DBP5_MAGO7
ID DBP5_MAGO7 Reviewed; 477 AA.
AC A4RIF1; G4MVD6;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=ATP-dependent RNA helicase DBP5;
DE EC=3.6.4.13;
GN Name=DBP5; ORFNames=MGG_07333;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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; CM001232; EHA55762.1; -; Genomic_DNA.
DR RefSeq; XP_003715569.1; XM_003715521.1.
DR AlphaFoldDB; A4RIF1; -.
DR SMR; A4RIF1; -.
DR STRING; 318829.MGG_07333T0; -.
DR PRIDE; A4RIF1; -.
DR EnsemblFungi; MGG_07333T0; MGG_07333T0; MGG_07333.
DR GeneID; 2683229; -.
DR KEGG; mgr:MGG_07333; -.
DR VEuPathDB; FungiDB:MGG_07333; -.
DR eggNOG; KOG0332; Eukaryota.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; A4RIF1; -.
DR OMA; EYCTPIQ; -.
DR OrthoDB; 608788at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
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..477
FT /note="ATP-dependent RNA helicase DBP5"
FT /id="PRO_0000294632"
FT DOMAIN 102..271
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 299..460
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 69..97
FT /note="Q motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT MOTIF 218..221
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 115..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 477 AA; 51559 MW; 7F31B74232E320A6 CRC64;
MSDLASRITA PAAATPATET DAPAAASSTL AVPDGAADGA NSSGLQESNY DVEVQLGDPD
TDSPLSSISS FSELGLPQGI IDGLLAMNFK KPSKIQARAL PLMLSNPPRN MIAQSQSGTG
KTGAFVVTIL SRVDFNQPNQ PQALALAPSR ELARQIQSVI QSIGQFCTGL VVDAAIPGAI
SRETGVKANV VVGTPGTVMD LIRRRQFDVS QLKLLVVDEA DNMLDQQGLG EQCVRVKNML
PKTIQTLLFS ATFPDHVKSY AEKFAPQANQ MKLRQQELTV KGISQMYMDC PSLKEKYEVL
CKLYGLMTIG SSVIFVKTRE SADEIQRRME ADGHKVSALH GAFQGQERDQ LLDDFRSGKS
KVLITTNVLA RGIDVSSVSM VINYDIPMKG PGDQSPDAET YLHRIGRTGR FGRVGVSISF
VHDRKSFTAL SSIAEHYGID LIQLSPDDWD DTEVKVQDVI KSSRAKPDYA PTQEKAA
