ID A0A3B3RRD9_9TELE Unreviewed; 2687 AA.
AC A0A3B3RRD9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=CHD6 {ECO:0000313|Ensembl:ENSPKIP00000021064.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000021064.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000021064.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 1676925.ENSPKIP00000021064; -.
DR Ensembl; ENSPKIT00000001690.1; ENSPKIP00000021064.1; ENSPKIG00000005578.1.
DR GeneTree; ENSGT00940000158986; -.
DR Proteomes; UP000261540; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 1.
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; 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 PANTHER; PTHR46850; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 1.
DR PANTHER; PTHR46850:SF1; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 1.
DR Pfam; PF00385; Chromo; 1.
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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 324..367
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 422..596
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 736..905
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1736..1797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1814..1966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2227..2284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2372..2391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2479..2534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2574..2687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1888..1907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1908..1925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1947..1961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2227..2255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2256..2272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2480..2494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2576..2593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2605..2619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2625..2639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2650..2676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2687 AA; 299232 MW; EAB75CDFE88C36E9 CRC64;
SSSPLSPAVL QMSTTQLLKH TSSSVAPTAT DQKAQSRFSS SPSGLQEQSR GSSGLTNHCM
AHSKQLSFGE VGPAAGRLSP RPQSTPLNGE EDDGGGGARV KKKRKKKDRK EVEPWHKGEK
DPKPKKKKEA VEGKELLPRR SKELKKGREP KLAKEPKKAK KSQEARAKSK LKASRDCKTL
PPLPCHLCRK RICKRRSGRQ VKRRKYNEDL DFKVVDDDGE TIAVLGTGRI QALSSATLAW
QAEEPPEDEA NIIEKILAVR MVKKERCFSS CPRSSYLHCK WATLEELEKD PRIHQKIKRF
RNKQAQMKHI FTEPDEDLFN PDYIEVDRVL EVAHTTDTET GEDVTHYLVK WCSLSYEEST
WELQEDVDPG KIQEFEDNKK IPELKHVERP LPDQWKKLEQ SRDYRNGNQL RKYQLEGMNW
LLFNWYNRKN CILADEMGLG KTIQSITFLY EIFLMGLRGP FLIIAPLSTI TNWEREFRTW
TEMNAIVFHG SQISRQMILQ YEMYHRDEQG NPILGMFKFH GVITTFEMIM ADCPELKKIR
WRCVVIDEAH RLKNRNCKLL EGLKLMNLEH KVLLTGTPLQ NSVEELFSLL NFLEPVQFPS
ETSFLEEFGD LKTEEQVKKL QAILKPMMLR RLKDDVEKNL APKEETIIEV ELTNIQKKYY
RAILEKNFTF LAKGANQHNM PNLINTMMEL RKCCNHPYLI TGAEEKILES FKKTHSPDAW
DFQLQAMIQA AGKLVLIDKL LPKLIAGGHK VLIFSQMVRC LDILEDYLIQ RRYTYERIDG
RVRGNLRQAA IDRFCKADSD RFVFLLCTRA GGLGINLTAA DTCIIFDSDW NPQNDLQAQA
RCHRIGQSKA VKVYRLITRN SYEREMFDKA SLKLGLDKAV LQDINRKGSL NGVQQLSKME
VEDLLRKGAY GALMDEEDEG SKFCEEDIDQ ILQRRTQTIT IQSEGKGSTF AKASFVSSGN
RTDISLDDPN FWQKWAKIAE LEVDSKAEKE SLVIDTPRVR KQTRHYNSFE DDELMEFSEL
DSDSEERPCR TRRLSDRNRR YLRAECFRVE KNLLIFGWGR WKDILTHGRF KWHLSEHDME
LLCRALLVYC VRHYKGDDQI KSFIWDLITP TKDGHDQALV NHSGLSAPVP RGRKGKKLKN
QLCQPELKNA DWLATCNPEV VLQDESYKKH LKQHCNKVLL RVRMLYYLKV EVLGEAAALA
MEGTPARKLD VALPDIDYVE IPAGWWDSEA DKSLLIGVHK HGYERYNAMR ADLDLCFLER
VGMPDVTALS AEQGGGEALA DVTDRQGICK SEESSVLPSD TYPPVFACSP PIAVTVSESV
DQGRALWPAS SALTARLRRL ITAYQRFTRR EPMRHDFLVP EGTGPMAWQF GEEFRRRVTE
PDPLFLEWQQ RWTRREQADF YRTVSSFGVV YDPEKKAFDW TQFRCFARLE RKTDESLERY
FCSFVSMCRT ACRLPPRKDE GPVDPTLFVE PITEERAART LYRIELLRKV REQVLRHPLL
GPRLQLCQPS LYLPVWWECG KHDGDLLVGV AKHGLSRTDY YILNDPQLSF LEAHRNYVQK
ESRRYPAAGV HPNPHPQHPH PCCPYEAGLS RCHSPQSAEF HVGPAHHSHA HLHGHGIHHV
PEAVGPDSVG PLGVGPAGRE SFLDCPPLDE SLDLTSLQHD GLASDSLHGK PTKEALNGFP
FNSATAGHSM LNPYGGQADT DPIPGKLRSD VLVGAPCPCE ETGLIAPSVQ LDDLQAPWDS
EDHGGTADMF DESDTILGPP SLETEFLDSG QPGESRGDGG LADCLGMPGS DSQGTAVEPL
QPSFLLFKDL SDSGPASGSD YVAPPASLSG VSLHPRGPGD EPEEKLSDSD VTRSVPSPGD
GVESVTFELD KEELSRDSQS LLGPEPGLEQ EKDQDQDENH EEGQGLEQEP EQAQSQDQGQ
EHSQGASLEP VEGRCDTGDE STLGGHAFPS GESSSPSLSA PSPSLVVPPA DAPVVSQFKS
EFPLETLEPD ITAPAFCRNA SLPPSSPPAL LEESRFAAAP QSVCEMPDSL TEVREPTIAQ
LLQEKALYSF SDWPKDRVII NRIDSICHAI LKGKWPTSGQ QYESPSCVRL RSTYWAPLVP
TPHPGVFQES LVGVPFLADL KRGRRVFEYE AEVPGKPCPA VEKIPVGMPH RAGALLLNGW
QEAAMDLSKA GELGMGGEPA AVGHAGPHKL PPLGPLQSSR GLDMASILQA GLIHPVTGQI
VNGNLRRDDA AMRRRRGRRR NVEGPEVDFP KSRELHTPDP QSTVSSSSSS TPPERPPVAP
HPEGLVLDRE AANKGLLEWL RQNPNYTMEL SPFSILHGFV ERPKQRRHRC KDPSKLDASA
LTGEERVPVV HKGTGRRGFL PEGKFTRILT EPVCRDPGPR KRGRRPRGDM SKAGILLSDS
HSGMGPLFMN GLIGNMDLMS LQNLRNVPGI PLSGLMGFPP GFTAVPAGED TKNGLSVLPM
MLHGMAAVQP HVFGVGGLMS QSAATGTPAP SATEPPGTQG GPEDGKQEKP PVEGKAGVAC
GHREPPATPV SGSGSHLTFN PFLIPGMSHG LLYPHMFLPH GGIMALQGVA CADGAGSPKR
KKKKVREEVA EDPAGKGSPQ TDGTALRGPA HSQTEGSSGV IVEPPGEVER READRGPRTP
PGEGVHQGTE ETDTVAEDME KAETRGQGEE PDEEGPGGGG KSPLPSF
//