ID A0A2K6SN05_SAIBB Unreviewed; 1880 AA.
AC A0A2K6SN05;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:ENSSBOP00000008779.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000008779.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000008779.1}
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; ENSSBOT00000025541.1; ENSSBOP00000008779.1; ENSSBOG00000020782.1.
DR GeneTree; ENSGT00940000155088; -.
DR Proteomes; UP000233220; 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; cd18056; DEXHc_CHD4; 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:SF22; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 4; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000233220};
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 346..393
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 425..472
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 505..562
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 598..633
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 714..898
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1030..1179
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..510
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1541..1563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1880 AA; 213904 MW; 8E88798F8FC618BB CRC64;
MASGLGSPSP CSAGSEEEDM DALLNNSLPP PHPGNIFPKG PGWEGGIWTL PSDSSGELGD
SSGEGPEFVE EEEEVALRSD SEGSDYTPGK KKKKKLGPKK EKKSKSKRKE EEEEEDDDDD
SKEPKSSAQL LEDWGMEDID HVFSEEDYRT LTNYKAFSQF VRPLIAAKNP KIAVSKMMMV
LGAKWREFST NNPFKGSSGA SVAAAAAAAV AVVESMVTAT EVAPPPPPVE VPIRKAKTKE
GKGPNARRKP KGSPRVPDAK KPKPKKVAPL KIKLGGFGSK RKRSSSEDDD LDVESDFDDA
SINSYSVSDG STSRSSRSRK KLRTTKKKKK GEEEVTAVDG YETDHQDYCE VCQQGGEIIL
CDTCPRAYHM VCLDPDMEKA PEGKWSCPHC EKEGIQWEAK EDNSEGEEIL EEVGGDLEEE
DDHHMEFCRV CKDGGELLCC DTCPSSYHIH CLNPPLPEIP NGEWLCPRCT CPALKGKVQK
ILIWKWGQPP SPTPVPRPPD ADPSTPSPKP LEGRPERQFF VKWQGMSYWH CSWVSELQLE
LHCQVMFRNY QRKNDMDEPP SGDFGGDEEK SRKRKNKDPK FAEMEERFYR YGIKPEWMMI
HRILNHSVDK KGHVHYLIKW RDLPYDQASW ESEDVEIQDY DLFKQSYWNH RELMRGEEGR
PGKKLKKVKL RKLERPPETP TVDPTVKYER QPEYLDATGG TLHPYQMEGL NWLRFSWAQG
TDTILADEMG LGKTVQTAVF LYSLYKEGHS KGPFLVSAPL STIINWEREF EMWAPDMYVV
TYVGDKDSRA IIRENEFSFE DNAIRGGKKA SRMKKEASVK FHVLLTSYEL ITIDMAILGS
IDWACLIVDE AHRLKNNQSK FFRVLNGYSL QHKLLLTGTP LQNNLEELFH LLNFLTPERF
HNLEGFLEEF ADIAKEDQIK KLHDMLGPHM LRRLKADVFK NMPSKTELIV RVELSPMQKK
YYKYILTRNF EALNARGGGN QVSLLNVVMD LKKCCNHPYL FPVAAMEAPK MPNGMYDGSA
LIRASGKLLL LQKMLKNLKE GGHRVLIFSQ MTKMLDLLED FLEHEGYKYE RIDGGITGNM
RQEAIDRFNA PGAQQFCFLL STRAGGLGIN LATADTVIIY DSDWNPHNDI QAFSRAHRIG
QNKKVMIYRF VTRASVEERI TQVAKKKMML THLVVRPGLG SKTGSMSKQE LDDILKFGTE
ELFKDEATDG GGDNKEGEDS SVIHYDDKAI ERLLDRNQDE TEDTELQGMN EYLSSFKVAQ
YVVREEEMGE EEEVEREIIK QEESVDPDYW EKLLRHHYEQ QQEDLARNLG KGKRIRKQVN
YNDGSQEDRD WQDDQSDNQS DYSVASEEGD EDFDERSEAP RRPSRKGLRN DKDKPLPPLL
ARVGGNIEVL GFNARQRKAF LNAIMRYGMP PQDAFTTQWL VRDLRGKSEK EFKAYVSLFM
RHLCEPGADG AETFADGVPR EGLSRQHVLT RIGVMSLIRK KVQEFEHVNG RWSMPELAEV
EENKKMSQPG SPSPKTPTPS TPGDTQPNTP APAPPAEDGI KIEENSLKEE ESIEGEKEVK
PAAPETAIEC TQPPAPASED EKVVVEPPDG EEKVEKAEVK ERTEEPMETE PKGKGSHILK
HYRPCVNHEE KKEEEEKKEV MLQNGETPKD LNDEKQKKNI KQRFMFNIAD GGFTELHSLW
QNEERAATVT KKTYEIWHRR HDYWLLAGII NHGYARWQDI QNDPRYAILN EPFKGEMNRG
NFLEIKNKFL ARRFKLLEQA LVIEEQLRRA AYLNMSEDPS HPSMALNTRF AEVECLAESH
QHLSKESMAG NKPANAVLHK VLKQLEELLS DMKADVTRLP ATIARIPPVA VRLQMSERNI
LSRLANRAPE PTPQQVAQQQ
//
