DBP5_ASPCL
ID DBP5_ASPCL Reviewed; 487 AA.
AC A1CFV3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=ATP-dependent RNA helicase dbp5;
DE EC=3.6.4.13;
GN Name=dbp5; ORFNames=ACLA_094520;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027052; EAW11752.1; -; Genomic_DNA.
DR RefSeq; XP_001273178.1; XM_001273177.1.
DR AlphaFoldDB; A1CFV3; -.
DR SMR; A1CFV3; -.
DR STRING; 5057.CADACLAP00008609; -.
DR EnsemblFungi; EAW11752; EAW11752; ACLA_094520.
DR GeneID; 4704748; -.
DR KEGG; act:ACLA_094520; -.
DR VEuPathDB; FungiDB:ACLA_094520; -.
DR eggNOG; KOG0332; Eukaryota.
DR HOGENOM; CLU_003041_1_0_1; -.
DR OMA; EYCTPIQ; -.
DR OrthoDB; 608788at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IEA:EnsemblFungi.
DR GO; GO:0005844; C:polysome; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IEA:EnsemblFungi.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006415; P:translational termination; IEA:EnsemblFungi.
DR GO; GO:0006409; P:tRNA export from nucleus; IEA:EnsemblFungi.
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..487
FT /note="ATP-dependent RNA helicase dbp5"
FT /id="PRO_0000281702"
FT DOMAIN 110..283
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 311..467
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 77..105
FT /note="Q motif"
FT MOTIF 230..233
FT /note="DEAD box"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 487 AA; 53704 MW; CE033410C1D400B4 CRC64;
MASEQPVEAA PLGGSLSDRI SKPDEPTASE TPEQTSDQAD GASAPLGGSD LREPEYNVEV
KLSDLQADPN NPLYSVKNFE DLGLDPRILK GLSAMNFRKP SKIQERALPL LLGNPPKNLV
GQSQSGTGKT AAFVLNALSR VDLSTEQMQK TPQALILAPT RELARQIVGV VSVMGQFLDG
LIIGTAVPAD INNRPKRLEC SIAVGTPGTV MDMIKRRIMV PNKLKVLVLD EADNMLDQQG
LGDQCIRVKA LLPRDIQVVL FSATFPDHVH AYAAKFAPNA NELTLQHEEL TVEGIKQLYL
DCSDEEDKYK TLVQLYGLLT VGSSIIFVQT RTSASEIEKR MVAEGHTVAS LTGGIDVTKR
DEIIDKFRSG EAKVLITTNV LARGIDVSTV SMVINYDIPE LHRPGVPERQ ADFQTYLHRI
GRTGRFGRVG VSISFVSNRE EWDMLNQIQR YFNTEIQRVD TKDWDEVEDI IKKTIKNTRA
NAQFGKQ
