DBP9_MAGO7
ID DBP9_MAGO7 Reviewed; 636 AA.
AC A4QTR1; G4N3L1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=ATP-dependent RNA helicase DBP9;
DE EC=3.6.4.13;
GN Name=DBP9; ORFNames=MGG_04993;
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 the biogenesis of 60S
CC ribosomal subunits and is required for the normal formation of 25S and
CC 5.8S rRNAs. {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: 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. DDX56/DBP9
CC subfamily. {ECO:0000305}.
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DR EMBL; CM001233; EHA52686.1; -; Genomic_DNA.
DR RefSeq; XP_003712493.1; XM_003712445.1.
DR AlphaFoldDB; A4QTR1; -.
DR SMR; A4QTR1; -.
DR STRING; 318829.MGG_04993T0; -.
DR EnsemblFungi; MGG_04993T0; MGG_04993T0; MGG_04993.
DR GeneID; 2675642; -.
DR KEGG; mgr:MGG_04993; -.
DR VEuPathDB; FungiDB:MGG_04993; -.
DR eggNOG; KOG0346; Eukaryota.
DR HOGENOM; CLU_003041_17_1_1; -.
DR InParanoid; A4QTR1; -.
DR OMA; GYEKDFK; -.
DR OrthoDB; 973872at2759; -.
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:0003678; F:DNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0033677; F:DNA/RNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); 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; 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; 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; rRNA processing.
FT CHAIN 1..636
FT /note="ATP-dependent RNA helicase DBP9"
FT /id="PRO_0000294671"
FT DOMAIN 74..253
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 264..489
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 43..71
FT /note="Q motif"
FT MOTIF 201..204
FT /note="DEAD box"
FT COMPBIAS 10..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 636 AA; 71099 MW; F727E873B1651DC7 CRC64;
MKRKLNENNE PVLVSGTNKK KSDTEVSSAV ANATPSSEAA SSSSFADLGL DPRLLQAVAQ
QSFQKPTLVQ SKAIPLALEG RDVLAKAKTG SGKTAAYVLP ILQAVLKRKQ INPGATYISS
LILVPTRELT VQVTKEVERF SAFCAKEVQV VGLTDKVSDA VQRSLLQSSS PDIVVSTPST
AWRNVDSGAL SLDKLTHLVL DEADLVLSYG YDEDLEKVAR GLPKGVQTVM TSATLTDEID
TLKGIFLRDP VLLDLEEPDA EGSEITQYIV KCGEDEKFLL AYILFKLQLI KGKVIIFVAD
VDRCYRLKLF FEQFGIRSCI LNSELPVNSR ISVVEEFNRN VYDIIIASDE NEMMGDEDRP
APNGDGKEEA EVDKKHENED EGQDGEASKA APRPKKKRKM DRKRDKQYGV SRGIDFKNVA
VVVNFDLPLS STSYTHRIGR TGRAGQAGMV LSFYVPKELF RKHIPTSIDS AENDEKVLAR
VIKQQKKLGR EIKPYNFDRD QVESFRYRMN DALRAVTKIA VREARTRELR QELLKSEKLK
RHFEENPAEL QHLVRHDGEL RTARANPELR HVPDYLLPKE GRKGLSAAEI GFVPLRKSSD
RQKKGRFFKK GGARSFKAGG RKPDPLKTFK AKRKTK
