ID   DBP10_MAGO7             Reviewed;         914 AA.
AC   A4R5B8; G4NF96;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=ATP-dependent RNA helicase DBP10;
DE            EC=3.6.4.13;
GN   Name=DBP10; ORFNames=MGG_04179;
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. DDX54/DBP10
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CM001236; EHA47278.1; -; Genomic_DNA.
DR   RefSeq; XP_003719645.1; XM_003719597.1.
DR   AlphaFoldDB; A4R5B8; -.
DR   SMR; A4R5B8; -.
DR   STRING; 318829.MGG_04179T0; -.
DR   PRIDE; A4R5B8; -.
DR   EnsemblFungi; MGG_04179T0; MGG_04179T0; MGG_04179.
DR   GeneID; 2677688; -.
DR   KEGG; mgr:MGG_04179; -.
DR   VEuPathDB; FungiDB:MGG_04179; -.
DR   eggNOG; KOG0337; Eukaryota.
DR   HOGENOM; CLU_003041_5_0_1; -.
DR   InParanoid; A4R5B8; -.
DR   OMA; MRWDKKS; -.
DR   OrthoDB; 268859at2759; -.
DR   Proteomes; UP000009058; Chromosome 6.
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; IPR012541; DBP10_C.
DR   InterPro; IPR033517; DDX54/DBP10.
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   PANTHER; PTHR24031:SF292; PTHR24031:SF292; 1.
DR   Pfam; PF08147; DBP10CT; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM01123; DBP10CT; 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; rRNA processing.
FT   CHAIN           1..914
FT                   /note="ATP-dependent RNA helicase DBP10"
FT                   /id="PRO_0000294666"
FT   DOMAIN          121..293
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          341..502
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          333..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          626..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          807..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           90..118
FT                   /note="Q motif"
FT   MOTIF           241..244
FT                   /note="DEAD box"
FT   COMPBIAS        336..363
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..658
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..781
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        837..857
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         134..141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   914 AA;  100728 MW;  A333D0E8C0ECD789 CRC64;
     MPRRAASPAA SEHEIDILGS IFANDNDTEV KAKAKKRTGG HDEIDLDIDA LLNGAEDGGD
     GDDEALIALQ QAASFRKTTN LKGKTGKKSG GFQAMGLNPS LLQAITRKGF AVPTPIQRKS
     IPLILDRRDV VGMARTGSGK TAAFVIPMIE RLRAHSARVG ARALIMSPSR ELALQTLKVV
     KEFGKGTDLK TVLLVGGDSL EDQFGFMTTN PDIIIATPGR FLHLKVEMSL DLSSIKYVVF
     DEADRLFEMG FATQLTEILH SLPPSRQTLL FSATLPRSLV EFARAGLQDP SLVRLDAETK
     ISPDLESAFF SVKGAEKEGA LLHILQDVIK MPTGTPEGFK EDKDEGSKKR KRGPDRPNAK
     EKPTEHSTII FTATKFHVEY LTSILVQAGY AVSHAYGALD QTARKIQVED FRRGKTNILV
     VTDVAARGID IPVLANVINY DFCDQPKVFV HRVGRTARAG QKGWSYSLVS DIDAPYLLDL
     QLFLGRRLVV GQDTSAGANF ASDVVLGALQ RNSIETNVEW VEKVVQESHD IALMRSVVVK
     AQKQYLRTRV SASSQSAKRA RELTASRAWS QPHLIFGINT DDTEALRVEM LAKISGFKPQ
     ETVFEIGHGG KGTISEAVEV MKQLRKRAPV RKSKTDKDAD DEDEDVPVIK RAKSDESSDE
     DASFDEDDFV AVNDDSDEEL EVTVSNNADS AKNASAWRDS EHFMTYTPRQ SNVAEERGYG
     VNAGSNGANF LEAARDVAMD IANDEKSTSF GAPTRTTMRW DKKNAKYVSR AHDEDGSRGN
     TKMIRGESGV KIAASFKSGR FDRWRKDNRL GKLPGVGEAE TGLPRGMGGG GFGGGGRRFN
     HKREDAPKEA DKFRDDYHVR KKRVAEAKEK RIGKFRDGEG SKREIKNNDD IRKARKIKEL
     KMRKNARPAR KKKN