ID   MOV10_CHICK             Reviewed;         967 AA.
AC   Q5ZKD7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Putative helicase MOV-10;
DE            EC=3.6.4.13;
GN   Name=MOV10; ORFNames=RCJMB04_11i10;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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   -!- FUNCTION: 5' to 3' RNA helicase contributing to UPF1 mRNA target
CC       degradation by translocation along 3' UTRs. Required for microRNA
CC       (miRNA)-mediated gene silencing by the RNA-induced silencing complex
CC       (RISC). Required for both miRNA-mediated translational repression and
CC       miRNA-mediated cleavage of complementary mRNAs by RISC. In cooperation
CC       with FMR1, regulates miRNA-mediated translational repression by AGO2
CC       (By similarity). May function as a messenger ribonucleoprotein (mRNP)
CC       clearance factor (By similarity). {ECO:0000250|UniProtKB:Q9HCE1}.
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|UniProtKB:Q9HCE1}.
CC       Cytoplasm, Cytoplasmic ribonucleoprotein granule
CC       {ECO:0000250|UniProtKB:Q9HCE1}. Cytoplasm, Stress granule
CC       {ECO:0000250|UniProtKB:Q9HCE1}. Nucleus {ECO:0000250|UniProtKB:P23249}.
CC       Cytoplasm {ECO:0000250|UniProtKB:P23249}.
CC   -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. SDE3 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ720147; CAG31806.1; -; mRNA.
DR   RefSeq; NP_001012861.1; NM_001012843.1.
DR   AlphaFoldDB; Q5ZKD7; -.
DR   SMR; Q5ZKD7; -.
DR   STRING; 9031.ENSGALP00000002366; -.
DR   PaxDb; Q5ZKD7; -.
DR   PRIDE; Q5ZKD7; -.
DR   GeneID; 419872; -.
DR   KEGG; gga:419872; -.
DR   CTD; 4343; -.
DR   VEuPathDB; HostDB:geneid_419872; -.
DR   eggNOG; KOG1804; Eukaryota.
DR   InParanoid; Q5ZKD7; -.
DR   OrthoDB; 286011at2759; -.
DR   PhylomeDB; Q5ZKD7; -.
DR   PRO; PR:Q5ZKD7; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISS:UniProtKB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR   GO; GO:0035195; P:miRNA-mediated gene silencing; ISS:UniProtKB.
DR   GO; GO:0035279; P:miRNA-mediated gene silencing by mRNA destabilization; ISS:UniProtKB.
DR   GO; GO:0010526; P:negative regulation of transposition, RNA-mediated; ISS:UniProtKB.
DR   GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
DR   GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IBA:GO_Central.
DR   GO; GO:0150011; P:regulation of neuron projection arborization; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; RNA-binding; RNA-mediated gene silencing.
FT   CHAIN           1..967
FT                   /note="Putative helicase MOV-10"
FT                   /id="PRO_0000374667"
FT   REGION          85..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           638..641
FT                   /note="DEAG box"
FT   BINDING         516..523
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   967 AA;  109051 MW;  E894F36240C094FB CRC64;
     MPRFSVAEAR RYGDQFVQFL RDPSREQESR REVLRDIYSQ EFRTRTDIRT PSFSSILYAL
     RVSHQAQVHG QTVHFKKARR RVVVADQYRR PRTDTEVSAP APGQQPSSGP PAPQSRAKKW
     AEFIRGKHGV EIVSEYDQAN GQIRFPVALD KTKTFTVQVQ NHGAEAVTLH RCRPLRRLQE
     LSFLDEQGVT QGQALVLHPG GAYPIQVRCL TSHNGFFRAV VMFEFSKEPD GSFSIGRSIA
     AIAQSPLARE LGPSAPYRPY QASLQRPITV VTEDGVPPVS SLKNELEKEI PLGTYPYPKS
     LKETIMLGPK TSPDSSWMKM QSLLEAPLQP ENYKQKFELL LHLEEIQLEV DIRRYDLQEV
     PMVQNRALLL LNVPGVAENR PSVLRGDHLF ASLSSERDSS PRVLYKGYVH GVELERVQLG
     FSPKLMKKFV NDLKFDVTFT FNRLPLQVQH RAAAMAMQKG LDSVLFPSAS CQRSLFTGIF
     QPRWFDRKVE ANEEQCQAVK HIVTGMSRPA PYLIFGPPGT GKTVTLVEAI KQVWSCFKDA
     RILACAPSNS AADLLCQRLL TNIAPRYIYR IMASSANYKD VPADVRPCCN WDDSEKCYVY
     PSKKLLKPYR ILITTLVTAG RLVSANFPPG YFSHVFIDEC GHAVEPESVV AIAGLLTTMD
     PDTNPNGGQL VLAGDPQQLG PVPRSPLAAQ HGLGTSLLER LMLHNALYAK SDEGYNPQFV
     TKLLWNYRSH KAILKVPNEL FYDSELKAYE GSEPDVRNFY CTWEELPNRG VPIIFHGVCG
     EDEREAKSPS FFNTAEIEVV VQYLQKLLQS QGRRGCPTIS PKEIGIISPY RKQVEKIRLA
     ITSKDPVLRA LPDIGQLKVG SVEEFQGQER RVILISTVRS CSEYLQLDQT FRLGFLKNPK
     RLNVALTRAK ALLIVVGNAA VLSKDPHWHR FLRYCRDEGA YRGYPYEEEP PEEDSLANHL
     DSLHLGN