ID   M10B2_DANRE             Reviewed;        1015 AA.
AC   Q1LXK5;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Putative helicase mov-10-B.2;
DE            EC=3.6.4.13;
GN   Name=mov10b.2; ORFNames=si:dkeyp-38g6.3;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
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., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., 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).
CC   -!- FUNCTION: Probable RNA helicase. Required for RNA-mediated gene
CC       silencing by the RNA-induced silencing complex (RISC). Required for
CC       both miRNA-mediated translational repression and miRNA-mediated
CC       cleavage of complementary mRNAs by RISC (By similarity). {ECO:0000250}.
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=3.6.4.13;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. SDE3 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BX323059; CAK11381.1; -; Genomic_DNA.
DR   RefSeq; NP_001037805.1; NM_001044340.2.
DR   AlphaFoldDB; Q1LXK5; -.
DR   SMR; Q1LXK5; -.
DR   STRING; 7955.ENSDARP00000072953; -.
DR   PaxDb; Q1LXK5; -.
DR   PRIDE; Q1LXK5; -.
DR   Ensembl; ENSDART00000078491; ENSDARP00000072953; ENSDARG00000056065.
DR   GeneID; 555950; -.
DR   KEGG; dre:555950; -.
DR   CTD; 555950; -.
DR   ZFIN; ZDB-GENE-060526-371; mov10b.2.
DR   eggNOG; KOG1804; Eukaryota.
DR   GeneTree; ENSGT00940000156024; -.
DR   HOGENOM; CLU_001666_6_1_1; -.
DR   InParanoid; Q1LXK5; -.
DR   OMA; YVDQWHT; -.
DR   OrthoDB; 286011at2759; -.
DR   PhylomeDB; Q1LXK5; -.
DR   TreeFam; TF323999; -.
DR   PRO; PR:Q1LXK5; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 8.
DR   Bgee; ENSDARG00000056065; Expressed in liver and 12 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043186; C:P granule; IBA:GO_Central.
DR   GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR   GO; GO:0032574; F:5'-3' RNA helicase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0035279; P:miRNA-mediated gene silencing by mRNA destabilization; ISS:UniProtKB.
DR   GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IBA:GO_Central.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR045055; DNA2/NAM7-like.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR026122; MOV-10.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10887; PTHR10887; 1.
DR   PANTHER; PTHR10887:SF322; PTHR10887:SF322; 1.
DR   Pfam; PF13086; AAA_11; 2.
DR   Pfam; PF13087; AAA_12; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome; RNA-binding; RNA-mediated gene silencing.
FT   CHAIN           1..1015
FT                   /note="Putative helicase mov-10-B.2"
FT                   /id="PRO_0000374669"
FT   REGION          94..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           677..680
FT                   /note="DEAG box"
FT   COMPBIAS        100..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         555..562
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1015 AA;  116510 MW;  0895FC71E3B7E815 CRC64;
     MSRRNRNNYL SIAAVRTIGL DFIEMLEETN RRSISDRNTL TDIYNTEFRD RDGGVKDPNF
     SRVLYALRNA NKARLSRTGR VYFNTNVRTG LHDQWFRPRR RQQNQANATP GNVSSVTPSS
     DQGPSCPESG VRARRKLVKY ILQRLNTTDR SHFIADKWGV RVSSELYIED GKIRISVDEA
     EVYELKLFVE NTGQEAVYFT YYTALCWLQY FTLEDSRKVT RNNPLRLEPR EKYEVIVRFK
     SSHVGVYSAT LAFEFKKNTQ PTTRSFHIVR FIEAEYRSKL AALLGPTEPY KPLRLNISEP
     ENCIIDEGFP PDGYLQNFLV NVLPLGKYIP PPDTTILAEL LKEDCSSRIF RGKLKDLQSL
     LQSPLTFDNY AERFDLLLYL EECQMHVDIK RYNKDSVTLH RDRDKRLMGL NLPGVSENRP
     SVLRGDHLLL TKSEEVTFSN VTKYKGYVHR VELDQVKLGL SKRFLKDVYI DKMKFRVEFT
     VNRIPVRLQH RAVHMAVQHN LKDVLFPMAS RSLNPVSPPA LRLFDRKLEY NFQQYSAVCN
     IVAGTSKPAP YLVFGPPGTG KTVTIVEAIK QVEKNIPDAY ILACAPSNSA ADQLCEKLIT
     SEHVDAHKIY RLYASSRNQK DIPKILKDNC NVDEEMIDFP CKEDLMSYKI LICTLVTAGR
     LVTGGFSEDH FTHNFVDEAG HAVESETIIS VAGLLNAEKG QLVLAGDPKQ LGPILRSPLA
     INHGLDVSLL ERLMTQNDLY KRGDVEFDNR YVSKLIMNYR SHPYILEVPN RLFYDGELKA
     CADEISSNQY CMWEHLPSKG FPVIFHGVPG KDERESNSPS FFNIYEINIL VDYLKKLLLT
     QPKKGISRIF PKDIGIIAPY RKQVEKIKRA IDADKDFQDY MGIDNLKVGS VEEFQGQERK
     VIMVSTVRSS VKYISLDETF NIGFLKNEKR FNVAVTRAKS LLIMVGNPMI LRTDESWGRF
     IDFCLERGGY TGISITSVER IDDVESRLLA LNIQDEETEE SPVQRYVDPE FRNDY