ID   DBP3_YEAS7              Reviewed;         523 AA.
AC   A6ZUA1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=ATP-dependent RNA helicase DBP3;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 3;
DE   AltName: Full=Helicase CA3;
GN   Name=DBP3; ORFNames=SCY_1984;
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-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; AAFW02000099; EDN62039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZUA1; -.
DR   SMR; A6ZUA1; -.
DR   IntAct; A6ZUA1; 2.
DR   MINT; A6ZUA1; -.
DR   TopDownProteomics; A6ZUA1; -.
DR   EnsemblFungi; EDN62039; EDN62039; SCY_1984.
DR   HOGENOM; CLU_003041_1_5_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.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..523
FT                   /note="ATP-dependent RNA helicase DBP3"
FT                   /id="PRO_0000310195"
FT   DOMAIN          143..315
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          344..493
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          20..54
FT                   /evidence="ECO:0000255"
FT   MOTIF           114..140
FT                   /note="Q motif"
FT   MOTIF           262..265
FT                   /note="DEAD box"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..48
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         156..163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   523 AA;  58850 MW;  A5142D821ADA5423 CRC64;
     MTKEEIADKK RKVVDEEVIE KKKSKKHKKD KKDKKEKKDK KHKKHKKEKK GEKEVEVPEK
     ESEKKPEPTS AVASEFYVQS EALTSLPQSD IDEYFKENEI AVEDPLNLAL RPLLSFDYLS
     LDSSIQAEIS KFPKPTPIQA VAWPYLLSGK DVVGVAETGS GKTFAFGVPA ISHLMNDQKK
     RGIQVLVISP TRELASQIYD NLIVLTDKVG MQCCCVYGGV PKDEQRIQLK KSQVVVATPG
     RLLDLLQEGS VDLSQVNYLV LDEADRMLEK GFEEDIKNII RETDASKRQT LMFTATWPKE
     VRELASTFMN NPIKVSIGNT DQLTANKRIT QIVEVVDPRG KERKLLELLK KYHSGPKKNE
     KVLIFALYKK EAARVERNLK YNGYNIAAIH GDLSQQQRTQ ALNEFKSGKS NLLLATDVAA
     RGLDIPNVKT VINLTFPLTV EDYVHRIGRT GRAGQTGTAH TLFTEQEKHL AGGLVNVLNG
     ANQPVPEDLI KFGTHTKKKE HSAYGSFFKD VDLTKKPKKI TFD