DED1_CANGA
ID DED1_CANGA Reviewed; 617 AA.
AC Q8TFK8; Q6FLJ6;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=ATP-dependent RNA helicase DED1;
DE EC=3.6.4.13;
GN Name=DED1; OrderedLocusNames=CAGL0L02915g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=12125055; DOI=10.1002/yea.890;
RA Walsh D.W., Wolfe K.H., Butler G.;
RT "Genomic differences between Candida glabrata and Saccharomyces cerevisiae
RT around the MRPL28 and GCN3 loci.";
RL Yeast 19:991-994(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; AY083607; AAM08102.1; -; Genomic_DNA.
DR EMBL; CR380958; CAG61868.1; -; Genomic_DNA.
DR RefSeq; XP_448898.1; XM_448898.1.
DR AlphaFoldDB; Q8TFK8; -.
DR SMR; Q8TFK8; -.
DR STRING; 5478.XP_448898.1; -.
DR PRIDE; Q8TFK8; -.
DR EnsemblFungi; CAG61868; CAG61868; CAGL0L02915g.
DR GeneID; 2890837; -.
DR KEGG; cgr:CAGL0L02915g; -.
DR CGD; CAL0135394; CAGL0L02915g.
DR VEuPathDB; FungiDB:CAGL0L02915g; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; Q8TFK8; -.
DR OMA; IMRGQPV; -.
DR Proteomes; UP000002428; Chromosome L.
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 Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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..617
FT /note="ATP-dependent RNA helicase DED1"
FT /id="PRO_0000232156"
FT DOMAIN 176..365
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 376..536
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 145..173
FT /note="Q motif"
FT MOTIF 309..312
FT /note="DEAD box"
FT COMPBIAS 567..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 189..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 617 AA; 67002 MW; 4D20D1695C736459 CRC64;
MTELAEQVSM PEGQQRRGGY VPPHIRNGGG RRGDSAPRGG FNNGGGRGGF FRNNGDRGGF
GFGGRGGGFG GNRGGFGGNR GGFGGGMRGR WVDGKHVPGQ RNERIELELF GAPEDPSFQS
SGINFDNYDD IPVEASGEDV PEAITEFTSP PLDSLLLENI KLARFTKPTP VQKYSVPIVS
KGRDLMACAQ TGSGKTGGFL FPVLSESFLT GPAEKAANDG YSYQRKAFPT AVVMAPTREL
ATQIFDEAKK FCYRSWVKPC VVYGGAPIGN QMREMDHGCD LLVATPGRLN DLLERGKVSL
SNVKYLVLDE ADRMLDMGFE PQIRHIVEDC DMPPTGERQT LMFSATFPHD IQHLARDFLH
DYIFLSVGRV GSTSENITQR ILYVENRDKN SALLDLLAAS NDNLTLIFVE TKRMADQLTD
FLIMQNFSAT AIHGDRSQAE RERALAAFRS GRANILVATA VAARGLDIPN VTHVINYDLP
SDVDDYVHRI GRTGRAGNTG VATAFFNRDN NNIVKGLYEI LEEANQEIPP FLEDCLREVS
FSRSGSNRST RGNRSSNTRD YRKHGGNGSF GQNSRNSSWG SARGGGFGGS TGGWGNDRAG
GSAGGWGASN TKTSSWW
