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Database: UniProt
Entry: A0A2Y9PXM2_DELLE
LinkDB: A0A2Y9PXM2_DELLE
Original site: A0A2Y9PXM2_DELLE 
ID   A0A2Y9PXM2_DELLE        Unreviewed;      2720 AA.
AC   A0A2Y9PXM2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   Name=CHD6 {ECO:0000313|RefSeq:XP_022448097.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022448097.1};
RN   [1] {ECO:0000313|RefSeq:XP_022448097.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022448097.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001665};
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007025}.
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DR   RefSeq; XP_022448097.1; XM_022592389.2.
DR   STRING; 9749.A0A2Y9PXM2; -.
DR   KEGG; dle:111184165; -.
DR   InParanoid; A0A2Y9PXM2; -.
DR   OrthoDB; 22878at2759; -.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18668; CD1_tandem_CHD5-9_like; 1.
DR   CDD; cd18663; CD2_tandem_CHD5-9_like; 1.
DR   CDD; cd18058; DEXHc_CHD6; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 2.40.50.40; -; 2.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR006576; BRK_domain.
DR   InterPro; IPR037259; BRK_sf.
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; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR46850; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 1.
DR   PANTHER; PTHR46850:SF1; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 1.
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; SSF160481; BRK domain-like; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          375..418
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          473..647
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          787..956
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1167..1186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1318..1390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1865..1913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2031..2065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2121..2149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2320..2356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2382..2452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2555..2609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2655..2720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1334..1354
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1364..1380
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2031..2054
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2327..2344
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2555..2574
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2575..2589
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2655..2670
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2720 AA;  305328 MW;  F49C22A033DD396A CRC64;
     MIMKIQKKEK QLSNLKVLNH SPMSDASVNF DYKSPSPFDH STDQEDKTED VARPCLPQKD
     LHTAEEDAET LFPRKTTSHN GTEDSGGGGT GVKKKRKKKD PGEQEGAAKG NKDREPKPKR
     KREPREPKEP RKAKEPRKAK EPKEPKQKDG AKKVRKPREA SGPKEAKEKR SGPDSAARTK
