ID A0A3Q1I9W0_ANATE Unreviewed; 1837 AA.
AC A0A3Q1I9W0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
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};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000001346.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000001346.2}
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; ENSATET00000001368.2; ENSATEP00000001346.2; ENSATEG00000000848.2.
DR GeneTree; ENSGT00940000158001; -.
DR Proteomes; UP000265040; 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; 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; 1.
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:UP000265040};
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 294..341
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 383..430
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 562..595
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 679..863
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 983..1148
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1248..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1744..1764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1837 AA; 208663 MW; F81FC03168E7CDF2 CRC64;
KKEKEGKPVK AKKRKKIDSD VERDSDRERE YGDNSDSVAS DYGTSEKKKK KKHKERKEKK
TKKKKKDDGD RDSKQKTSAQ LAKEWGLEDV DHTFTEEDYR ELTNYKAFSQ FMRPMIAKKN
PKIPMSKMMT ILGAKWREFS SNNPFKGNAA AVAAAAAAAA IAVAEQVSAA TASPPQPPPL
RKAKTKEGKG PGYKKRSKSP RVPDKKKASA VAKAKKMAPI RIKLSPIGAK RKKSCSSDDM
DEDDSEQEDS SVHSSSVRSD SSGRVKKNKR GRPSKKKKKI PGEEEGDGYE TDHQDYCEVC
QQGGEIILCD TCPRAYHLVC LEPELEKAPE GKWSCPHCEK EGIQWEAKDE DFEDFEEDSE
DRVISEVGVG IHTGAEEEDD DHMEFCRVCK DGGELLCCDT CTSSYHIHCL NPPLPEIPNG
EWLCPRCMCP PIKGRVQKIL HWRWGEPPPP IPVPPAPDAP PDAPPPPPMK GRAEREFFVK
FVGQSYWHCT WITELQLEIF HSVMYRNYQR KTDMDEPPSL DYGSGGEDEN GVGKSEKRRA
KDPHYAILED KYYKYGIKPE WMMIHRIINH SVDKKGMYHY LVKWRDLTYD QCTWERDDLD
IPDFAIYKTN YWRHRDTIMK EDPEKPRKMR NKNQEGEEES PAASPVTDPT IKYEEQPDFV
SSTGGTLHLY QLEGLNWLRF SWAQGTDTIL ADEMGLGKTI QTIVFLYSLF KEGHTKGPFL
VSAPLSTIIN WEREFEMWAP DFYVVTYTGD KDSRAIIREN EFSFDDTAVK GGKKAFKLRR
EAPIKFHVLL TSYELVTIDQ TALKSIDWAC LVVDEAHRLK NNQSKFFRRL NDYKIDHKLL
LTGTPLQNNL EELFHLLNFL TPNRFNENKL SRMLLSFKSN SKEEKPYLKM CHTWFTLHLC
RAGVIVLSFF NRKYYKLILT KNFEALNSKG GGNQVSLLNI MMDLKKCCNH PYLFPVASME
AQKTPSGAYE GSALTKASGK LMLLQKMLRK LKEQGHRVLV FSQMTKMLDL LEDFLDYEGY
KYERIDGGIT GALRQEAIDR FNAPGACQFC FLLSTRAGGL GINLATADTV IIFDSDWNPH
NDIQAFSRAH RIGQANKVMI YRFVTRASVE ERITQVAKRK MMLTHLVVRP GLGSKAGSMT
KQELDDILKF GTEELFKDEG EGDKVEDEGN VIHYDSTAIE RLLDRSQDAT DDSDVQNMNE
YLSSFKVAQY MVREEDKIEE IEREIIKQEE NVDPDYWEKL LRHHYEQQQE DLASKLGKGK
RNRKPVNYND AAQEDQDNQS EYSVGSEEED EDFDDRPEGR RQSRRQLRNE KDKPLPPLLA
RVGGNLEVLG FNTRQRKAFL NAVMRWGMPS QDAFSSQWLV RDLRGKTEKE FKAYVSLFMR
HLCEPVADGA ETFADGVPRE GLCRQPVLTR IGVMSLVKKK IQEFEHINGR WSLPELKPEV
SLDKSSSRAS SPAVKTATPT PDASYNNTPC TSKPGSQTSH TGYLRYTITH APDPVEGALR
KGHLIKLTLD MTSSNVYDAG KEVVPKEVPK GNGKPPIERP RFMFNIADGG FTELHTLWQN
EERAAISSGK MNEIWHRRHD FWLLAGIVIH GYARWQDIQN DPQFAIVNEP FKTQANKGNF
LEMKNKFLAR RFKLLEQALV IEEQLRRAAY LNMTQDPSHP AMALNARFAE VECLAESHQH
LSKESLAGNK PANAVLHKVL NQLEELLSDM KADVTRLPAT LSRVPPITAR LQMSERSILS
RLASKGTETH TPPPIPPGPY ATPQNYGAPF TPAPPSALHM GGANYSQMPP GSFISGQCLK
GGVIAIVASS AGTDLQLSRG FNPLIVDDHS NSRRTAE
//
