ID U3JQC8_FICAL Unreviewed; 1915 AA.
AC U3JQC8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=CHD4 {ECO:0000313|Ensembl:ENSFALP00000004982.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000004982.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000004982.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000004982.2}
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 RefSeq; XP_005038501.1; XM_005038444.2.
DR STRING; 59894.ENSFALP00000004982; -.
DR Ensembl; ENSFALT00000005006.2; ENSFALP00000004982.2; ENSFALG00000004785.2.
DR GeneID; 101813593; -.
DR KEGG; fab:101813593; -.
DR CTD; 1108; -.
DR eggNOG; KOG0383; Eukaryota.
DR GeneTree; ENSGT00940000155088; -.
DR HOGENOM; CLU_000315_22_2_1; -.
DR Proteomes; UP000016665; Chromosome 1.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016581; C:NuRD complex; IEA:Ensembl.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR GO; GO:0090734; C:site of DNA damage; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0001221; F:transcription coregulator binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR CDD; cd18056; DEXHc_CHD4; 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; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF22; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 4; 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; 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:UP000016665};
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 364..411
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 443..490
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 523..580
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 616..651
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 732..916
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1048..1197
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1519..1665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1893..1915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..67
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..531
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1554
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1559..1580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1899..1915
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1915 AA; 218043 MW; 093D36D4F70A7A8B CRC64;
MASGIGSPSP CSGGSDDDEM EILLNNAIPQ HPEPEEEPEE ELLSEADTPK IKKKKKPKKL
KEPKVPKLSK RQKKELGDSS GEGNEFVEEE EEVLRSDSEG SDYTPGKKKK KKLGPKKEKK
NKAKRKEEEE EEEEDDDSKE PKSSAQLLED WGMEDIDHIF TEEDYRTLTN YKAFSQFVRP
LIAAKNPKIA VSKMMMVLGA KWREFSTNNP FKGSSGASVA AAAAAAVAVV ESMVTNVDAV
LPQPPVDVPL RKAKTKEGKG PNARRKPKAS PRIPDIKKPK TKKVAPLKIK LGGFGSKRKR
SSSEDDDLDV ESDFDDASIN SYSVSDGSTS RSSRSRKKLK AGKKKKKGEE DSTVAVDGYE
TDHQDYCEVC QQGGEIILCD TCPRAYHMVC LDPDMEKAPE GKWSCPHCEK EGIQWEAKED
NSEGEEILED VVGDAEEEDD HHMEFCRVCK DGGELLCCDA CPSSYHIHCL NPPLPEIPNG
EWLCPRCTCP ALKGKVQKIL IWKWGQPPVG PAPPRPPDAD PNAPPPKPLE GRPERQFFVK
WQGMSYWHCS WVSELQLELH CQVMFRNYQR KNDMDEPPSG DFGGEEEKSR KRKNKDPKYA
EMEERFYRYG IKPEWMMIHR ILNHSVDKKG NVHYLIKWRD LPYDQASWES EDVDIQDYDL
YKQAYWNHRE LMRGEEGRPG KKLKKVKMRK LERPPETPTV DPTVKYDRQP EYLDVTGGTL
HPYQLEGLNW LRFSWAQGTD TILADEMGLG KTVQTAVFLY SLYKEGHSKG PFLVSAPLST
IINWEREFEM WAPDMYVVTY VGDKDSRAII RENEFTFEDN AIRGGKKASR MKKEAAVKFH
VLLTSYELIT IDMAILGSID WACLIVDEAH RLKNNQSKFF RVLNGYSLQH KLLLTGTPLQ
NNLEELFHLL NFLTPERFHN LEGFLEEFAD IAKEDQIKKL HDMLGPHMLR RLKADVFKNM
PSKTELIVRV ELSPMQKKYY KYILTRNFEA LNARGGGNQV SLLNVVMDLK KCCNHPYLFP
VAAMEAPKMP NGMYDGSALI RASGKLLLLQ KMLKNLKEGG HRVLIFSQMT KMLDLLEDFL
EHEGYKYERI DGGITGNLRQ EAIDRFNAPG AQQFCFLLST RAGGLGINLA TADTVIIYDS
DWNPHNDIQA FSRAHRIGQN KKVMIYRFVT RASVEERITQ VAKKKMMLTH LVVRPGLGSK
TGSMSKQELD DILKFGTEEL FKDETTEGGD NKEGEDSSVI HYDDKAIERL LDRNQDETED
TELQGMNEYL SSFKVAQYVV REEEMGEEEE VEREIIKQEE SVDPDYWEKL LRHHYEQQQE
DLARNLGKGK RIRKQVNYND GSQEDRDWQD DQSDNQSDYS VASEEGDEDF DERSEAARRP
SRKGLRNDKD KPLPPLLARV GGNIEVLGFN ARQRKAFLNA IMRYGMPPQD AFTTQWLVRD
LRGKSEKEFK AYVSLFMRHL CEPGADGAET FADGVPREGL SRQHVLTRIG VMSLIRKKVQ
EFEHVNGRWS MPELAEIEEN KKLSQPSSPS PKTPTPSTPG DTQPNTPAPV PPPEDGVKVE
EGASAKEQGE PSEPEKELSA SATETEAPME QCAQPVEPQE AKSPVNSTEA DEKKAEESEV
KERPDEPMEV ESKADVEKVE DRAAAENPSD PPIITLDEKD EKKDDDKRDV VMLQNGEMLK
ESVDERHKKA VKQRFMFNIA DGGFTELHSL WQNEERAATV TKKTYEIWHR RHDYWLLAGI
INHGYARWQD IQNDPRYAIL NEPFKGEMNR GNFLEIKNKF LARRFKLLEQ ALVIEEQLRR
AAYLNMSEDP SHPSMALNTR FAEVECLAES HQHLSKESMA GNKPANAVLH KVLKQLEELL
SDMKADVTRL PATIARIPPV AVRLQMSERN ILSRLANRSS EPPPPPPPQQ VAQQQ
//
