DED1_PICGU
ID DED1_PICGU Reviewed; 637 AA.
AC A5DQS0;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=ATP-dependent RNA helicase DED1;
DE EC=3.6.4.13;
GN Name=DED1; ORFNames=PGUG_05621;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDK41523.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CH408161; EDK41523.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001482601.1; XM_001482551.1.
DR AlphaFoldDB; A5DQS0; -.
DR SMR; A5DQS0; -.
DR STRING; 4929.XP_001482601.1; -.
DR EnsemblFungi; EDK41523; EDK41523; PGUG_05621.
DR GeneID; 5124152; -.
DR KEGG; pgu:PGUG_05621; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; A5DQS0; -.
DR OrthoDB; 595675at2759; -.
DR Proteomes; UP000001997; 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 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..637
FT /note="ATP-dependent RNA helicase DED1"
FT /id="PRO_0000294613"
FT DOMAIN 200..389
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 400..560
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 169..197
FT /note="Q motif"
FT MOTIF 333..336
FT /note="DEAD box"
FT COMPBIAS 48..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 213..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 637 AA; 68004 MW; AA83D9EAEE305C66 CRC64;
MSDITHKMNE LSVGDGANRA SGAAAGGETP SGSSGRSQYV PPHLRNRPNG GSTPSRRGDF
GSRSNGFGSG RRGDFNSSGF QFGSGRRGNS GFGGRGGFGG GSGRYNSPKP GVGQWVDGKH
EPAAPNERLE KELFGVAEDP SVQSSGINFD NYDDIPVEAT GDGVPEPISA FTAPPLDPLI
VENIKLSRFT KPTPVQKYSV PIVASGRDLM ACAQTGSGKT GGFLFPVLSE SYMNGPDAVP
ESQGAFSSHK VHPTALVMAP TRELVSQIFE EAKKFSYRSW VRPCVVYGGA DIGTQIRNLD
RGCDLLVATP GRLKDLLERG RVSLSNIKYL VLDEADRMLD MGFEPQIRHI VQECDMPGVE
SRQTLMFSAT FPRDIQMLAR DFLKDYIFLS VGRVGSTSEN ITQKVLYVED DEKKSVLLDL
LSANDNGLTI IFTETKRMAD NLADFLYDQG FPATAIHGDR SQYEREKALA AFKSGTAPIL
VATAVAARGL DIPNVSHVVN YDLPGDIDDY VHRIGRTGRA GNVGIATAFF NRNNRNVVKG
MIELLSEANQ EVPDFLQKIS REGSYGSKGG FGSMRGGAGR GVLGGGSRGG SRDFRRSGGG
FGSSGSSGSN WGSSSSGNGG YRSSSNYGNP SSGNSWW
