ID A0A3P8S9Q9_AMPPE Unreviewed; 2095 AA.
AC A0A3P8S9Q9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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|Ensembl:ENSAPEP00000008832.1};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000008832.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000008832.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000008832.1}
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 Ensembl; ENSAPET00000009080.1; ENSAPEP00000008832.1; ENSAPEG00000006341.1.
DR GeneTree; ENSGT00940000158001; -.
DR Proteomes; UP000265080; Chromosome 23.
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; 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; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding 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; IPR009057; Homeobox-like_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; IPR036388; WH-like_DNA-bd_sf.
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; 2.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 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:UP000265080};
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 363..410
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 452..499
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 631..664
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 747..931
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1063..1228
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 24..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1535..1713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1955..1984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..67
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1536..1568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1575..1616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2095 AA; 236620 MW; 1EA908178AFC97E0 CRC64;
MVRGGTAYPD VTMSTKEVSL SWNMLTQNSS NEEAEISDRE VPCRKKGRPK KKKDTKKKDK
EGKPAKAKKR KKIDSDVERD SDRERDNGEN SDSVASDYGS GEKKKKKKHK ERKEKKTKKK
KKDDGDRDSS QEETTKQPIE QKTSAQLAKE WGLEDVDHTF TEEDYRELTN YKAFSQFMRP
MIAKKNPKIP MSKMMTILGA KWREFSSNNP FKGNAAAVAA AAAAAAIAVA EQVSAATASP
EPPPQPPPIR KAKTKEGKGP GYKKRSKSPR VPDKKKASAV AKAKKMAPIR IKLSPIGAKR
KKSCSSEDMD EDESEQEDSS VHSSSVRSDS SGRVKKNKRG RPAKKKKKIP GEEEGDGYET
DHQDYCEVCQ QGGEIILCDT CPRAYHLVCL EPELDKAPEG KWSCPHCEKE GIQWEAKDEE
FEDFEEDSED RVISEVSVGV PTGADEEDDD HMEFCRVCKD GGELLCCDTC TSSYHIHCLN
PPLPEIPNGE WLCPRCTCPP IKGRVQKILH WRWGEPPPPI PVPPAPDAPP DAPPPPPMKG
RAEREFFVKL TGQSYWHCTW ITELQLEIFH SVMYRNYQRK TDMDEPPSLD YGSGAEDENG
VGKSEKRRAK DPQYAILEDK YYKYGIKPEW MMIHRIINHS VDKKGTYHYL VKWRDLTYDQ
CTWERDDLEI PDFGIYKASY WRHRDNIMKE DPDKPKKIRS KNSEGEEESP ASPVTDPTIK
YEEQPDFVTS TGGTLHLYQL EGLNWLRFSW AQGTDTILAD EMGLGKTIQT IVFLYSLFKE
GHTKGPFLVS APLSTIINWE REFEMWAPDF YVVTYTGDKD SRAIIRENEF SFDDTAVKGG
KKAFKLRREV PIKFHVLLTS YELVTIDQTA LKSIDWACLV VDEAHRLKNN QSKFFRRLND
YKIDHKLLLT GTPLQNNLEE LFHLLNFLTP NRFNNLEGFL EEFADISKED QIKKLHDLLG
PHMLRRLKAD VFKNMPAKTE LIVRVELSPM QKKYYKLILT KNFEALNSKG GGNQVSLLNI
MMDLKKCCNH PYLFPVASME AQKTPSGAYE GSALTKASGK LMLLQKMLRK LKEQGHRVLV
FSQMTKMLDL LEDFLDYEGY KYERIDGGIT GALRQEAIDR FNAPGACQFC FLLSTRAGGL
GINLATADTV VIFDSDWNPH NDIQAFSRAH RIGQANKVMI YRFVTRASVE ERITQVAKRK
MMLTHLVVRP GLGSKAGSMS KQELDDILKF GTEELFKDEG EGMKNSAGDK VEDEGSVIHY
DTTAIERLLD RSQDATDDSD VQNMNEYLSS FKVAQYMVRE EDKIEEIERE IIKQEENVDP
DYWEKLLRHH YEQQQEDLAS KLGKGKRNRK PVNYNDAAQE DQEWHADISD NQSEYSVGSE
EEDEDFDDRP EGRRQSRRQL RNEKDKPLPP LLARVGGNLE VLGFNTRQRK AFLNAVMRWG
MPSQDAFSSQ WLVRDLRGKT EKEFKAYVSL FMRHLCEPVA DGAETFADGV PREGLCRQPV
LTRIGVMSLV KKKIQEFEHI NGRWSLPELK PEVNIDKSSS RASSPAVKTA TPTPDASYNN
TPCTSKPATP APSEKLEKNG KEVEKEEDKE EAEGTLEKEK AKEKDEGKEV EGNKTGDPEE
LSSSTKETSQ NAAPDGKEES DPKDDEKKET TDAPAATTEE KKEESKEETK HTSKQDTDVK
EEKSEGEKAG EEKEKREETP TTTEATDVKD KAEVADLKKE EVKGEKDVVK EVKAAKEEAP
KGNGKPPIER PRFMFNIADG GFTELHTLWQ NEERAAISSG KMNEIWHRRH DFWLLAGIVI
HGYARWQDIQ NDPQFAIVNE PFKSQANKGN FLEMKNKFLA RRFKLLEQAL VIEEQLRRAA
YLNMTQDPSH PAMALNARFA EVECLAESHQ HLSKESLAGN KPANAVLHKV LNQLEELLSD
MKADVTRLPA TLSRVPPIAA RLQMSERSIL SRLASKGTET HTPPPIPPGP YATPQNYGAP
FTPAPPSALH LGGANYSQMP PGSFISEAAA AAGATGGAAG GATGGPTAAG VCQKTKEHDV
VQRQRVVDLW KDGKSEGAIG QELRMPKSTV HSIIVKYRLS NTVENLPRNG RPKKP
//