DBP8_MAGO7
ID DBP8_MAGO7 Reviewed; 579 AA.
AC A4R8G3; G4N6Z5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 3.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=ATP-dependent RNA helicase DBP8;
DE EC=3.6.4.13;
GN Name=DBP8; ORFNames=MGG_06483;
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 40S ribosomal subunit
CC biogenesis and is required for the normal formation of 18S rRNAs
CC through pre-rRNA processing at A0, A1 and A2 sites. Required for
CC vegetative growth (By similarity). {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. DDX49/DBP8
CC subfamily. {ECO:0000305}.
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DR EMBL; CM001234; EHA50759.1; -; Genomic_DNA.
DR RefSeq; XP_003717078.1; XM_003717030.1.
DR AlphaFoldDB; A4R8G3; -.
DR SMR; A4R8G3; -.
DR STRING; 318829.MGG_06483T0; -.
DR EnsemblFungi; MGG_06483T0; MGG_06483T0; MGG_06483.
DR GeneID; 2684638; -.
DR KEGG; mgr:MGG_06483; -.
DR VEuPathDB; FungiDB:MGG_06483; -.
DR eggNOG; KOG0340; Eukaryota.
DR HOGENOM; CLU_003041_1_1_1; -.
DR InParanoid; A4R8G3; -.
DR OMA; EIKQESM; -.
DR OrthoDB; 744428at2759; -.
DR Proteomes; UP000009058; Chromosome 4.
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:0006364; P:rRNA processing; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..579
FT /note="ATP-dependent RNA helicase DBP8"
FT /id="PRO_0000294656"
FT DOMAIN 179..359
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 391..537
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 148..176
FT /note="Q motif"
FT MOTIF 301..304
FT /note="DEAD box"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..79
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 192..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 579 AA; 64046 MW; 4DAF14A714F2CFD3 CRC64;
MAKIKSQRQL VSMTKDSSPR QPASEPHSSD SDSSDEESDH LDAVSSRKKR KLSVDFSQEE
GDDEDDNQDE SDDDDDVDED GGKMKQPVAK PTFAFNAPSR IKRHPAKGDS ERIGKGQPVT
DAEMEDAVQS VAQAAGKKRI LAPTDQNTTF ESLGVEPWLV QSLANLAVKR PTGIQKGCIG
EILKGRDCIG GSRTGSGKTI AFAVPILQKY AQDPSAIFAV VLTATRELAL QIYEQFKAVS
SPHVLKAALI IGGSDMRSQA IALAQRPSIV IATPGRLADH IRSSGEDTIC GLRRVKFLVL
DEADRLLSSK GPGSMLPHID ECMAVLPPPE DRQTLLFTAT VTPEVRALKE MPTRPGKEPV
HVCEVDTQVL AIPDSLKQSY IQLTVTHREH FLHEFLLTAA NTERSIIIFV NRTSTAQFLH
HLLRLLDHRV TSLHSKLRQQ QRIDNLGRFR ASAARILVAT DVASRGLDIP EVSVVVNYDL
PRDPDDYIHR VGRTARAGRK GEAVNFVGQR DVELVLAIEK RVGRPMEKWE EEGVNLETRV
IRDSLKLVSE KKREALLNIE ENREVGGRRK RQKLKLGAE
