ID A0A1S3WBR6_ERIEU Unreviewed; 1805 AA.
AC A0A1S3WBR6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=CHD3 {ECO:0000313|RefSeq:XP_016043762.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016043762.1};
RN [1] {ECO:0000313|RefSeq:XP_016043762.1}
RP IDENTIFICATION.
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_016043762.1; XM_016188276.1.
DR CTD; 1107; -.
DR OrthoDB; 2910821at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR CDD; cd18055; DEXHc_CHD3; 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; 1.10.10.60; Homeodomain-like; 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; IPR012957; CHD_C2.
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; 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; PF08074; CHDCT2; 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; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
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; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
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 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
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 217..264
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 294..341
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 374..431
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 469..505
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 586..770
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 902..1067
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 59..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..83
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..122
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..290
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1404..1433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1805 AA; 204219 MW; A7E4674BCEBED8F8 CRC64;
MRPLIAKKNP KIPMSKMMTI LGAKWREFSA NNPFKGSAAA VAAAAAAAAA AVAEQVSAAV
SSATPIAPSG PPTLPPPPAA DIHLPPIRRA KTKEGKGPGH KRRSKSPRVP DGRKKLRGKK
MAPLKIKLGL LGGKRKKAGS PRGYGQYILQ SDEGPEPEAE ESDLDCGSIH SASGRPDGPV
RTKKLKRGRP GRKKKKILGC PAVAGEEEVD GYETDHQDYC EVCQQGGEII LCDTCPRAYH
LVCLDPELDR APEGKWSCPH CEKEGVQWEA KEEEEEYEEE GEEEGEKEEE DDHMEYCRVC
KDGGELLCCD ACVSSYHIHC LNPPLPDIPN GEWLCPRCTC PVLKGRVQKI LHWRWGEPPV
TVPAPQQADG NPDAPPPRPL QGRSEREFFV KWVGLSYWHC SWAKELQLEI FHLVMYRNYQ
RKNDMDEPPP LDYGSGEDDG KSDKRKVKDP HYAEMEEKYY RFGIKPEWMT VHRIINHSVD
KKGNYHYLVK WRDLPYDQST WEEDEMNIPE YEDHKQSYWR HRELIMGEDP SQPRKYKKKK
KELQGDGPPS SPTNDPTVKY ETQPRFITAT GGTLHMYQLE GLNWLRFSWA QGTDTILADE
MGLGKTIQTI VFLYSLYKEG HTKGPFLVSA PLSTIINWER EFQMWAPKFY VVTYTGDKDS
RAIIRENEFS FEDNAIKGGK KAFKMKREAQ VKFHVLLTSY ELITIDQAAL GSIRWACLVV
DEAHRLKNNQ SKFFRVLNGY KIDHKLLLTG TPLQNNLEEL FHLLNFLTPE RFNNLEGFLE
EFADISKEDQ IKKLHDLLGP HMLRRLKADV FKNMPAKTEL IVRVELSPMQ KKYYKYILTR
NFEALNSRGG GNQVSLLNIM MDLKKCCNHP YLFPVAAMES PKLPSGAYEG GALIKASGKL
MLLQKMLCKL KEQGHRVLIF SQMTKMLDLL EDFLDYEGYK YERIDGGITG ALRQEAIDRF
NAPGAQQFCF LLSTRAGGLG INLATADTVI IFDSDWNPHN DIQAFSRAHR IGQANKVMIY
RFVTRASVEE RITQVAKRKM MLTHLVVRPG LGSKAGSMSK QELDDILKFG TEELFKDENE
GENKEEDSSV IHYDNEAIAR LLDRNQDATE DTDVQNMNEY LSSFKVAQYV VREEDKIEEI
EREIIKQEEN VDPDYWEKLL RHHYEQQQED LARNLGKGKR VRKQVNYNDA AQEDQDNQSE
YSVGSEEEDE DFDERPEGRR QSKRQLRNEK DKPLPPLLAR VGGNIEVLGF NTRQRKAFLN
AVMRWGMPPQ DAFTTQWLVR DLRGKTEKEF KAYVSLFMRH LCEPGADGSE TFADGVPREG
LSRQQVLTRI GVMSLVKKKV QEFEHINGRW SMPELMPDPS ADSKRSSRAS SPTKTSPTTP
EASTTNSPCN SKPATPAPSE KGESLRTPLE KDDVENHEEK PEKNSKIGEK METEADAPSP
ALSLGERLET RKTPLEDEVP GVPAEMDPET GYRGDREKSD DTKGDRELRP GPPRDEPRPS
VRREEKAEKP RFMFNIADGG FTELHTLWQN EERAAISSGK LNEIWHRRHD YWLLAGIVLH
GYARWQDIQN DAQFAIINEP FKTEANKGNF LEMKNKFLAR RFKLLEQALV IEEQLRRAAY
LNLSQEPAHP AMALHARFAE AECLAESHQH LSKESLAGNK PANAVLHKVL NQLEELLSDM
KADVTRLPAT LSRIPPIAAR LQMSERSILS RLASKGTEPH PTPAFPPGPY ATPPGYGVAF
STAPIGALAA AGANYSQMPA GSFITAATNG PPVLVKKEKE MVGALVSDGL DRKEPRAGEV
ICIDD
//
