ID   DBP8_PICST              Reviewed;         445 AA.
AC   A3LP87;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=ATP-dependent RNA helicase DBP8;
DE            EC=3.6.4.13;
GN   Name=DBP8; ORFNames=PICST_40593;
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 40S ribosomal subunit
CC       biogenesis and is required for the normal formation of 18S rRNAs
CC       through pre-rRNA processing at A0, A1 and A2 sites. Required for
CC       vegetative growth (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. DDX49/DBP8
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CP000496; ABN64453.2; -; Genomic_DNA.
DR   RefSeq; XP_001382482.2; XM_001382445.1.
DR   AlphaFoldDB; A3LP87; -.
DR   SMR; A3LP87; -.
DR   STRING; 4924.XP_001382482.2; -.
DR   PRIDE; A3LP87; -.
DR   EnsemblFungi; ABN64453; ABN64453; PICST_40593.
DR   GeneID; 4837198; -.
DR   KEGG; pic:PICST_40593; -.
DR   eggNOG; KOG0340; Eukaryota.
DR   HOGENOM; CLU_003041_1_1_1; -.
DR   InParanoid; A3LP87; -.
DR   OMA; EIKQESM; -.
DR   OrthoDB; 744428at2759; -.
DR   Proteomes; UP000002258; Chromosome 2.
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   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; 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..445
FT                   /note="ATP-dependent RNA helicase DBP8"
FT                   /id="PRO_0000285151"
FT   DOMAIN          32..208
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          247..387
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          408..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1..29
FT                   /note="Q motif"
FT   MOTIF           154..157
FT                   /note="DEAD box"
FT   COMPBIAS        408..433
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         45..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   445 AA;  49232 MW;  9F4257BD00F4182F CRC64;
     MSFEDLGVSR WLSEALAAMK IHTPTAIQSG CIPKILSGHD CIGGAKTGSG KTIAFAAPML
     TQWSEDPFGI FGLVLTPTRE LALQIAEQFA ALGASMNIKI SVVVGGEDFV KQTLELQKKP
     HFVIATPGRL ADHILNSGEE TISGLRRIKY LVLDEADRLL SNSFGGDLER CFSVLPPSEK
     RQTCLFTATV TDAVRALKEK PPAQGKPPVF LHEVETVDQV AIPSTLSIKY VFVPSYVKEA
     YLNSILRLPQ YEKSTAVIFV NRTTTAEVLR RTLRKLEFRV ASLHSEMPQS ERTNSVQRFK
     AGAARILIAT DVASRGLDIP SVELVVNFDI PADPDDFIHR VGRTARAGRS GDAVTIIAEK
     DIDRIASIEE RINKKMELLE EVTDDSVITD SLTATSVAKR ESLMEMDKEN FGEKRKINRK
     KRGLETEKIR VVKSKKEKSK KSLRQ