ID   DBP6_YEAS7              Reviewed;         629 AA.
AC   A6ZSB3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=ATP-dependent RNA helicase DBP6;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 6;
GN   Name=DBP6; ORFNames=SCY_4824;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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. Interacts with DBP9
CC       and RSA3. Together with NOP8, URB1, URB2 and RSA3, forms an RNA-
CC       independent complex, which is required during early maturation of
CC       nascent 60S ribosomal subunits (By similarity). {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; AAFW02000067; EDN62845.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZSB3; -.
DR   SMR; A6ZSB3; -.
DR   PRIDE; A6ZSB3; -.
DR   EnsemblFungi; EDN62845; EDN62845; SCY_4824.
DR   HOGENOM; CLU_003041_15_2_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..629
FT                   /note="ATP-dependent RNA helicase DBP6"
FT                   /id="PRO_0000310240"
FT   DOMAIN          221..401
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          437..603
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           197..205
FT                   /note="Q motif"
FT   MOTIF           341..344
FT                   /note="DEAD box"
FT   COMPBIAS        90..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         234..241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53734"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53734"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53734"
SQ   SEQUENCE   629 AA;  70366 MW;  22C255505B092A4E CRC64;
     MFASRFDPSQ LTAPAASAPE GIVGTTPPAI VPLKRQATES DNEEYGSHQD SDESSNSSSE
     EDEDRMQVDY GASEEDSSEV EEEESKPSTH STVLSRFKQT VSLQERLGAS DIAESKEDES
     IEDEAASTHQ LKQIPQPEFV KNPMNLNTNS LQFKSTGWLN TEKIYYDNSL IKPFSDYANE
     LEAKLLQNIC KNFSTNTFPI QSIILDSILP VLNFTLNVSK RNFTRRIGDI LVNAATGSGK
     TLAYSIPIVQ TLFKRQINRL RCIIIVPTKL LINQVYTTLT KLTQGTSLIV SIAKLENSLK
     DEHKKLSNLE PDILITTPGR LVDHLNMKSI NLKNLKFLII DEADRLLNQS FQGWCPKLMS
     HLKTDKLDTL PGNVIKMIFS ATLTTNTEKL NGLNLYKPKL FLKQTDKLYQ LPNKLNEFNI
     NIPTAKSIYK PLILLYSICQ FMAHSPIAAK ILIFVKSNES SIRLSKLLQL ICESRSQSSV
     LKNLQNLAVS INSVNSNNSK AENKKIVANF SHPSESAGIT ILITTDIMSR GIDINDITQV
     INYDPPMSSQ QYVHRVGRTA RANELGSAYN LLVGRGERTF FDDLNKDLDR DGKSVQPLEL
     DFTLLESDSE LYTSSLESLK NYHNNTAQA