DDX6_CHICK
ID DDX6_CHICK Reviewed; 483 AA.
AC Q5ZKB9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
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; ORFNames=RCJMB04_11n24;
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: Essential for the formation of P-bodies, cytosolic membrane-
CC less ribonucleoprotein granules involved in RNA metabolism through the
CC coordinated storage of mRNAs encoding regulatory functions. Plays a
CC role in P-bodies to coordinate the storage of translationally inactive
CC mRNAs in the cytoplasm and prevent their degradation.
CC {ECO:0000250|UniProtKB:P26196}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:P26196}.
CC Cytoplasm {ECO:0000250|UniProtKB:P26196}. Nucleus
CC {ECO:0000250|UniProtKB:P26196}. Note=Upon cellular stress, relocalizes
CC to stress granules. {ECO:0000250|UniProtKB:P26196}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ720165; CAG31824.1; -; mRNA.
DR RefSeq; NP_001268976.1; NM_001282047.3.
DR RefSeq; XP_015153490.1; XM_015298004.1.
DR AlphaFoldDB; Q5ZKB9; -.
DR SMR; Q5ZKB9; -.
DR BioGRID; 680837; 1.
DR STRING; 9031.ENSGALP00000039796; -.
DR PaxDb; Q5ZKB9; -.
DR Ensembl; ENSGALT00000058124; ENSGALP00000046305; ENSGALG00000033064.
DR Ensembl; ENSGALT00000107898; ENSGALP00000065105; ENSGALG00000033064.
DR GeneID; 419783; -.
DR KEGG; gga:419783; -.
DR CTD; 1656; -.
DR VEuPathDB; HostDB:geneid_419783; -.
DR eggNOG; KOG0326; Eukaryota.
DR GeneTree; ENSGT00900000141067; -.
DR InParanoid; Q5ZKB9; -.
DR OMA; VCADEAP; -.
DR OrthoDB; 583315at2759; -.
DR PhylomeDB; Q5ZKB9; -.
DR TreeFam; TF300440; -.
DR PRO; PR:Q5ZKB9; -.
DR Proteomes; UP000000539; Chromosome 24.
DR Bgee; ENSGALG00000033064; Expressed in cerebellum and 12 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: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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; RNA-binding.
FT CHAIN 1..483
FT /note="Probable ATP-dependent RNA helicase DDX6"
FT /id="PRO_0000274533"
FT DOMAIN 127..298
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 308..468
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 96..124
FT /note="Q motif"
FT MOTIF 246..249
FT /note="DEAD box"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 483 AA; 54418 MW; 3BDAD7762260AC94 CRC64;
MSTARTENPV IMGLSSQNGQ LRGPVKPSGG PGGGGTQTQQ QMNQLKNANT INNGTQQQAQ
SMTTTIKPGD DWKKTLKLPP KDLRIKTSDV TSTKGNEFED YCLKRELLMG IFEMGWEKPS
PIQEESIPIA LSGRDILARA KNGTGKSGAY LIPLLERLDL KKDNIQAMVI VPTRELALQV
SQICIQVSKH MGGAKVMATT GGTNLRDDIM RLDDTVHVVI ATPGRILDLI KKGVAKVEHV
QMIVLDEADK LLSQDFVQIM EDIILTLPKN RQILLYSATF PLSVQKFMNS HLQKPYEINL
MEELTLKGVT QYYAYVTERQ KVHCLNTLFS RLQINQSIIF CNSSQRVELL AKKISQLGYS
CFYIHAKMRQ EHRNRVFHDF RNGLCRNLVC TDLFTRGIDI QAVNVVINFD FPKLAETYLH
RIGRSGRFGH LGLAINLITY DDRFNLKSIE EQLGTEIKPI PSNIDKSLYV AEYHSEPVED
EKQ
