ID H2QC61_PANTR Unreviewed; 2058 AA.
AC H2QC61; A0A2J8KP69;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 81.
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:ENSPTRP00000014854.3,
GN ECO:0000313|VGNC:VGNC:9234};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000014854.3, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000014854.3, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000014854.3}
RP IDENTIFICATION.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; AC192612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_512012.3; XM_512012.5.
DR STRING; 9598.ENSPTRP00000014854; -.
DR PaxDb; 9598-ENSPTRP00000014854; -.
DR Ensembl; ENSPTRT00000016052.4; ENSPTRP00000014854.3; ENSPTRG00000008714.5.
DR GeneID; 455278; -.
DR CTD; 1107; -.
DR VGNC; VGNC:9234; CHD3.
DR eggNOG; KOG0383; Eukaryota.
DR GeneTree; ENSGT00940000158001; -.
DR HOGENOM; CLU_000315_22_3_1; -.
DR InParanoid; H2QC61; -.
DR OrthoDB; 2910821at2759; -.
DR TreeFam; TF106448; -.
DR Proteomes; UP000002277; Chromosome 17.
DR Bgee; ENSPTRG00000008714; Expressed in lymph node and 20 other cell types or tissues.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016581; C:NuRD complex; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; IEA:Ensembl.
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:0000976; F:transcription cis-regulatory region binding; IEA:Ensembl.
DR GO; GO:0007098; P:centrosome cycle; IEA:Ensembl.
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 GO; GO:0007051; P:spindle organization; IEA:Ensembl.
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; IPR023779; Chromodomain_CS.
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; PS00598; CHROMO_1; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000002277};
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 437..484
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 514..561
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 594..651
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 689..725
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 806..990
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1122..1287
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1571..1765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..49
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..125
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..175
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..310
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..348
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..510
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1689..1765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2058 AA; 232892 MW; 624696113797E725 CRC64;
MASPLRDEEE EEEEMVVSEE EEEEEEEGDE EEEEVEAADE DDEEDDDEGV LGRGPGHDRG
RDRHSPPGCH LFPPPPPPPP PLPPPPPPPP PDKDDIRLLP SALGVKKRKR GPKKQKENKP
GKPRKRKKRD SEEEFGSERD EYREKSESGG SEYGTGPGRK RRRKHREKKE KKTKRRKKGE
GDGGQKQVEQ KSSATLLLTW GLEDVEHVFS EEDYHTLTNY KAFSQFMRPL IAKKNPKIPM
SKMMTILGAK WREFSANNPF KGSAAAVAAA AAAAAAAVAE QVSAAVSSAT PIAPSGPPAL
PPPPAADIQP PPIRRAKTKE GKGPGHKRRS KSPRVPDGRK KLRGKKMAPL KIKLGLLGGK
RKKGGSYVFQ SDEGPEPEAE ESDLDSGSVH SASGRPDGPV RTKKLKRGRP GRKKKKVLGC
PAVAGEEEVD GYETDHQDYC EVCQQGGEII LCDTCPRAYH LVCLDPELDR APEGKWSCPH
CEKEGVQWEA KEEEEEYEEE GEEEGEKEEE DDHMEYCRVC KDGGELLCCD ACISSYHIHC
LNPPLPDIPN GEWLCPRCTC PVLKGRVQKI LHWRWGEPPV AVPAPQQADG NPDVPPPRPL
QGRSEREFFV KWVGLSYWHC SWAKELQLEI FHLVMYRNYQ RKNDMDEPPP LDYGSGEDDG
KSDKRKVKDP HYAEMEEKYY RFGIKPEWMT VHRIINHSVD KKGNYHYLVK WRDLPYDQST
WEEDEMNIPE YEEHKQSYWR HRELIMGEDP AQPRKYKKKK 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 GALIKSSGKL MLLQKMLRKL 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 EASATNSPCT SKPATPAPSE
KGEGIRTPLE KEEAENQEEK PEKNSRIGEK METEADAPSP APSLGERLEP RKIPLEDEVP
GVPGEMEPEP GYRGDREKSA TESTPGERGE EKPLDGQEHR ERPEGETGDL GKREDVKGDR
ELRPGPRDEP RSNGRREEKT EKPRFMFNIA DGGFTELHTL WQNEERAAIS SGKLNEIWHR
RHDYWLLAGI VLHGYARWQD IQNDAQFAII NEPFKTEANK GNFLEMKNKF LARRFKLLEQ
ALVIEEQLRR AAYLNLSQEP AHPAMALHAR FAEAECLAES HQHLSKESLA GNKPANAVLH
KVLNQLEELL SDMKADVTRL PATLSRIPPI AARLQMSERS ILSRLASKGT EPHPTPAFPP
GPYATPPGYG AAFSAAPVGA LAAAGANYSQ MPAGSFITAA TNGPPVLVKK EKEMVGALVS
DGLDRKEPRA GEVICIDD
//
