DED1_ASPOR
ID DED1_ASPOR Reviewed; 675 AA.
AC Q2UGK3;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=ATP-dependent RNA helicase ded1;
DE EC=3.6.4.13;
GN Name=ded1; ORFNames=AO090023000809;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007157; BAE59312.1; -; Genomic_DNA.
DR RefSeq; XP_001821314.1; XM_001821262.2.
DR AlphaFoldDB; Q2UGK3; -.
DR SMR; Q2UGK3; -.
DR STRING; 510516.Q2UGK3; -.
DR EnsemblFungi; BAE59312; BAE59312; AO090023000809.
DR GeneID; 5993316; -.
DR KEGG; aor:AO090023000809; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR OMA; CYRSWVR; -.
DR Proteomes; UP000006564; Chromosome 3.
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..675
FT /note="ATP-dependent RNA helicase ded1"
FT /id="PRO_0000232154"
FT DOMAIN 217..410
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 421..582
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 186..214
FT /note="Q motif"
FT MOTIF 354..357
FT /note="DEAD box"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 230..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 675 AA; 71887 MW; 12C1D36BBA651278 CRC64;
MADSLKMGSL SLNESQHAPA PNSSGRAAYI PPHLRQRQTG ANMDGAPAAA PPAPGPSGPG
NSWGSRGGPR GGNWANANAP DFSPRGPNPN GNTSWTPTEG SRRSFNPDAY GNPGHGGSYG
GGSARGSGDG QWRDGKHIPG PANARVEREL FGLPNDPTKQ NTGINFANYD DIPVEASGQN
VPEPVNAFTN PPLDDHLIAN ITLAHYQTPT PVQKYSIPIV MNGRDLMACA QTGSGKTGGF
LFPILSQAFQ NGPSPTPAPA SGQFSYGRQR KAYPTSLILA PTRELVSQIF DEARKFAYRS
WVRPCVVYGG ADIGSQLRQI ERGCDLLVAT PGRLVDLIER GRISLVNIKY LILDEADRML
DMGFEPQIRR IVEGEDMPHV NDRQTLMFSA TFPRDIQMLA RDFLKDYVFL SVGRVGSTSE
NITQKVEYVE DHDKRSVLLD ILHTHGTSGL TLIFVETKRM ADSLSDFLLN QRFPATAIHG
DRTQRERERA LEMFRSGRCP ILVATAVAAR GLDIPNVTHV INYDLPTDID DYVHRIGRTG
RAGNTGIATA FFNRGNRGVV RDLIDLLKEA HQEVPSFLES IAREGSGYGG RGGRGGRGRG
ANATRDMRRV GGGMGGPPSF GGSSYGGPSA GYGGSYGGGA PSYGGSGGGS YGYGGSGGGG
GYGNPSGPTG PSSWW
