DBP2_NEOFI
ID DBP2_NEOFI Reviewed; 545 AA.
AC A1DGZ7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=ATP-dependent RNA helicase dbp2;
DE EC=3.6.4.13;
GN Name=dbp2; ORFNames=NFIA_086090;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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 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; DS027696; EAW18654.1; -; Genomic_DNA.
DR RefSeq; XP_001260551.1; XM_001260550.1.
DR AlphaFoldDB; A1DGZ7; -.
DR SMR; A1DGZ7; -.
DR STRING; 36630.CADNFIAP00007673; -.
DR EnsemblFungi; EAW18654; EAW18654; NFIA_086090.
DR GeneID; 4587109; -.
DR KEGG; nfi:NFIA_086090; -.
DR VEuPathDB; FungiDB:NFIA_086090; -.
DR eggNOG; KOG0331; Eukaryota.
DR HOGENOM; CLU_003041_16_9_1; -.
DR OMA; STMPKFE; -.
DR OrthoDB; 638613at2759; -.
DR Proteomes; UP000006702; 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:0003729; F:mRNA binding; IEA:EnsemblFungi.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0030515; F:snoRNA binding; IEA:EnsemblFungi.
DR GO; GO:1990120; P:messenger ribonucleoprotein complex assembly; IEA:EnsemblFungi.
DR GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IEA:EnsemblFungi.
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 GO; GO:0006369; P:termination of RNA polymerase II transcription; 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; Nonsense-mediated mRNA decay;
KW Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA processing.
FT CHAIN 1..545
FT /note="ATP-dependent RNA helicase dbp2"
FT /id="PRO_0000281694"
FT DOMAIN 150..325
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 353..500
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 119..147
FT /note="Q motif"
FT MOTIF 273..276
FT /note="DEAD box"
FT BINDING 163..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 545 AA; 60044 MW; 6A6A9529C9B09CF8 CRC64;
MSSYGGGYQR ESRGDSYRSR GGHDGGYQNG NGYSGGGGYG GGYGNGYGRG GGAAGGDRMS
NLGAGLKKQD WDLDTLPKFE KSFYKEHPDV AARSEREVEE FRKKHEMTVQ GRNVPRPVEN
FDEAGFPQYV LSEVKAQGFE RPTAIQSQGW PMALSGRDVV GIAETGSGKT LTYCLPAIVH
INAQPLLAPG DGPIVLILAP TRELAVQIQT EISKFGKSSR IRNTCVYGGV PKGPQIRDLS
RGVEVCIATP GRLIDMLEAG RTNLRRVTYL VLDEADRMLD MGFEPQIRKI ISQIRPDRQT
CMWSATWPKE VRQLATDFLN DYIQVNIGSM DLSANHRITQ IVEVVSDFEK RDKMIKHLEK
IMENRGNKCL IFTGTKRIAD EITRFLRQDG WPALSIHGDK QQQERDWVLN EFKTGKSPIM
VATDVASRGI DVRDITHVLN YDYPNNSEDY IHRIGRTGRA GAKGTAITFF TTENSKQARD
LVTILTEAKQ QIDPRLAEMV RYSGGGGGHG GYGRWGGRGG RGGGRGRGGS YTASNAAPLG
NARRW
