DBP5_YEAS7
ID DBP5_YEAS7 Reviewed; 482 AA.
AC A6ZNQ1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=ATP-dependent RNA helicase DBP5;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 5;
DE AltName: Full=Helicase CA5/6;
DE AltName: Full=Ribonucleic acid-trafficking protein 8;
GN Name=DBP5; Synonyms=RAT8; ORFNames=SCY_5119;
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 associated with the nuclear pore
CC complex and essential for mRNA export from the nucleus. May participate
CC in a terminal step of mRNA export through the removal of proteins that
CC accompany mRNA through the nucleopore complex. May also be involved in
CC early transcription (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 -!- SUBUNIT: Associates with the nuclear pore complex. Interacts with
CC NUP159, GLE1, GFD1 and ZDS1. The interaction with NUP159 is necessary
CC for the association to the nuclear pore complex. Interacts also with
CC the TFIIH complex subunits TFB1, TFB2 and RAD3 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore
CC complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore
CC complex cytoplasmic fibrils. {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. DDX19/DBP5
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFW02000030; EDN63916.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZNQ1; -.
DR SMR; A6ZNQ1; -.
DR PRIDE; A6ZNQ1; -.
DR EnsemblFungi; EDN63916; EDN63916; SCY_5119.
DR HOGENOM; CLU_003041_1_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; 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:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR GO; GO:0015031; P:protein transport; 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; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein transport; RNA-binding; Translocation; Transport.
FT CHAIN 1..482
FT /note="ATP-dependent RNA helicase DBP5"
FT /id="PRO_0000310206"
FT DOMAIN 125..292
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 303..480
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 92..120
FT /note="Q motif"
FT MOTIF 239..242
FT /note="DEAD box"
FT BINDING 138..145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20449"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20449"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20449"
SQ SEQUENCE 482 AA; 53874 MW; C50CAFE8C060D46B CRC64;
MSDTKRDPAD LLASLKIDNE KEDTSEVSTK ETVKSQPEKT ADSIKPAEKL VPKVEEKKTK
QEDSNLISSE YEVKVKLADI QADPNSPLYS AKSFDELGLA PELLKGIYAM KFQKPSKIQE
RALPLLLHNP PRNMIAQSQS GTGKTAAFSL TMLTRVNPED ASPQAICLAP SRELARQTLE
VVQEMGKFTK ITSQLIVPDS FEKNKQINAQ VIVGTPGTVL DLMRRKLMQL QKIKIFVLDE
ADNMLDQQGL GDQCIRVKRF LPKDTQLVLF SATFADAVRQ YAKKIVPNAN TLELQTNEVN
VDAIKQLYMD CKNEADKFDV LTELYGLMTI GSSIIFVATK KTANVLYGKL KSEGHEVSIL
HGDLQTQERD RLIDDFREGR SKVLITTNVL ARGIDIPTVS MVVNYDLPTL ANGQADPATY
IHRIGRTGRF GRKGVAISFV HDKNSFNILS AIQKYFGDIE MTRVPTDDWD EVEKIVKKVL
KD
