ID   M10B1_DANRE             Reviewed;        1013 AA.
AC   Q1LXK4;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Putative helicase mov-10-B.1;
DE            EC=3.6.4.13;
GN   Name=mov10b.1; ORFNames=si:dkeyp-38g6.2;
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;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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; BX323059; CAK11382.2; -; Genomic_DNA.
DR   EMBL; BC171375; AAI71375.1; -; mRNA.
DR   RefSeq; NP_001037807.2; NM_001044342.2.
DR   AlphaFoldDB; Q1LXK4; -.
DR   SMR; Q1LXK4; -.
DR   STRING; 7955.ENSDARP00000081380; -.
DR   PaxDb; Q1LXK4; -.
DR   Ensembl; ENSDART00000086946; ENSDARP00000081380; ENSDARG00000061177.
DR   GeneID; 556024; -.
DR   KEGG; dre:556024; -.
DR   CTD; 556024; -.
DR   ZFIN; ZDB-GENE-030131-9089; mov10b.1.
DR   eggNOG; KOG1804; Eukaryota.
DR   GeneTree; ENSGT00940000156024; -.
DR   HOGENOM; CLU_001666_6_1_1; -.
DR   InParanoid; Q1LXK4; -.
DR   OMA; NSIAEMW; -.
DR   OrthoDB; 286011at2759; -.
DR   PhylomeDB; Q1LXK4; -.
DR   TreeFam; TF323999; -.
DR   PRO; PR:Q1LXK4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 8.
DR   Bgee; ENSDARG00000061177; Expressed in spleen and 17 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; IPR003593; AAA+_ATPase.
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   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome; RNA-binding; RNA-mediated gene silencing.
FT   CHAIN           1..1013
FT                   /note="Putative helicase mov-10-B.1"
FT                   /id="PRO_0000374668"
FT   REGION          91..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           672..675
FT                   /note="DEAG box"
FT   COMPBIAS        91..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         550..557
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1013 AA;  116407 MW;  47A227CE99D1CC9F CRC64;
     MSRKYRKKLS RDDIRAVGFD FIEFLDDRET RSTTDRNTLK EIYNEQFRDR DGVRDPNFSS
     VLFALTRSSR TRVTRSEVFF DKKIRVRQND QWSRPYRSQQ NHATPHLNDA ISRPSTTRVS
     DPSSVPEPEN RVIARRRLAK TIMRQGNSED MSVFFADKYG VRVSSELQIE DGKIHWCVEG
     AEVHELKLFV ENTGQEAILF TCFSALHYLQ YFTLDDSQRV RKDNPHRLEP NETYEVILRF
     KSDQIGVYPA TLAFEFKENQ DTRPFHIVRF IEAQHRSELT AQLGPTEPFR PKRLDTNQPM
     KWSIDEGFKP ESSSQNFLKF VVPLDNYNCP SYTSALIEVL KGNRSSGKQL QEHQLTLESD
     LSFNNYMDRF DLLLYLEEDQ MRMDIKRYNK KDVSMVRDRD KKLLVLELPG VSENRPSVLR
     GDHLLLTKSE ELQNSNVTKY KGYVHRVELD QVKLGFSKRL LERFIDNMKF SVEFTINRLP
     LRLQHRAVHM VVQHHLKDVL FPVASRRLNP VSPSALRLFD QKLEKNPEQK TAVCNIVAGT
     SKPAPYLVFG PPGTGKTVTI VEAIKQVEKN TGGARILACA PSNSAADQLG EKLITSQHVD
     ARNIYRIYAS SRNPKEIPKV LENNSNVEGE NIIFPCKEDL MPYKIVVCTL VTAGRLVSGG
     FPVGHFSHIF VDEAGHAVEP EIVISVAGLL NAETGQLVLA GDPKQLGPIL RSPFAIKYGL
     GLSLLERLMT QNELYQKGDT GFDNRYVTKL LQNYRSHPSI LKVPNELFYD NELKACADEI
     SSRQYCTWEH LPKRGFPVIF HGVVGKDERE STSPSFFNTS EIDKIMDYLK KLLLTQAKKG
     IAKISPKDIG IIAPYRKQVE KIRQAIKIHR ELKSLSGIEE LKVGSVEEFQ GQERKVIIVS
     TVRSSKEHII LDDKFNIGFL KNEKRFNVAV TRAKALLIMV GNPIILRTDE IWGRFMNYCI
     QERGYTGYDI THLEETDVIA ERLLSLNIRQ EITVETEESV VQQFLSPPWR HEH