ID   DBP3_PICST              Reviewed;         526 AA.
AC   A3LRW2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=ATP-dependent RNA helicase DBP3;
DE            EC=3.6.4.13;
GN   Name=DBP3; ORFNames=PICST_82655;
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-dependent RNA helicase required for 60S ribosomal subunit
CC       synthesis. Involved in efficient pre-rRNA processing, predominantly at
CC       site A3, which is necessary for the normal formation of 25S and 5.8S
CC       rRNAs (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. DDX5/DBP2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CP000497; ABN65800.1; -; Genomic_DNA.
DR   RefSeq; XP_001383829.1; XM_001383792.1.
DR   AlphaFoldDB; A3LRW2; -.
DR   SMR; A3LRW2; -.
DR   STRING; 4924.XP_001383829.1; -.
DR   EnsemblFungi; ABN65800; ABN65800; PICST_82655.
DR   GeneID; 4837793; -.
DR   KEGG; pic:PICST_82655; -.
DR   eggNOG; KOG0331; Eukaryota.
DR   HOGENOM; CLU_003041_1_5_1; -.
DR   InParanoid; A3LRW2; -.
DR   OMA; KKKTHDM; -.
DR   OrthoDB; 471730at2759; -.
DR   Proteomes; UP000002258; Chromosome 3.
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   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..526
FT                   /note="ATP-dependent RNA helicase DBP3"
FT                   /id="PRO_0000285139"
FT   DOMAIN          147..318
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          334..496
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           118..144
FT                   /note="Q motif"
FT   MOTIF           265..268
FT                   /note="DEAD box"
FT   COMPBIAS        1..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         160..167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   526 AA;  58438 MW;  09B2A8FFAFABA05A CRC64;
     MVEEHKNKKR RQEDGPADVP EKKVKVSKSE KKDKKEKKEK KEKKEKKEKK EKKEKKEKKE
     KKKKYEHTAT ISGSAQSSQG YTQSESLTNL PQSEIDSFLA TNEVTIEDPH SLNLRPLLSF
     DQIQLNSKIS AVVNKFPTPT PIQSVAWPYL LSGKDVIGVA ETGSGKTFAF GVPAINNILT
     LGKSGLSVLC ISPTRELASQ IYDNLVDLTS NTNVKCVCVY GGVPKHDQVK NLKNANVVVA
     TPGRLLDLIE DGAVNLGTVD YLVLDEADRM LETGFEDAIK AIIGGTKKEN RQTLMFTATW
     PQEVRKLAST FMNQPVKVSI GDRDELAANK RITQIVEVIE PFDKEKKLLG LLRQYQSGSK
     KNDKVLIFAL YKKEATRIEG LLRRNSYNVA AIHGDLSQQQ RTNALNSFKK GESSLLLATD
     VAARGLDIPN VKVVINLTFP LTVEDYVHRI GRTGRAGQTG TAHTLFTEHE KHLSGALMNI
     LRGANQPVPD ELLKFGGHTK KKAHSAYGAF FKDVDMTKTA KKIKFD