ID   DDX6_XENTR              Reviewed;         481 AA.
AC   Q0IHV9; B1WAU0;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Probable ATP-dependent RNA helicase ddx6;
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:P26196};
DE   AltName: Full=DEAD box protein 6;
GN   Name=ddx6;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula, and Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent RNA helicase that is an integral component of
CC       messenger ribonucleoprotein complexes (mRNPs), storage particles that
CC       mask maternal mRNAs from the translational apparatus during oocyte
CC       maturation. {ECO:0000250|UniProtKB:P54824}.
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         Evidence={ECO:0000250|UniProtKB:P26196};
CC   -!- SUBUNIT: Component of a ribonucleoprotein (RNP) complex, composed at
CC       least of cpeb1, lsm14b/rap55b, ddx6/Xp54, ybx2/frgy2, pat1/P100,
CC       eif4enif1/4E-T and eif4e1b. Component of a ribonucleoprotein (RNP)
CC       complex, composed at least of elavl1/elrA and/or elavl2/elrB,
CC       igf2bp3/vg1RBP, ddx6/Xp54, ybx2/frgy2, lsm14b/rap55b and, in a subset
CC       of RNP complexes, stau1/staufen. Component of a ribonucleoprotein (RNP)
CC       complex, composed at least of lsm14a/rap55a, ybx2/frgy2, ddx6/Xp54 and
CC       eif4enif1/4E-T. Interacts with lsm14a/rap55a (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:P26196}.
CC       Cytoplasm {ECO:0000250|UniProtKB:P26196}. Nucleus
CC       {ECO:0000250|UniProtKB:P26196}. Note=Mostly cytoplasmic. Upon cellular
CC       stress, relocalizes to stress granules. {ECO:0000250|UniProtKB:P26196}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1
CC       subfamily. {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; BC122944; AAI22945.1; -; mRNA.
DR   EMBL; BC161499; AAI61499.1; -; mRNA.
DR   RefSeq; NP_001072584.1; NM_001079116.1.
DR   AlphaFoldDB; Q0IHV9; -.
DR   SMR; Q0IHV9; -.
DR   STRING; 8364.ENSXETP00000058366; -.
DR   PaxDb; Q0IHV9; -.
DR   DNASU; 780039; -.
DR   GeneID; 780039; -.
DR   KEGG; xtr:780039; -.
DR   CTD; 1656; -.
DR   Xenbase; XB-GENE-922227; ddx6.
DR   eggNOG; KOG0326; Eukaryota.
DR   HOGENOM; CLU_003041_30_0_1; -.
DR   InParanoid; Q0IHV9; -.
DR   OrthoDB; 583315at2759; -.
DR   PhylomeDB; Q0IHV9; -.
DR   Reactome; R-XTR-430039; mRNA decay by 5' to 3' exoribonuclease.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000010061; Expressed in skeletal muscle tissue and 13 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000932; C:P-body; 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:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISS:UniProtKB.
DR   GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR   GO; GO:0033962; P:P-body assembly; ISS:UniProtKB.
DR   GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR   GO; GO:0034063; P:stress granule assembly; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Developmental protein; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribonucleoprotein;
KW   RNA-binding.
FT   CHAIN           1..481
FT                   /note="Probable ATP-dependent RNA helicase ddx6"
FT                   /id="PRO_0000274534"
FT   DOMAIN          126..297
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          307..467
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           95..123
FT                   /note="Q motif"
FT   MOTIF           245..248
FT                   /note="DEAD box"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         139..146
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   481 AA;  53984 MW;  A5D4F136641E37DC CRC64;
     MSTARTENPV LMGMSSQNGQ LRGPLKPSAG PGGGGTQTQQ INQLKNASTI NSGSQQQAQS
     MSSVIKPGDD WKKTLKLPPK DLRIKTSDVT STKGNEFEDY CLKRELLMGI FEMGWEKPSP
     IQEESIPIAL SGRDILARAK NGTGKSGAYL IPLLERLDLK KDCIQAMVIV PTRELALQVS
     QICIQVSKHM GGVKVMATTG GTNLRDDIMR LDDTVHVVIA TPGRILDLIK KGVAKVDHIQ
     MIVLDEADKL LSQDFVQIME DIIITLPKNR QILLYSATFP LSVQKFMTSH LQKPYEINLM
     EELTLKGVTQ YYAYVTERQK VHCLNTLFSR LQINQSIIFC NSSQRVELLA KKISQLGYSC
     FYIHAKMRQE HRNRVFHDFR NGLCRNLVCT DLFTRGIDIQ AVNVVINFDF PKLAETYLHR
     IGRSGRFGHL GLAINLITYD DRFNLKSIEE QLGTEIKPIP SSIDKSLYVA EYHSESGEDK
     P