ID A0A3P8YQ30_ESOLU Unreviewed; 1563 AA.
AC A0A3P8YQ30;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000017986.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000017986.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000017986.2}
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR Ensembl; ENSELUT00000027722.2; ENSELUP00000017986.2; ENSELUG00000017677.2.
DR GeneTree; ENSGT00940000156579; -.
DR Proteomes; UP000265140; LG23.
DR Bgee; ENSELUG00000017677; Expressed in embryo and 15 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR CDD; cd18666; CD1_tandem_CHD1-2_like; 1.
DR CDD; cd18661; CD2_tandem_CHD1-2_like; 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 InterPro; IPR040793; CDH1_2_SANT_HL1.
DR InterPro; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
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 PANTHER; PTHR45623:SF7; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF18375; CDH1_2_SANT_HL1; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 102..194
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 219..282
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 322..492
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 621..772
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1464..1563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..935
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1563 AA; 180373 MW; 0693A45C2ED2E118 CRC64;
MKHVGLKALV QNPRNHLSPV RATARNGKKS SVQRKKPSAG SSSEDNYDGK KKKKSSSSNQ
GPRRQATQNV SYKEDEEQKT DSDDLVEVCG EDVPPPEEDE FETLERVMET RIGRRGATGG
TTTVYAVEAD GDPNVNFNPA KEAGEQQYLI KWKGWSHIHN TWETEETLKM QNVKGMKKLD
NFKKKESDKR KWIKSSSPED VEYFNCQQEL MDDLHSQYQL VERIIGHSNQ KSAAGYPDYL
CKWQGLPYSE CSWEDGALIA RKYQKSIDDY MRRNQSKTIP SRDCKVLKQR PRFIPMKKQP
PYIGGDGLEL RDYQLDSLNW MAHSWCKGNS CILADEMGLG KTIQTISFLN YLFHEHQLYG
PFLLVVPLST LVSWQREIQL WAPLMNVVVY LGDISSRGMI RTHEWMHVQT KRLKLNILLT
TYEILLKDKA FLGHVPWAFI GVDEAHRLKN DDSLLYKTMM EFKSNHRLLI TGTPLQNSLK
ELWSLLHFIM PDKFHSWELF EEEHGKGRDS GYTSLHKELE PFLLRRVKKD VEKSLPAKVE
QILRVEMSAI QKQYYKWILT RNYKALSKGT KGSTSGFLNV MMELKKCCNH CYLIKPPEDT
EYYNKQEALQ HLIRSSGKLV LLDKLLLRLR ERGHRVLIFS QMVRMLDILA EYLKSRQFLF
QRLDGSIKGE MRKQALDHFN AEGSEDFCFL LSTRAGGLGI NLASADTVVI FDSDWNPQND
LQAQARAHRI GQKRQVNIYR LVTKSSVEEE IIERAKKKMV LDHLVIQRMD TTGKTVLHTG
TAPSSATPFN KEELSAILKF GAEELFKEPE GEEQEPQDMD IDDILKRAET RENDPGPSTV
GEELLSQFKV ANFSMMEEEE IVMDSGRHHR GWDEIIPEAQ RRQMEEEERQ KELEEIYLLP
RMRNCAKQIS FNGNESRRSR NRRYSGSDSD STSGRKRPKK RGRPRTIPRE NIKGFSDAEI
RRFIKSYKKF GGPLERLDAI ARDAELVDKS EFDLKRLAET VHNGCLKTLR ENPCGPEKTS
GGRRGKVKGP TFRISGVQVN AKLVISHEEE LAPLHKAIPA DPEERKRYTI PCHSKAAHFD
IDWGKEDDSS LLIGIYEYGY GSWEMIKMDP DLNLTHKLLP DDPDKKPQAK QLQTRADYLI
KLLSKDLAKK EAQRQAGTAN SRKRKPRSKK NKAVKPAKVD EVVKSPSSEP PSDKSSEEGD
DIEDEKVCGT PIPWEEEEEP HEPEVPSPTE EDEELKEREI KKDIKKEKKE ESRDVKEKKD
TKPLEPPSEL KAEIRDKAEV RDKAELREKP KKASDMPVHI TAAGDNVPIS EESEELDQKT
FSVCKERMRP VKAALKQLDR PEKGLSEREQ LEHTRQCLIK IGDHITECLK EYSNPEHIKQ
WRKNLWIFVS KFTEFDARKL HKLYKHAIKK RQENAQHNAF VPLWISGCKN GWNLCVGFLC
WSVVLMVVVP PCLRYYSDSK HRKVDDHRSS WDGRADSKER SHSDHRSGAD YPSSHQRSSS
RGDSYRYHTD WQMDHRASAS GPRSPRDQRS PYDGRSPLGH RSPFEYSSDH KSTPEQNWSS
RKT
//
