DDX3_DICDI
ID DDX3_DICDI Reviewed; 712 AA.
AC Q54QS3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable ATP-dependent RNA helicase ddx3;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 3;
GN Name=ddx3; ORFNames=DDB_G0283661;
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: Probable ATP-binding RNA helicase which may be involved in
CC translation initiation. {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 {ECO:0000250}.
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. DDX3/DED1
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000056; EAL65597.1; -; Genomic_DNA.
DR RefSeq; XP_638950.1; XM_633858.1.
DR AlphaFoldDB; Q54QS3; -.
DR SMR; Q54QS3; -.
DR STRING; 44689.DDB0233447; -.
DR PaxDb; Q54QS3; -.
DR PRIDE; Q54QS3; -.
DR EnsemblProtists; EAL65597; EAL65597; DDB_G0283661.
DR GeneID; 8624189; -.
DR KEGG; ddi:DDB_G0283661; -.
DR dictyBase; DDB_G0283661; ddx3.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; Q54QS3; -.
DR OMA; KTAWANR; -.
DR PhylomeDB; Q54QS3; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q54QS3; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; ISS:dictyBase.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd17967; DEADc_DDX3_DDX4; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044763; Ded1/Dbp1_DEADc.
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; Initiation factor;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..712
FT /note="Probable ATP-dependent RNA helicase ddx3"
FT /id="PRO_0000327417"
FT DOMAIN 278..467
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 477..638
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 247..275
FT /note="Q motif"
FT MOTIF 411..414
FT /note="DEAD box"
FT COMPBIAS 1..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 267..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 291..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 712 AA; 78958 MW; 3F4231A6C9241F45 CRC64;
MPIGNNKDND GTTLNISGLT ISDKSSSTSS NNNTTTTTTQ TSEPYVPPSR RNKMNNSSGS
SRDDYPSPSD RDNRDSPFNR DRRDDGYRGG NNFRENNSNN NNNSRDNYKS PSFSRNNNSN
GGGSSSGSGG WDNGPREQGP PRGNSYSYSP NNSFSRGGNQ GGYGNRGGSG SSFGKPANKN
DRYYDRWSNF RDSRNHPEMK REFIDLEEHK AEEIFKKNDD NIGIDFNAYD DDDISIETSE
HICAPLNSFA DVDLGDVLLG NIKHAKYTKP TPVQKSALPI ILKNRDLMAC AQTGSGKTAA
FLFPIISGIL LDGAPEAPPA YKPGVPRAAC PRALVLAPTR ELAQQIFDEA NKFSYGSPVS
SVVIYGGAEV FHQINELDRG CDILVATTGR LVDLLMRGRV SLSKIKYLVL DEADRMLDMG
FEPQIRQIIS EFDMPGCRDR QTLMFSATFP KQIQNLAADF LYNYIFLKVG VVGTTQNITQ
RIEYVVEEDK NSYLLDYLSG LKSDGLCLIF VETKRSCDTL TYFLNQRNFP TTCIHGDLTQ
PERENALQSF RSFATPFLVA TDIASRGLHI GNVNLVINFD LPTDIHIYVH RIGRTGRAGK
KGLAISFFNE KNKPVGAELL KLMKASNQDI PDWFEKMVHN LRMSKGPSNS KSNSPFNKSY
NSHHNRDDNR GGYGGGGGGN GGYSNNRNDR REDKSDYSMH HPYFSNNGGS YN
