ID   DRS1_SCLS1              Reviewed;         801 AA.
AC   A7F4L5;
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 drs1;
DE            EC=3.6.4.13;
GN   Name=drs1; ORFNames=SS1G_12540;
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 ribosome assembly.
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   -!- SUBUNIT: Associates with pre-ribosomal particles. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {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. DDX27/DRS1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CH476641; EDN97686.1; -; Genomic_DNA.
DR   RefSeq; XP_001586553.1; XM_001586503.1.
DR   AlphaFoldDB; A7F4L5; -.
DR   SMR; A7F4L5; -.
DR   STRING; 665079.A7F4L5; -.
DR   EnsemblFungi; EDN97686; EDN97686; SS1G_12540.
DR   GeneID; 5482731; -.
DR   KEGG; ssl:SS1G_12540; -.
DR   VEuPathDB; FungiDB:sscle_06g053970; -.
DR   eggNOG; KOG0338; Eukaryota.
DR   HOGENOM; CLU_003041_3_1_1; -.
DR   InParanoid; A7F4L5; -.
DR   OMA; AAHTDIR; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IEA:EnsemblFungi.
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:0000027; P:ribosomal large subunit assembly; IEA:EnsemblFungi.
DR   GO; GO:0006364; P:rRNA processing; 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; 2.
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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ribosome biogenesis; RNA-binding.
FT   CHAIN           1..801
FT                   /note="ATP-dependent RNA helicase drs1"
FT                   /id="PRO_0000310214"
FT   DOMAIN          299..473
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          503..682
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           268..296
FT                   /note="Q motif"
FT   MOTIF           421..424
FT                   /note="DEAD box"
FT   COMPBIAS        33..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..180
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..215
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..243
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..769
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..784
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         312..319
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   801 AA;  88085 MW;  9A824CE27108621E CRC64;
     MAPKRNRDDD FVLTLSDNEG EDLTNVIEEE LPLDPSSNKK RKRNDDIAST KKSKKSKKKS
     EDEDVEEEEI WGIKDADDGA MDSDFEFALE ADGKGGADLE EFEGWGFDGA KKGLNGGDKK
     AVDIDEIIAR RREKKKATGK KGEAEDEVIA EKEDVVASDE EQDAPEEMDF EDEDDEFMAE
     DGFGMGAGSA EESGAEEDSE ASDNEGAEDD DSDNDSVASP APHPDDAASE ASDDDEDIDE
     DPEEAAKREA FFAPEEKPVK GAKPELNSTF QSMSLSRPIL RGLATVGFTQ PTPIQSKTIP
     VALLGKDVVG GAVTGSGKTA AFIVPVLERL LYRPKKVPTS RVAILMPTRE LAIQCHAVAT
     KLASHTDIKF CLAVGGLSLK VQEAELRLRP DVIIATPGRF IDHMRNSPSF TVDTLEILVL
     DEADRMLEAG FADELNEILT TIPKSRQTML FSATMSSSVD NLIRVGLNRP VRLLVDSQKS
     TAGTLTQEFI RLRPGREGKR MGYLLYLCAN VYTDRVIVFF RQKKEAHRAR IIFGLSGLKA
     TELHGSMSQE QRIKSVEAFR DGKASFLLAT DLASRGLDIK GVDTVINYEA PQSHDIYLHR
     VGRTARAGRS GRACTIAAEP DRKVVKAAVK ASRTQGAKVV SRVIEASEAD SWSEKVDEMA
     DEIEEILKEE KEDKILAQAE MEVRKGQNFM DHEAEIKGRP KRTWFESEKE KLAAKKLGME
     ELNGVVGGKK KGKLSNKDKK KLDDKGERLE GRVWKKGRQE RDGKGVLAKE KGKKKVKGGK
     PAGLGKKKAM KPMRTGGAKR R