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Database: UniProt
Entry: A6RUH2
LinkDB: A6RUH2
Original site: A6RUH2 
ID   DRS1_BOTFB              Reviewed;         801 AA.
AC   A6RUH2;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   16-OCT-2019, entry version 68.
DE   RecName: Full=ATP-dependent RNA helicase drs1;
DE            EC=3.6.4.13;
GN   Name=drs1; ORFNames=BC1G_03746;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
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.,
RA   Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S.,
RA   Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M.,
RA   Pradier J.-M., Quevillon E., Sharon A., Simon A., ten Have A.,
RA   Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V.,
RA   Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z.,
RA   Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C.,
RA   Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S.,
RA   Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M.,
RA   Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C.,
RA   Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H.,
RA   Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C.,
RA   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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX27/DRS1
CC       subfamily. {ECO:0000305}.
DR   EMBL; CH476857; EDN21725.1; -; Genomic_DNA.
DR   RefSeq; XP_001557482.1; XM_001557432.1.
DR   SMR; A6RUH2; -.
DR   GeneID; 5438076; -.
DR   KEGG; bfu:BCIN_10g04050; -.
DR   EuPathDB; FungiDB:Bcin10g04050; -.
DR   KO; K13181; -.
DR   OMA; HEPERSW; -.
DR   OrthoDB; 268859at2759; -.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
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   Ribosome biogenesis; RNA-binding.
FT   CHAIN         1    801       ATP-dependent RNA helicase drs1.
FT                                /FTId=PRO_0000310213.
FT   DOMAIN      299    473       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      503    682       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     312    319       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       268    296       Q motif.
FT   MOTIF       421    424       DEAD box.
FT   COMPBIAS    145    241       Asp-rich.
FT   COMPBIAS    709    788       Lys-rich.
SQ   SEQUENCE   801 AA;  87835 MW;  3952520B349EAA8D CRC64;
     MAPKRNRDDD FVLTLSDNEG EDLTNAVEEE LPLDPSSNKK RKRSDDTAST KKSKKSKKKP
     EEEDVEEEGI WGIKDADDGA MDSDFEFALE ADGTGGADLE EFEGWGFDGA KKGLNGGDKK
     AVDIDEIIAR RREKKKASGK KGEADDEVMV DQDDAAASNE EQDAPEGIDF EDEDDEFMAE
     DGFGMGAGSA EESGAEEDSD AEDDEEGEDD DSDNDSVASP APHPDDAASE ASDEDEDMDD
     DPEEAAKREA FFAPEEKPVK GAKQELNTTF QSMSLSRPIL RGLATVGFTQ PTPIQSKTIP
     VALLGKDVVG GAVTGSGKTA AFVVPVLERL LYRPKKVPTS RVAILMPTRE LAIQCHAVAT
     KLASHTDIKF CLAVGGLSLK VQEAELRLRP DVIIATPGRF IDHMRNSPSF TVDTLEILVL
     DEADRMLEAG FADELNEILT TIPKSRQTML FSATMSSSVD NLIRVGLNRP VRLLVDSQKS
     TAGTLVQEFI RLRPGREGKR MGYLLYLCAN VYTDRVIVFF RQKKEAHRAR IIFGLSGLKA
     TELHGSMSQE QRIKSVEAFR DGKASFLLAT DLASRGLDIK GVDTVINYEA PQSHDIYLHR
     VGRTARAGRS GRACTIAAEP DRKVVKAAVK ASRTQGAKVV SRVIEASEAD SWSEKVDEMA
     DEIEEILKEE KEDKILAQAE MEVRKGQNFI DHEAEIKGRP KRTWFETEKE KLAAKKLGVE
     ELNGVVGGKK KGKLSNKDKK KLDDKGERLE GRVWKKGRQE RDGKGVLAKE KGKKKVKGGK
     PPGPGGKKPM RPMRTGGAKR K
//
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