CHD6_RAT
ID CHD6_RAT Reviewed; 2698 AA.
AC D3ZA12;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 6;
DE Short=CHD-6;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase CHD6;
GN Name=Chd6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH PPARA.
RX PubMed=12189208; DOI=10.1073/pnas.182426699;
RA Surapureddi S., Yu S., Bu H., Hashimoto T., Yeldandi A.V., Kashireddy P.,
RA Cherkaoui-Malki M., Qi C., Zhu Y.-J., Rao M.S., Reddy J.K.;
RT "Identification of a transcriptionally active peroxisome proliferator-
RT activated receptor alpha-interacting cofactor complex in rat liver and
RT characterization of PRIC285 as a coactivator.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11836-11841(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1852, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: DNA-dependent ATPase that plays a role in chromatin
CC remodeling. Regulates transcription by disrupting nucleosomes in a
CC largely non-sliding manner which strongly increases the accessibility
CC of chromatin. Activates transcription of specific genes in response to
CC oxidative stress through interaction with NFE2L2.
CC {ECO:0000250|UniProtKB:Q8TD26}.
CC -!- CATALYTIC ACTIVITY:
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:Q8TD26};
CC -!- SUBUNIT: Interacts with NFE2L2; involved in activation of the
CC transcription (By similarity). May interact with PPARA
CC (PubMed:12189208). {ECO:0000250|UniProtKB:Q8TD26,
CC ECO:0000269|PubMed:12189208}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q8TD26}. Note=Enriched at sites of mRNA
CC synthesis. {ECO:0000250|UniProtKB:Q8TD26}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000250|UniProtKB:A3KFM7}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AABR06027401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06027402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06027403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06027404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06027405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06027406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06027407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06027408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06027409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474005; EDL96607.1; -; Genomic_DNA.
DR RefSeq; NP_001101267.1; NM_001107797.1.
DR AlphaFoldDB; D3ZA12; -.
DR SMR; D3ZA12; -.
DR BioGRID; 259994; 1.
DR STRING; 10116.ENSRNOP00000022861; -.
DR iPTMnet; D3ZA12; -.
DR PhosphoSitePlus; D3ZA12; -.
DR jPOST; D3ZA12; -.
DR PaxDb; D3ZA12; -.
DR PeptideAtlas; D3ZA12; -.
DR PRIDE; D3ZA12; -.
DR GeneID; 311607; -.
DR KEGG; rno:311607; -.
DR CTD; 84181; -.
DR RGD; 1310465; Chd6.
DR VEuPathDB; HostDB:ENSRNOG00000016744; -.
DR eggNOG; KOG0384; Eukaryota.
DR HOGENOM; CLU_000315_5_1_1; -.
DR InParanoid; D3ZA12; -.
DR OrthoDB; 7181at2759; -.
DR TreeFam; TF313572; -.
DR PRO; PR:D3ZA12; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000016744; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; D3ZA12; baseline and differential.
DR Genevisible; D3ZA12; RN.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISS:UniProtKB.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006576; BRK_domain.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..2698
FT /note="Chromodomain-helicase-DNA-binding protein 6"
FT /id="PRO_0000429354"
FT DOMAIN 291..342
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 374..438
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 472..646
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 786..955
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1435..1489
FT /note="Myb-like"
FT REGION 1..746
FT /note="Required for DNA-dependent ATPase activity"
FT /evidence="ECO:0000250"
