAIR; AT4G13460; SUVH9.
DR   eggNOG; KOG1082; Eukaryota.
DR   HOGENOM; CLU_004556_4_0_1; -.
DR   InParanoid; Q9T0G7; -.
DR   OMA; IGCYCAQ; -.
DR   OrthoDB; 5481936at2759; -.
DR   PhylomeDB; Q9T0G7; -.
DR   PRO; PR:Q9T0G7; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9T0G7; baseline and differential.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009294; P:DNA-mediated transformation; IMP:TAIR.
DR   GO; GO:0080188; P:gene silencing by RNA-directed DNA methylation; IMP:UniProtKB.
DR   CDD; cd10545; SET_AtSUVH-like; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 2.30.280.10; SRA-YDG; 1.
DR   InterPro; IPR025794; H3-K9-MeTrfase_plant.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR036987; SRA-YDG_sf.
DR   InterPro; IPR003105; SRA_YDG.
DR   PANTHER; PTHR45660:SF3; HISTONE-LYSINE N-METHYLTRANSFERASE FAMILY MEMBER SUVH9; 1.
DR   PANTHER; PTHR45660; HISTONE-LYSINE N-METHYLTRANSFERASE SETMAR; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF02182; SAD_SRA; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00466; SRA; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS51575; SAM_MT43_SUVAR39_2; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS51015; YDG; 1.
DR   Genevisible; Q9T0G7; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Centromere; Chromatin regulator; Chromosome; DNA-binding;
KW   Metal-binding; Nucleus; Reference proteome; Zinc.
FT   CHAIN           1..650
FT                   /note="Histone-lysine N-methyltransferase family member
FT                   SUVH9"
FT                   /id="PRO_0000186080"
FT   DOMAIN          205..352
FT                   /note="YDG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00358"
FT   DOMAIN          432..490
FT                   /note="Pre-SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT   DOMAIN          493..637
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         434
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         434
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         436
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         440
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         440
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT   BINDING         444
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         446
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         472
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         472
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT   BINDING         476
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         478
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT   BINDING         482
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT   HELIX           140..167
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   HELIX           178..192
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          215..217
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   HELIX           219..224
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          234..238
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          242..246
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          249..256
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          268..272
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   HELIX           291..301
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          306..312
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          322..338
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          344..352
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   HELIX           360..372
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   HELIX           374..376
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          382..385
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          391..394
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          396..399
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   HELIX           407..410
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          411..413
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   HELIX           445..449
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   TURN            450..452
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   HELIX           487..489
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          495..499
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          501..511
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          518..521
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          525..527
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   HELIX           529..537
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   HELIX           545..547
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   HELIX           551..553
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   TURN            554..557
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   TURN            560..562
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          580..582
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          584..587
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   HELIX           589..592
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          600..609
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          617..624
FT                   /evidence="ECO:0007829|PDB:4NJ5"
FT   STRAND          633..635
FT                   /evidence="ECO:0007829|PDB:4NJ5"
SQ   SEQUENCE   650 AA;  72174 MW;  B2F291C5FA18A6E9 CRC64;
     MGSSHIPLDP SLNPSPSLIP KLEPVTESTQ NLAFQLPNTN PQALISSAVS DFNEATDFSS
     DYNTVAESAR SAFAQRLQRH DDVAVLDSLT GAIVPVEENP EPEPNPYSTS DSSPSVATQR
     PRPQPRSSEL VRITDVGPES ERQFREHVRK TRMIYDSLRM FLMMEEAKRN GVGGRRARAD
     GKAGKAGSMM RDCMLWMNRD KRIVGSIPGV QVGDIFFFRF ELCVMGLHGH PQSGIDFLTG
     SLSSNGEPIA TSVIVSGGYE DDDDQGDVIM YTGQGGQDRL GRQAEHQRLE GGNLAMERSM
     YYGIEVRVIR GLKYENEVSS RVYVYDGLFR IVDSWFDVGK SGFGVFKYRL ERIEGQAEMG
     SSVLKFARTL KTNPLSVRPR GYINFDISNG KENVPVYLFN DIDSDQEPLY YEYLAQTSFP
     PGLFVQQSGN ASGCDCVNGC GSGCLCEAKN SGEIAYDYNG TLIRQKPLIH ECGSACQCPP
     SCRNRVTQKG LRNRLEVFRS LETGWGVRSL DVLHAGAFIC EYAGVALTRE QANILTMNGD
     TLVYPARFSS ARWEDWGDLS QVLADFERPS YPDIPPVDFA MDVSKMRNVA CYISHSTDPN
     VIVQFVLHDH NSLMFPRVML FAAENIPPMT ELSLDYGVVD DWNAKLAICN
//