ID DED1_COCIM Reviewed; 665 AA.
AC Q1DJF0; A0A0D6K9M7; J3K0D9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=ATP-dependent RNA helicase DED1;
DE EC=3.6.4.13;
GN Name=DED1; ORFNames=CIMG_09563;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
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).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704915; EAS28359.2; -; Genomic_DNA.
DR RefSeq; XP_001239942.2; XM_001239941.2.
DR AlphaFoldDB; Q1DJF0; -.
DR SMR; Q1DJF0; -.
DR STRING; 246410.Q1DJF0; -.
DR GeneID; 4558926; -.
DR KEGG; cim:CIMG_09563; -.
DR VEuPathDB; FungiDB:CIMG_09563; -.
DR InParanoid; Q1DJF0; -.
DR OMA; CYRSWVR; -.
DR OrthoDB; 5480645at2759; -.
DR Proteomes; UP000001261; 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 CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR PANTHER; PTHR47958:SF32; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..665
FT /note="ATP-dependent RNA helicase DED1"
FT /id="PRO_0000255986"
FT DOMAIN 212..405
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 416..576
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 579..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 181..209
FT /note="Q motif"
FT MOTIF 349..352
FT /note="DEAD box"
FT BINDING 225..232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 665 AA; 71139 MW; 513D5C022649C51F CRC64;
MADSLKMAGL SLEDSQHAPS HATGRAPYIP PHLRGQQRAG PTMPVDGAAP QGRPPMNPGS
WGPNGAPPNN WAPRGANNIN GAPAWGAAGG GGARFDPNAY GHPGHRGGQS HGGAGSGAAR
GSGDGQWRDG KHIPGPPNAR LERELFGVPN DPSKQHTGIN FANYDDIPVE ASGHDVPEPV
TTFTNPPLDD HLISNIKLAT YKTPTPVQKY SIPIVMGGRD LMACAQTGSG KTGGFLFPIL
SQAFKNGPSA VPTQNANQFS YGRQRKAYPT SLILAPTREL VSQIYDEARK FAYRSWVRPC
VVYGGADIGS QLRQIERGCD LLVATPGRLV DLIERGRISL CNIKYLVLDE ADRMLDMGFE
PQIRRIVEGE DMPPVNGRQT LMFSATFPRD IQMLARDFLK DYVFLSVGRV GSTSENITQK
VEYVEDADKR SVLLDILHTH GTGLTLIFVE TKRMADSLSE FLINQNFPAT AIHGDRTQRE
RERALEYFRN GRCPILVATA VAARGLDIPN VTHVVNYDLP TDIDDYVHRI GRTGRAGNTG
LSTAFFNRGN RGVVRDLIEL LKEAHQEVPA FLENIAREGS GYGGRGGGRG GGRGRGANAT
RDMRRMGGGG PPMSGTPSYS GGYGGGANNY GGSYSSAPSY GGYGGGYGGG SYGNPSGPTG
PSSWW
//