FT REGION 1..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1707..1731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1935..2046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2111..2137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2308..2337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2359..2387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2538..2587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2626..2698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 597..600
FT /note="DEAH box"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1935..1952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1976..1990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2005..2036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2550..2569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2633..2649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2662..2678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2680..2698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 485..492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 1852
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 2698 AA; 303449 MW; F765D9859107CB37 CRC64;
MKMKIQKKEK QLSKLRALNH SPMSDASVNF DYKSPSPFDC SPDQGENIEE AANHCLPQKD
FYTTEEEADT LFSRKLMSHN GMEDNGGRGT GVKKKRKKKE PGEQEGTKAS KDREPKPKRK
REPKEPKEPR RAKEPKRAKE PKEAKQKDGV KKPRKPREAS GTKEGKEKRS CTDCGPRTKP
KKASKDQGPT PVERKKKGKR KNETTVESLE LDQSLPNPSL QSPEEPSESA DSQKRRSGRQ
VKRRKYNEDL DFKVVDDDGE TIAVLGAGRT SALSASTLAW QAEEPPEDDA NIIEKILASK
TVQEVHPGEP PFDLELFYVK YRNFSYLHCK WATMEELEKD PRIAQKIKRF RNKQAQMKHI
FTEPDEDLFN PDYIEIDRIL EVAHTKDAET GEEVTHYLVK WCSLPYEEST WELEEDVDPA
KVKEFESLQI LPEVKPVERP ASDAWQKLET SREYKNSNRL REYQLEGMNW LLFNWYNRKN
CILADEMGLG KTIQSIAFLS EIFVRGIHGP FLIIAPLSTI TNWEREFRTW TEMNAIVYHG
SQISRQMIQQ YEMVYRDAQG NPLSGVFKFH VVITTFEMIL ADCPELKKIH WSCVVIDEAH
RLKNRNCKLL EGLKLMALEH KVLLTGTPLQ NSVEELFSLL NFLEPSQFPS ETAFLEEFGD
LKTEEQVKKL QSILKPMMLR RLKDDVEKNL APKQETIIEV ELTNIQKKYY RAILEKNFSF
LTKGANQHNM PNLINTMMEL RKCCNHPYLI NGAEEKILED FRKAHSSEAS DFQLQAMIQA
AGKLVLIDKL LPKLIAGGHK VLIFSQMVRC LDILEDYLIQ RRYTYERIDG RVRGNLRQAA
IDRFCKPDSD RFVFLLCTRA GGLGINLTAA DTCIIFDSDW NPQNDLQAQA RCHRIGQSKA
VKVYRLITRN SYEREMFDKA SLKLGLDKAI LQDINRKGST NGVQQLSKME VEDLLRKGAY
GALMDEEDEG SKFCEEDIDQ ILQRRTHTIT IQSEGKGSTF AKASFVASGN RTDISLDDPN
FWQKWAKIAE LDTEANNEKE SLVIDRPRVR KQTKHYNSFE EDELMEFSEL DSDSDERPTR
SRRLSDKARR YLRAECFRVE KNLLTFGWGR WKDILTHGRF KWPLNEKDME VICRALLVYC
VKHYKGDEKI KSFIWELITP SKDGQVQTLQ NHSGLSAPVP RGRKGKKTKN QLLLPELKTA
DWLATCNPEV VLHDDGYKKH LKQHCNKVLL RVRMLYYLKA EILGEAADKA FEGTPARELD
VLLPDIDYVE IPVDWWDAEA DKSLLIGVFK HGYERYNAMR ADPALCFLEK VGMPDEKSLS
AEQGVTDGTS DIPERGNIDK EDSAEDKVDG LQKQTASPSD GSDGIFGEKK DDSQAVSSAL
TARLRRLVTI YQRCNRKELC RPEILGPGNQ GYWVQEEVFR RTSDMDLINK EAQKRWTRRE
QADFYRTVSS FGVVYDQEKE AFDWTQFRAI SRLDKKSDEN LEHYFHSFVA MCRNVCRLPT
WKDDGPPDAS IYVEPITEER AAKTLYRIEL LRKVREQVLT CPQLHERLQL CRPSLYLPVW
WECGKHDRDL LIGTAKHGLN RTDYYIMNDP QLSFLDAYRN YAQHKRTDTQ APGSLCCLYQ
GNSKLYESLT YTPMSRTSES LESEPENLVK MDSRDDHLCL PEAGLPDITC ENFVSKVQEV
ISLDHDESLL PESLENMMYG KTGLSQEPRS FQEAPSTNMQ SRKKTVTVSA SRDESCQLPG
IEAEITSASS LMSSLEAGVA KMNIKNGKHL LVSISEEGEP CCSETGRSPE SRGRLEARCL
ASPTLDTGHE SGFVDLCSLS VYDSKRNFSS DQQLIDLLEN KSLENKLILN QSDEEEEENE
KETLAIVAST TEKPAVLDFT QPTASIPRGK NLSFHQDEAK KGRLEVGSKT PGPQRAFPPS
ANQCHCKHIE RWAHGLGSEE SEGEKPKAYE PDPYRSKANN TTVEGEPAII PTEPFKLKHE
LLKEPWKESS EGGKSFSMYV PEGSEPKSEE MDFENKDDYE KDGACHSQDY PGKYSEEESK
SSASGIAGDL GEEAQEVRAP TIAQLLQEKT LYSFSEWPKD RVIINRLDNI CHVVLKGKWP
CSHQYEPSGA LPTPVLSSSA GSRSSLSEPE ATEHSFSNGA ALAAQIQKES FLAPVFTKDE
QKHRRPYEFE VERDAKARSL EEYSASHGRP PIVLNGWHGE SAIDLSCSSE GSPGATSPFP
VSASTPKIGA ISSLQGALGM DLSGILQAGL IHPVTGQIVN GSLRRDDAAM RRRRGRRKHI
EGGMDLIFLK EQTLQAGILE VHEDAGQTTL NTTHPEGPGA ASSASEPTAA ASSQAEKAVP
SKSLLDWLRQ QADYSLDVPG FGASFSDKPK QRRPRCKEPG KLDIGSLGGE ERVSAVPKEP
GLRGFLPESK FNHTLAEPVL RDAGPRRRGR RPRNELLKAP AIVADSPSGM GPLFMNGLIA
GMDLVGLQNV RNIPGIPLTG LVGFPAGFAT MPTGEDVKNT LSMLPMMLPG MATVPQMFGV
GGLLNTPMAT TCTTTASASL ASTKSGASAT EKTTEDELSG RDVKADSLVE DKPGPSPFSD
QSEPTITTSS PVAFNPFLIP GVSPGLIYPS MFLSPGMGMA LPAMQQGRHS EMAGLETQKR
KKKKTKGDNP TPEPASVCER EPGSDQNCTE SSVTVSPERE HVAQAREEGL KDSNDDTN
