DED1_ASPCL
ID DED1_ASPCL Reviewed; 681 AA.
AC A1CH78;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=ATP-dependent RNA helicase ded1;
DE EC=3.6.4.13;
GN Name=ded1; ORFNames=ACLA_046980;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: ATP-binding RNA helicase involved in translation initiation.
CC Remodels RNA in response to ADP and ATP concentrations by facilitating
CC disruption, but also formation of RNA duplexes (By similarity).
CC {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; DS027054; EAW10233.1; -; Genomic_DNA.
DR RefSeq; XP_001271659.1; XM_001271658.1.
DR AlphaFoldDB; A1CH78; -.
DR SMR; A1CH78; -.
DR STRING; 5057.CADACLAP00004486; -.
DR PRIDE; A1CH78; -.
DR EnsemblFungi; EAW10233; EAW10233; ACLA_046980.
DR GeneID; 4704355; -.
DR KEGG; act:ACLA_046980; -.
DR VEuPathDB; FungiDB:ACLA_046980; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_16_3_1; -.
DR OMA; CYRSWVR; -.
DR OrthoDB; 595675at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IEA:EnsemblFungi.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:EnsemblFungi.
DR GO; GO:1990625; P:negative regulation of cytoplasmic translational initiation in response to stress; IEA:EnsemblFungi.
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..681
FT /note="ATP-dependent RNA helicase ded1"
FT /id="PRO_0000281686"
FT DOMAIN 220..413
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 424..585
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 189..217
FT /note="Q motif"
FT MOTIF 357..360
FT /note="DEAD box"
FT COMPBIAS 75..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 233..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 681 AA; 72165 MW; 0605F9D822DA46FD CRC64;
MADGLNMGNL SLNDSQHAPA GPGNTGRAAY IPPHLRGRAG GANVDAAAAA APPPGPAAWN
GPRQGAPPRG GNWANANASD FSPRAPSGPN GNNSWTPSEG QRRPFDPHAY GHPGHGGSYG
GSQGASTRGS GDGQWRDGKH IPGPANARLE RELFGVPNDP TKQSTGINFA NYDDIPVEAS
GQDVPEPVNA FTNPPLDDHL ISNIKLARYQ TPTPVQKYSI PIVMNGRDLM ACAQTGSGKT
GGFLFPILSQ AFQKGPSAVP AQASGQMSYG RQRKAYPTSL ILAPTRELVS QIFDEARKFA
YRSWVRPCVV YGGADIGSQL RQIERGCDLL VATPGRLVDL IERGRISLVN INYLVLDEAD
RMLDMGFEPQ IRRIVEGEDM PSVNERQTLM FSATFPRDIQ MLARDFLKDY VFLSVGRVGS
TSENITQKVE YVEDVDKRSV LLDILHTHGT SGLTLIFVET KRMADALSDF LINQRFPATA
IHGDRTQRER ERALEMFRSA RCPILVATAV AARGLDIPNV THVINYDLPT DIDDYVHRIG
RTGRAGNTGI ATAFFNRGNR GVVRELIDLL KEAHQEVPSF LESIAREGSG YGGRGGRGGR
GRGGNANRDV RRMGGAMGGG APSFGGGSYG GPGGSYGGGS YGGGAAAPSY GGGYGGASGG
GGSYGGSYGN PSGPTGPSSW W
