ID I3K598_ORENI Unreviewed; 1715 AA.
AC I3K598;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 77.
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:ENSONIP00000016293.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000016293.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000016293.2}
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 -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR Ensembl; ENSONIT00000016308.2; ENSONIP00000016293.2; ENSONIG00000012953.2.
DR GeneTree; ENSGT00940000155088; -.
DR Proteomes; UP000005207; Linkage group LG11.
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; 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; 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:SF55; DNA HELICASE; 1.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF06461; CHDII_SANT-like; 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:UP000005207};
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 182..229
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 263..310
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 349..400
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 438..473
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 555..739
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 871..1036
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 49..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..113
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..254
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1715 AA; 195429 MW; F2FB97690F323C0A CRC64;
MMTLMMAKWR EFSTNNPLKG CATANAALAA ANVAAAVENM VVAGTESGAD TAPATLTPPV
STPAAAPAPI APPAAPAPPL RKAKTKEGKG PNARRRSKPT SKPPPKPKPK KVAPLKIKLG
GLNSKRKNVC NVGGLFNKSK VKAEVKADIP YVSVLCTYFF LLLFCLFSVE TEDGDGYETD
HQDYCEVCQQ GGEIILCDTC PRAYHMVCLD PDMEKAPEGK WSCPHCEKEG IQWEARDDLS
EAEGEDDDDR RDEGMEEEDD HHIEFCRVCK DGGELLCCDT CPSSYHIHCL NPPLPEIPNG
EWICPRCKCP PMKGKVQKVL TWRWGEAPAP MPVPRPADLP ADAPDPPPLA GRREREFFVK
WCNMSYWHCS WVQELQLELN CQVMFRNYQR KTDMDEPPPA DFGGEGDDDK STKRKNKDPL
FVHMEEEFCR YGVKMEWLMI HRVLNHSVDK KNNVHYLIKW RDLPYDQSTW ESEDMDIPEY
DTYKQTYWNH RELMMGEEGR PGKKLKKTVK VKKAERPPAN PVVDPTIKFD RQPDYLDSTG
GTLHPYQLEG LNWLRFSWAQ ATDTILADEM GLGKTVQTAV FLYSLYKEGH SKGPFLVSAP
LSTIINWERE FEMWAPDMYV VTYIGDKDSR AVIRENEFSF EGNAIRGGKK ASKMKKDSPV
KFHVLLTSYE LITIDQAVLG SIEWACLVVD EAHRLKNNQS KFFRVLNNYP LQHKLLLTGT
PLQNNLEELF HLLNFLTPER FNNLEGFLEE FADIAKEDQI KKLHDMLGPH MLRRLKADVF
KHMPSKTELI VRVELSSMQK KYYKFILTRN FEALNTRGGG NQVSLLNVVM DLKKCCNHPY
LFPAAANEAP KLPNGMYEGT SLTKASGKLM LLQKMMRRLK EGGHRVLVFS QMTKMLDLLE
DFLENEGYKY ERIDGGVTGN LRQEAIDRFN APGAQQFAFL LSTRAGGLGI NLASADTVII
YDSDWNPHND IQAFSRAHRI GQNRKVMIYR FVTKASVEER ITQVAKKKMM LTHLVVRPGL
GSKMGSMSKQ ELDDILKFGT EELFKDEVGD GDNKEDDSSV IHYDDQAIDR LLDRNQDATD
DTELQSMNEY LSSFKVAQYV VKDEDDEEEV EREVIKQEES VDPDYWEKLL RHHYEQQQED
LARNLGKGKR TRKPVNYNDD WQEDQSDNQS DYSVASEEGD EDFDERTEGK PNRKGLRNDR
DKPLPPLLAR VGGNIEVLGF NARQRKAFLN AVMRYGMPPQ DAFTNQWLVR DLRGKSEKEF
KAYVSLFMRH LCEPGADGAE TFADGVPREG LSRQHVLTRI GVMSLIRKKV QEFEHVNGQW
SMPWMAELEE NKRAASEKSP VLDKKEEADS AAEKEDREKE TDGVEGKEKE AEDMSKEKEE
KSVEKDASAE IKGEGSESKM DLVEGRSREQ KEEKDSVKPD ESGKLQNGEN AKDGGTAAPV
VNVSEEKKKA TKQRFMFNIA DGGFTELHSL WQNEERAATV TKKTFEIWHR RHDYWLLAGI
IQHGYARWQD VQNDVRFAIL NEPFKGEMSR GNFLEIKNKF LARRFKLLEQ ALVIEEQLRR
AAYLNMTEDP AHPSMALNTR FSEVECLAES HQHLSKESMS GNKPANAVLH KVLKQLEELL
SDMKADVTRL PATIARIPPV AVRLQMSERN ILSRLASRGP EVTAQNQSQT AQQMQVGLDR
RESSMFGVYW CFVVTFGLFQ TSRDFIVLVF TFRKL
//
