ID A0A2Y9T2L7_PHYMC Unreviewed; 1870 AA.
AC A0A2Y9T2L7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 2.
DT 27-MAR-2024, entry version 27.
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_023983792.2};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023983792.2};
RN [1] {ECO:0000313|RefSeq:XP_023983792.2}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023983792.2};
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_023983792.2; XM_024128024.3.
DR Proteomes; UP000248484; 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:UP000248484};
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 377..424
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 454..501
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 534..591
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 629..665
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 746..930
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1062..1227
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..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1511..1706
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 431..450
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1523..1554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1629..1706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1870 AA; 212747 MW; CC5DB3A907B8E6DA CRC64;
MGRGDIWEEP APFSLTETSG EKAKDLALLK ADKDDIRLLP SALGVKKRKR GPKKQKENKP
GKPRKRKKLD SEEEFGSERD EYREKSESGG SEYGTGPGRK RRRKHREKKE KKTKRRKKGE
GDGGQKQVEQ KSSATLLLTW GLEDVEHVFS EEDYHTLTNY KAFSQFMRPL IAKKNPKIPM
SKMMTILGAK WREFSANNPF KGSAAAVAAA AAAAAAAVAE QVSAAVSSAT PIAPSGPPAL
PPPPAADIQP PPIRRAKTKE GKGPGHKRRS KSPRVPDGRK KLRGKKMAPL KIKLGLLGSK
RKKGGSYVFQ SDEGPEPEAE ESDLDSGSVH SASGRPDGPV RTKKLKRGRP GRKKKKVLGC
PAVAGEEEVD GYETDHQDYC EVCQQGGEII LCDTCPRAYH LVCLDPELDR APEGKWSCPH
CEKEGVQWEA KEEEEDYEEE GEEEGEKEEE DDHMEYCRVC KDGGELLCCD ACISSYHIHC
LNPPLPDIPN GEWLCPRCTC PVLKGRVQKI LHWRWGEPPV AVPAPQQADG NPDAPPARPL
QGRSEREFFV KWVGLSYWHC SWAKELQLEI FHLVMYRNYQ RKNDMDEPPP LDYGSGEDDG
KSDKRKVKDP HYAEMEEKYY RFGIKPEWMT VHRIINHSVD KKGNYHYLVK WRDLPYDQST
WEEDEMNIPE YEDHKQSYWR 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 GALIKASGKL 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 EASAANSPCT SKPATPAPSE
KGDGIRTPLE KDEAENQEEK PEKNSKIGEK METEADTPSP APSLGERLEP RKIPLEDEVP
GVPGEMEPEP GYRGDREKSA TESTPGERGE EKPMDGQEHR ERPEGETGDL GKRAEDVKGD
RELRPGPPRD EPRSNGRREE KAEKPRFMFN IADGGFTELH TLWQNEERAA ISSGKLNEIW
HRRHDYWLLA GIVLHGYARW QDIQNDAQFA IINEPFKTEA NKGNFLEMKN KFLARRFKLL
EQALVIEEQL RRAAYLNLSQ EPAHPAMALH ARFAEAECLA ESHQHLSKES LAGNKPANAV
LHKVTDSWPL
//