     SKKASKEQGP TPVEKKKKGK RKSETTVESL ELDQGLPNPS LRSPEESTES ADSQKRRSGR
     QVKRRKYNED LDFKVVDDDG ETIAVLGAGR TSALSASTLA WQAEEPPEDD ANIIEKILAS
     KTVQEVHPGE PPFDLELFYV KYRNFSYLHC KWATMEELEK DPRIAQKIKR FRNKQAQMKH
     IFTEPDEDLF NPDYVEVDRI LEVAHTKDAE TGEEVTHYLV KWCSLPYEES TWELEEDVDP
     AKVKEFESLQ VLPEVKHVER PASDSWQKLE KSREYKNSNQ LREYQLEGMN WLLFNWYNRK
     NCILADEMGL GKTIQSITFL SEIFLRGIHG PFLIIAPLST ITNWEREFRT WTEMNAIVYH
     GSQISRQMIQ QYEMVYRDAQ GNPLSGVFKF HVVITTFEMI LADCPELKKI HWSCVIIDEA
     HRLKNRNCKL LEGLKLMALE HKVLLTGTPL QNSVEELFSL LNFLEPSQFP SETAFLEEFG
     DLKTEEQVKK LQSILKPMML RRLKDDVEKN LAPKQETIIE VELTNIQKKY YRAILEKNFS
     FLTKGANQHN MPNLINTMME LRKCCNHPYL INGAEEKILE DFRKTHSPDA PDFQLQAMIQ
     AAGKLVLIDK LLPKLIAGGH KVLIFSQMVR CLDILEDYLI QRRYTYERID GRVRGNLRQA
     AIDRFCKPDS DRFVFLLCTR AGGLGINLTA ADTCIIFDSD WNPQNDLQAQ ARCHRIGQSK
     AVKVYRLITR NSYEREMFDK ASLKLGLDKA VLQDINRKGS TNGVQQLSKM EVEDLLRKGA
     YGALMDEEDE GSKFCEEDID QILQRRTHTI TIQSEGKGST FAKASFVASG NRTDISLDDP
     NFWQKWAKIA ELDTEAKSEK ESLVIDRPRV RKQTKHYNSF EEDELMEFSE LDSDSDERPT
     RSRRLNDKTR RYLRAECFRV EKNLLIFGWG RWKDILTHGR FKWHLSEKDM EMVCRALLAY
     CVRHYKGDEK IKSFIWELIT PTKDGQAQTL QNHSGLSAPV PRGRKGKKTK NQLLLPELKN
     ADWLATCNPE VVLHDDGYKK HLKQHCNKVL LRVRMLYYLK AEILGEAADK AFEGTPAREL
     DVPLPDIDCV EIPVDWWDAE ADKSLLIGVF KHGYERYNAM RADPALCFLE KVGMPDEKSL
     SAEQGVTDGT SDIPERGNTD KEDNTEDKVD GLQKQMESSS DGGDGIFGEK KDDSRAAQDG
     SDPDKSPWPV SSALTARLRR LVTIYQRCNR KELCRPEILG PGNQGYWVQE EMFRRSSEMD
     LINKEAQKRW TRREQADFYR TVSSFGVVYD QEKKTFDWTQ FRIISRLDKK SDESLEHYFH
     SFVAMCRHVC RLPAWKDGGP PDPSICVEPI TEERAARTLY RIELLRKVRE QVLQCPQLHE
     RLQLCRPSLS LPVWWECGKH DRDLLIGTAK HGLNRTDYYI MTDPQLSFLD AYRNYAQHKR
     TDPQAPGSLC CLYQTNSKLY ESLAYTQMSR TSESLENEPE NLVKIEGRDD HLGPPRGSLS
     DMTCENFISK VQDVISITHD ESLLPESLES MMYGKKALSQ EPVSFQESPG TNTESRQDAV
     ALATSRDGNF QPGGHEAEIA SGPSFMDTLE AGVAQMNIKN GKHLLVSLSQ EGELCCSEAG
     QRPESLGQLE TKYIASPSLD QGNESGFVDM CNLSVYDSKR NLSSDQQLID LLECKSLESK
     LILGRNHSDE EEEEEENEEE NLDLAAGTRE RPEVSPLTEP TARMAGEKSR SGFLVDEAKK
     GSLAARSQHP GPQGAFLPAA CQCHCKHMER WTQGLENDQF EVEKPQGYNP DPYKSKANNV
     TVGGELTAVP PELFQVKHEL LKEPWKESAE GKQGFPTYLE GSELKAEDVD FESKDDYDRD
     GNCRSQDYPG KYSEEESKNS TSGIVGDLRD NLQEARAPTI AQLLQEKTLY SFSEWPKDRV
     IINRLDNICH VVLKGKWPSN QQYEPSAALP TPVLTSGAGP RSSLSEPEAS EHVFSSGAAL
     VAQMQKESFL ASVFTKEEQK HRRPYEFEVE RDAKTRRLEQ FPATHGHPPI VLNGWHGESA
     IDLSCPSEGS PGATSPFPVS ASTPKIGAIG SLQGALGMDL SGILQAGLIH PVTGQIVNGS
     LRRDDAATRR RRGRRKHVDG GVDLIFLKEP TLQAGILEVH EDPGPAPLST SHPPEGPVPA
     TSTPEPAPVA GSQPEKAIPS KSLLDWLRQQ ADCPLEVPGF GANFSDKPKQ RRPRCKDTGK
     LDVNSLSGEE RVPAVPKEPG LRGFLPENKF NHTLPEPVLR DSGPRRRGRR PRSELLKAPA
     LVADSPSGMG PLFMNGLIAG MDLVGLQNMR NMPSIPLTGL VGFPASFAAM PTGEEVKSTL
     SMLPMVLPGM AAVPQMFGVG GLLNAPMTTT CASAVPAPLS STTKSGTSVA EKTAEDQPSG
     RDVKTDTSAE DKPGPSPFSD QAEPPITTSS PVAFNPFLIP GVSPGLIYPS MFVSPGMGMA
     LPAMQQARHS EIVGLESQKR MRKKTKGDNP DPSPEPAPGL EREPGGAQSC PESRAPAPPE
     RGHAAQAGEG GPQDSNSVTN
//
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