DBP5_DEBHA
ID DBP5_DEBHA Reviewed; 493 AA.
AC Q6BRE4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=ATP-dependent RNA helicase DBP5;
DE EC=3.6.4.13;
GN Name=DBP5; OrderedLocusNames=DEHA2D17072g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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. {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; CR382136; CAG87398.1; -; Genomic_DNA.
DR RefSeq; XP_459226.1; XM_459226.1.
DR AlphaFoldDB; Q6BRE4; -.
DR SMR; Q6BRE4; -.
DR STRING; 4959.XP_459226.1; -.
DR EnsemblFungi; CAG87398; CAG87398; DEHA2D17072g.
DR GeneID; 2901091; -.
DR KEGG; dha:DEHA2D17072g; -.
DR VEuPathDB; FungiDB:DEHA2D17072g; -.
DR eggNOG; KOG0332; Eukaryota.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q6BRE4; -.
DR OMA; EYCTPIQ; -.
DR OrthoDB; 608788at2759; -.
DR Proteomes; UP000000599; Chromosome D.
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:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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; Protein transport;
KW Reference proteome; RNA-binding; Translocation; Transport.
FT CHAIN 1..493
FT /note="ATP-dependent RNA helicase DBP5"
FT /id="PRO_0000232222"
FT DOMAIN 136..303
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 331..491
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 103..131
FT /note="Q motif"
FT MOTIF 250..253
FT /note="DEAD box"
FT COMPBIAS 26..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149..156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 493 AA; 54753 MW; F1817C055E908FB6 CRC64;
MSKEDTRVES DAAELLSSLS LDKKEQTEAT VPKVDAKEDK SNDESKQTIK PASTEESKPA
DVKDATKSEE QEAESNLIKS SYEVKVKLAD LQADPNSPLY SVKSFEELGL SSELLKGLYA
MKFNKPSKIQ EKALPLLISN PPKNMIGQSQ SGTGKTAAFS LTMLSRVDES DPNTQCICLA
PARELARQTL EVITTMSKFT KITSQLIVPD AMQRGQSTCA HVLVGTPGTL LDLIRRKLIN
TSKVKVFVLD EADNMLESQG LGDQCVRVKR TLPKATQLVL FSATFPDEVR KYAEKFVPNA
NSLELKQEEL NVEGIKQLYM DCDSANHKFE VLSELYGLLT IGSSIIFVKT KDTANILYAK
MKKEGHKCSI LHAGLETSER DRLIDDFREG RSKVLITTNV LARGIDIASV SMVVNYDLPV
DQKGAPDPST YLHRIGRTGR FGRVGVSISF VHDQKSYQDL MAIRSYFGNI EMTRVPTDDW
DEVEKIVKKV IKN
