ID   DBP6_PICST              Reviewed;         591 AA.
AC   A3LSJ2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=ATP-dependent RNA helicase DBP6;
DE            EC=3.6.4.13;
GN   Name=DBP6; ORFNames=PICST_35694;
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   -!- SUBUNIT: Associated with pre-ribosomal particles. {ECO:0000250}.
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. DDX51/DBP6
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CP000497; ABN65577.2; -; Genomic_DNA.
DR   RefSeq; XP_001383606.2; XM_001383569.1.
DR   AlphaFoldDB; A3LSJ2; -.
DR   SMR; A3LSJ2; -.
DR   STRING; 4924.XP_001383606.2; -.
DR   PRIDE; A3LSJ2; -.
DR   EnsemblFungi; ABN65577; ABN65577; PICST_35694.
DR   GeneID; 4837855; -.
DR   KEGG; pic:PICST_35694; -.
DR   eggNOG; KOG0350; Eukaryota.
DR   HOGENOM; CLU_003041_15_2_1; -.
DR   InParanoid; A3LSJ2; -.
DR   OMA; HLEWLVI; -.
DR   OrthoDB; 973872at2759; -.
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..591
FT                   /note="ATP-dependent RNA helicase DBP6"
FT                   /id="PRO_0000285152"
FT   DOMAIN          195..377
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          414..570
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           153..181
FT                   /note="Q motif"
FT   MOTIF           315..318
FT                   /note="DEAD box"
FT   COMPBIAS        13..31
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         208..215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   591 AA;  66322 MW;  77ED0F3F5DBEA3AF CRC64;
     MFGARFDPTA DDSSSDESEE ESEEEENENE NVVNNDVAKD IDSVESEESE DSDHSNDPND
     AMDVDSEVNT EVDVDYVSKY KSVFDKFKKS VPETKKIDSE SSSEEEDDVE MQDLMPLPQP
     ALPRDKRLIS SNSHLKNLDW LATPIYASPE DSKPFSEFEI SPFLLKNLER DNFTTAFSVQ
     IAIMDILLHD IKRNRLEPDV KGDILVNAAT GSGKTLAYSI PIIEALHNRV VPRVRAIVLV
     PTKPLINQVK ATFVQLSRGT NLSVVSLRND VSIKEEGIKI VNSPPDIIVS TPGRLVEHIS
     NKSINLNSLQ FLVIDEADRL LNQSFQNWCQ VLISSLEGDV NIAEEWKITP QKLIFSATLT
     TDSGKLSALK FQKPRLVIVN DRKQLVNEIF NVPSSLSEYT IQFGTAKASI KPLILAKYLL
     ENNKLSNVLI FTKSNEASIR LCKLLELMFG KLHPSMNIAY INSTNNKSAI RTKILKDFST
     QKINILVATD LIARGIDILS ITDVINYDLP NSSREYVHRV GRTARANQTG HAYTLCFGKG
     EAKWFKKIIS DVGRGDKTIE KVEIELKELI VAEDENVYNE CLESLSKQVF H