ID   DBP7_YEAS7              Reviewed;         742 AA.
AC   A6ZZY8;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=ATP-dependent RNA helicase DBP7;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 7;
GN   Name=DBP7; ORFNames=SCY_3398;
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   -!- 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. DDX31/DBP7
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAFW02000152; EDN59931.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZZY8; -.
DR   SMR; A6ZZY8; -.
DR   EnsemblFungi; EDN59931; EDN59931; SCY_3398.
DR   HOGENOM; CLU_003041_26_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; IPR025313; DUF4217.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
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   Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..742
FT                   /note="ATP-dependent RNA helicase DBP7"
FT                   /id="PRO_0000310220"
FT   DOMAIN          178..372
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          405..605
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          45..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           143..172
FT                   /note="Q motif"
FT   MOTIF           307..310
FT                   /note="DEAD box"
FT   COMPBIAS        69..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..726
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         191..198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   742 AA;  83322 MW;  8088C8685072A45A CRC64;
     MSDEDSMLLN FTTNEDTAGS SYKQAAKVTG GRWKDRRRMK MKLEGKTVSR KRKANTTGDE
     GIIPGRGENS IKKLHKESSY SSEEQEKYKG RNAHNTQGRT LPADSQFVSS LFTSNREITT
     AVNTNIHDEN VAINPSNAPL KGDQFASLGV TSLLVSHLEQ KMRIKKPTSI QKQAIPQIIG
     NAGKNDFFIH AQTGSGKTLS YLLPIISTIL NMDTHVDRTS GAFALVIAPT RELASQIYHV
     CSTLVSCCHY LVPCLLIGGE RKKSEKARLR KGCNFIIGTP GRVLDHLQNT KVIKEQLSQS
     LRYIVLDEGD KLMELGFDET ISEIIKIVHD IPINSEKFPK LPHKLVHMLC SATLTDGVNR
     LRNVALKDYK LISNGTKKDS DIVTVAPDQL LQRITIVPPK LRLVTLAATL NNITKDFIAS
     GQQSKTLRTI VFVSCSDSVE FHYDAFSGSD GHHKNLTGDS VRLLTKGNTM FPCFSDSRDP
     DVVIYKLHGS LSQQMRTSTL QHFARDNEAT KGKHLIMFCT DVASRGLDLP HVGSVIELDP
     PFAVEDHLHR VGRTARAGEK GESLLFLLPG EEEKYMDYIQ PYHPMGWELL KFDKEILMPA
     FKDVNVNRND KFIRKDEKSS KNKDVGDKEY EWDTNATTWH LNIERRVVGD SAFKNLAVKG
     FISHVRAYAT HISQEKKFFN VKFLHLGHLA KSFGLRERPK AMGLQSSKDG NSEKKPTKEN
     SKNKMFRMAR MAEKQIASEF NY