ID A0A3P9ABI0_ESOLU Unreviewed; 1508 AA.
AC A0A3P9ABI0;
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:ENSELUP00000038060.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000038060.2, 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:ENSELUP00000038060.2}
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 STRING; 8010.ENSELUP00000038060; -.
DR Ensembl; ENSELUT00000028227.2; ENSELUP00000038060.2; ENSELUG00000017981.2.
DR GeneTree; ENSGT00940000155888; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000265140; LG19.
DR Bgee; ENSELUG00000017981; Expressed in nose and 14 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; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.140.1440; -; 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 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:SF19; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 2; 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 1..68
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 87..164
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 204..374
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 502..653
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 763..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1062
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1377..1393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1508 AA; 173930 MW; 4E65D0C0D14A1CF7 CRC64;
VEENGDPGAD FDPEKDEGET HYLIKWKGWS YIHNTWESIE SLTQQKVKGL KKIENFKKKN
DDKASPEDSE YFNCQQELTT DLNKQFHILE RVIASKTGKT QGPSDFPCNH KNASSSNEPE
YLCKWMGLPY SECSWEDGAL LKKKYQHCID SFINRNSSKT VPSKDCKVLK QRPRFVALKK
QPSYIGDENL QLRDYQLDGL NWLAHSWCRC NSVILADEMG LGKTIQTISF LSYLFHQHQL
YGPFLVVVPL STLTSWQREF ETWAPDMNVV VYLGDVMSRK SIRDYEWVCH QTKRIKFNAL
ITTYEILLKD KAVLGNINWA FLGVDEAHRL KNDDSLLYKT LIEFRSNHRL LITGTPLQNS
LKELWSLLHF LMPDKFENWE DFESEHGKGT DNGYQSLHKV LEPFLLRRVK KDVEKSLPAK
VEQILRVDMS AVQKQYYKWI LTRNYRALQK GTRGSSSGFL NIVMELKKCT NHGFLIKQPE
EECETQQEHL QALVRGSGKL VLLDKLLTRL RERGNRVLIF SQMVRMLDIL AEYLALKRYP
FQRLDGSIKG EIRKQALDHF NAEGSEDFCF LLSTRAGGLG INLASADTVV IFDSDWNPQN
DLQAQARAHR IGQKKQVNIY RLVTKGTVEE DIIERAKKKM VLDHLVIQRM DTTGRTVLDN
NSGNSNSNPF NKDELTAILK FGAEDLFKEA EGEETEPTEM DIDEILRLAE TRESDQGSSA
TDELLSQFKV ANFSNMEESA PELVERMVPD WDDIIPEDQR RRLEEEQKQK EMEDIYMLPR
SRSSNKRAQA NDSDSDVGSK LKHHSSGSES ETDDSDDDKK PKRRGRPRAR KNNVEGFTDA
EIRRFIKAYK KFGAPLERLE CVARDSELVD KSQADLKRLG ELIHNSCVTA VQEHEEHLRE
NPGEAKGPGK RRGINIKISG VQVNAKSIIQ HEEEFESLHK AVSANPAERN KFELTCRVKV
PHFDVDWDLQ DDTQLLLGVY EHGYGNWDLI KTDPELKLSE KILPDDTEKK PQGKQLQARV
DYLLKILKKE AENKDATKEE AKVKKRKPWV RKENKAPKDE QGNDISSPRL SDNPSEEGEV
KDEGTEKAPI KKRQKKKDNK ENKEKQGTTK KEKEGDKEKK RPKPKKEKAK GAKGKKPQGP
VHITAGSDPV PIGEEDDELD QETFSVCKER MRPVKKALKQ LDKPDDGLSV QEQLQHTRTC
LLKIGDRITE CLKAYSDPEH VKTWRRNLWI FVSKFTEFGA RKLHKLYKMA QKKRSQEEEE
HRKKGDDVSS KKKPFRAEAS GSSRDSTSTQ PSSKSHSGMP HPSPTSPHGH HREGYNQSNK
RHFGNDDRGD WQRDRKYNYP GNSNQSWQGE RHHPYDAHRY KDHHYGDRHP REDSYRSSSS
SYRSGSSSSP RKRPYDQYDN DRDHRDRRAY YDRHQDSKRR RGDDFRPPQE FRSGGGHPQD
FRGRMPEHRG PPGPAGPEHF TRPYPDNKPP LLLDPRSPQA QKSPQDSRSP PAEQKPAGSD
VNWNNRKT
//
