ID   DBP9_NEUCR              Reviewed;         676 AA.
AC   Q7S6F3;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=ATP-dependent RNA helicase dbp-9;
DE            EC=3.6.4.13;
GN   Name=dbp-9; ORFNames=NCU07070;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM002241; EAA31099.1; -; Genomic_DNA.
DR   RefSeq; XP_960335.1; XM_955242.2.
DR   AlphaFoldDB; Q7S6F3; -.
DR   SMR; Q7S6F3; -.
DR   STRING; 5141.EFNCRP00000006969; -.
DR   PRIDE; Q7S6F3; -.
DR   EnsemblFungi; EAA31099; EAA31099; NCU07070.
DR   GeneID; 3876484; -.
DR   KEGG; ncr:NCU07070; -.
DR   VEuPathDB; FungiDB:NCU07070; -.
DR   HOGENOM; CLU_003041_17_1_1; -.
DR   InParanoid; Q7S6F3; -.
DR   OMA; GYEKDFK; -.
DR   Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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..676
FT                   /note="ATP-dependent RNA helicase dbp-9"
FT                   /id="PRO_0000232344"
FT   DOMAIN          126..304
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          317..541
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          633..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           95..123
FT                   /note="Q motif"
FT   MOTIF           251..254
FT                   /note="DEAD box"
FT   COMPBIAS        23..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..676
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         139..146
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   676 AA;  76617 MW;  989954EF5A634E8C CRC64;
     MAKRKLNETD EPSVVTEPQT QKKTKKSSTE KKEKKEKKSK SQSVKPQEEK PEATQQQAQQ
     QTEEEQELEQ QLKDEQKQQD EKDEKKQSEK DDADLTFSDL GLDPRLVQAV AKQSFEKPTL
     VQRKAIPLAL AGQDVLCKAK TGSGKTAAYV LPVLSGILKR KATDPTPFTS ALILVPTREL
     ADQVHKAIDA FSAFCTKDIQ SAKLTDNVSD AVLRSLLANA PDVIVSTPAR AWHNIESGAL
     SVAKLQYLVL DEADLVLSYG YDEDMENIAR SLPKGGVQTT MMSATLVSDE LDTLKGFFCR
     NPTMLDLKEE FSNEDEKLTQ FYVKCGEDDK WLISYLIFKL QLIKGPCLVF VADIDRAYRL
     KLFFEQFSIR SCVLNSELPI NTRIKIIEEF NRGIYDIIIA SDERSEVFLE DEKTEEKKEE
     QGEKKEGDEK KNGKGKKKKG RRDQEYGVSR GIDFKNVAAV INFDMPTSSS SYIHRIGRTA
     RAGRAGIALS MVVPHDLFGK HKPTSIKQCE KDEKVLAKVM RQQAKLNRKL EPYNFNKDQM
     EAFRYRMNDA LRAVTKVAIR EARTRELRQE LLRSETLKRY FEENPHELSH LRHDGELGTK
     MRQQAHLKHV PDYLLPQDGK NALTETQIGF VPFKKQGDDK KTRGKKGAKG GKGGHGKYKK
     GPGGRKNVLK TFRVRK