DBP5_AJECN
ID DBP5_AJECN Reviewed; 497 AA.
AC A6RC50;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=ATP-dependent RNA helicase DBP5;
DE EC=3.6.4.13;
GN Name=DBP5; ORFNames=HCAG_07208;
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC unclassified Histoplasma.
OX NCBI_TaxID=2059318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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; CH476662; EDN10747.1; -; Genomic_DNA.
DR RefSeq; XP_001537786.1; XM_001537736.1.
DR AlphaFoldDB; A6RC50; -.
DR SMR; A6RC50; -.
DR STRING; 339724.A6RC50; -.
DR EnsemblFungi; EDN10747; EDN10747; HCAG_07208.
DR GeneID; 5444063; -.
DR KEGG; aje:HCAG_07208; -.
DR VEuPathDB; FungiDB:HCAG_07208; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR OMA; EYCTPIQ; -.
DR OrthoDB; 608788at2759; -.
DR Proteomes; UP000009297; 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..497
FT /note="ATP-dependent RNA helicase DBP5"
FT /id="PRO_0000310203"
FT DOMAIN 122..293
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 304..477
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 89..117
FT /note="Q motif"
FT MOTIF 240..243
FT /note="DEAD box"
FT COMPBIAS 21..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 497 AA; 54465 MW; B14A310BDC1D3C12 CRC64;
MATETPAGGP LEARISRAEP KTDASATSEP ATGDTTETPA ATKPSAADGQ TDGASEGFGG
SQLQEPEYSV NVKLSDLQAD PNNPLYSIKS FEELGLHPSI LQGLHSMSFR RPSKIQEKAL
PLLLNNPPAN MIGQSQSGTG KTAAFVLNIL SRLDLSPQME LAPQALVLAP SRELARQIVG
VIQVMGSYVD KLKVATAVPM ESNRNQKVEA PVVVGTPGTV MDLIRKRLFN PQHLKVIVLD
EADNMLDQQG LGDQCIRVKG LLPKNIQVVL FSATFPDHVV RYANKFAPNA NQITLKHEEL
TVEGIKQLYL DCDSDEHKFD ILVKFYGLLT IGSSIIFVKT RASAVEIERR MVAEGHTVVS
LTGGVEGQKR DEIIDKFRQG DAKVLITTNV LARGIDVQTV SMVINYDIPE LHAPKATKRI
ADAQTYLHRI GRTGRFGRVG VAVSFVASKE EWQMLQDIKT YFNTEIQRVN TQDWDEVEEV
VKTIIRSSRA GSNFQRS
