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DED1_KLULA
ID   DED1_KLULA              Reviewed;         627 AA.
AC   Q6CLR3;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=ATP-dependent RNA helicase DED1;
DE            EC=3.6.4.13;
GN   Name=DED1; OrderedLocusNames=KLLA0F01034g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382126; CAG97833.1; -; Genomic_DNA.
DR   RefSeq; XP_455126.1; XM_455126.1.
DR   AlphaFoldDB; Q6CLR3; -.
DR   SMR; Q6CLR3; -.
DR   STRING; 28985.XP_455126.1; -.
DR   EnsemblFungi; CAG97833; CAG97833; KLLA0_F01034g.
DR   GeneID; 2895858; -.
DR   KEGG; kla:KLLA0_F01034g; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   HOGENOM; CLU_003041_16_3_1; -.
DR   InParanoid; Q6CLR3; -.
DR   OMA; NQNIVKG; -.
DR   Proteomes; UP000000598; Chromosome F.
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..627
FT                   /note="ATP-dependent RNA helicase DED1"
FT                   /id="PRO_0000232160"
FT   DOMAIN          190..379
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          406..550
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           159..187
FT                   /note="Q motif"
FT   MOTIF           323..326
FT                   /note="DEAD box"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         203..210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   627 AA;  67274 MW;  00A91E0350B3C7AD CRC64;
     MSDIAENMSN LSVQDNDSGA TSGDSRRSYV PPHVRGQQRS GSGNYRGRSD NFGGNERSFF
     GNERRGGGYS RGGRGSVNWG GSNWGGRNDS RGSGGYGGGN SSGRWIDGKH VPAAKNANLE
     LELFGVAEDK SFQSSGINFD NYDDIPVEAS GNDVPEPISE FHSPPLDPLL LDNIKLARFT
     KPTPVQKYSV PIVAAGRDLM ACAQTGSGKT GGFLFPVLSE SFSSGPASTP EAAGNSYIKK
     VYPTAVILAP TRELATQIYD EAKKFTYRSW VKPMVVYGGA SIDNQIKQMR YGCNLLVATP
     GRLTDLLERR YISLANVKYL VLDEADRMLD MGFEPQIRRI VEGSDMPSVD NRQTLMFSAT
     FPSEIQHLAS DFLKDYVFLS VGRVGSTSEN ITQKILYVED FDKNDTLLDL LAASNEGLTL
     IFVETKRAAD SLTDFLIMEG FKATAIHGDR TQGERERALS AFKTGRATIL VATAVAARGL
     DIPNVTHVIN FDLPNDIDDY VHRIGRTGRA GNTGVATTFF NRGNKNVAKE LVSLLSEANQ
     EVPSFLTTIM REASSGRGGA RGGRGGYNRG NSTRDFRRGG APSGGFSSGG GSSGGWGNGG
     GSSGGWGNSS GNWGNSSNSS NSNSGWW
 
 
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