DRS1_MAGO7
ID DRS1_MAGO7 Reviewed; 790 AA.
AC A4QYM6; G4N080;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=ATP-dependent RNA helicase DRS1;
DE EC=3.6.4.13;
GN Name=DRS1; ORFNames=MGG_07718;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EHA53115.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CM001233; EHA53115.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_003712922.1; XM_003712874.1.
DR AlphaFoldDB; A4QYM6; -.
DR SMR; A4QYM6; -.
DR STRING; 318829.MGG_07718T0; -.
DR GeneID; 2683645; -.
DR KEGG; mgr:MGG_07718; -.
DR eggNOG; KOG0338; Eukaryota.
DR InParanoid; A4QYM6; -.
DR OrthoDB; 268859at2759; -.
DR Proteomes; UP000009058; Chromosome 3.
DR GO; GO:0005730; C:nucleolus; 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:0042254; P:ribosome biogenesis; 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; Coiled coil; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding.
FT CHAIN 1..790
FT /note="ATP-dependent RNA helicase DRS1"
FT /id="PRO_0000294641"
FT DOMAIN 286..460
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 490..634
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 19..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 631..677
FT /evidence="ECO:0000255"
FT MOTIF 255..283
FT /note="Q motif"
FT MOTIF 408..411
FT /note="DEAD box"
FT COMPBIAS 127..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..208
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 299..306
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 790 AA; 86592 MW; EC7A4B3F7AE6D633 CRC64;
MAPSSKRKAI NDDFITTISD NEADEFVEEE EVIQEEAPPK KKSKTIPKKK QKRSSKKASN
DDDAEDEEDG HIEGVWGQND DDDGAMDSDF EFVTGAGVED LDDNPEFEGW GFDGAKKAMG
QGNGVDLDEI IRRRREKKEG GTKGAAEPEA KAEEEGEALG LDDDDDEVLA RDAFGMGAGS
DDEDSAEASE GQDGSEASEG EEGDSDDESV ASPVPHPDDD QESESEQDED EEEAAKMKEF
FAADEPKSDT NKGNASFQSM SLSRPILRGL TSVGFAKPTP IQSKTIPIAL MGKDVVGGAV
TGSGKTAAFV VPILERLLYR PKKVPTSRVV ILAPTRELAI QCHAVATKLA SHTDIKFCLA
VGGLSLKVQE SELRLRPDVI IATPGRFIDH MRNSASFAVD TVEILVLDEA DRMLEDGFAD
ELNEILTTLP KSRQTMLFSA TMTSSVDNLI RVGLNKPVRL MVDSQKKTVV TLTQEFVRLR
PGREEKRMGY LVYLCKNLYT ERVIIFFRQK KIAHHARIIF GLLGLSCAEL HGSMSQIQRI
QSVEAFRDGK VSFLLATDLA SRGLDIKGVD TVINYEAPQS LEIYVHRVGR TARAGRSGTA
ITLAAEPDRK VVKAAVKAGK AQGAKISSRI IDAADADSWQ AKIDELEDEV EAVMREEKEE
KVLAQADMEM RKGENMIRYE DDIKARPKRT WFETEKDKKA AREAGRAALN GVREALKKKH
GGKNLSNKDK KKLDAMAEAK EARVWKKGAA ERAGKGAVLN FKKDKSSKKG PVVGGRVAKK
GAPRGKPRRR
