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 22-FEB-2023, entry version 55.
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 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 CDD; cd17956; DEADc_DDX51; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR24031:SF68; ATP-DEPENDENT RNA HELICASE DDX51; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//
