ID DBP1_YEAST Reviewed; 617 AA.
AC P24784; D6W3P9; P20446;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 27-MAR-2024, entry version 195.
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; OrderedLocusNames=YPL119C; ORFNames=LPH8C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=DBY939;
RX PubMed=1857205; DOI=10.1111/j.1365-2958.1991.tb00753.x;
RA Jamieson D.J., Beggs J.D.;
RT "A suppressor of yeast spp81/ded1 mutations encodes a very similar putative
RT ATP-dependent RNA helicase.";
RL Mol. Microbiol. 5:805-812(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 316-500.
RX PubMed=2406722; DOI=10.1073/pnas.87.4.1571;
RA Chang T.-H., Arenas J., Abelson J.;
RT "Identification of five putative yeast RNA helicase genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:1571-1575(1990).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION.
RX PubMed=14763975; DOI=10.1046/j.1365-2958.2003.03898.x;
RA Berthelot K., Muldoon M., Rajkowitsch L., Hughes J., McCarthy J.E.G.;
RT "Dynamics and processivity of 40S ribosome scanning on mRNA in yeast.";
RL Mol. Microbiol. 51:987-1001(2004).
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. {ECO:0000250, ECO:0000269|PubMed:14763975,
CC ECO:0000269|PubMed:1857205}.
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 -!- INTERACTION:
CC P24784; P06634: DED1; NbExp=3; IntAct=EBI-5596, EBI-5744;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
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 -!- MISCELLANEOUS: Present with 1480 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC subfamily. {ECO:0000305}.
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DR EMBL; X55993; CAA39465.1; -; Genomic_DNA.
DR EMBL; U43503; AAB68243.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11315.1; -; Genomic_DNA.
DR PIR; S62003; S62003.
DR RefSeq; NP_015206.1; NM_001183933.1.
DR AlphaFoldDB; P24784; -.
DR SMR; P24784; -.
DR BioGRID; 36062; 111.
DR DIP; DIP-2576N; -.
DR IntAct; P24784; 9.
DR MINT; P24784; -.
DR STRING; 4932.YPL119C; -.
DR MaxQB; P24784; -.
DR PaxDb; 4932-YPL119C; -.
DR PeptideAtlas; P24784; -.
DR EnsemblFungi; YPL119C_mRNA; YPL119C; YPL119C.
DR GeneID; 855984; -.
DR KEGG; sce:YPL119C; -.
DR AGR; SGD:S000006040; -.
DR SGD; S000006040; DBP1.
DR VEuPathDB; FungiDB:YPL119C; -.
DR eggNOG; KOG0335; Eukaryota.
DR GeneTree; ENSGT00940000157507; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; P24784; -.
DR OMA; CYRSWVR; -.
DR OrthoDB; 5480645at2759; -.
DR BioCyc; YEAST:G3O-34018-MONOMER; -.
DR BioGRID-ORCS; 855984; 0 hits in 10 CRISPR screens.
DR PRO; PR:P24784; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P24784; Protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0033677; F:DNA/RNA helicase activity; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:SGD.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:1901195; P:positive regulation of formation of translation preinitiation complex; IDA:SGD.
DR GO; GO:0006413; P:translational initiation; IMP:SGD.
DR CDD; cd17967; DEADc_DDX3_DDX4; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR PANTHER; PTHR47958:SF32; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Initiation factor;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..617
FT /note="ATP-dependent RNA helicase DBP1"
FT /id="PRO_0000055016"
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"
FT CONFLICT 43..44
FT /note="ST -> RS (in Ref. 1; CAA39465)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="E -> K (in Ref. 1; CAA39465)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="G -> R (in Ref. 1; CAA39465)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="E -> QK (in Ref. 1; CAA39465)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="V -> I (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 617 AA; 67917 MW; 8152404B7628671D CRC64;
MADLPQKVSN LSINNKENGG GGGKSSYVPP HLRSRGKPSF ERSTPKQEDK VTGGDFFRRA
GRQTGNNGGF FGFSKERNGG TSANYNRGGS SNYKSSGNRW VNGKHIPGPK NAKLEAELFG
VHDDPDYHSS GIKFDNYDNI 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
//
