DBP2_AJECN
ID DBP2_AJECN Reviewed; 542 AA.
AC A6RGE3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=ATP-dependent RNA helicase DBP2;
DE EC=3.6.4.13;
GN Name=DBP2; ORFNames=HCAG_08709;
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 involved nonsense-mediated mRNA
CC decay and ribosome biogenesis through rRNA processing. {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 polysomes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {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. DDX5/DBP2
CC subfamily. {ECO:0000305}.
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DR EMBL; CH476666; EDN05055.1; -; Genomic_DNA.
DR RefSeq; XP_001536388.1; XM_001536338.1.
DR AlphaFoldDB; A6RGE3; -.
DR SMR; A6RGE3; -.
DR STRING; 339724.A6RGE3; -.
DR EnsemblFungi; EDN05055; EDN05055; HCAG_08709.
DR GeneID; 5442762; -.
DR KEGG; aje:HCAG_08709; -.
DR VEuPathDB; FungiDB:HCAG_08709; -.
DR HOGENOM; CLU_003041_16_9_1; -.
DR OMA; STMPKFE; -.
DR OrthoDB; 638613at2759; -.
DR Proteomes; UP000009297; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; 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; Nonsense-mediated mRNA decay;
KW Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA processing.
FT CHAIN 1..542
FT /note="ATP-dependent RNA helicase DBP2"
FT /id="PRO_0000310186"
FT DOMAIN 156..331
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 346..507
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 514..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 125..153
FT /note="Q motif"
FT MOTIF 279..282
FT /note="DEAD box"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 542 AA; 59260 MW; C8529852606B062D CRC64;
MSYGGGYGSS RDHYGGGGGG GYSRGGGYGN GYGNSNGYSH GHSSGGYGSY GGAGGYGGGT
GGDRMSNLGA GLKTQNWDLS TMPKFEKSFY KEHPNVSQRS THEVDAFRKE HEITVQGKNV
PRPVETFDEA GFPQYVMSEV KAQGFARPTA IQAQGWPMAL SGRDVVGIAE TGSGKTLTYC
LPAIVHINAQ PLLAPGDGPI VLVLAPTREL AVQIQTEITK FGKSSRIRNT CVYGGVPKGP
QIRDLTRGVE VCIATPGRLI DMLEAGKTNL RRVTYLVLDE ADRMLDMGFE PQIRKIVSQI
RPDRQTCMWS ATWPKDVRQL AQDFLHDYIQ VNIGSMDLSA NHRITQIVEI VSEFEKRDRM
AKHLDRIMEA NKHSKVLIFT GTKRVADDIT RFLRQDGWPA LSIHGDKQQN ERDWVLNEFK
TGKSPIMVAT DVASRGIDVR DITHVLNYDY PNNSEDYVHR IGRTGRAGAK GTAITLFTTD
NAKQARDLVA ILSESKQQID PRLAEMARYG SGGGGNRWGG RGRGRGGFTA SNAAPLGNNR
RW