DBP1_YEAS7
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 03-AUG-2022, entry version 55.
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; 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 translation initiation.
CC Remodels RNA in response to ADP and ATP concentrations by facilitating
CC disruption, but also formation of RNA duplexes (By similarity).
CC Redundant to DED1, may be required in conditions in which DED1
CC 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 box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFW02000135; EDN61025.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZWD3; -.
DR SMR; A6ZWD3; -.
DR EnsemblFungi; EDN61025; EDN61025; SCY_5610.
DR HOGENOM; CLU_003041_16_3_1; -.
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: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:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd17967; DEADc_DDX3_DDX4; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044763; Ded1/Dbp1_DEADc.
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; Cytoplasm; Helicase; Hydrolase; Initiation factor;
KW Nucleotide-binding; Protein biosynthesis; RNA-binding.
FT CHAIN 1..617
FT /note="ATP-dependent RNA helicase DBP1"
FT /id="PRO_0000310185"
FT DOMAIN 185..374
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 385..545
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 154..182
FT /note="Q motif"
FT MOTIF 318..321
FT /note="DEAD box"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 198..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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
