DED1_SCLS1
ID DED1_SCLS1 Reviewed; 678 AA.
AC A7EJY3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=ATP-dependent RNA helicase ded1;
DE EC=3.6.4.13;
GN Name=ded1; ORFNames=SS1G_05629;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476627; EDO03149.1; -; Genomic_DNA.
DR RefSeq; XP_001592708.1; XM_001592658.1.
DR AlphaFoldDB; A7EJY3; -.
DR SMR; A7EJY3; -.
DR STRING; 665079.A7EJY3; -.
DR EnsemblFungi; EDO03149; EDO03149; SS1G_05629.
DR GeneID; 5488949; -.
DR KEGG; ssl:SS1G_05629; -.
DR VEuPathDB; FungiDB:sscle_05g048480; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; A7EJY3; -.
DR OMA; CYRSWVR; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IEA:EnsemblFungi.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:EnsemblFungi.
DR GO; GO:1990625; P:negative regulation of cytoplasmic translational initiation in response to stress; IEA:EnsemblFungi.
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..678
FT /note="ATP-dependent RNA helicase ded1"
FT /id="PRO_0000310182"
FT DOMAIN 217..408
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 419..579
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 186..214
FT /note="Q motif"
FT MOTIF 352..355
FT /note="DEAD box"
FT COMPBIAS 79..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 230..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 678 AA; 71220 MW; 1A51B4785A785234 CRC64;
MADQLNMNGL NLNGGEPRSY IPPHMRGKMG GPAPAGPPAN LNGSAWAPQG NGYANGPRPA
GGDSWANAPD FTPRGNGAPR GGNNWNPSGP PSFNKNAYGN PAAGAGGPGS AGGAGGAGGG
AGQARGGGDG QWRDGKHIAG PANARLEREL FGIADDPTKQ QTGINFEKYD DIPVEASGQD
VPEPVLKFTN PPLDDHLIKN IELAHYKVPT PVQKYSIPIV MGGRDLMACA QTGSGKTGGF
LFPILSQAFQ TGPSPIPANA AGSFGRTRKA YPTSLILAPT RELVSQIFDE SRKFAYRSWV
RPCVVYGGAD IGSQLRQMER GCDLLVATPG RLVDLIERGR ISLQNIKYLV LDEADRMLDM
GFEPQIRRIV EGEDMPGVQN RQTLMFSATF PRDIQMLARD FLKDYVFLSV GRVGSTSENI
TQKVEYVEDI DKRSVLLDIL HTHGAGLTLI FVETKRMADS LSDFLINQNF PATSIHGDRT
QRERERALEM FRNGRCPILV ATAVAARGLD IPNVTHVVNY DLPTDIDDYV HRIGRTGRAG
NTGISTAFFN RGNRGVVRDL IELLKEANQE IPAFLENIAR EGAGFGGGRG GRSGGRGRGG
GANRDFRKFG GGGGGGFNGG GGFGGPPASG GYGGGGGFGG PPAPASYGPP PGQYGGGGYG
GGGGAYGNPS AGGGQSWW
