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Database: UniProt
Entry: A0A3B3RRD9_9TELE
LinkDB: A0A3B3RRD9_9TELE
Original site: A0A3B3RRD9_9TELE 
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
//
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