DDX6_DICDI
ID DDX6_DICDI Reviewed; 423 AA.
AC Q54E49;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Probable ATP-dependent RNA helicase ddx6;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 6;
GN Name=ddx6; ORFNames=DDB_G0291804;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: ATP-dependent RNA helicase which may be involved in mRNA
CC turnover. {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|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 -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000185; EAL61523.1; -; Genomic_DNA.
DR RefSeq; XP_629938.1; XM_629936.1.
DR AlphaFoldDB; Q54E49; -.
DR SMR; Q54E49; -.
DR STRING; 44689.DDB0234196; -.
DR PaxDb; Q54E49; -.
DR EnsemblProtists; EAL61523; EAL61523; DDB_G0291804.
DR GeneID; 8628344; -.
DR KEGG; ddi:DDB_G0291804; -.
DR dictyBase; DDB_G0291804; ddx6.
DR eggNOG; KOG0326; Eukaryota.
DR HOGENOM; CLU_003041_30_0_1; -.
DR InParanoid; Q54E49; -.
DR OMA; VCADEAP; -.
DR PhylomeDB; Q54E49; -.
DR Reactome; R-DDI-430039; mRNA decay by 5' to 3' exoribonuclease.
DR PRO; PR:Q54E49; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:0033962; P:P-body assembly; IBA:GO_Central.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; mRNA processing;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..423
FT /note="Probable ATP-dependent RNA helicase ddx6"
FT /id="PRO_0000327431"
FT DOMAIN 80..250
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 260..420
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 49..77
FT /note="Q motif"
FT MOTIF 198..201
FT /note="DEAD box"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 423 AA; 48171 MW; A17EFF57544AF924 CRC64;
MNSQQNKLPQ QPQQPPSSIV DDDNWKSQLK LPPRDERRQT EDVTATEGND FDDLHLKRDL
LRGIFEKGYV KPSPIQEKAI PIALAGRDIM ARAKNGTGKT ASFLIPALEK TDPTKDVIQV
LILVPTRELA LQTSQVCKEL GKYMNVQVMA STGGTSLKDD IMRLYNPVHI LVATPGRVLD
LAQKNVANLS NCHTMIMDEA DKLLSQEFQP LVEQLINFLP QQRQILLFSA TFPVTVKSFK
EHYLQQAFEI NLMEELTLKG VTQYYAFVEE RQKIHCLNTL FSKLQINQSI IFCNSVNRVE
LLAKKITELG YSCFFIHAKM VQAHRNRVFH DFRNGACRNL VSSDLFTRGI DIQDVNVVIN
FDFPKHSETY LHRIGRSGRF GHLGLAINLI TYEDRFSLYK IEQELGTEIK PIPPVIDKSL
YAA
