GenomeNet

Database: UniProt
Entry: A6ZWD3
LinkDB: A6ZWD3
Original site: A6ZWD3 
ID   DBP1_YEAS7              Reviewed;         617 AA.
AC   A6ZWD3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   31-JUL-2019, entry version 47.
DE   RecName: Full=ATP-dependent RNA helicase DBP1;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 1;
DE   AltName: Full=Helicase CA1;
GN   Name=DBP1; ORFNames=SCY_5610;
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 translation
CC       initiation. Remodels RNA in response to ADP and ATP concentrations
CC       by facilitating disruption, but also formation of RNA duplexes (By
CC       similarity). Redundant to DED1, may be required in conditions in
CC       which DED1 expression is decreased (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: Cytoplasm {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. DDX3/DED1
CC       subfamily. {ECO:0000305}.
DR   EMBL; AAFW02000135; EDN61025.1; -; Genomic_DNA.
DR   SMR; A6ZWD3; -.
DR   PRIDE; A6ZWD3; -.
DR   EnsemblFungi; EDN61025; EDN61025; SCY_5610.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   Initiation factor; Nucleotide-binding; Protein biosynthesis;
KW   RNA-binding.
FT   CHAIN         1    617       ATP-dependent RNA helicase DBP1.
FT                                /FTId=PRO_0000310185.
FT   DOMAIN      185    374       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      385    545       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     198    205       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       154    182       Q motif.
FT   MOTIF       318    321       DEAD box.
FT   COMPBIAS    551    610       Gly-rich.
SQ   SEQUENCE   617 AA;  67990 MW;  45AD0F3A7D940571 CRC64;
     MADLPQKVSN LSINNKENGG DGGKSSYVPP HLRSRGKPSF ERSTPKQEDK VTGGDFFRRA
     GRQTGNNGGF FGFSKERNGG TSANYNRGGS SNYKSSGNRW VNGKHIPGPK NAKLEAELFG
     VHEDPDYHSS GIKFDNYDDI PVDASGKDVP EPILDFSSPP LDELLMENIK LASFTKPTPV
     QKYSIPIVTK GRDLMACAQT GSGKTGGFLF PLFTELFRSG PSPVPEKAQS FYSRKGYPSA
     LVLAPTRELA TQIFEEARKF TYRSWVRPCV VYGGAPIGNQ MREVDRGCDL LVATPGRLND
     LLERGKVSLA NIKYLVLDEA DRMLDMGFEP QIRHIVEECD MPSVENRQTL MFSATFPVDI
     QHLARDFLDN YIFLSVGRVG STSENITQRI LYVDDMDKKS ALLDLLSAEH KGLTLIFVET
     KRMADQLTDF LIMQNFKATA IHGDRTQAER ERALSAFKAN VADILVATAV AARGLDIPNV
     THVINYDLPS DIDDYVHRIG RTGRAGNTGV ATSFFNSNNQ NIVKGLMEIL NEANQEVPTF
     LSDLSRQNSR GGRTRGGGGF FNSRNNGSRD YRKHGGNGSF GSTRPRNTGT SNWGSIGGGF
     RNDNEKNGYG NSNASWW
//
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