DBP2_YEAS7
ID DBP2_YEAS7 Reviewed; 546 AA.
AC A6ZRX0;
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 DBP2;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 2;
DE AltName: Full=p68-like protein;
GN Name=DBP2; ORFNames=SCY_4681;
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-dependent RNA helicase involved nonsense-mediated mRNA
CC decay and ribosome biogenesis through rRNA processing. {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 -!- SUBUNIT: Associates with polysomes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {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. DDX5/DBP2
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFW02000067; EDN62702.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZRX0; -.
DR SMR; A6ZRX0; -.
DR IntAct; A6ZRX0; 2.
DR MINT; A6ZRX0; -.
DR PRIDE; A6ZRX0; -.
DR EnsemblFungi; EDN62702; EDN62702; SCY_4681.
DR HOGENOM; CLU_003041_16_9_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
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; 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; Isopeptide bond;
KW Nonsense-mediated mRNA decay; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Ribosome biogenesis; RNA-binding; rRNA processing; Ubl conjugation.
FT CHAIN 1..546
FT /note="ATP-dependent RNA helicase DBP2"
FT /id="PRO_0000310190"
FT DOMAIN 144..319
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 347..494
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 113..141
FT /note="Q motif"
FT MOTIF 267..270
FT /note="DEAD box"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 157..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24783"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24783"
FT CROSSLNK 474
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P24783"
SQ SEQUENCE 546 AA; 60985 MW; 30FE3C637CF98120 CRC64;
MTYGGRDQQY NKTNYNSRGG DFRGGRNSDR NSYNDRPQGG NYRGGFGGRS NYNQPQELIK
PNWDEELPKL PTFEKNFYVE HESVRDRSDS EIAQFRKENE MTISGHDIPK PITTFDEAGF
PDYVLNEVKA EGFDKPTGIQ CQGWPMALSG RDMVGIAATG SGKTLSYCLP GIVHINAQPL
LAPGDGPIVL VLAPTRELAV QIQTECSKFG HSSRIRNTCV YGGVPKSQQI RDLSRGSEIV
IATPGRLIDM LEIGKTNLKR VTYLVLDEAD RMLDMGFEPQ IRKIVDQIRP DRQTLMWSAT
WPKEVKQLAA DYLNDPIQVQ VGSLELSASH NITQIVEVVS DFEKRDRLNK YLETASQDNE
YKTLIFASTK RMCDDITKYL REDGWPALAI HGDKDQRERD WVLQEFRNGR SPIMVATDVA
ARGIDVKGIN YVINYDMPGN IEDYVHRIGR TGRAGATGTA ISFFTEQNKG LGAKLISIMR
EANQNIPPEL LKYDRRSYGG GHPRYGGGRG GRGGYGRRGG YGGGRGGYGG NRQRDGGWGN
RGRSNY
