ID H2SZ78_TAKRU Unreviewed; 1977 AA.
AC H2SZ78;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
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:ENSTRUP00000017716.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000017716.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000017716.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000017716.3}
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 -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR STRING; 31033.ENSTRUP00000017716; -.
DR Ensembl; ENSTRUT00000017790.3; ENSTRUP00000017716.3; ENSTRUG00000007202.3.
DR GeneTree; ENSGT00940000155088; -.
DR InParanoid; H2SZ78; -.
DR OMA; TWRWAVR; -.
DR Proteomes; UP000005226; Chromosome 7.
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; 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; 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; 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; 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:UP000005226};
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 385..432
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 466..513
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 552..603
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 641..676
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 758..942
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1074..1223
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1555..1738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..313
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..457
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..550
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1977 AA; 223342 MW; 8BE01B875919E7EC CRC64;
MSGSEDERED FGAADEHSLL PGEDDLDDAL SEVEEVPKSK KKKKAKKSSR ESRSSKRQRP
IREEFPVSSP EHLIGSEAAD RDPDEGAMRS ESEGSDYAPG KKKKKRSSSA KDKKKSASAE
KGSSSASKSK RKDPEPDDDD DDEEDCQPKS SAQLLEAWGM KDIDHVFTQE DYNALTNYKA
FSQFVRPLIA AKNPKIAVSK MMTLMMAKWR EFSTNNPLKG SATANAALAA ANVAAAVENM
VATGTDGASE TAVAASAAPA APAVAAAAPV VPQPAPAPPL RKAKTKEGKG PNARKKSKPA
PKPPPKPKPK KVAPLKIKLG GLNSKRKRSS SDEDEPDVDS DFDDGSFSVS DGSNRSSRPK
KKPKSSKKKK KVETEDGDGY ETDHQDYCEV CQQGGEIILC DTCPRAYHMV CLDPDMEKAP
EGKWSCPHCE KEGIQWEAKD ELSEGEGEDE EDRRDEGVEE EDDHHIEFCR VCKDGGELLC
CDTCPSSYHI HCLNPPLPEI PNGEWICPRC KCPPMKGKVQ KVLTWRWGEP PAPTPVPRPA
DLPPDAPDPP PLAGRREREF FVKWCNMSYW HCSWVLELQL ELNCQVMFRN YQRKTDMDEP
PPVDFGGEGD DDKSSKRKNK DPLFARMEEE ICRYGVKMEW LMIHRVLNHS VDKKNNVHYL
IKWRDLPYDQ STWESEDMDI PEYDPYKQTY WNHRELMVGE EGRPGKKLKK TVKVKKAERP
PANPVVDPTI KFDRQPDYLD STGGTLHPYQ LEGLNWLRFS WAQATDTILA DEMGLGKTVQ
TAVFLYSLYK EGHSKGPFLV SAPLSTIINW EREFEMWAPD MYVVTYVGDK DSRAVIRENE
FSFEGNAIRG GKKASKMKKD STVKFHVLLT SYELITIDQA VLGSIEWACL VVDEAHRLKN
NQSKFFRVLN NYQLQHKLLL TGTPLQNNLE ELFHLLNFLT PERFNNLEGF LEEFADIAKE
DQIKKLHDML GPHMLRRLKA DVFKHMPSKT ELIVRVELSP MQKKYYKFIL TRNFEALNTR
GGGNQVSLLN VVMDLKKCCN HPYLFPAAAT EAAKLPNGMY EGNSLVKSSG KLMLLQKMMR
KLKEGGHRVL VFSQMTKMLD LLEDFLENEG YKYERIDGGV TGNMRQEAID RFNAPGAPQF
AFLLSTRAGG LGINLASADT VIIYDSDWNP HNDIQAFSRA HRIGQNRKVM IYRFVTKASV
EERITQVAKK KMMLTHLVVR PGLGSKTGSM SKQELDDILK FGTEELFKDE IGDGDNKEDD
SSVIHYDDHA IDRLLDRNQD ATEDTELQSM NEYLSSFKVA QYVVKDEDDE EEEVEREVIK
QEESVDPDYW EKLLRHHYEQ QQEDLARNLG KGKRTRKPVN YNDGSQEERG IRQDWQEDQS
DNQSDYSVAS EEGDEDFDER SEANSRRPNR KGLRNDRDKP LPPLLARVGG NIEVLGFNAR
QRKAFLNAVM RYGMPPQDAF TNQWLVRDLR GKSEKEFKAY VSLFMRHLCE PGADGAETFA
DGVPREGLSR QHVLTRIGVM SLIRKKVQEF EHVNGQWSMP WMAELEENKR AAALAAGEDP
KTPSTGTPAD TQPNTPIPED LSKSDEKEEG KKDCEDGKGT KKMDDSEIIE IPDESEKSPD
LEKKEVDSTA EKEEKSTGNG EGGKEKEAED AGKDKEEKDK TSELDDAPAE VKAEGSDGKN
SEAEVGKDEK MDTSSPVEEK KELKEEKDGV KTEEATKLQN GENAKEGATA APVVNVSEEK
KKATKQRFMF NIADGGFTEL HSLWQNEERA ATVTKKTFEI WHRRHDYWLL AGIIQHGYAR
WQDVQNDVRF AILNEPFKGE MSRGNFLEIK NKFLARRFKL LEQALVIEEQ LRRAAYLNMT
EDPAHPSMAL NTRFSEVECL AESHQHLSKE SMSGNKPANA VLHKVLKQLE ELLSDMKADV
TRLPATIARI PPVAVRLQMS ERNILSRLAS RGPEGQFHSP HRHVADVLPL SIRVQSH
//
