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Database: UniProt
Entry: A6ZZY8
LinkDB: A6ZZY8
Original site: A6ZZY8 
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   31-JUL-2019, entry version 48.
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;
OC   Saccharomycetes; 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.,
RA   Wang X., Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S.,
RA   Li Y., Davis R.W., Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces
RT   cerevisiae 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
CC       60S ribosomal subunits and is required for the normal formation of
CC       25S and 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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC       subfamily. {ECO:0000305}.
DR   EMBL; AAFW02000152; EDN59931.1; -; Genomic_DNA.
DR   PRIDE; A6ZZY8; -.
DR   EnsemblFungi; EDN59931; EDN59931; SCY_3398.
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: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   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   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Ribosome biogenesis; RNA-binding;
KW   rRNA processing.
FT   CHAIN         1    742       ATP-dependent RNA helicase DBP7.
FT                                /FTId=PRO_0000310220.
FT   DOMAIN      178    372       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      405    605       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     191    198       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       143    172       Q motif.
FT   MOTIF       307    310       DEAD box.
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
//
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