ID H2LS61_ORYLA Unreviewed; 1603 AA.
AC H2LS61;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=CHD3 {ECO:0000313|Ensembl:ENSORLP00000008921.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000008921.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000008921.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000008921.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000008921.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000008921.2};
RG Ensembl;
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 STRING; 8090.ENSORLP00000008921; -.
DR Ensembl; ENSORLT00000008922.2; ENSORLP00000008921.2; ENSORLG00000007107.2.
DR eggNOG; KOG0383; Eukaryota.
DR GeneTree; ENSGT00940000158001; -.
DR HOGENOM; CLU_000315_22_2_1; -.
DR InParanoid; H2LS61; -.
DR TreeFam; TF106448; -.
DR Proteomes; UP000001038; Chromosome 18.
DR Bgee; ENSORLG00000007107; Expressed in brain and 12 other cell types or tissues.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016581; C:NuRD complex; 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: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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR CDD; cd00084; HMG-box_SF; 1.
DR CDD; cd15531; PHD1_CHD_II; 1.
DR CDD; cd15532; PHD2_CHD_II; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
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; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR036910; HMG_box_dom_sf.
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 InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623:SF9; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF47095; HMG-box; 1.
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.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 338..385
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 427..474
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 604..637
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 681..863
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 995..1160
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 35..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1463..1578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1584..1603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..77
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1494..1513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1603 AA; 181901 MW; 73BF5EFC5D1F9FA7 CRC64;
MRSPAVFHYA QMGLSFLSMP LSFSRSDSCL SSFVLSLPPD DDRSDREVPI RKKGRPKKKK
DAKKKDKDGK PPKTKKRKKI VRCVCGFLFS GSVLALNSDS AASDYGSGEK KKKKKHKEKK
ERKTKKKKKD DGDRDSEQKT SAQLAKEWGL EDVDHTFTEE DYRELTNYKA FSQFMRPMIA
KKNPKIPMSK MMTILGVKWR EFSSNNPFKG NAAAVAAAAA AAAIAVAEQV SAATASPEPP
PQPPPIRKAK TKEGKGPGYK KRSKSPRVPD KKKALAAAKA KKMAPIRIKL SPIGAKRKKS
CSRIVTKMSK FSHPGSSSAP LCVVMGEEEG DGYETDHQDY CEVCQQGGEI ILCDTCPRAY
HLVCLEPELD KAPEGKWSCP HCEKEGIQWE AKDEDFEDFE EDSEDRVISE VSSGVPAGGD
DEDDDHMEFC RVCKDGGELL CCDTCTSSYH IHCLNPPLPE IPNGEWLCPR CLPIKGRVQK
ILHWRWGEPP SPIPVPPPPD APPDVPPPPP MKGRPEREFF VKLVGQSYWH CTWITELQLE
IFHSVMYRNY QRKTDMDEPP SLDYGSGGEE ENSVGKSEKR RAKDPQFAIL EDKYYKYGIK
PEWMMIHRII NHSLDKKGVY HYLVKWRDLT YDQCTWERDD MTIPDFAIYK PTIKYEEQPD
FVTATGGTLH MYQLEGLNWL RFSWAQGTDT ILADEMGLGK TIQTIVFLYS LFKEGHTKGP
FLVSAPLSTI INWEREFEMW APDFYVVTYT GDKDSRAIIR ENEFSFDDTA VKGGKKAFKL
RAPIKFHVLL TSYELVTIDQ TALKSIEWAC LVVDEAHRLK NNQSKFFRRL NDYKIDYKLL
LTGTPLQNNL EELFHLLNFL TPNRFNNLEG FLEEFADISK EDQIKKLHDL LGPHMLRRLK
ADVFKNMPAK TELIVRVELS PMQKKYYKLI LTKNFEALNS KGGGNQVSLL NIMMDLKKCC
NHPYLFPVAS MEAQKTPSGA YEGSALTKAS GKLMLLQKML RKLKEQGHRV LVFSQMTKML
DLLEDFLDHE GYKYERIDGG ITGALRQEAI DRFNAPGACQ FCFLLSTRAG GLGINLATAD
TVIIFDSDWN PHNDIQAFSR AHRIGQANKV MIYRFVTRAS VEERITQVAK RKMMLTHLVV
RPGLGSKAGS MTKQELDDIL KFGTEELFKD EGEGDKVEDE GNVIHYDSTA IERLLDRSQD
ATDDTDVQNM NEYLSSFKVA QYMVREEDKI EEIEREIIKQ EENVDPDYWE KLLRHHYEQQ
QEDLASKLGK GKRNRKPVNY NDAAQEDQEW HADISDNQSE YSVGSEEEDE DFDDRPEGRR
QSRRQLRNDK DKPLPPLLAR VGGNLEVLGF NTRQRKAFLN AVMRWGMPSQ DAFSSQWLVR
DLKGKSEKEF KAYVSLFMRH LCEPVADGAE TFADGVPREG LCRQPVLTRI GVMSLVKKKV
HEFEHINGRW SLPELKPEIS IDKASSRASS PTVKTATPTT DASYNSTPCP SKPGDLKEET
KLESKHETKE KPGKTPSNGL IKAEFGGEFM TLTSVGDEVR EEKESQDVKG EREAGKELKA
PKEEAPRGNG KPASERPRFM FNIADGGFTG ELEEPGGELE SDM
//
