ID A0A2Y9Q0Z6_DELLE Unreviewed; 2151 AA.
AC A0A2Y9Q0Z6;
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=CHD3 {ECO:0000313|RefSeq:XP_022451111.1};
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_022451111.1};
RN [1] {ECO:0000313|RefSeq:XP_022451111.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022451111.1};
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_022451111.1; XM_022595403.2.
DR Proteomes; UP000248483; 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; 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; 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; 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; 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; SSF47095; HMG-box; 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:UP000248483};
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 373..420
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 450..497
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 530..587
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 625..661
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 742..926
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1058..1223
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1507..1701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1976..2151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..63
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..115
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..250
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..288
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..446
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1370..1390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1519..1550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1560..1589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1625..1701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2057..2080
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2122..2151
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2151 AA; 242223 MW; C798FC13D73985DE CRC64;
MGRGDIWEEP APFSLTETSG EKARDLALLK ADKDDIRLLP SALGVKKRKR GPKKQKENKP
GKARKRKKLD SEEEFGSERD EYREKSESGG SEYGTGPGRK RRRKHREKKE KKTKRRKKGE
GDGGQKQVEQ KSSATLLLTW GLEDVEHVFS EEDYHTLTNY KAFSQFMRPL IAKKNPKIPM
SKMMTILGAK WREFSANNPF KGSAAAVAAA AAAAAAAVAE QVSAAVSSAT PIAPSGPPAL
PPPPAADTQP PPIRRAKTKE GKGPGHKRRS KSPRVPDGRK KLRGKKMAPL KIKLGLLGGK
RKKGGSSDEG PEPEAEESDL DSGSVHSASG RPDGPVRTKK LKRGRPGRKK KKVLGCPAVA
GEEEVDGYET DHQDYCEVCQ QGGEIILCDT CPRAYHLVCL DPELDRAPEG KWSCPHCEKE
GVQWEAKEEE EDYEEEGEEE GEKEEEDDHM EYCRVCKDGG ELLCCDACIS SYHIHCLNPP
LPDIPNGEWL CPRCTCPVLK GRVQKILHWR WGEPPVAVPA PQQADGNPDA PPARPLQGRS
EREFFVKWVG LSYWHCSWAK ELQLEIFHLV MYRNYQRKND MDEPPPLDYG SGEDDGKSDK
RKVKDPHYAE MEEKYYRFGI KPEWMTVHRI INHSVDKKGN YHYLVKWRDL PYDQSTWEED
EMNIPEYEDH KQSYWRHREL IMGEDPAQPR KYKKKKKELQ GDGPPSSPTN DPTVKYETQP
RFITATGGTL HMYQLEGLNW LRFSWAQGTD TILADEMGLG KTIQTIVFLY SLYKEGHTKG
PFLVSAPLST IINWEREFQM WAPKFYVVTY TGDKDSRAII RENEFSFEDN AIKGGKKAFK
MKREAQVKFH VLLTSYELIT IDQAALGSIR WACLVVDEAH RLKNNQSKFF RVLNGYKIDH
KLLLTGTPLQ NNLEELFHLL NFLTPERFNN LEGFLEEFAD ISKEDQIKKL HDLLGPHMLR
RLKADVFKNM PAKTELIVRV ELSPMQKKYY KYILTRNFEA LNSRGGGNQV SLLNIMMDLK
KCCNHPYLFP VAAMESPKLP SGAYEGGALI KASGKLMLLQ KMLRKLKEQG HRVLIFSQMT
KMLDLLEDFL DYEGYKYERI DGGITGALRQ EAIDRFNAPG AQQFCFLLST RAGGLGINLA
TADTVIIFDS DWNPHNDIQA FSRAHRIGQA NKVMIYRFVT RASVEERITQ VAKRKMMLTH
LVVRPGLGSK AGSMSKQELD DILKFGTEEL FKDENEGENK EEDSSVIHYD NEAIARLLDR
NQDATEDTDV QNMNEYLSSF KVAQYVVREE DKIEEIEREI IKQEENVDPD YWEKLLRHHY
EQQQEDLARN LGKGKRVRKQ VNYNDAAQED QDNQSEYSVG SEEEDEDFDE RPEGRRQSKR
QLRNEKDKPL PPLLARVGGN IEVLGFNTRQ RKAFLNAVMR WGMPPQDAFT TQWLVRDLRG
KTEKEFKAYV SLFMRHLCEP GADGSETFAD GVPREGLSRQ QVLTRIGVMS LVKKKVQEFE
HINGRWSMPE LMPDPSADSK RSSRASSPTK TSPTTPEASA ANSPCTSKPA TPAPSEKGDG
VRTPLEKDEA ENQEEKPEKN SKIGEKMETE ADTPSPAPSL GERLEPRKIP LEDEVPGVPG
EMEPEPGYRG DREKSATEST PGERGEEKPM DGQEHRERPE GETGDLGKRA EDVKGDRELR
PGPPRDEPRS NGRREEKAEK PRFMFNIADG GFTELHTLWQ NEERAAVSSG KLNEIWHRRH
DYWLLAGIVL HGYARWQDIQ NDAQFAIINE PFKTEANKGN FLEMKNKFLA RRFKLLEQAL
VIEEQLRRAA YLNLSQEPAH PAMALHARFA EAECLAESHQ HLSKESLAGN KPANAVLHKV
WDVLTTPRPH VFRCPPSPIS LFSIFPFPFF FLSICVLCGD LVSLPLYLTL FLVPELLFFS
TSVISLVSDS STSVPSSLSF SDCICPCDSS SLFLAPSLPF PVFLLPFFLR GPGPSSEPAG
GVAERHEGGR DPPASHAVPN TPHRSPPSDV RAQHPQPAGQ QGHGASPHTG LPPGAVRYTS
GVRGGLQRRT RRGPGRRRRQ LQPDACRVLH HSRHQRPSSA GEEGEGNGGG IGVRRAGSEG
APSRGGDLYR RLTGSQACPS PRPRPRGRPP AQALGPVASP PPSPPLGPPL G
//