ID A0A383YTT8_BALAS Unreviewed; 1814 AA.
AC A0A383YTT8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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=CHD5 {ECO:0000313|RefSeq:XP_007166268.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007166268.1};
RN [1] {ECO:0000313|RefSeq:XP_007166268.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007166268.1};
RG RefSeq;
RL Submitted (JAN-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_007166268.1; XM_007166206.1.
DR STRING; 310752.A0A383YTT8; -.
DR KEGG; bacu:102999193; -.
DR CTD; 26038; -.
DR InParanoid; A0A383YTT8; -.
DR OrthoDB; 2910821at2759; -.
DR Proteomes; UP000261681; 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; cd18057; DEXHc_CHD5; 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; IPR028727; DEXHc_CHD5.
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:SF6; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 5; 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; 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:UP000261681};
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 206..253
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 279..326
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 360..417
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 455..488
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 575..759
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 891..1056
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 91..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1388..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1460..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1774..1814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1814 AA; 207115 MW; 1EB8BA050F229C49 CRC64;
MAEWGLDDVD YLFSEADYHT LTNYKAFSQF LRPLIAKKNP KIPMSKMMTV LGAKWREFSA
NNPFKGSSAA AAAAAVAAAV ETVTIAPPLA ISPQQAPQPV PVRKAKTKEG KGPGVRKKIK
GSKDVKKKGK GRKVAGLKFR FGGVGSKRKK GSSSEEEERE ESDFDSASIH SSSVRSECSA
LLGRKSKRRR QKKRIDDGDG YETDHQDYCE VCQQGGEIIL CDTCPRAYHL VCLDPELEKA
PEGKWSCPHC EKEGIQWEPK DDDDDEEEGG CEEEEDDHME FCRVCKDGGE LLCCDACPSS
YHLHCLNPPL PEIPNGEWLC PRCTCPPLKG KVQRILHWRW TEPPAPFMVG LPGSDVEPGV
PPPKPLEGIP EREFFVKWAG LSYWHCSWVK ELQLELYHTV MYRNYQRKND MDEPPPFDYG
SGDEDGKSEK RKNKDPLYAK MEERFYRYGI KPEWMVIHRI LNHSFDKKGD VHYLIKWKDL
PYDQCTWEID DIDIPYYDNL KQAYWGHREL MLGEDARLPK RLVKKGKKLK DDKQEKPPDT
PIVDPTVKFD KQPWYIDSTG GTLHPYQLEG LNWLRFSWAQ GTDTILADEM GLGKTVQTIV
FLYSLYKEGH SKGPYLVSAP LSTIINWERE FEMWAPDFYV VTYTGDKESR SVIRENEFSF
EDNAIRSGKK VFRMKKEVQI KFHVLLTSYE LITIDQAILG SIEWACLVVD EAHRLKNNQS
KFFRVLNSYK IDYKLLLTGT PLQNNLEELF HLLNFLTPER FNNLEGFLEE FADISKEDQI
KKLHDLLGPH MLRRLKADVF KNMPAKTELI VRVELSQMQK KYYKFILTRN FEALNSKGGG
NQVSLLNIMM DLKKCCNHPY LFPVAAVEAP VLPNGSYDGS SLVKSSGKLM LLQKMLKKLR
DEGHRVLIFS QMTKMLDLLE DFLEYEGYKY ERIDGGITGG LRQEAIDRFN APGAQQFCFL
LSTRAGGLGI NLATADTVII YDSDWNPHND IQAFSRAHRI GQNKKVMIYR FVTRASVEER
ITQVAKRKMM LTHLVVRPGL GSKSGSMTKQ ELDDILKFGT EELFKDDVEG MMSQGQRPAT
PIPDVQSSKG GALAASAKKK HGSTPPGDNK DVEDSSVIHY DDAAISKLLD RNQDATDDTE
LQNMNEYLSS FKVAQYVVRE EDGVEEVERE IIKQEENVDP DYWEKLLRHH YEQQQEDLAR
NLGKGKRIRK QVNYNDASQE DQEWQDELSD NQSEYSIGSE DEDEDFEERP EGQSGRRQSR
RQLKSDRDKP LPPLLARVGG NIEVLGFNAR QRKAFLNAIM RWGMPPQDAF NSHWLVRDLR
GKSEKEFRAY VSLFMRHLCE PGADGAETFA DGVPREGLSR QHVLTRIGVM SLVRKKVQEF
EHVNGKYSTP DLIPEGPEGK KPGEVISSDP NTPVPASPAH LLSAPLGLPD KMEAQLGYLE
EKELGVQKPK KPPEIQALPA ALDRAEGEDK HENSEGKERA REERLEETEK AQPSPEQLPK
EEVLAEKEKI LDKLELSLIH SRGDGSDFRP DDTKAEEKEP IETQQNGDKE EDEEGKREDK
IGKFKFMFNI ADGGFTELHT LWQNEERAAV SSGKIYDIWH RRHDYWLLAG IVTHGYARWQ
DIQNDPRYMI LNEPFKSEIH KGNYLEMKNK FLARRFKLLE QALVIEEQLR RAAYLNMTQD
PNHPAMALNA RLAEVECLAE SHQHLSKESL AGNKPANAVL HKVLNQLEEL LSDMKADVTR
LPSMLSRIPP VAARLQMSER SILSRLTNRA GDPTIQQISS RPRDFPLLPG SFPVEPRLPG
PLPDPRRREK LPPF
//
