ID   DBP4_ASPCL              Reviewed;         823 AA.
AC   A1CTZ2;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=ATP-dependent RNA helicase dbp4;
DE            EC=3.6.4.13;
GN   Name=dbp4; ORFNames=ACLA_084740;
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 required for ribosome biogenesis.
CC       Involved in the release of U14 snoRNA in pre-ribosomal complexes.
CC       Required for pre-rRNA cleavage at site A2 (By similarity).
CC       {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: Interacts with the U3 and U14 snoRNAs. Associates with pre-
CC       ribosomal complexes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {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. DDX10/DBP4
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS027060; EAW06779.1; -; Genomic_DNA.
DR   RefSeq; XP_001268205.1; XM_001268204.1.
DR   AlphaFoldDB; A1CTZ2; -.
DR   SMR; A1CTZ2; -.
DR   STRING; 5057.CADACLAP00007759; -.
DR   PRIDE; A1CTZ2; -.
DR   EnsemblFungi; EAW06779; EAW06779; ACLA_084740.
DR   GeneID; 4700335; -.
DR   KEGG; act:ACLA_084740; -.
DR   VEuPathDB; FungiDB:ACLA_084740; -.
DR   eggNOG; KOG0343; Eukaryota.
DR   HOGENOM; CLU_003041_26_1_1; -.
DR   OMA; YDKMFER; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032040; C:small-subunit processome; 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:0034512; F:box C/D RNA binding; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034511; F:U3 snoRNA binding; IEA:EnsemblFungi.
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; IPR025313; DUF4217.
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; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..823
FT                   /note="ATP-dependent RNA helicase dbp4"
FT                   /id="PRO_0000281699"
FT   DOMAIN          80..254
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          280..439
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           49..77
FT                   /note="Q motif"
FT   MOTIF           202..205
FT                   /note="DEAD box"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..545
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..598
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..615
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..800
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         93..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   823 AA;  92965 MW;  6484DB93DD0F96B0 CRC64;
     MAPTTGPRNT KNAKPAVQRS KTLKRKRGQE ELSSLIQRVE GLDLKESFES FSDLPLSEPT
     LSGLTSSHFK TLTDIQSRAI SHALKGRDVL GAAKTGSGKT LAFLVPVLEN LYRRQWAEHD
     GLGALILSPT RELAIQIFEV LRKIGRYHTF SAGLVIGGKS LREEQERLGR MNILVCTPGR
     MLQHLDQTAL FDTYNLQMLV LDEADRILDL GFQQTVDAIV GHLPKERQTL LFSATQTKKV
     SDLARLSLRD PEYVAVHETA STATPAKLQQ HYVIAPLPQK LDILWSFIRS NLKSKTMVFF
     SSGKQVRFVY ESFRHMQPGI PLMHLHGRQK QGGRLDIMTN FSQAKHCVLF STDVAARGLD
     FPAVDWVIQM DCPEDADTYI HRVGRTARYG RDGRAVLFLD PSEEEGMLKR LEQKKVPIEK
     INIKANKQQS IKDQLQNMCF KDPELKYIGQ KAFISYVKSV YIQKDKEIFK LKELKLDEFA
     SSLGLPGAPR IKFIKGDDTK QRKNAPRAAA HLSSDDEAGS DAEEGEPKTK KKEEPQVRTK
     YDRMFERRNQ DVLAEHYSKL INDDGTMVAP PNAGAGADAD EDDDFLSVKR RFDVGDETLG
     MSSDDSDEED DDDDETSPKK ETKVVHIDGK EALVIDSKRR EKLLKSKKKL LKFKGKGTKL
     VYDDEGNAHE VYELEDEDQF KARGDAKEQK AKFLEEEAER TRLADLEDKE IAKQKRREKK
     EKRKAREREL LAEAEDEEET VVQLPPYEGD HDMDGGFSAS EEEEEAARPS KKPKVKFAEP
     DESDKGSEPW YKKSKRTDDK GGSQAPQIQT LEDLESLASG LLG