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Database: UniProt
Entry: A0A3P8S9Q9_AMPPE
LinkDB: A0A3P8S9Q9_AMPPE
Original site: A0A3P8S9Q9_AMPPE 
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
//
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