ID   DBP9_PICST              Reviewed;         581 AA.
AC   A3LV40;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=ATP-dependent RNA helicase DBP9;
DE            EC=3.6.4.13;
GN   Name=DBP9; ORFNames=PICST_84074;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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; CP000499; ABN66707.1; -; Genomic_DNA.
DR   RefSeq; XP_001384736.1; XM_001384699.1.
DR   AlphaFoldDB; A3LV40; -.
DR   SMR; A3LV40; -.
DR   STRING; 4924.XP_001384736.1; -.
DR   EnsemblFungi; ABN66707; ABN66707; PICST_84074.
DR   GeneID; 4839681; -.
DR   KEGG; pic:PICST_84074; -.
DR   eggNOG; KOG0346; Eukaryota.
DR   HOGENOM; CLU_003041_17_1_1; -.
DR   InParanoid; A3LV40; -.
DR   OMA; GYEKDFK; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000002258; Chromosome 5.
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; 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..581
FT                   /note="ATP-dependent RNA helicase DBP9"
FT                   /id="PRO_0000285156"
FT   DOMAIN          47..231
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          260..461
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          334..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          546..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           15..43
FT                   /note="Q motif"
FT   MOTIF           177..180
FT                   /note="DEAD box"
FT   COMPBIAS        334..353
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..569
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         60..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   581 AA;  66365 MW;  C93061B7ADAD617A CRC64;
     MSTTSASEAY VDDNSSWDSF HLDARLVQAI DQLGFEHPTL IQASAIPLAL EEKRDIIAKA
     STGSGKTGAY VIPIIHNLLT DAEVESGNHH IKSIILVPTR ELSNQVLQFV EKLLVYSNNR
     INAINLSANL SDQVVNSLLM NKPEIIISTP AKLIQVLEKN ANKDLIDLST VRNLTIDEVD
     LVLSYGYLED LQKLETYLPI KKNLQTFLMS ATVNDDLNDL KTRFCSRPAI LKLNDEESAQ
     NKLIQYYART TEFDKFLLAY VIFKLNLIKG KTLVFVNNID RGYRLKLFLE QFGIRCCILN
     SELPINSRLH IVEEYNKNVY NLLIATDETN DFTVEKDEQQ QEESQDKKAS SAKTKQSKKS
     KKQKKDTEYG VSRGVDFRNV ACVLNFDLPT TSKAYIHRIG RTARAGKAGM ALSFVLPIKE
     VGKHKTASLS TAKKDEKILR RIVKQQSKNG FEIKPYQFDM KQVEGFRYRS EDAFRAVTQT
     AIREARIKEL KNELINSDKL KRFFEENPQD LASLRHDKEL HPTRVQSHLK RVPDYLLPES
     ARQDPKKIGF VPFHKNKVHK NRKKKPTGRK ADPLKSFKNR K