ID Q498Z7_DANRE Unreviewed; 639 AA.
AC Q498Z7; A0A0R4ICY7; A0A8M1N9Y1; F1Q4T3;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN Name=recql {ECO:0000313|EMBL:AAI00013.1,
GN ECO:0000313|Ensembl:ENSDARP00000130578,
GN ECO:0000313|RefSeq:NP_001038561.2,
GN ECO:0000313|ZFIN:ZDB-GENE-050809-134};
GN Synonyms=zgc:110631 {ECO:0000313|RefSeq:NP_001038561.2};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI00013.1};
RN [1] {ECO:0000313|EMBL:AAI00013.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Singapore local strain {ECO:0000313|EMBL:AAI00013.1};
RC TISSUE=Embryo {ECO:0000313|EMBL:AAI00013.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSDARP00000130578, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000130578};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|RefSeq:NP_001038561.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore {ECO:0000313|RefSeq:NP_001038561.2};
RX PubMed=24922577;
RA van der Vaart M., Korbee C.J., Lamers G.E., Tengeler A.C., Hosseini R.,
RA Haks M.C., Ottenhoff T.H., Spaink H.P., Meijer A.H.;
RT "The DNA damage-regulated autophagy modulator DRAM1 links mycobacterial
RT recognition via TLR-MYD88 to autophagic defense [corrected].";
RL Cell Host Microbe 15:753-767(2014).
RN [4] {ECO:0000313|RefSeq:NP_001038561.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore {ECO:0000313|RefSeq:NP_001038561.2};
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [5] {ECO:0000313|Ensembl:ENSDARP00000130578}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000130578};
RG Ensembl;
RL Submitted (NOV-2015) to UniProtKB.
RN [6] {ECO:0000313|RefSeq:NP_001038561.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore {ECO:0000313|RefSeq:NP_001038561.2};
RX PubMed=27189481;
RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA Bobe J.;
RT "Gene evolution and gene expression after whole genome duplication in fish:
RT the PhyloFish database.";
RL BMC Genomics 17:368-368(2016).
RN [7] {ECO:0000313|RefSeq:NP_001038561.2}
RP IDENTIFICATION.
RC STRAIN=Singapore {ECO:0000313|RefSeq:NP_001038561.2};
RG RefSeq;
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 ECO:0000256|RuleBase:RU364117};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364117}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446, ECO:0000256|RuleBase:RU364117}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX510924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX914215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU463209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC100012; AAI00013.1; -; mRNA.
DR RefSeq; NP_001038561.2; NM_001045096.2.
DR PaxDb; 7955-ENSDARP00000091972; -.
DR Ensembl; ENSDART00000162204.2; ENSDARP00000134146.1; ENSDARG00000007175.12.
DR Ensembl; ENSDART00000172169.2; ENSDARP00000130578.2; ENSDARG00000007175.12.
DR GeneID; 566018; -.
DR KEGG; dre:566018; -.
DR AGR; ZFIN:ZDB-GENE-050809-134; -.
DR CTD; 5965; -.
DR ZFIN; ZDB-GENE-050809-134; recql.
DR eggNOG; KOG0353; Eukaryota.
DR HOGENOM; CLU_001103_12_5_1; -.
DR OrthoDB; 5474026at2759; -.
DR Proteomes; UP000000437; Chromosome 4.
DR Bgee; ENSDARG00000007175; Expressed in testis and 38 other cell types or tissues.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR CDD; cd18015; DEXHc_RecQ1; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF72; ATP-DEPENDENT DNA HELICASE Q1; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364117};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364117};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364117};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364117}; Nucleus {ECO:0000256|RuleBase:RU364117};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q498Z7};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT DOMAIN 106..281
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 304..455
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 587..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..38
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 591..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 639 AA; 72099 MW; ACA8B1DCD54B3F12 CRC64;
MANVDDAREE LDSVEAELEM VELQISELLE KQTRLNSRKN KLLKVLEGAC SSAQPSGSGK
TPKSSFSKQD LQHYEDSDFS WSKEVQVNLC NIFQLSKFRP LQRAAINLSM SGKDLFLVMP
TGRGKSLCYQ LPALCSKGFT LVIAPLVSLM EDQLMYLQSV NVPAVTLNAS SSKEDSKRIL
AGMTDKNSPF KLLYVTPEKI AKSKLLMSKL EKAFNMGLLA RIAVDEVHCC SQWGHDFRPD
YKLLGILKRQ FPNVPLIGLT ATATSNVLKD CQKILCVQEP VTLTAPFNRP NLYYEVRFKD
NEDCTDQIAS LIRGRYKNQS GIVYVFSQKD AEVVATELQK RDIVAQPYHA NMEPSHKSLV
HQRWSSKKIQ VVVATVAFGM GIDKADVRFV IHHTISKSIE NYYQESGRAG RDDSPADCIV
FFGFMDIFRI STMVVMENTG QQKLHNMVAY CQNVDRCRRA MMAIHFDEVW NDEECNEMCD
VCRHGNDYIT MDITQHARDV LHIVELASSM DEKLTPLKVC DAWLGKGPAK QRKMIKLTSL
SRLEVESVII HLLLHGYFSE DFSFTPYTTH FYLKLGRKAA LLKNSGHSIT MKMRRRGTSQ
STVKKVSESS GEKSRSKVEG KRPAESGDQK SAKKVKPLP
//
