ID   DBP9_PHANO              Reviewed;         597 AA.
AC   Q0UZ59;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=ATP-dependent RNA helicase DBP9;
DE            EC=3.6.4.13;
GN   Name=DBP9; ORFNames=SNOG_02955;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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; CH445328; EAT89686.1; -; Genomic_DNA.
DR   RefSeq; XP_001793547.1; XM_001793495.1.
DR   AlphaFoldDB; Q0UZ59; -.
DR   SMR; Q0UZ59; -.
DR   STRING; 13684.SNOT_02955; -.
DR   PRIDE; Q0UZ59; -.
DR   EnsemblFungi; SNOT_02955; SNOT_02955; SNOG_02955.
DR   GeneID; 5970404; -.
DR   KEGG; pno:SNOG_02955; -.
DR   eggNOG; KOG0346; Eukaryota.
DR   HOGENOM; CLU_003041_17_1_1; -.
DR   InParanoid; Q0UZ59; -.
DR   OMA; GYEKDFK; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
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..597
FT                   /note="ATP-dependent RNA helicase DBP9"
FT                   /id="PRO_0000256051"
FT   DOMAIN          78..249
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          260..469
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           47..75
FT                   /note="Q motif"
FT   MOTIF           197..200
FT                   /note="DEAD box"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         91..98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   597 AA;  66468 MW;  98C96773EA1031C9 CRC64;
     MAMKRKLNEH DVPEPESPQS PKRRASDASQ SEPASPPAPT PAKEVVASFA ELQLEPRLLR
     GIRDQKWGSP TAVQSKAIPL ALQGRDILAR SGTGTGKTGA YLLPILHNTL LRKGKTSLIL
     VPTKELALQI TKVAKALSAH CGQAVRIQNI AGKESEVVTK AKLADNPDIV IATPARASAN
     INTGALAVTE LAHLVVDEGD LVMGYGFKED LDQIAQNIPK GVQMFLMSAT LNTEVESLGS
     LLCNDPVVLK LDDLDKDSKR VKQYVIKCAE EEKFLLIYAM FKLGLIKGKT IVFVGDTDRS
     YRVKLFLEQF GIKSCVLNSE LPLASRLHIV EEFNKNIYNI LIASDETEIL GSQKKADESR
     PKKKPKTDKE AKNDSGVSRG IDFLNVSCVL NFDFPATYKS YFHRIGRTAR AGKSGTAISF
     IIPKDKYRKH KSTTFAGCEN DEEVLKKVEK HQEAGQKLEN YNFDMKRLEP FRYRFGDALR
     SVTRIAIREA RIKEIRLELS KSQKLSRYFE ENPEALAHLR HDQTLNHPAR IQPHLKHVPD
     YLLPGGSRKP ADVGFVGLNV PRVNKRQYVK GKGRKVVRRN GKVDPLKTFN ARGKGKK