ID   DED1_AJECN              Reviewed;         694 AA.
AC   A6R3L3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=ATP-dependent RNA helicase DED1;
DE            EC=3.6.4.13;
GN   Name=DED1; ORFNames=HCAG_04221;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476658; EDN07711.1; -; Genomic_DNA.
DR   RefSeq; XP_001540381.1; XM_001540331.1.
DR   AlphaFoldDB; A6R3L3; -.
DR   SMR; A6R3L3; -.
DR   STRING; 339724.A6R3L3; -.
DR   EnsemblFungi; EDN07711; EDN07711; HCAG_04221.
DR   GeneID; 5446979; -.
DR   KEGG; aje:HCAG_04221; -.
DR   VEuPathDB; FungiDB:HCAG_04221; -.
DR   HOGENOM; CLU_003041_16_3_1; -.
DR   OMA; CYRSWVR; -.
DR   OrthoDB; 595675at2759; -.
DR   Proteomes; UP000009297; 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   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..694
FT                   /note="ATP-dependent RNA helicase DED1"
FT                   /id="PRO_0000310180"
FT   DOMAIN          234..423
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          434..596
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           203..231
FT                   /note="Q motif"
FT   MOTIF           367..370
FT                   /note="DEAD box"
FT   COMPBIAS        97..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         247..254
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   694 AA;  73918 MW;  6FD15D35116198AF CRC64;
     MANGLNIGSL KIDDSQRPAG PNTTGRAAYI PPHLRGSVAR PPMGLDGSGP AQAVPGLNAS
     TWAPNNAGPH PGAGHNWANA QNFTPRDRPP GAPAGPPSMN GNTTWGNAPP RQFNANDYGK
     PGPNSFRGSS YGGGRSGGTR GIGGHGYWDE NGKHAQGPEN KRLERELFGE ADDPTKQHTG
     INFSNYDSIP VEASGHDVPE SITAFTNPPL HEHLLSNIVL ARYTVPTPVQ KYSIPIVMGG
     RDLMACAQTG SGKTGGFLFP ILSQSLHTRG PEAEAARGLG RQQKAYPTAL ILGPTRELVS
     QIYDEARKFC YRTALHPRVV YGGAEMGNQL RQLDQGCNVL VATPGRLVDM MERGRISLAH
     IQYLVLDEAD RMLDMGFEPQ IRRIVQGSDM PDKHMRQTLM FSATFPPDIQ KLAEEFLKDH
     IFLSVGRVGS TSENITQRIV ECESDKDKDS ALLDILCSDS TGLTLVFVET KRQADMLSDF
     LLDHRLPATA IHGDRTQRER ERALELFRTG RCPILVATAV AARGLDIPNV THVINYDLPN
     EIDDYVHRIG RTGRAGNTGI STAFFSRSKN FKIARSLVDL LKDANQEVPD FLEKLGRQGN
     YYGSSGGGRG GRGGGRGRGG SSSTRDIRRT GGGYGGGGMG GSRPAYGGGY GDSGAGGPYG
     YGGGSGGYGG GYGGGYGGGG YGNPSGPTGP SSWW